DRAMP_ID Sequence Sequence_Length Name Swiss_Prot_Entry Family Gene Source Activity Protein_existence Structure Structure_Description PDB_ID Comments Target_Organism Hemolytic_activity Linear/Cyclic/Branched N-terminal_Modification C-terminal_Modification Other_Modifications Stereochemistry Cytotoxicity Binding_Traget Pubmed_ID Reference Author Title DRAMP00005 SLGPAIKATRQVCPKATRFVTVSCKKSDCQ 30 Epicidin 280 (Bacteriocin) O54220 Belongs to the lantibiotic family (Class I bacteriocin) eciA Staphylococcus epidermidis BN 280 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Gram-positive bacteria: Staphylococcus simulans 22 (MIC=0.304 μg/ml), Staphylococcus epidermidis 5 (MIC=3.85 μg/ml), Micrococcus luteus ATCC4698 (MIC=9.7 μg/ml), Staphylococcus carnosus TM300 (MIC=0.175 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic (very possibly) Oxypropionylation Not metioned clearly There are possible lanthionine(Lan)/3-methyllanthionine(Me-Lan) structure association between Thr9 and Cys13, Thr21 and Cys24, Ser23 and Cys29. L No cytotoxicity information found Not found 9726851 Appl Environ Microbiol. 1998 Sep;64(9):3140-3146. Heidrich C, Pag U, Josten M, Metzger J, Jack RW, Bierbaum G, Jung G, Sahl HG. Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analysis of its biosynthetic gene cluster. DRAMP00017 VTSWSLCTPGCTSPGGGSNCSFCC 24 Microbisporicin A1 (Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Microbispora corallina (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Microbisporicins A1 displayed similar antibacterial activity by selectively blocking peptidoglycan biosynthesis, leading to cytoplasmic accumulation of the UDP-linked precursor. PTM: Microbisporicin A1 contains five ether rings: S3-C7, T8-C11, S13-C20, S18-C23, and S21-C24. Also, residues T2 and S5 are dehydrated, Trp4 is chlorinated and Pro14 is hydroxylated (3,4-dihydroxylation)." Human pathogens: L100 Staphylococcus aureus ATCC6538P (MIC≤0.13 μg/ml), L819 Staphylococcus aureus Smith ATCC19636 (MIC≤0.13 μg/ml), L1400 S. aureus MRSA (MIC≤0.13 μg/ml), L613 S. aureus MRSA (MIC≤0.13 μg/ml), L3798 S. aureus VISA (MIC=2 μg/ml), L3798 Staphylococcus epidermidis ATCC12228 (MIC≤0.13 μg/ml), L1729 Staphylococcus haemolyticus met-r (MIC=8 μg/ml), L49 Streptococcus pyogenes (MIC≤0.13 μg/ml), L44 Streptococcus pneumoniae (MIC≤0.13 μg/ml), L559 Enterococcus faecalis (MIC=1 μg/ml), L560 Enterococcus faecalis Van A (MIC=0.5 μg/ml), LA533 Enterococcus faecalis Van A (MIC=1 μg/ml), L568 Enterococcus faecium (MIC=2 μg/ml), L569 Enterococcus faecium Van A (MIC=1 μg/ml), LB518 E. faecium Van A (MIC=2 μg/ml), L884 Lactobacillus garviae (MIC=1 μg/ml), L148 Lactobacillus delbrueckii ATCC04797 (MIC=4 μg/ml), L3607 Clostridium perfringens ATCC13124 (MIC≤0.125 μg/ml), L4018 Clostridium difficile (MIC≤0.125 μg/ml), L4043 Clostridium butyricum (MIC≤0.125 μg/ml), Propionibacterium granulosum ATCC25564 (MIC=0.03 μg/ml), L1329 Propionibacterium acnes (MIC=0.5 μg/ml), Propionibacterium limphophylum ATCC27250 (MIC=0.015 μg/ml), L970 Haemophilus influenzae ATCC19418 (MIC=32 μg/ml), L76 Moraxella catarrhalis ATCC8176 (MIC=0.25 μg/ml), L1613 Neisseria meningitidis ATCC13090V (MIC=0.5 μg/ml), L997 Neisseria gonorrhoeae (MIC=0.25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation and Cyclization ①There are five thioether intramolecular bridges which link Ala3 and Ala7, Ala8 and Ala11, Ala13 and Ala20, Ala18 and Ala23, respectively. ②The residue at position 2 is (Z)-2,3-didehydrobutyrine (Dhb). ③The residue at position 4 is chloro-tryptophan (ClTrp). ④The residue at position 5 is 2,3-didehydroalanine. ⑤The residue at position 8 is 2-Aminobutyric acid (Abu). ⑥The residue at position 14 is bis-hydroxylated proline. L No cytotoxicity information found Not found 18215770 Chem Biol. 2008 Jan;15(1):22-31. Castiglione F, Lazzarini A, Carrano L, Corti E, Ciciliato I, Gastaldo L, Candiani P, Losi D, Marinelli F, Selva E, Parenti F. Determining the structure and mode of action of microbisporicin, a potent lantibiotic active against multiresistant pathogens. DRAMP00032 GNGVLKTISHECNMNTWQFLFTCC 24 Ruminococcin A (RumA; Bacteriocin) P83674, P83676, P83677, Q8VLK0, Q9K381, P83675, P83679, P83680, Q8VLK0 Belongs to the type A lantibiotic family (Class I bacteriocin) rumA1 AND rumA2 AND Ruminococcus gnavus & Ruminococcus hansenii (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin exhibiting activity against a wide range of pathogenic clostridia and B.longum. Developmental stage: Highest expression in mid to late logarithmic growth phase, after which expression decreases slowly before leveling off in the stationary growth phase. Induction: By trypsin. PTM: There are one didehydrobutyrine (Dhb) at T16, one lanthionine (S9-23) and two Beta-methyllanthionines (T7-C12; T22-C24)." Gram-positive bacteria: Bifidobacterium longum (strain: ATCC 15707) (MIC=75 µg/ml), Bacillus cereus (strain: Z4222, TZ415) (MIC=75 µg/ml), Eubacterium contortum (strain: ATCC 25540) (MIC=32.5 µg/ml), Ruminococcus obeum (strain: ATCC 29174) (MIC=32.5 µg/ml), R. gnavus (strain: ATCC 29149) (MIC=75 µg/ml), Clostridium perfringens (strain: CpA) (MIC=75 µg/ml), Clostridium difficile serogroup A (strain: B-1) (MIC=75 µg/ml), C. difficile serogroup C (strain: C253) (MIC=75 µg/ml), C. difficile serogroup S3 (strain: 79685) (MIC=75 µg/ml), C. botulinum type A (strain: CIP 38) (MIC=75 µg/ml), C. botulinum type B (strain: NCTC 7273) (MIC=75 µg/ml), C. botulinum type E (strain: NCTC 8266) (MIC=75 µg/ml), C. bifermentans (strain: NCTC 506) (MIC=75 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic (very possibly) Free Cyclization (possibly) ① It is highly probable that (i) Ser9 and the putative Cys23 and (ii) the putative His22 and Thr24 are associated in a Lanthionine (Lan) and a 3-methyllanthionine (Me-Lan) residue, respectively. ②The residues at position 7 and 16 are (Z)-2,3-didehydrobutyrine (Dhb). L No cytotoxicity information found Cell membrane 11526013##11741840##12089024 Appl Environ Microbiol. 2001 Sep;67(9):4111-4118.##J Bacteriol. 2002 Jan;184(1):18-28.##Appl Environ Microbiol. 2002 Jul;68(7):3424-3431. Dabard J, Bridonneau C, Phillipe C, Anglade P, Molle D, Nardi M, Ladiré M, Girardin H, Marcille F, Gomez A, Fons M.##Gomez A, Ladiré M, Marcille F, Fons M.##Marcille F, Gomez A, Joubert P, Ladiré M, Veau G, Clara A, Gavini F, Willems A, Fons M. Ruminococcin A, a new lantibiotic produced by a Ruminococcus gnavus strain isolated from human feces.##Trypsin mediates growth phase-dependent transcriptional tegulation of genes involved in biosynthesis of ruminococcin A, a lantibiotic produced by a Ruminococcus gnavus strain from a human intestinal microbiota.##Distribution of genes encoding the trypsin-dependent lantibiotic ruminococcin A among bacteria isolated from human fecal microbiota. DRAMP00063 SSSGWLCTLTIECGTIICACR 21 Lantibiotic michiganin-A (Bacteriocin) Q09T02 Belongs to the type B lantibiotic family (Class I bacteriocin) micA Clavibacter michiganensis subsp. Michiganensis (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "MOA: The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 62-67 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor" Clavibacter michiganensis subspecies sepedonicus strain 2136 (MIC=30 pmol/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free All of the threonine residues undergo dehydration, and three of them interact with cysteines via thioether bonds to form methyllanthionine bridges L No cytotoxicity information found Not found 16957199 Appl Environ Microbiol. 2006 Sep;72(9):5814-5821. Holtsmark I, Mantzilas D, Eijsink VG, Brurberg MB. Purification, characterization, and gene sequence of michiganin A, an actagardine-like lantibiotic produced by the tomato pathogen Clavibacter michiganensis subsp. michiganensis. DRAMP00068 MSWLNFLKYIAKYGKKAVSAAWKYKGKVLEWLNVGPTLEWVWQKLKKIAGL 51 Aureocin A53 (Bacteriocin) Q8GPI4 Belongs to the class II bacteriocin aucA Staphylococcus aureus A53 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found 2N8O Function: Antibacterial peptide. It causes membrane permeation. Gram-positive bacteria: Listeria monocytogenes, Staphylococcus simulans (MIC=100 nM), Staphylococcus aureus (MRSA), Streptococcus agalactiae, Micrococcus luteus (MIC=0.15 nM). [Ref.12054867] No hemolytic activity was detected when purified aureocin A53 was spotted on sheep blood agar plates (data not shown in the reference). Linear Formylation Free L No cytotoxicity information found Cell membrane 12054867 J Mol Biol. 2002 Jun 7;319(3):745-756. Netz DJ, Pohl R, Beck-Sickinger AG, Selmer T, Pierik AJ, Bastos Mdo C, Sahl HG. Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus. DRAMP00069 EYHLMNGANGYLTRVNGKTVYRVTKDPVSAVFGVISNCWGSAGAGFGPQH 50 Garvieacin Q (GarQ; Bacteriocin) No entry found Belongs to the class II bacteriocin Not found Lactococcus garvieae BCC 43578 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus coagulans JCM 2257, Listeria monocytogenes ATCC 19115, L. garvieae strains, E. faecium D48S52, Lactobacillus plantarum BCC 9546, Lactobacillus sakeii JCM 1157, L. ivanovii DMST 9012 (MIC=0.1-1.6 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22210221] Purified GarQ, up to 1 mg/mL, was not cytotoxic to Vero (African green monkey kidney), HepG (human liver hepatocarcinoma) and Caco-2 (human colon adenocarcinoma) cell lines. Vero, HepG2 and Caco-2 have 94 ± 8, 97 ± 4 and 89 ± 7 % survival with indicated concentration (1mg/mL) of purified garvieacin Q compared to that of untreated control using the MTT assay. Not found 22210221 Appl Environ Microbiol. 2012 Mar;78(5):1619-1623. Tosukhowong A, Zendo T, Visessanguan W, Roytrakul S, Pumpuang L, Jaresitthikunchai J, Sonomoto K. Garvieacin Q, a novel class II bacteriocin from Lactococcus garvieae BCC 43578. DRAMP00074 ATRSYGNGVYCNNSKCWVNWGEAKENIAGIVISGWASGLAGMGH 44 Enterocin P (Pediocin-like peptide; Bacteriocin) O30434, Q0GFE0 Belongs to the class IIa bacteriocin entP Enterococcus faecium P13 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found "Function: Bacteriocin that inhibits the growth of wide range of Gram-positive bacterial species. Does not inhibit the growth of several strains of Gram-negative bacteria. No hemolytic activity against calf blood. Biophysicochemical properties: pH dependence (Stable between pH 3.0 and pH 7.0); Temperature dependence (Thermostable, retains activity after heating at 100 and 121 degrees Celsius). PTM: Contains one disulfide bond 11-16." [Ref.9361419]Gram-positive bacteria: Pediococcus acidilactici (MIC=69 ng/ml), Pediococcus pentosaceus FBB61 (MIC=136 ng/ml), P. pntosaceus FBB63 (MIC=18 ng/ml), Lactococcus lactis BB24 (MIC=22 ng/ml), Enterococcus faecium (MIC=2 ng/ml), E. faecalis (MIC=238 ng/ml), Staphylococcus carnosus (MIC=139 ng/ml), Bacillus cereus (MIC=286 ng/ml), Clostridium sporogenes (MIC=4 ng/ml), Clostridium tyrobutyricum 3, 5CT (MIC=559 ng/ml), C. tyrobutyricum 1754 (MIC=412 ng/ml), Propionibacteruim sp P4 (MIC=37 ng/ml), Propionibacteruim sp P6 (MIC=26 ng/ml), Clostridium tyrobutyricum (MIC=4 ng/ml), Clostridium botulinum (MIC=259 ng/ml), Listeria monocytogenes 7973 (MIC=35 ng/ml), L. monocytogenes LI5sv1/2 (MIC=33 ng/ml), L. monocytogenes 5105 (MIC=18 ng/ml), L. monocytogenes L11sv4 (MIC=39 ng/ml), L. monocytogenes Scott A (MIC=125 ng/ml), Listeria innocua (MIC=395 ng/ml), Streptococcus aureus 137 (MIC=190 ng/ml), S. aureus 196E (MIC=407 ng/ml), S. aureus 349 (MIC=221 ng/ml), S. aureus 361 (MIC=294 ng/ml), S. aureus 472 (MIC=269 ng/ml), Lactobacillus curvatus (MIC=17 ng/ml), L. fermentum (MIC=1 ng/ml), L. sake (MIC=144 ng/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 9361419##17103378 Appl Environ Microbiol. 1997 Nov;63(11):4321-4330.##Mol Nutr Food Res. 2006 Dec;50(12):1229-1238. Cintas LM, Casaus P, H¥varstein LS, Hern¡ndez PE, Nes IF.##Arlindo S, Calo P, Franco C, Prado M, Cepeda A, Barros-Vel¡zquez J. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum.##Single nucleotide polymorphism analysis of the enterocin P structural gene of Enterococcus faecium strains isolated from nonfermented animal foods. DRAMP00089 TTKNYGNGVCNSVNWCQCGNVWASCNLATGCAAWLCKLA 39 Bacteriocin E50-52 (Preclinical) P85148 Belongs to the class IIa bacteriocin Not found Enterococcus faecium (Streptococcus faecium) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Bacteriocin active against the Gram-negative bacteria and the Gram-positive bacteria. When added to the drinking water of chickens, causes a decrease in the levels of Campylobacter jejuni and S. enteritidis in the ceca, and in the levels of S.enteritidis in the liver and spleen. Gram-negative bacteria: Campylobacter jejuni (MIC=0.025-6.4 µg/ml), Yersinia enterocolitica, Yersinia pseudotuberculosis, Escherichia coli O157:H7 (MIC<1.6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=0.2-0.8 µg/ml), Staphylococcus epidermidis (MIC=0.2-0.8 µg/ml), Listeria monocytogenes (MIC=2-8 µg/ml), Listeria grayi, Listeria innocua, Listeria ivanovii, Listeria denitrificans (MIC=32 µg/ml), Morganella morganii, Salmonella spp., Shigella dysenteriae. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 18293921 J Agric Food Chem. 2008 Mar 26;56(6):1942-1948. Svetoch EA, Eruslanov BV, Perelygin VV, Mitsevich EV, Mitsevich IP, Borzenkov VN, Levchuk VP, Svetoch OE, Kovalev YN, Stepanshin YG, Siragusa GR, Seal BS, Stern NJ. Diverse antimicrobial killing by Enterococcus faecium E 50-52 bacteriocin. DRAMP00090 VNYGNGVSCSKTKCSVNWGQAFQERYTAGINSFVSGVASGAGSIGRRP 48 Carnobacteriocin B2 (CbnB2; Bacteriocin) P38580 Belongs to the class IIa bacteriocin cbnB2 Carnobacterium piscicola LV18B (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 24 residues) CbnB2 forms a disulfide bond and that this peptide has full antimicrobial activity. NMR results indicate that CbnB2 in TFE has a well-defined central helical structure (residues 18-39) but a disordered N terminus. And the central helical structure is conserved. 1CW5 resolved by NMR. "Function: Has antibacterial activity against Listeria and Enterococcus. PTM: Contains one disulfide bond 9-14." [Ref.8163526]Gram-positive bacteria: Lactobacillus plantarum ATCC 4008 (MIC=2 AU/μg), Pediococcus parvulus ATCC 19371 (MIC=8 AU/μg), Listeria monocytogenes ATCC 15313 (MIC=32 AU/μg), Listeria innocua ATCC 33090 (MIC=16 AU/μg), Enterococcus faecium ATCC 11576 (MIC=16 AU/μg), Enterococcus faecalis ATCC 19433 (MIC=16 AU/μg), Enterococcus faecium ATCC 19434 (MIC=4 AU/μg). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free [Ref.8163526 & Ref.10569926] CbnB2 can easily form a disulfide bond between Cys9 and Cys14 L No cytotoxicity information found Not found 8163526##9353214##10569926 J Biol Chem 1994; 269: 12204-12211.##Curr Microbiol. 1997 Dec;35(6):319-326.##Biochemistry. 1999 Nov 23;38(47):15438-15447. Quadri LE et al Stiles ME.##Herbin S, Mathieu F, Brul© F, Branlant C, Lefebvre G, Lebrihi A.##Wang Y, Henz ME, Gallagher NL, Chai S, Gibbs AC, Yan LZ, Stiles ME, Wishart DS, Vederas JC. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV18B.##Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese.##Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria. DRAMP00105 SNDSLWYGVGQFMGKQANCITNHPVKHMIIPGYCLSKILG 40 Enterocin X alpha (Two-peptide bacteriocin) No entry found Belongs to the class IIa bacteriocin enxA Enterococcus faecium KU-B5 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: EntXalpha and EntXbeta encode a double-glycine-type prepeptide with an 18-residue leader sequence, representing the typical structure of class II bacteriocin prepeptides. When combined, Xalpha and Xbeta display variably enhanced or reduced antibacterial activity toward a panel of indicators compared to each peptide individually. Gram-positive bacteria: Enterococcus faecalis JCM 5803 (MIC=50.8 nM), Enterococcus faecalis OU510 (MIC=102 nM), Enterococcus faecium TUA 1344L (MIC=50.8 nM), Enterococcus hirae ATCC 10541 (MIC=50.8 nM), Lactobacillus plantarum ATCC 14917 (MIC=102 nM), Lactobacillus sakeii ssp.sakei JCM 1157 (MIC=50.8 nM), Lactococcus lactis ssp.cremoris ATCC 19257 (MIC=813 nM), Listeria innocua ATCC 33090 (MIC=25.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 20418437 Appl Environ Microbiol. 2010 Jul;76(13):4542-4545. Hu CB, Malaphan W, Zendo T, Nakayama J, Sonomoto K. Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides. DRAMP00106 IAPIIVAGLGYLVKDAWDHSDQIISGFKKGWNGGRRK 37 Enterocin X beta (Two-peptide bacteriocin) No entry found Belongs to the class IIa bacteriocin enxB Enterococcus faecium KU-B5 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: EntXalpha and EntXbeta encode a double-glycine-type prepeptide with an 18-residue leader sequence, representing the typical structure of class II bacteriocin prepeptides. When combined, Xalpha and Xbeta display variably enhanced or reduced antibacterial activity toward a panel of indicators compared to each peptide individually. Gram-positive bacteria: Enterococcus faecalis JCM 5803 (MIC=813 nM), Enterococcus faecalis OU510 (MIC=813 nM), E. faecium TUA 1344L (MIC=813 nM), Enterococcus hirae ATCC 10541 (MIC=406 nM), Lactobacillus plantarum ATCC 14917 (MIC=813 nM), Lactobacillus sakeii ssp.sakei JCM 1157 (MIC=102 nM), Bacillus circulans JCM 2504 (MIC=3250 nM), Bacillus coagulans JCM 2257 (MIC=3250 nM), Bacillus subtilis JCM 1465 (MIC=3250 nM), Listeria innocua ATCC 33090 (MIC=3250 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 20418437 Appl Environ Microbiol. 2010 Jul;76(13):4542-4545. Hu CB, Malaphan W, Zendo T, Nakayama J, Sonomoto K. Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides. DRAMP00107 TNYGNGVGVPDAIMAGIIKLIFIFNIRQGYNFGKKAT 37 Bacteriocin L-1077 No entry found Belongs to the class IIa bacteriocin Not found Lactobacillus salivarius L-1077 (NRRL B-50053) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Salmonella Enteritidis 1 (MIC=0.19 ug/ml), S. Enteritidis 4 (MIC=0.38 ug/ml), S. Enteritidis 204 (MIC=0.38 ug/ml), S. Enteritidis 237 (MIC=0.19 ug/ml), Salmonella Choleraesuis 434/4 (MIC=0.38 ug/ml), S. Choleraesuis 370 (MIC=0.19 ug/ml), Salmonella Typhimurium 483/6 (MIC=0.19 ug/ml), S. Typhimurium 44/8 (MIC=0.19 ug/ml), Salmonella Gallinarum-Pullorum (MIC=0.19 ug/ml), Escherichia coli HB 101 (MIC=0.19 ug/ml), E. coli-600 (MIC=0.19 ug/ml), E. coli O157:H7 Y-63 (MIC=0.19 ug/ml), E. coli O157:H7 G-35 (MIC=0.19 ug/ml), E. coli O157:H7 OD 30 (MIC=0.19 ug/ml), E. coli O157:H7 T lab 39 (MIC=0.19 ug/ml), Yersinia enterocolitica 03 (MIC=0.76 ug/ml), Y. enterocolitica 09 (MIC=0.76 ug/ml), Y. enterocolitica 11 (MIC=0.76 ug/ml), Citrobacter freundii (MIC=0.76 ug/ml), Klebsiella pneumoniae (MIC=0.76 ug/ml), Shigella dysenteriae (MIC=0.76 ug/ml), Yersinia pseudotuberculosis 4 (MIC=0.76 ug/ml), Y. pseudotuberculosis 99/14 (MIC=0.76 µg/ml), Pseudomonas aeruginosa 508 (MIC=0.38 ug/ml), Proteus mirabilis (MIC=0.38 ug/ml), Morganella morganii (MIC=0.38 µg/ml), Proteus vulgaris 7A (MIC=1.5 ug/ml),Campylobacter jejuni L-4 (MIC=0.09 ug/ml);##Gram-positive bacteria: Clostridium perfringens 13124 (MIC=0.7 ug/ml), Listeria monocytogenes A 9-72 (MIC=0.19 ug/ml), Staphylococcus aureus (MIC=0.76 ug/ml), Staphylococcus epidermidis (MIC=0.76 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 21378051 Appl Environ Microbiol. 2011 Apr;77(8):2749-2754. Svetoch EA, Eruslanov BV, Levchuk VP, Perelygin VV, Mitsevich EV, Mitsevich IP, Stepanshin J, Dyatlov I, Seal BS, Stern NJ. Isolation of Lactobacillus salivarius 1077 (NRRL B-50053) and characterization of its bacteriocin, including the antimicrobial activity spectrum. DRAMP00126 FNRGGYNFGKSVRHVVDAIGSVAGIRGILKSIR 33 Plantaricin E (PlnE; Bacteriocin) P71470, Q7AKV7 Belongs to the class IIb bacteriocin plnE Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (3 helices; 19 residues) In DPC micelles, PlnE has an N-terminal alpha-helix (residues 10-21), and a C-terminal alpha-helix-like structure (residues 25-31). Both helices in plnE are amphiphilic, while the helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. PlnE has two GxxxG motifs which are putative helix-helix interaction motifs, one at residues 5 to 9 and one at residues 20 to 24. 2JUI resolved by NMR. Comment: No comments found on DRAMP database Gram-positive bacteria: Pediococcus pentosaceus Pac 1.0 (MIC=5 nM), Lactobacillus plantarum 965 (MIC=7 nM), Lactobacillus casei subsp.casei NCDO 161 (MIC=20 nM), Lactobacillus casei NCDO 2713 (MIC=150 nM), Lactobacillus sakei NCDO 2714 (MIC=4 nM), Lactobacillus viridescens NCDO 1655 (MIC=2 nM), Pediococcus pentosaceus NCDO 990 (MIC=30 nM), Lactobacillus sakei 706 (MIC=100 nM), Pediococcus acidilactici CH (MIC=10 nM), Lactobacillus curvatus 89 (MIC=5 nM). [PlnE:PlnF=1:1] No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free There is a possible hydrogen bond/salt bridge between Asp17 and Arg26 L No cytotoxicity information found Not found 8117074##18555030 Appl Environ Microbiol. 1994 Jan;60(1):160-166.##Biochim Biophys Acta. 2008 Nov;1784(11):1711-1719. Diep DB, Håvarstein LS, Nissen-Meyer J, Nes IF.##Fimland N, Rogne P, Fimland G, Nissen-Meyer J, Kristiansen P.E. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system.##Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. DRAMP00127 VFHAYSARGVRNNYKSAVGPADWVISAVRGFIHG 34 Plantaricin F (PlnF; Bacteriocin) P71469, Q7AKV8 Belongs to the class IIb bacteriocin plnF Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 26 residues) In DPC micelles, PlnF has a long central alpha-helix (residues 7-32) with a kink of 38+/-7 degrees at Pro20. There is some flexibility in the helix in the kink region. The helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. plnF has one such motif at residues 30 to 34. The helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. PlnF has one GxxxG motif at residues 30 to 34. 2RLW resolved by NMR. Function: A strain-specific antagonistic activity was detected at nanomolar concentrations when PlnE and PlnF were combined. Complementary peptides were at least 103 times more active when they were combined than when they were present individually, and optimal activity was obtained when the complementary peptides were present in approximately equal amounts. Gram-positive bacteria: Pediococcus pentosaceus Pac 1.0 (MIC=5 nM), Lactobacillus plantarum 965 (MIC=7 nM), Lactobacillus casei subsp.casei NCDO 161 (MIC=20 nM), Lactobacillus casei NCDO 2713 (MIC=150 nM), Lactobacillus sakei NCDO 2714 (MIC=4 nM), Lactobacillus viridescens NCDO 1655 (MIC=2 nM), Pediococcus pentosaceus NCDO 990 (MIC=30 nM), Lactobacillus sakei 706 (MIC=100 nM), Pediococcus acidilactici CH (MIC=10 nM), Lactobacillus curvatus 89 (MIC=5 nM). [PlnE:PlnF=1:1] No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free There is a possible hydrogen bond/salt bridge between Asn12/Asn13 and Asp22 L No cytotoxicity information found Not found 9603847##19538999##18555030 Appl Environ Microbiol. 1994 Jan;60(1):160-166.##Appl Environ Microbiol. 1998 Jun;64(6):2269-2272.## Diep DB, Håvarstein LS, Nissen-Meyer J, Nes IF.##Anderssen EL, Diep DB, Nes IF, Eijsink VG, Nissen-Meyer J.##Fimland N, Rogne P, Fimland G, Nissen-Meyer J, Kristiansen P.E. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system.##Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A.##Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. DRAMP00128 GAWKNFWSSLRKGFYDGEAGRAIRR 25 Plantaricin J (PlnJ; Bacteriocin) P71461, Q7AKW6 Belongs to the class IIb bacteriocin plnJ Lactobacillus plantarum C11 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix In DPC micelles, PlnJ has an N-terminal amphiphilic alpha-helix between Trp-3 and Tyr-15. Crucial residues: Gly-13 in PlnJ is very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. Gly-20 in PlnJ was replaced, the activity was reduced less than 10-fold. 2KHF, 2KHG resolved by NMR. Function: A 1:1 ratio of PlnK and PlanJ is at least 1000 times more active than the individual peptide. Gram-positive bacteria: Pediococcus pentosaceus Pac 1.0 (MIC=50 nM), Lactobacillus plantarum 965 (MIC=0.1 nM), L. sake NCDO 2714 (MIC=50 nM), Leptostylus viridescens NCDO 1655 (MIC=5 nM). [PlnJ:PlnK=1:1] No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 9603847##19538999 Appl Environ Microbiol. 1998 Jun;64(6):2269-2272.##Peptides. 2009 Sep;30(9):1613-1621. Anderssen EL, Diep DB, Nes IF, Eijsink VG, Nissen-Meyer J.##Rogne P, Haugen C, Fimland G, Nissen-Meyer J, Kristiansen PE. Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A.##Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. DRAMP00129 RRSRKNGIGYAIGYAFGAVERAVLGGSRDYNK 32 Plantaricin K (PlnK; Bacteriocin) P71460 Belongs to the class IIb bacteriocin plnK Lactobacillus plantarum C11 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix In DPC micelles, PlnK forms a central amphiphilic alpha-helix between Gly-9 and Leu-24. Crucial residues: Gly-17 in PlnK is very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. Gly-7, Gly-9, Gly-24 and Gly-25 in PlnK were replaced, the activity was reduced less than 10-fold. 2KEG, 2KEH resolved by NMR. Function: A 1:1 ratio of PlnK and PlanJ is at least 1000 times more active than the individual peptide. Gram-positive bacteria: Pediococcus pentosaceus Pac 1.0 (MIC=50 nM), Lactobacillus plantarum 965 (MIC=0.1 nM), L. sake NCDO 2714 (MIC=50 nM), Leptostylus viridescens NCDO 1655 (MIC=5 nM). [PlnJ:PlnK=1:1] No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 9603847##19538999 Appl Environ Microbiol. 1998 Jun;64(6):2269-2272.##Peptides. 2009 Sep;30(9):1613-1621. Anderssen EL, Diep DB, Nes IF, Eijsink VG, Nissen-Meyer J.##Rogne P, Haugen C, Fimland G, Nissen-Meyer J, Kristiansen PE. Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A.##Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. DRAMP00136 NRWYCNSAAGGVGGAAVCGLAGYVGEAKENIAGEVRKGWGMAGGFTHNKACKSFPGSGWASG 62 Enterocin E-760 (Bacteriocin) P85147 Belongs to the class IIb bacteriocin Not found Enterococcus sp. (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: The enterocin demonstrated thermostability by retaining activity after 5 min at 100 degrees C and was stable at pH values between 5.0 and 8.7. However, activity was lost below pH 3.0 and above pH 9.5. No hemolytic activity. [Ref.18086839]Gram-positive bacteria: Listeria monocytogenes 9-72 (MIC=0.1 μg/ml), Staphylococcus epidermidis (MIC=1.6 μg/ml), S. aureus (MIC=1.6 μg/ml);##Gram-negative bacteria: S. enterica serovar Enteritidis 1 (MIC=0.2 μg/ml), S. enterica serovar Enteritidis 4 (MIC=0.4 μg/ml), S. enterica serovar Enteritidis 204 (MIC=0.2 μg/ml), S. enterica serovar Enteritidis 237 (MIC=0.2 μg/ml), S. enterica serovar Choleraesuis 434/4 (MIC=0.4 μg/ml), S. enterica serovar Choleraesuis 370 (MIC=0.4 μg/ml), S. enterica serovar Typhimurium 383/60 (MIC=0.4 μg/ml), S. enterica serovar Typhimurium 320 (MIC=0.2 μg/ml), S. enterica serovar Gallinarum biovar Pullorum (MIC=0.4 μg/ml), Escherichia coli HB101 (MIC=0.1 μg/ml), E. coli C600 (MIC=0.1 μg/ml), E. coli O157:H7 Y-63 (MIC=1.6 μg/ml), E. coli O157:H7 G-3 (MIC=1.6 μg/ml), E. coli O157:H7 OD-3 (MIC=1.6 μg/ml), E. coli O157:H7 T-39 (MIC=1.6 μg/ml), Yersinia enterocolitica 03 (MIC=0.1 μg/ml), Y. enterocolitica 09 (MIC=0.1 μg/ml), Y. enterocolitica 04 (MIC=0.1 μg/ml), Y. pseudotuberculosis ser 4 (MIC=3.2 μg/ml), Y. pseudotuberculosis 14 (MIC=3.2 μg/ml), Citrobacter freundii (MIC=1.6 μg/ml), Klebsiella pneumoniae (MIC=3.2 μg/ml), Shigella dysenteriae (MIC=0.1 μg/ml), Campylobacter jejuni L4 (MIC=0.1 μg/ml), Campylobacter P 1-R (MIC=0.2 μg/ml), Campylobacter P-45 (MIC=0.4 μg/ml), Campylobacter lari R (MIC=0.2 μg/ml), Campylobacter LB 6-R (MIC=0.1 μg/ml), Campylobacter C/D (MIC=0.2 μg/ml),. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 18086839 Antimicrob Agents Chemother. 2008 Mar;52(3):1094-1100. Line JE, Svetoch EA, Eruslanov BV, Perelygin VV, Mitsevich EV, Mitsevich IP, Levchuk VP, Svetoch OE, Seal BS, Siragusa GR, Stern NJ. Isolation and purification of enterocin E-760 with broad antimicrobial activity against gram-positive and Gram-negative bacteria. DRAMP00171 LIDHLGAPRWAVDTILGAIAVGNLASWVLALVPGPGWAVKAGLATAAAIVKHQGKAAAAAW 61 Lactocyclicin Q (Bacteriocin) B9ZZY0 Belongs to the class IIc bacteriocin lycQ Lactococcus sp. strain QU 12 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found Comment: No comments found on DRAMP database "Gram-positive bacteria: Lactococcus sp.strain QU 12 (MIC=34.3 µM), Lactococcus lactis subsp.lactis JCM 7638 (MIC=0.141 µM), L. lactis subsp.lactis ATCC 19435 (MIC=0.141 µM), L. lactis subsp.lactis IL1403 (MIC=0.141 µM), L. lactis QU 1 (MIC=0.141 µM), L. lactis subsp.cremoris ATCC 19275 (MIC=0.283 µM), Lactococcus raffinolactis JCM 5706 (MIC=0.71 µM), Lactobacillus sakei subsp.sakei JCM 1157 (MIC=0.015 µM), Lactobacillus casei subsp.casei JCM 1134 (MIC=2.27 µM), Leuconostoc brevis JCM 1059 (MIC=1.14 µM), L. acidophilus JCM 1132 (MIC=2.86 µM), L. coryniformis subsp.coryniformis JCM 1164 (MIC=2.86 µM), L. kimchii JCM 10707 (MIC=0.71 µM), L. mesenteroides subsp.mesenteroides JCM 6124 (MIC=1.03 µM), Weissella cibaria JCM 12495 (MIC=0.71 µM), Pediococcus pentosaceus JCM 5885 (MIC=0.55 µM), P. pentosaceus JCM 5890 (MIC=2.86 µM), P. acidilactici JCM 8797 (MIC=2.86 µM), P. dextrinicus JCM 5887 (MIC=0.141 µM), Enterococcus faecium JCM5804 (MIC=0.71 µM), E. hirae ATCC 10541 (MIC=0.71 µM), E. durans NBRC 100479 (MIC=0.71 µM), E. faecalis JCM 5803 (MIC=0.26 µM), Streptococcus salivarius JCM 5707 (MIC=22.9 µM), S. bovis JCM 5802 (MIC=22.9 µM), Bacillus coagulans JCM 2257 (MIC=0.015 µM), B. circulans JCM 2504 (MIC=0.031 µM), B. subtilis JCM 1465 (MIC=0.064 µM), B. cereus JCM 2152 (MIC=11.4 µM), Micrococcus luteus IFO 12708 (MIC=5.7 µM), Listeria innocua ATCC 33090 (MIC=1.03 µM), L. monocytogenes ATCC BAA-679 (MIC=1.03 µM), Staphylococcus aureus subsp.aureus ATCC 12600 (MIC=91.6 µM); Gram-negative bacteria: Escherichia coli JM109 (MIC=34.3 µM), E. coli NBRC 3301 (MIC=17.3 µM)." No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) The whole peptide has a cyclic structure in which N and C termini are bound to each other. L No cytotoxicity information found Not found 19139222##21948835 Appl Environ Microbiol. 2009 Mar;75(6):1552-1558.##Appl Environ Microbiol. 2011 Nov;77(22):8164-8170. Sawa N, Zendo T, Kiyofuji J, Fujita K, Himeno K, Nakayama J, Sonomoto K.##Masuda Y, Ono H, Kitagawa H, Ito H, Mu F, Sawa N, Zendo T, Sonomoto K. Identification and characterization of lactocyclicin Q, a novel cyclic bacteriocin produced by Lactococcus sp. strain QU 12.##Identification and characterization of leucocyclicin Q, a novel cyclic bacteriocin produced by Leuconostoc mesenteroides TK41401. DRAMP00173 LVNQLGISKSLANTILGAIAVGNLASWVLALVPGPGWATKAALATAETIVKHEGKAAAIAW 61 Leucocyclicin Q (Bacteriocin) G5ELQ0 Belongs to the class IIc bacteriocin lcyQ Leuconostoc mesenteroides TK41401 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Function: This precursor showed high similarity to the precursor of lactocyclicin Q, a cyclic bacteriocin produced by Lactococcus sp. strain QU 12. This is the first report of a cyclic bacteriocin produced by a strain of the genus Leuconostoc. Gram-positive bacteria: Lactococcus lactis ssp. lactis JCM 7638 (MIC=0.038 µM), L. lactis ssp. lactis ATCC 19435 (MIC=0.038 µM), L. sp. QU 12 (MIC=1.203 µM), Lactobacillus sakei ssp. sakei JCM 1157 (MIC=0.038 µM), Weissella cibaria JCM 12495 (MIC=2.405 µM), W. paramesenteroides JCM 9890 (MIC=0.075 µM), Pediococcus pentosaceus JCM 5885 (MIC=2.405 µM), P. dextrinicus JCM 5887 (MIC=0.038 µM), Enterococcus faecium JCM 5804 (MIC=0.038 µM), E. faecalis JCM 5803 (MIC=0.15 µM), Streptococcus salivarius JCM 5707 (MIC=2.405 µM), S. bovis JCM 5802 (MIC=0.601 µM), S. mutans JCM 5705 (MIC=19.25 µM), Bacillus coagulans JCM 2257 (MIC=0.075 µM), B. subtilis ssp. subtilis JCM 1465 (MIC=0.601 µM), B. cereus JCM 2152 (MIC=2.405 µM), Kocuria rhizophila NBRC 12708 (MIC=9.623 µM), Listeria innocua ATCC 33090 (MIC=0.601 µM), Leuconostoc mesenteroides ssp. mes. JCM 6124 (MIC=0.3 µM), Escherichia coli JM109 (MIC=38.49 µM), E. coli NBRC 3301 (MIC=38.49 µM) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) The whole peptide has a cyclic structure in which N and C termini are bound to each other. L No cytotoxicity information found Not found 21948835 Appl Environ Microbiol. 2011 Nov;77(22):8164-8170. Masuda Y, Ono H, Kitagawa H, Ito H, Mu F, Sawa N, Zendo T, Sonomoto K. Identification and characterization of leucocyclicin Q, a novel cyclic bacteriocin produced by Leuconostoc mesenteroides TK41401. DRAMP00177 ENDHRMPNNLNRPNNLSKGGAKCGAAIAGGLFGIPKGPLAWAAGLANVYSKCN 53 Enterocin B (EntB; Bacteriocin) O34017 Belongs to the class IId bacteriocin entB Enterococcus faecium T136 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Enterococcus faecalis JCM 5803 (MIC=86.9 nM), Enterococcus faecalis OU510 (MIC=174 nM), E. faecium TUA 1344L (MIC=43.4 nM), E. hirae ATCC 10541 (MIC=5.44 nM), Lactobacillus plantarum ATCC 14917 (MIC=86.9 nM), L. sakei ssp. sakei JCM 1157 (MIC=5.44 nM), Bacillus coagulans JCM 2257 (MIC=89000 nM), Bacillus subtilis JCM 1465 (MIC=44500 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free The peptide has forms a disulfide bond between Cys-23 and Cys-52 L No cytotoxicity information found Not found 10224016##9245817 Appl Environ Microbiol. 1999 May;65(5):2170-2178.##Microbiology. 1997 Jul;143 (Pt 7):2287-2294. Franz CM, Worobo RW, Quadri LE, Schillinger U, Holzapfel WH, Vederas JC, Stiles ME.##Casaus P, Nilsen T, Cintas LM, Nes IF, Hern¡ndez PE, Holo H. Atypical genetic locus associated with constitutive production of enterocin B by Enterococcus faecium BFE 900.##Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A. DRAMP00178 MLAKIKAMIKKFPNPYTLAAKLTTYEINWYKQQYGRYPWERPVA 44 Enterocin EJ97 (EntEJ97; Bacteriocin) Q8KMU4 Belongs to the class IId bacteriocin ej97a Enterococcus faecalis EJ97 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus circulans (MIC=12 µg/ml), Bacillus coagulans CECT 12 (MIC=2 µg/ml), Bacillus megaterium (MIC=4 µg/ml), Bacillus stearothermophilus CECT 49 (MIC=14 µg/ml), Bacillus stearothermophilus CECT 148 (MIC=12 µg/ml), Bacillus subtilis (MIC=12 µg/ml), Paenibacillus macerans CECT 19 (MIC=4 µg/ml), Enterococcus faecalis ssp.faecalis S-13 (MIC=6 µg/ml), E. faecalis ssp.faecalis S-14 (MIC=8 µg/ml), E. faecalis ssp.faecalis S-32 (MIC=12 µg/ml), E. faecalis ssp.faecalis S-86 (MIC=8 µg/ml), E. faecalis ssp.liquefaciens S-39 (MIC=6 µg/ml), E. faecalis ssp.liquefaciens S-40 (MIC=8 µg/ml), E. faecalis ssp. liquefaciens S-47 (MIC=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 12620853##20385607##9871020 Appl Environ Microbiol. 2003 Mar;69(3):1633-1641.##Protein Eng Des Sel. 2010 Jul;23(7):507-518.##Arch Microbiol. 1998 Dec;171(1):59-65. S¡nchez-Hidalgo M, Maqueda M, G¡lvez A, Abriouel H, Valdivia E, Mart­nez-Bueno M.##Neira JL, Contreras LM, de los Pa±os OR, S¡nchez-Hidalgo M, Mart­nez-Bueno M, Maqueda M, Rico M.##G¡lvez A, Valdivia E, Abriouel H, Camafeita E, Mendez E, Mart­nez-Bueno M, Maqueda M. The genes coding for enterocin EJ97 production by Enterococcus faecalis EJ97 are located on a conjugative plasmid.##Structural characterisation of the natively unfolded enterocin EJ97.##Isolation and characterization of enterocin EJ97, a bacteriocin produced by Enterococcus faecalis EJ97. DRAMP00189 KGLGKLIGIDWLLGQAKDAVKQYKKDYKRWH 31 Leucocin Q (Bacteriocin) No entry found Belongs to the class IId bacteriocin LccQ Leuconostoc pseudomesenteroides QU 15 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Leuc.pseudomesenteroides QU 15 (isolated from Nukadoko) produce at least three bacteriocins, leucocin A, and two novel bacteriocins termed leucocin Q and leucocin Gram-positive bacteria: Bacillus circulans JCM 2504T (MIC=4.10 µmol/L), Listeria innocua ATCC 33090 (MIC=0.03 µmol/L), Listeria monocytogenes ATCC BAA-679 (MIC=1.03 µmol/L), Enterococcus faecalis JCM 5803 (MIC=4.10 µmol/L), Lactobacillus plantarum ATCC 14917 (MIC=4.10 µmol/L), Lactobacillus sakei ssp. sakei JCM 1157 (MIC=1.04 µmol/L), Leuconostoc mesenteroides ssp. mesenteroides JCM 6124 (MIC=4.10 µmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 20070442 J Appl Microbiol. 2010 Jul;109(1):282-291. Sawa N, Okamura K, Zendo T, Himeno K, Nakayama J, Sonomoto K. Identification and characterization of novel multiple bacteriocins produced by Leuconostoc pseudomesenteroides QU 15. DRAMP00190 MNKEYNSISNFKKITNKDLQNINGGFIGRAIGDFVYFGAKGLRESGKLLNYYYKHKH 57 Leucocin N (Bacteriocin) No entry found Belongs to the class IId bacteriocin LccN Leuconostoc pseudomesenteroides QU 15 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Leuc.pseudomesenteroides QU 15 (isolated from Nukadoko) produce at least three bacteriocins, leucocin A, and two novel bacteriocins termed leucocin Q and leucocin N. Gram-positive bacteria: Bacillus circulans JCM 2504T (MIC=5.20 µmol/L), Listeria innocua ATCC 33090 (MIC=1.30 µmol/L), Listeria monocytogenes ATCC BAA-679 (MIC=1.30 µmol/L), Enterococcus faecalis JCM 5803 (MIC=5.20 µmol/L), Lactobacillus plantarum ATCC 14917 (MIC=2.60 µmol/L), Lactobacillus sakei ssp. sakei JCM 1157 (MIC=1.30 µmol/L), Leuconostoc mesenteroides ssp. mesenteroides JCM 6124 (MIC=2.60 µmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 20070442 J Appl Microbiol. 2010 Jul;109(1):282-291. Sawa N, Okamura K, Zendo T, Himeno K, Nakayama J, Sonomoto K. Identification and characterization of novel multiple bacteriocins produced by Leuconostoc pseudomesenteroides QU 15. DRAMP00191 GGAGHVPEYFVGIGTPISFYG 21 Microcin J25 (MccJ25; Bacteriocin) Q9X2V7 Belongs to the class I microcin mcjA Escherichia coli AY25 (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Beta strand MccJ25 does not have a head-to-tail cyclic structure but rather a side chain to backbone cyclization between Glu8 and the N-terminus. This creates an embedded ring that is threaded by the C-terminal tail of the molecule, forming a noose-like feature. The three-dimensional structure deduced from NMR data suggests that slippage of the noose is prevented by two aromatic residues flanking the embedded ring. 1Q71, 1PP5 resolved by NMR. "Function: Microcin J25 is a 21 amino acid bacterial peptide that has potent antibacterial activity against Gram-negative bacteria, resulting from its interaction with RNA polymerase. Induction: At the onset of stationary growth phase. PTM: Isoglutamyl glycine isopeptide between G1 and E8." Gram-negative bacteria: Escherichia coli BM21 (MIC=0.08 µg/ml), E. coli AB1133 (MIC=0.02 µg/ml), E. coli RYC816 (MIC=0.04 µg/ml), E. coli AY29 (MIC=0.04 µg/ml), Salmonella species, Shigella flexneri. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal between Gly and Glu Free L No cytotoxicity information found Not found 1429464##10092860##14531690##14531661 J Bacteriol. 1992 Nov;174(22):7428-7435.##Eur J Biochem. 1999 Feb;259(3):747-755.##J Am Chem Soc. 2003 Oct 15;125(41):12464-74.##J Am Chem Soc. 2003 Oct 15;125(41):12382-3. Salom³n RA, Far­as RN.##Blond A, P©duzzi J, Goulard C, Chiuchiolo MJ, Barth©l©my M, Prigent Y, Salom³n RA, Far­as RN, Moreno F, Rebuffat S.##Rosengren KJ, Clark RJ, Daly NL, Göransson U, Jones A, Craik DJ.##Bayro MJ, Mukhopadhyay J, Swapna GV, Huang JY, Ma LC, Sineva E, Dawson PE, Montelione GT, Ebright RH. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli.##The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli.##Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone.##Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot. DRAMP00201 SCNCVCGVCCSCSP 14 Amythiamicin A/B (Bacteriocin) P0C912 Belongs to the thiocillin family Not found Amycolatopsis sp. (strain MI481-42F4 / FERM P-12739) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has bacteriocidal activity against Gram-positive bacteria: including multi-drug resistant strains such as Staphylococcus aureus MS9610 and Methicillin-resistant S.aureus, but is not active against most Gram-negative bacteria and fungi. PTM: ①Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings. ②Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with the alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser. ③The diketopiperazine ester in form C may be formed by cyclization and transesterification of the C-terminal dipeptide." Gram-positive bacteria: Staphylococcus aureus MS9610 (MIC=0.2 µg/ml), Methicillin-resistant S. aureus (MIC=0.2 µg/ml), Staphylococcus aureus FDA209P (MIC=0.1 µg/ml), Micrococcus luteus FDA16 (MIC=0.1 µg/ml), M. luteus IFO3333 (MIC=0.78 µg/ml), M. luteus PCI1001 (MIC=0.2 µg/ml), Bacillus anthracis (MIC=0.1 µg/ml), B. subtilis NRRL B-558 (MIC=0.2 µg/ml), B. subtilis PCI219 (MIC=0.2 µg/ml), B. cereus ATCC 10702 (MIC=0.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8040071 J Antibiot (Tokyo). 1994 Jun;47(6):668-674. Shimanaka K, Kinoshita N, Iinuma H, Hamada M, Takeuchi T. Novel antibiotics, amythiamicins. I. Taxonomy, fermentation, isolation, physico-chemical properties, and antimicrobial activity. DRAMP00204 STNCFCYICCSCSS 14 Thiocillin GE37468 (Antibiotic GE37468; Bacteriocin) P0C8P9, G1ECL0 Belongs to the thiocillin family getA Streptomyces sp. (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has bacteriocidal activity against both aerobic and anaerobic Gram-positive bacteria. Has poor activity against Gram-negative bacteria, with the exception of B.fragilis. Inhibits bacterial protein biosynthesis by acting on elongation factor Tu ( Gram-positive bacteria: Bacillus subtilis (MIC=0.047 µg/ml), Staphylococcus aureus (MRSA) (MIC=0.047 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization Free ①GE37468 has a macrocyclic ring composed of 10 residues (Ser1 to Cys10). ②Cys6 converts to a thiazoline while four other Cys residues (Cys4, Cys9, Cys10 and Cys12) are fully desaturated to thiazoles in GE37468. ③Ile8 converts to β-methyl-δ-hydroxy-proline(mhP) through a predicted tandem double hydroxylation/cyclization mechanism. L No cytotoxicity information found Not found 21788474 Proc Natl Acad Sci U S A. 2011 Aug 9;108(32):13053-13058. Young TS, Walsh CT. Identification of the thiazolyl peptide GE37468 gene cluster from Streptomyces ATCC 55365 and heterologous expression in Streptomyces lividans. DRAMP00218 RCTCTTIISSSSTF 14 Plantazolicin (PZN; Bacteriocin) D3VML5, B3A0N7 Not found pznA Bacillus amyloliquefaciens FZB42 & Bacillus pumilus (Bacillus mesentericus) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Peptide antibiotic inhibiting growth of Gram-positive bacteria: in the dimethylated form plantazolicin A. The desmethyl form plantazolicin B has no antibiotic activity. The mode of action appears to be disruption of cell walls and lysis of cells. Has antibacterial activity. Gram-positive bacteria: Bacillus subtilis HB0042, Bacillus subtilis strain 168, Bacillus megaterium 7A1, Bacillus anthracis (MIC=2-4 µg/ml), Bacillus brevis strain ATCC 8246, Bacillus cereus strain ATCC 14579 and strain CU1065, Bacillus licheniformis strain ATCC 9789, Micrococcus luteus, Bacillus sphaericus, Paenibacillus granivorans and Streptococcus pyogenes (MIC=128 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic (possibly) Free Free 10 residues (Cys, Ser/Thr) potentially serve as a site of heterocycle formation L No cytotoxicity information found Not found 20971906 J Bacteriol. 2011 Jan;193(1):215-224. Scholz R, Molohon KJ, Nachtigall J, Vater J, Markley AL, S¼ssmuth RD, Mitchell DA, Borriss R. Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42. DRAMP00222 GETDPNTQLLNDLGNNMAWGAALGAPGGLGSAALGAAGGALQTVGQGLIDHGPVNVFIPVLIGPSWNGSGSGYNSATSSSGSGS 84 Microcin E492 (MccE492; Bacteriocin) Q9Z4N4 Not found mceA Klebsiella pneumoniae RYC492 (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Channel-forming bacteriocin. Forms cation-selective channels. Active on enterobacteria, with highest activity against Escherichia coli. The unmodified protein is active against Escherichia coli and S. enteritidis. When the siderophore ester is present at Ser-99, antibacterial activity against these species is increased and activity is also detected against E. cloacae and K. pneumoniae. PTM: The C-terminal Ser is modified by attachment to a siderophore similar to enterobactin, which can bind one atom of iron. The modification consists of an ester linkage of the serine carboxyl to O6 of a glucose which is linked by a C-glycosidic bond to the 5'-benzoyl of a linear triester of N-(2,3-dihydroxybenzoyl)serine. Presence of the siderophore ester increases the antibacterial activity of the protein." Gram-negative bacteria: Escherichia coli F (MIC=0.14 µM), Escherichia coli 363 (MIC=0.02 µM), Escherichia coli ML35p (MIC=0.14 µM), Escherichia coli GM1 (MIC=0.04 µM), Escherichia coli GM1 KP1060(MIC=0.65 µM), Escherichia coli W3110 (MIC=0.02 µM), Escherichia coli W3110-KP1344 Pms7 (MIC=0.08 µM), Escherichia coli W3110-6 (MIC=0.32 µM), Escherichia coli C600 (MIC=0.08 µM), Escherichia coli C600 pHX405 (MIC=0.16 µM), Salmonella enteritidis (MIC=0.6 µM), Salmonella typhimurium (MIC=1.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Attachment to a siderophore ester [Ref.15102848] The post-translational modification consists of a trimer of N-(2,3-dihydroxybnenzoyl)-L-serine linked via a C-glycosidic linkage to a β-D-glucose moiety, itself linked to the MccE492m Ser-84-carboxyl through an O-glycosidic bond. L No cytotoxicity information found Not found 12890026##15102848##7682973 Mol Microbiol. 2003 Aug;49(4):1031-1041.##J Biol Chem. 2004 Jul 2;279(27):28233-28242.##FEBS Lett. 1993 Apr 26;321(2-3):145-148. Destoumieux-Garz³n D, Thomas X, Santamaria M, Goulard C, Barth©l©my M, Boscher B, Bessin Y, Molle G, Pons AM, Letellier L, Peduzzi J, Rebuffat S.##Thomas X, Destoumieux-Garz³n D, Peduzzi J, Afonso C, Blond A, Birlirakis N, Goulard C, Dubost L, Thai R, Tabet JC, Rebuffat S.##Lagos R, Wilkens M, Vergara C, Cecchi X, Monasterio O. Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.##Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.##Microcin E492 forms ion channels in phospholipid bilayer membrane. DRAMP00232 ATPATPTVAQFVIQGSTICLVC 22 Cypemycin (Bacteriocin) E5KIB6 Belongs to the linaridin family cypA Streptomyces sp. OH-4156 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibiotic peptide structurally related to lantibiotics. Has cytotoxic activity against mouse P388 leukemia cells (IC50=1.3 μg/ml). Micrococcus luteus (MIC=0.2 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Cyclic [Ref. 10.1016/S0040-4039(00)78407-3] Dimethylation on Ala1 [Ref. 10.1016/S0040-4039(00)78407-3] Decarboxylation and Cyclization on D-Cys64 [Ref. 10.1016/S0040-4039(00)78407-3] ①Thr2, Thr5, Thr7 and Thr17 converts to (E)-2,3-didehydrobutyrine. ②Ile13 and Ile18 converts to L-allo-isoleucine. ③Maturation involves the enzymatic conversion of Cys-19 into 2,3-didehydroalanine followed by formation of a thioether bond with Cys-22. The C-terminal meso-lanthionine then undergoes decarboxylation. [Ref. 10.1016/S0040-4039(00)78407-3] Mixed (D-Cys19) [Ref.7802859] IC50 = 1.3 μg/mL against P388 leukemia cells in vitro. Not found 7802859##Pubmed ID is not available J Antibiot (Tokyo). 1993 Nov;46(11):1666-1671.##Tetrahedron Lett. 1994 Oct;35(43):8001-8004. Komiyama K, Otoguro K, Segawa T, Shiomi K, Yang H, Takahashi Y, Hayashi M, Otani T, Omura S.##Minami Y, Yoshida K, Azuma R, Urakawa A, Kawauchi T, Otani T, Komiyama K, Omura S A new antibiotic, cypemycin. Taxonomy, fermentation, isolation and biological characteristics. ##STRUCTURE OF CYPEMYCIN, A NEW PEPTIDE ANTIBIOTIC. DRAMP00244 XTPATPFTPAITEITAAVIAX 21 Hominicin (Bacteriocin) No entry found Not found Not found Staphylococcus hominis MBBL 2-9 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Hominicin exhibited heat stability up to 121 degrees C for 15min and activity under both acidic and basic conditions (from pH 2.0 to 10.0). Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=0.06 µg/ml), S. aureus ATCC (MRSA) 11435 (MIC=0.96 µg/ml), S. aureus (vancomycin-intermediate VISA) CCARM 3501 (MIC=3.82 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Dimethylation on Ile1 Free ①The residue X at position 1 is DmIle (N1, N1-dimethyl-isoleucine).②The residues T at position 2, 5, 8 and 15 are dehydrobutyrine. ③The residue at position 21 is a distinct residue Dmp (N2, N2-dimethyl-1,2-propanediamine) rarely found from biosynthetic antimicrobial peptides. L No cytotoxicity information found Not found 20654578 Biochem Biophys Res Commun. 2010 Aug 20;399(2):133-138. Kim PI, Sohng JK, Sung C, Joo HS, Kim EM, Yamaguchi T, Park D, Kim BG. Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2-9. DRAMP00254 WFYQGMNIAIYANIGGVANIIGYTEAAVATLLGAVVAVAPVVP 43 Propionicin-F (Bacteriocin) Q6E3K9 Not found pcfA Propionibacterium freudenreichii subsp. Freudenreichii LMGT 2946 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Bacteriocin with specific antibacterial activity. Gram-positive bacteria: Propionibacterium freudenreichii ssp. freudenreichii ATCC 6207T (MIC=0.7 nM), P. freudenreichii ssp.shermanii ATCC 9614T (MIC=5.0 nM), P. freudenreichii ATCC 9616 (MIC=20 nM), P. freudenreichii IFO12426 (MIC=2.5 nM), P. freudenreichii LMGT 2842 (MIC=5.0 nM), P. freudenreichii LMGT 3001 (MIC=5.0 nM), P. freudenreichii LMGT 2946, P. freudenreichii LMGT 2956, P. freudenreichii ISU-P24 (MIC=0.7 nM), P. freudenreichii ISU-P59 (MIC=2.5 nM), P. freudenreichii ISU-P83 (MIC=5.0 nM), P. freudenreichii ISU-P98 (MIC=1.3 nM), P. freudenreichii ISU-P104 (MIC=0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 15574930 Appl Environ Microbiol. 2004 Dec;70(12):7303-7310. Brede DA, Faye T, Johnsborg O, Odeg¥rd I, Nes IF, Holo H. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. DRAMP00275 GSSFCDSKCKLRCSKAGLADRCLKYCGICCEECKCVPSGTYGNKHECPCYRDKKNSKGKSKCP 63 Snakin-1 (StSN1; Cys-rich; Plant defensin) Q948Z4 Not found SN1 Solanum tuberosum (potato) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria. Tissue specificity: Expressed in tubers, stems, axillary and young floral buds, sepals, petals, stamens and carpels, but not in roots, stolons, shoot apex meristem or young leaves. Induction: No responses to methyl jasmonate, ethylene, abscisic acid, salicylic acid, isonicotinic acid, indolacetic acid, gibberellic acid and infection with incompatible bacterial or compatible fungual pathogens. PTM: Six disulfide bonds may be present." [Ref.9885189] Gram-positive bacteria: Listeria monocytogenes (MIC=10 µg/mL), Listeria innocua (MIC=10 µg/mL), Listeria ivanovii (MIC=10 µg/mL), Clavibacter michiganensis (EC50=1 µM), Ralstonia solanacearum (rfa-) (EC50=30 µM), Rhizobium meliloti (EC50=8 µM).##Fungi: Botrytis cinerea (EC50=2 µM), Fusarium solani (EC50=3 µM), Fusarium culmorum (EC50=2 µM), Fusarium oxysporum f. sp. conglutinans (EC50=10 µM), Fusarium oxysporum f. sp. lycopersici (EC50=20 µM), Plectosphaerella cucumerina (EC50=10 µM), Colletotrichum graminicola (EC50=10 µM), Colletotrichum lagenarium (EC50=10 µM), Bipolaris maydis (EC50=20 µM), Aspergillus flavus (EC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free [Ref.9885189] Six disulfide bonds may be present L No cytotoxicity information found Not found 11891250##9885189 Plant Physiol. 2002 Mar;128(3):951-961.##Mol Plant Microbe Interact. 1999 Jan;12(1):16-23. Marta Berrocal-Lobo, Ana Segura, Manuel Moreno, Gemma López, Francisco García-Olmedo, Antonio Molina##A Segura, M Moreno, F Madueño, A Molina, F García-Olmedo Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection.##Snakin-1, a peptide from potato that is active against plant pathogens. DRAMP00336 IPCGESCVWIPCITAIAGCSCKNKVCYT 28 ChaC7 (Chassatide C7; uncyclotides; Plant defensin) No entry found Belongs to the Bracelet subfamily, Rubiaceae family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "IC50=1.2 µM, HD50=11.6 µM. Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells)." Gram-negative bacterium: Escherichia coli (MIC=6.4 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50 = 11.6 μM against on human red blood cells (Type A). Kalata B1 and melittin were used as the positive control. Linear Free Free L [Ref.22467870] IC50 = 1.2 μM targeting on HeLa cells. Kalata B1 was used as the positive control. Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00337 AIPCGESCVWIPCISTVIGCSCSNKVCYR 29 ChaC8 (Chassatide C8; uncyclotides; Plant defensin) No entry found Belongs to the Bracelet subfamily, Rubiaceae family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "IC50=1.0 µM, HD50=25.5 µM. Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells)." Gram-negative bacterium: Escherichia coli (MIC=6.6 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50 = 25.5 μM against human red blood cells (Type A). Kalata B1 and melittin were used as the positive control. Linear Free Free L [Ref.22467870] IC50 = 1.0 μM targeting on HeLa cells. Kalata B1 was used as the positive control. Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00338 IPCGESCVWIPCISGMFGCSCKDKVCYS 28 ChaC11 (Chassatide C11; uncyclotides; Plant defensin) No entry found Belongs to the Bracelet subfamily, Rubiaceae family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "IC50=1.2 µM, HD50=13.3 µM. Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells)." Gram-negative bacterium: Escherichia coli (MIC=8.5 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50 = 13.3 μM against human red blood cells (Type A). Kalata B1 and melittin were used as the positive control. Linear Free Free L [Ref.22467870] IC50 = 5.0 μM targeting on HeLa cells. Kalata B1 was used as the positive control. Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00384 GNEGGGHGGHGGYGGYHHHGGGGGGYGGYHGGGGS 35 Cc-GRP (Gly-rich; Plants) No entry found Not found Not found Coffea canephora Antimicrobial, Antifungal Not found Rich Not found Comment: The sequence displayed is only the N-terminal sequence of 7 kD peptide. The peptide was located in the cell wall, cell surface and nucleus of Fusarium oxysporum. Fungi: Candida albicans (MIC=90 µg/ml), Candida tropicalis (MIC=180 µg/ml), Colletotrichum lindemuthianum (MIC=90 µg/ml), Fusarium oxysporium (MIC=90 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 23500079 Biochim Biophys Acta. 2013 Mar 15.[Epub ahead of print] Zottich U, Da Cunha M, Carvalho AO, Dias GB, Casarin N, Vasconcelos IM, Gomes VM. An antifungal peptide from Coffea canephora seeds with sequence homology to glycine-rich proteins exerts membrane permeabilization and nuclear localization in fungi. DRAMP00385 QLPICGETCVLGGCYTPNCRCQYPICVR 28 Panitide L2 (plants) No entry found Not found Not found Panicum laxum Antimicrobial, Antibacterial, Anti-Gram- Not found Bridge Not found PTM: N-terminus is a pyruglutamyl. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Pyroglutamyl modification Free There are three disulfide bonds in the peptide structure L [Ref.23195955] IC50 = 6.0 μM against HeLa cells. Not found 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-3380. Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants. DRAMP00416 KLCERSSGTWSGVCGNNNACKNQCIRLEGAQHGSCNYVFPAHKCICYFPC 50 Raphanus sativus Antifungal Protein 3 (Rs-AFP3; Plant defensin) O24332, Q39313 Belongs to the DEFL family AFP3 Raphanus sativus (Radish) & Brassica napus (Rape) Antimicrobial, Antifungal Protein inferred from homology Bridge Not found "Function: Possesses antifungal activity sensitive to inorganic cations (By similarity). PTM: Problely contains four disulfide bonds 3-50; 14-35; 20-44; 24-46." Fungi: Alternaria brassicicola (MIC=2 µg/ml), Botrytis cinerea (MIC=2 µg/ml), Fusarium culmorum (MIC=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are four disulfide bonds between Cys3 and Cys50, Cys14 and Cys35, Cys20 and Cys44, Cys24 and Cys51. L No cytotoxicity information found Not found 7780308##8422949 Plant Cell. 1995 May;7(5):573-588.##FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Eggermont K, Kovaleva V, Raikhel NV, Osborn RW, Kester A, Rees SB, Torrekens S, Van Leuven F, Vanderleyden J, et al.##Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. Small cysteine-rich antifungal proteins from radish: their role in host defense.##A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP00417 QKLCERSSGTWSGVCGNNNACKNQCINLEGARHGSCNYIFPYHRCICYFPC 51 Raphanus sativus Antifungal Protein 4 (Rs-AFP4; Plant defensin) O24331 Belongs to the DEFL family AFP4 Raphanus sativus (Radish) Antimicrobial, Antifungal Protein inferred from homology Bridge Not found PTM: Contains four disulfide bonds 4-51;15-36;21-45;25-47, and Pyrrolidone carboxylic acid at position 1. Fungi: Alternaria brassicicola (MIC=5 µg/ml), Botrytis cinerea (MIC=9 µg/ml), Fusarium culmorum (MIC=11 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal glutamine (Conversion to pyrrolidone carboxylic acid) Free There are four disulfide bonds between Cys4 and Cys51, Cys15 and Cys36, Cys21 and Cys45, Cys25 and Cys47. L No cytotoxicity information found Not found 7780308 Plant Cell. 1995 May;7(5):573-588. Terras FR, Eggermont K, Kovaleva V, Raikhel NV, Osborn RW, Kester A, Rees SB, Torrekens S, Van Leuven F, Vanderleyden J, et al. Small cysteine-rich antifungal proteins from radish: their role in host defense. DRAMP00422 QKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC 51 Defensin-like protein 1 (Sa-AFP1; Plant defensin) P30231 Belongs to the DEFL family Not found Sinapis alba (White mustard) (Brassica hirta) Antimicrobial, Antifungal Protein level Bridge Not found 1AYJ Function: Possesses antifungal activity sensitive to inorganic cations. Fungi: Alternaria brassicola (MIC=1.2 µg/ml), Botrytis cinerea (MIC=1.8 µg/ml), Fusarium culmorum (MIC=4 µg/ml), Fusarium oxysporum f.sp.lycopersici (MIC=6 µg/ml), Pyricularia oryzae (MIC=0.5 µg/ml), Verticillium dahliae (MIC=1.5 µg/ml).##NOTE: In synthetic low ionic strength fungal growth medium. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal glutamine (Conversion to pyrrolidone carboxylic acid) Free There are four disulfide bonds between Cys4 and Cys51, Cys15 and Cys36, Cys21 and Cys45, Cys25 and Cys47. L No cytotoxicity information found Not found 8422949##8836771 FEBS Lett. 1993 Feb 1;316(3):233-240.##Int J Pept Protein Res. 1996 Jun;47(6):437-446. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF.##Neumann GM, Condron R, Polya GM. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species.##Purification and mass spectrometry-based sequencing of yellow mustard (Sinapis alba L.) 6 kDa proteins. Identification as antifungal proteins. DRAMP00423 QKLCQRPSGTWSGVCGNNNACRNQCINLEKARHGSCNYVFPAHKCICYFPC 50 Defensin-like protein 2 (Sa-AFP2; Plant defensin) P30232 Not found Not found Sinapis alba (White mustard) (Brassica hirta) Antimicrobial, Antifungal Not found Not found Not found Function: Possesses antifungal activity sensitive to inorganic cations. Fungi: Alternaria brassicola (MIC=4.5 µg/ml), Botrytis cinerea (MIC=3.5 µg/ml), Fusarium culmorum (MIC=2.3 µg/ml), Fusarium oxysporum f.sp.lycopersici (MIC=2.3 µg/ml), Pyricularia oryzae (MIC=0.3 µg/ml), Verticillium dahliae (MIC=1.2 µg/ml).##NOTE: In synthetic low ionic strength fungal growth medium. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal glutamine (Conversion to pyrrolidone carboxylic acid) Free ①There are four disulfide bonds between Cys4 and Cys51, Cys15 and Cys36, Cys21 and Cys45, Cys25 and Cys47. ②The residue at position 8 is phosphorylated. L No cytotoxicity information found Not found 8422949 FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP00425 LMCTHPLDCSN 11 Tn-AFP1 (Trapa natans antifungal peptide; Plant defensin) No entry found Not found Not found Trapa natans Antimicrobial, Antifungal Not found Not found Not found Function: Tn-AFP1 has no adverse effect on red blood cells at concentration of 32 μg/mL. Yeast: Candida tropicalis (MIC=32 µg/ml). Tn-AFP1 has no adverse effect on red blood cells at concentration of 32 μg mL−1 Cyclic Free Free There is a disulfide bond between Cys3 and Cys9 L No cytotoxicity information found Not found 21736910 Peptides. 2011 Aug;32(8):1741-1747. Mandal SM, Migliolo L, Franco OL, Ghosh AK. Identification of an antifungal peptide from Trapa natans fruits with inhibitory effects on Candida tropicalis biofilm formation. DRAMP00431 KTCMTKKEGWGRCLIDTTCAHSCRKYGYMGGKCQGITRRCYCLLNC 46 Defensin-like protein 2 (Cp-thionin II; Cp-thionin-2; Gamma-thionin II; Plant defensin) P84920 Belongs to the DEFL family Not found Vigna unguiculata (Cowpea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli and P. syringae. Does not have antibacterial activity against the phytopathogenic bacteria R. solanacearum, Rhataybacter sp and Erwinia sp. Does not inhibit trypsin, chymotrypsin or alpha-amylases. Tissue specificity: Present in seeds, cotyledons and leaves. Not found in roots or stems. Developmental stage: Present in seeds and seedlings, levels decrease with seedling age. Light increases the rate of degradation. Present until 9 days in seedlings kept in the dark, not found after 6 days in seedings kept in the light. PTM: Contains four disulfide bonds 3-46; 13-33; 19-40; 23-42." Gram-positive bacterium: Staphylococcus aureus ATTC 25923 (MIC=128 mg/ml);##Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=64 mg/ml), Pseudomonas syringae (MIC=42 mg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There are four disulfide bonds between Cys3 and Cys46, Cys13 and Cys33, Cys19 and Cys40, Cys23 and Cys42 L No cytotoxicity information found Not found 16824043 FEBS J. 2006 Aug;273(15):3489-3497. Franco OL, Murad AM, Leite JR, Mendes PA, Prates MV, Bloch C Jr. Identification of a cowpea gamma-thionin with bactericidal activity. DRAMP00436 KTCEHLADTYRGVCFTNASCDDHCKNKAHLISGTCHNWKCFCTQNC 46 Pisum sativum defensin 1 (Psd1; Plant defensin) P81929 Belongs to the DEFL family Not found Pisum sativum (Garden pea) Antimicrobial, Antifungal Protein level Combine helix and strand structure The protein has a globular fold with a triple-stranded antiparalell beta-sheet and an alpha-helix (from residue Asn17 to Leu27). 1JKZ resolved by NMR. PTM: Contains four disulfide bonds 3-46; 14-35; 20-40; 24-42. PD: Aspergillus niger (MIC=12.1 µg/ml), Aspergillus versicolor (MIC<5.0 µg/ml), Fusarium moniliforme (MIC=21.7 µg/ml), Fusarium oxysporum (MIC>100 µg/ml), Fusarium solani (MIC=12.1 µg/ml), Neurospora crassa (MIC=0.04 µg/ml), Saccharomyces cerevisae (MIC>100 µg/ml), Trichophyton mentagrophytes (MIC>100 µg/ml).##PD+: Aspergillus niger (MIC=7.4 µg/ml), Fusarium moniliforme (MIC=33.2 µg/ml), Fusarium oxysporum (MIC=100 µg/ml), Fusarium solani (MIC=79.2 µg/ml), Neurospora crassa (MIC=0.05 µg/ml).##NOTE: PD+: potato dextrose medium supplemented with 1 mM CaCl2. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There are four disulfide bonds between Cys3 and Cys46, Cys14 and Cys35, Cys20 and Cys40, Cys24 and Cys42 L No cytotoxicity information found It interacts with cell-cycle-realted protein cyclin F as the target. 10860545##11697857##11812144 Arch Biochem Biophys. 2000 Jun 15;378(2):278-286.##Arch Biochem Biophys. 2001 Nov 15;395(2):199-207.##J Mol Biol. 2002 Jan 25;315(4):749-757. Almeida M.S, Cabral K.M, Zingali R.B, Kurtenbach E.##Almeida MS, Cabral KS, de Medeiros LN, Valente AP, Almeida FC, Kurtenbach E.##Almeida MS, Cabral KM, Kurtenbach E, Almeida FC, Valente AP. Characterization of two novel defense peptides from pea (Pisum sativum) seeds.##cDNA cloning and heterologous expression of functional cysteine-rich antifungal protein Psd1 in the yeast Pichia pastoris.##Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. DRAMP00437 KTCENLSGTFKGPCIPDGNCNKHCRNNEHLLSGRCRDDFRCWCTNRC 47 Pisum sativum defensin 2 (Psd2; Plant defensin) P81930 Belongs to the DEFL family Not found Pisum sativum (Garden pea) Antimicrobial, Antifungal Protein level Bridge Not found PTM: Contains four disulfide bonds 3-47; 14-35; 20-41; 24-43. PD: Aspergillus niger (MIC=10.2 µg/ml), Aspergillus versicolor (MIC=0.34 µg/ml), Fusarium moniliforme (MIC=10.0 µg/ml), Fusarium oxysporum (MIC>100 µg/ml), Fusarium solani (MIC=8.5 µg/ml), Neurospora crassa (MIC<0.5 µg/ml), Saccharomyces cerevisae (MIC>100 µg/ml), Trichophyton mentagrophytes (MIC<100 µg/ml).##PD+: Aspergillus niger (MIC=7.8 µg/ml), Aspergillus versicolor (MIC=5.9 µg/ml), Fusarium moniliforme (MIC=25 µg/ml), Fusarium oxysporum (MIC>100 µg/ml), Fusarium solani (MIC=5.0 µg/ml).##NOTE: PD+ = potato dextrose medium supplemented with 1 mM CaCl2. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There are four disulfide bonds between Cys3 and Cys47, Cys14 and Cys35, Cys20 and Cys41, Cys24 and Cys43. L No cytotoxicity information found Not found 10860545 Arch Biochem Biophys. 2000 Jun 15;378(2):278-286. Almeida M.S, Cabral K.M, Zingali R.B, Kurtenbach E. Characterization of two novel defense peptides from pea (Pisum sativum) seeds. DRAMP00450 QKLCQRPSGTWSGVCGNNNACRNQCINLEKARHGSCNYVFPAHKCICYFPC 51 Defensin-like protein 2A (AFP2A; M2A; Plant defensin) P30232 Belongs to the DEFL family Not found Sinapis alba (White mustard) (Brassica hirta) Antimicrobial, Antifungal Protein level Rich Not found "Function: Possesses antifungal activity sensitive to inorganic cations. Subunit structure: Forms oligomers in its native state. PTM: Contains four disulfide bonds (By similarity)." Fungi: Alternaria brassicola (MIC=4.5 µg/ml), Botrytis cinerea (MIC=3.5 µg/ml), Fusarium culmorum (MIC=2.3 µg/ml), Fusarium oxysporum f.sp. lycopersici (MIC=2.3 µg/ml), Pyricularia oryzae (MIC=0.3 µg/ml), Verticillium dahliae (MIC=1.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic [Ref.8422949] Cyclization of a N-terminal glutamine (Conversion to pyrrolidone carboxylic acid) Cyclization of a C-terminal Cys residue (forming a disulfide bond) ①There are four disulfide bonds between Cys4 and Cys51, Cys15 and Cys36, Cys21 and Cys45, Cys25 and Cys47. ②[Ref.8836771] The residue at position 8 is phosphorylated. L No cytotoxicity information found Not found 8422949##8836771 FEBS Lett. 1993 Feb 1;316(3):233-240.##Int J Pept Protein Res. 1996 Jun;47(6):437-446. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF.##Neumann GM, Condron R, Polya GM. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species.##Purification and mass spectrometry-based sequencing of yellow mustard (Sinapis alba L.) 6 kDa proteins. Identification as antifungal proteins. DRAMP00454 ATCKAECPTWDSVCINKKPCVACCKKAKFSDGHCSKILRRCLCTKEC 47 Petunia hybrida defensin 1 (PhD1; Cys-rich; Plant defensin) Q8H6Q1 Belongs to the DEFL family D1 Petunia hybrida (Petunia) Antimicrobial, Antifungal Protein level Combine helix and strand structure PhD1 has the fold of the cysteine-stabilized alphabeta motif, consisting of an alpha-helix and a triple-stranded antiparallel beta-sheet, except that it contains a fifth disulfide bond from the first loop to the alpha-helix. 1N4N resolved by NMR. "Function: Plant defense peptide with antifungal activity. Tissue specificity: Petals. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Biophysicochemical properties: pH dependence (Stable under extremes of pH); Temperature dependence (Stable under extremes of temperature). PTM: Contains five disulfide bonds 3-47; 7-23; 14-34; 20-41; 24-43." Fungi: Fusarium oxysporum (MIC=10 µg/ml), Botrytis cinerea (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free When compared to other plant defensins, the petunia defensins have an additional fifth disulfide bond. There are five disulfide bonds between Cys3 and Cys47, Cys7 and Cys23, Cys14 and Cys34, Cys20 and Cys41, Cys24 and Cys43. L No cytotoxicity information found Not found 12644678##12846570 Plant Physiol. 2003 Mar;131(3):1283-1293.##Biochemistry. 2003 Jul 15;42(27):8214-8222. Lay FT, Brugliera F, Anderson MA.##Janssen BJ, Schirra HJ, Lay FT, Anderson MA, Craik DJ. Isolation and properties of floral defensins from ornamental tobacco and petunia.##Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds. DRAMP00764 KSLRPRCWIKIKFRCKSLKF 20 Piceain 1 (Plants) No entry found Not found Not found Picea sitchensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Beta strand (CD) Not found "Function: Active against both Gram-postive and Gram-negative bacteria, fungi. It showed weak hemolysis activity against human and rabbit red cells. PTM: Contains one disulfide bond." Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=9.38 µg/ml), S. aureus ATCC 43300 (MIC=9.38 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=18.75 µg/ml), Escherichia coli ML-35P (MIC=18.75 µg/ml), Escherichia coli 08040722 (CI) (MIC=75 µg/ml), Escherichia coli 08A866 (CI) (MIC=37.5 µg/ml), Pseudomonas aeruginosa PA01 (MIC=9.38 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=9.38 µg/ml), Pseudomonas aeruginosa 08031014 (CI) (MIC=37.5 µg/ml).##Yeast: Candida albicans ATCC 20032 (MIC=9.38 µg/ml). [Ref.21644248] At the concentration of 0.0625 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 0.7% & 1.5%; At the concentration of 0.125 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 0.8% & 7.2%; At the concentration of 0.25 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 5.9%&7.8%; At the concentration of 0.5 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 7.6% & 9.5%; At the concentration of 1 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 7.8% & 57.1%. Cyclic Free Free There is one intra-molecular disulfide bridge formed by Cys7 and Cys15. L No cytotoxicity information found Not found 21644248 J Pept Sci. 2011 Sep;17(9):627-631. Liu R, Mu L, Liu H, Wei L, Yan T, Chen M, Zhang K, Li J, You D, Lai R. Two antimicrobial and nematicidal peptides derived from sequences encoded Picea sitchensis. DRAMP00765 RPRCWIKIKFRCKSLKF 17 Piceain 2 (Plants) No entry found Not found Not found Picea sitchensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found "Function: Active against both Gram-postive and Gram-negative bacteria, fungi. It showed weak hemolysis activity against human and rabbit red cells. PTM: Contains one disulfide bond." Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=9.38 µg/ml), S. aureus ATCC 43300 (MIC=18.75 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=37.5 µg/ml), Escherichia coli ML-35P (MIC=37.5 µg/ml), Escherichia coli 08040722 (CI) (MIC=75 µg/ml), Escherichia coli 08A866 (CI) (MIC=37.5 µg/ml), Pseudomonas aeruginosa PA01 (MIC=9.38 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=18.75 µg/ml), Pseudomonas aeruginosa 08031014 (CI) (MIC=37.5 µg/ml).##Yeast: Candida albicans ATCC 20032 (MIC=18.75 µg/ml). [Ref.21644248] At the concentration of 0.0625 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 0.6% & 2.2%; At the concentration of 0.125 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 0.8% & 4.7%; At the concentration of 0.25 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 5.2%&5.2%; At the concentration of 0.5 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 5.3% & 12.4%; At the concentration of 1 mg/ml, Piceain 1 induced human & rabbit red cell hemolysis of 11.3% & 66.3%. Cyclic Free Free There is one intra-molecular disulfide bridge formed by Cys4 and Cys12. L No cytotoxicity information found Not found 21644248 J Pept Sci. 2011 Sep;17(9):627-631. Liu R, Mu L, Liu H, Wei L, Yan T, Chen M, Zhang K, Li J, You D, Lai R. Two antimicrobial and nematicidal peptides derived from sequences encoded Picea sitchensis. DRAMP00766 KVFLGLK 7 JCpep7 (Plants) No entry found Not found Not found Jatropha curcas Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: JCpep7 killed microbes principally via breaking of their cell walls and membranes, followed by cell lysis. Gram-negative bacteria: Salmonella typhimurium ATCC 50013 (MIC=48 µg/ml), Shigella dysenteriae ATCC 51302 (MIC=48 µg/ml), Pseudomonas aeruginosa ATCC 27553 (MIC=64 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=40 µg/ml), Bacillus subtilis ATCC 23631 (MIC=24 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=56 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 21268582 J Agric Food Chem. 2011 Feb 23;59(4):1145-1151. Xiao J, Zhang H, Niu L, Wang X. Efficient Screening of a Novel Antimicrobial Peptide from Jatropha curcas by Cell Membrane Affinity Chromatography. DRAMP00774 GTRCGETCFVLPCWSAKFGCYCQKGFCYRN 30 Hedyotide B1 (hB1; Plants) No entry found Belongs to the cyclotide family Not found Hedyotis biflora (aerial tissues) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=3.4 µM);##Gram-positive bacteria: Streptococcus salivarius(MIC=5.9 µM), Staphylococcus epidermidis (MIC>80 µM), S. aureus (MIC>80 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are three disulfide bonds in the peptide structure L No cytotoxicity information found Not found 21979955 J Biol Chem. 2011 Dec 30;286(52):44833-44844. Nguyen GK, Zhang S, Wang W, Wong CT, Nguyen NT, Tam JP. Discovery of a linear cyclotide from the bracelet subfamily and its disulfide mapping by top-down mass spectrometry. DRAMP00795 GIPCGESCVFIPCITAAIGCSCKSKVCYRN 30 Cliotide T1 (cT1; Plant defensin) No entry found Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found "Function: Cliotide T1 shows stronger antimicrobial activity against the Gram-negative bacteria than the Gram-positive bacteria. It also has hemolytic activity against human type A erythrocytes (HD50=7.1 µM) and cytotoxicity against HeLa Cells (IC50=0.6 µM). [Note: HD50 refers to the peptide concentration that causes 50% lysis of red blood cells; IC50 refers to the peptide concentration that causes 50% death of HeLa cells]. " [Ref.21596752]Gram-positive bacteria: Staphylococcus aureus ATCC12600, Enterococcus faecalis ATCC 47077 (less active);##Gram-negative bacteria: Escherichia coli ATCC 700926 (MIC=1.1 µM), Pseudomonas aeruginosa ATCC 39018 (MIC=2.7 µM), Klebsiella pneumonia ATCC 13883 (MIC=4.7 µM). [Ref.21596752] HD50 = 7.1 μM against human red blood cells Cyclic Free Free There are three disulfide bonds between Cys4 and Cys20, Cys8 and Cys22, Cys13 and Cys27. L [Ref.21596752] IC50=0.6 µM against HeLa cells. Not found 21596752 J Biol Chem. 2011 Jul 8;286(27):24275-24287. Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, Hardjojo A, Tam JP. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. DRAMP00798 GIPCGESCVFIPCITGAIGCSCKSKVCYRN 30 Cliotide T4 (cT4; Plant defensin) No entry found Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found "Function: Cliotide T4 shows stronger antimicrobial activity against the Gram-negative bacteria than the Gram-positive bacteria. It also has hemolytic activity against human type A erythrocytes (HD50=8.4 µM) and cytotoxicity against HeLa Cells (IC50=0.6 µM). [Note: HD50 refers to the peptide concentration that causes 50% lysis of red blood cells; IC50 refers to the peptide concentration that causes 50% death of HeLa cells]. " [Ref.21596752]Gram-positive bacteria: Staphylococcus aureus ATCC12600, Enterococcus faecalis ATCC 47077 (less active);##Gram-negative bacteria: Escherichia coli ATCC 700926 (MIC=1.3 µM), Pseudomonas aeruginosa ATCC 39018 (MIC=1.9 µM), Klebsiella pneumonia ATCC 13883 (MIC=1.5 µM). [Ref.21596752] HD50 = 8.4 μM against human red blood cells Cyclic Free Free There are three disulfide bonds between Cys4 and Cys20, Cys8 and Cys22, Cys13 and Cys27. L [Ref.21596752] IC50=0.6 µM against HeLa cells. Not found 21596752 J Biol Chem. 2011 Jul 8;286(27):24275-24287. Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, Hardjojo A, Tam JP. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. DRAMP00856 GLPVCGETCVGGTCNTPGCTCSWPVCTRN 29 Kalata-B1 (Plant defensin) P56254 Belongs to the cyclotide family OAK1 Oldenlandia affinis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Beta strand (3 strands; 7 residues) Not found 2KHB resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S. aureus. Relatively ineffective against Gram-negative bacteria such as E. coli and P. aeruginosa. Inhibitory effect on the growth and development of larvae from H. punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost. MOA: a small number of cyclotides bind to the membrane surface and then insert first into the outer membrane leaflet followed by penetration through the membrane and pore formation. At higher concentrations of cyclotides, destabilization of membranes occurs. Tissue specificity: Leaves and stems. Lower in roots. Pharmaceutical use: The uteroactive properties of Kalata have been discovered by African traditional medicine. It is used as an ingredient of a herbal tea to accelerate childbirth. PTM: Kalata-B1 is a cyclic peptide which contains three disulfide bonds 5-19; 11-21; 14-26." [Ref.10430870]Gram-positive bacterium: Staphylococcus aureus (MIC=0.26 µM), Micrococcus luteus (MIC=40.4 µM);##Gram-negative bacterium: Klebsiella oxytoca (MIC=54.8 µM);##Fungi: Candida kefyr (MIC=21.4 µM).##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=140 nM). [Ref.12779323] HD50 = 300 μM against Human type A red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) [Ref.7703226] There are three disulfide bonds between Cys5 and Cys19, Cys9 and Cys21, Cys14 and Cys26. L [Ref.18008336]CEM-SS cells:IC50=3500 nM. Cell membrance 18008336##10430870##7703226##17534989##23129773 Biopolymers. 2008;90(1):51-60.##Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.##Biochemistry. 1995 Apr 4;34(13):4147-4158.##Chembiochem. 2007 Jun 18;8(9):1001-1011.##J Biol Chem. 2012 Dec 21;287(52):43884-98. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. ##Tam JP, Lu YA, Yang JL, Chiu KW.##Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG.##Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.##Wang CK, Wacklin HP, Craik DJ. Cyclotides as natural anti-HIV agents.##An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.##Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1.##The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.##Cyclotides insert into lipid bilayers to form membrane pores and destabilize the membrane through hydrophobic and phosphoethanolamine-specific interactions. DRAMP00877 GIPCGESCVWIPCISAALGCSCKNKVCYRN 30 Circulin-A (CIRA; Plant defensin) P56871 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Protein level Alpha helix (1 helices; 4 residues) "The molecule is stabilised by three disulfide bonds, two of which form an embedded loop completed by the backbone fragments connecting the cysteine residues. A third disulfide bond threads through the centre of this loop to form a ""cystine-knot"" motif. This motif is present in a range of other biologically active proteins, including omega-contoxin GVIA and Cucurbita maxima trypsin inhibitor." 1BH4 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has antibiotic activity. Inhibits the cytopathic effects and replication of the human immunodeficiency virus. Relatively ineffective against Gram-negative bacteria such as E. coli and P. aeruginosa. PTM: This is a cyclic peptide which contains three disulfide bonds 1-17; 5-19; 10-24." [Ref.10430870]Gram-positive bacterium: Staphylococcus aureus (MIC=0.19 µM).##Gram-negative bacterium: Proteus vulgaris (MIC=54.6 µM).##Fungi: Candida kefyr (MIC=18.6 µM) and Candida tropicalis (MIC=19.4 µM).##NOTE: Medium with 10 mM phosphate buffer.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40-260 nM). [Ref.10430870] EC50 = 1020 μM against blood type A human erythrocytes. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) [Ref.8920961] There are three disulfide bonds between Cys4 and Cys20, Cys8 and Cys22, Cys13 and Cys27 L [Ref.18008336]CEM-SS cells:IC50=500 nM. Not found 18008336##10430870##9878410##8920961 Biopolymers. 2008;90(1):51-60. doi: 10.1002/bip.20886. ##Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.##J. Mol. Biol. 1999; 285:333-345. ##Biochem Biophys Res Commun. 1996 Nov 12;228(2):632-8. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##Tam JP, Lu YA, Yang JL, Chiu KW.##Daly NL, Koltay A, Gustafson KR, Boyd MR, Casas-Finet JR, Craik DJ.##R Derua 1, K R Gustafson, L K Pannell Cyclotides as natural anti-HIV agents.##An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.##Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity.##Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides DRAMP00878 GVIPCGESCVFIPCISTLLGCSCKNKVCYRN 31 Circulin-B (CIRB; Plant defensin) P56879 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Protein level Beta strand (5 strands; 10 residues) Cyclotides are mini-proteins derived from plants that have the characteristic features of a head-to-tail cyclised peptide backbone and a knotted arrangement of their three disulfide bonds. 2ERI resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has antibiotic activity. Inhibits the cytopathic effects and replication of the human immunodeficiency virus. Active against both Gram-positive and Gram-negative bacteria. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." [Ref.10430870]Gram-positive bacterium: (L-salt): Staphylococcus aureus (MIC=13.5 µM).##Gram-negative bacteria: (L-salt, H-salt) (MIC µM): Escherichia coli (0.41, >500), Pseudomonas aeruginosa (25.5, 48), Proteus vulgaris (6.8, >500), Klebsiella oxytoca (8.2, 15.6).##Fungi (H-salt): Candida kefyr (MIC=29 µM).##NOTE: L-salt = Medium with 10 mM phosphate buffer; H-salt = L-salt supplemented with 100 mM NaCl.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40-260 nM). [Ref.10430870] EC50 = 550 μM against blood type A human erythrocytes. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) [Ref.8920961] There are three disulfide bonds between Cys5 and Cys19, Cys9 and Cys21, Cys14 and Cys27. L [Ref.10430870] It caused 50% cell growth inhibition of mouse fibroblasts at 820 μM.##[Ref.18008336]CEM-SS cells:IC50=500 nM. Not found 10430870##18008336##8920961 Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.##Biopolymers. 2008;90(1):51-60.##Biochem Biophys Res Commun. 1996 Nov 12;228(2):632-8. doi: 10.1006/bbrc.1996.1708. Tam JP, Lu YA, Yang JL, Chiu KW.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.##R Derua 1, K R Gustafson, L K Pannell An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.##Cyclotides as natural anti-HIV agents.##Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides DRAMP01374 GFLDTFKNLALNAAKSAGVSVLNSLSCKLFKTC 33 Odorranain-D1 (OdD1; Frogs, amphibians, animals) A6MBK7 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-D1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Has no hemolytic activity against red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=16.32 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8.16 μg/ml), Bacillus subtilis (MIC=8.16 μg/ml).##Yeast: Candida albicans (MIC=4.08 μg/ml). [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Cyclic Free Cyclization(Cys27 and Cys33) Disulfide bridge between Cys27 and Cys33. L [Ref.17272268]No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01373 GVLGAVKDLLIGAGKSAAQSVLKTLSCKLSNDC 33 Odorranain-C1 (OdC1; Frogs, amphibians, animals) A6MBF6 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-C1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=8.21 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=4.11 μg/ml), Bacillus subtilis (MIC=16.42 μg/ml).##Yeast: Candida albicans (MIC=2.05 μg/ml). [Ref:17272268] No detectable hemolytic activity against rabbit red blood cells. Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) [Ref:17272268] There are one disulfide bond between Cys27 and Cys33 L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01372 AALKGCWTKSIPPKPCFGKR 20 Odorranain-B1 (OdB1; Frogs, amphibians, animals) E7EKD9 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Odorrana hainanensis (Odor frog) (Rana hainanensis) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Homology Not found Odorranain-B1 adopts 5.9 % "Function: Odorranain-B1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Has no hemolytic activity against red cell. Tissue specificity: Expressed by the skin glands." [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=3.21 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=5.83 μg/ml), Bacillus subtilis (MIC=1.85 μg/ml).##Yeast: Candida albicans (MIC=2.4 μg/ml). [Ref:17272268] No detectable hemolytic activity against rabbit red blood cells. Cyclic Free Free [Ref:17272268] There are one disulfide bond between Cys6 and Cys16 L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP00933 SAFTVWSGPGCNNRAERYSKCGCSAIHQKGGYDFSYTGQTAALYNQAGCSGVAHTRFGSSARACNPFGWKSIFIQC 76 Antimicrobial peptide 1 (AMP1; MiAMP1; Plant defensin) P80915 Not found Not found Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Antifungal Protein level Combine helix and strand structure MiAMP1 is made up of eight beta-strands which are arranged in two Greek key motifs. These Greek key motifs associate to form a Greek key beta-barrel. This structure is unique amongst plant antimicrobial proteins and forms a new class which we term the beta-barrelins. (Ref.2) 1C01 resolved by NMR. "Function: Antimicrobial peptide which inhibits the growth of a variety of fungi, oomycetes, Gram-positive bacterial phytopatogenes and S.cerevisiae in vitro. No activity against E.coli. Miscellaneous: Its antimicrobial activity is diminished by calcium an" Alternaria helianthi (MIC=2-5 µg/ml), Botrytis cinerea (MIC=5-10 µg/ml), Ceratocystis parodoxa (MIC=20 µg/ml), Colletotrichum gloeosporioides (MIC=2-5 µg/ml), Fusurium oxysporum (MIC=2-5 µg/ml), Leptosphaeria maculans (MIC=5 µg/ml), Macrophomina phaseolina (MIC<25 µg/ml), Phytophthoru cryptogea (MIC=5-10 µg/ml), Pythium graminicola (MIC=5 µg/ml), Sclerotinia sclerotiorum spores (MIC=5 µg/ml), Sclerotinia sclerotiorum mycelia (MIC=50 µg/ml), Verticilium dahliae (MIC=2 µg/ml), Clavibacter michiganensis (MIC<10 µg/ml), Saccharomyces cerevisiae (MIC=2-5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) [Ref.10543955] There are three disulfide bonds between Cys11 and Cys64, Cys21 and Cys76, Cys23 and Cys49 L No cytotoxicity information found Not found 9108242##10543955 Eur J Biochem. 1997 Mar 15;244(3):743-749.##J Mol Biol. 1999 Oct 29;293(3):629-638. Marcus JP, Goulter KC, Green JL, Harrison SJ, Manners JM.##McManus AM, Nielsen KJ, Marcus JP, Harrison SJ, Green JL, Manners JM, Craik DJ. Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia.##MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins. DRAMP01004 PQRGEGGRAGNLLREEQEI 19 Cucurmoschin (Plants) P84158 Not found Not found Cucurbita maxima (winter squash) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Inhibits cell-free translation in rabbit reticulocyte lysate system. Fungi: Botrytis cinerea (MIC=375 µM), Fusarium oxysporum (MIC=375 µM), Mycosphaerella arachidicola (MIC=375 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 14499274 Peptides. 2003 Jul;24(7):969-972. Wang HX, Ng TB. Isolation of cucurmoschin, a novel antifungal peptide abundant in arginine, glutamate and glycine residues from black pumpkin seeds. DRAMP01012 RESPSSRMECYEQAERYGYGGYGGGRYGGGYGSGRGQPVGQGVERSHDDNRNQPR 55 Pg-AMP (Gly-rich; Plants) P86030 Not found Not found Psidium guajava (Guava) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-negative bacteria. Does not have antifungal activity against the human and plant pathogenic fungi F. oxysporum, A. fumigatus and R. solani. Subunit structure: Monomer and homodimer. Might act by homodimer formation." Gram-negative bacteria: Klebsiella sp., Proteus sp., Escherichia coli ATCC 8739 (MIC=72 mg/ml), Klebsiella pneumoniae (MIC=32 mg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 18448201 Peptides. 2008 Aug;29(8):1271-1279. Pelegrini PB, Murad AM, Silva LP, Dos Santos RC, Costa FT, Tagliari PD, Bloch C Jr, Noronha EF, Miller RN, Franco OL. Identification of a novel storage glycine-rich peptide from guava (Psidium guajava) seeds with activity against Gram-negative bacteria. DRAMP01016 QCIGNGGRCNENVGPPYCCSGFCLRQPGQGYGYCKNR 37 Antimicrobial peptide 1 (MJ-AMP1; Plant defensin) P25403 Belongs to the AMP family AMP1 Mirabilis jalapa (Garden four-o'clock) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Function: Possesses antifungal activity and is also active on two tested Gram-positive bacteria: but is non-toxic for Gram-negative bacteria and cultured human cells. Tissue specificity: Found only in seeds. PTM: Contains three disulfide bonds 2-19; 9-23;" Fungi: Alternaria brassicola (MIC=20 µg/ml), Ascochyta pisi (MIC=200 µg/ml), Botrytis cinerea (MIC=50 µg/ml), Cercospora beticola (MIC=10 µg/ml), Colletotrichum lindemuthianum (MIC=6 µg/ml), Fusarium culmorum (MIC=30 µg/ml), Fusarium oxysporum f.sp.pisi (MIC=15 µg/ml), Fusarium oxysporum f.sp.lycopersici (MIC=200 µg/ml), Nectria haematococca (MIC=15 µg/ml), Phoma betae (MIC=25 µg/ml), Pyrenophora tritici-repentis (MIC=300 µg/ml), Pyricularia oryzae (MIC=6 µg/ml), Rhizoctonia solani (MIC=60 µg/ml), Verticillium dahliae (MIC=12 µg/ml), Venturia inequalis (MIC=12 µg/ml).##Gram-positive bacteria: Bacillus megaterium (MIC=6 µg/ml), Sarcina lutea (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Pyroglutamyl modification (Cyclization of a N-terminal glutamine) Free There are three disulfide bonds between Cys2 and Cys19, Cys9 and Cys23, Cys18 and Cys34. L No cytotoxicity information found Not found 1733929##7647302 J. Biol. Chem. 1992;267:2228-2233.##Plant Mol. Biol. 1995;28:713-721. Cammue B.P.A, de Bolle M.F.C, Terras F.R.G, Proost P, van Damme J, Rees S.B, Vanderleyden J, Broekaert W.F.##de Bolle M.F, Eggermont K, Duncan R.E, Osborn R.W, Terras F.R.G, Broekaert W.F. Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa L. seeds.##Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L. DRAMP01017 CIGNGGRCNENVGPPYCCSGFCLRQPNQGYGVCRNR 36 Antimicrobial peptide 2 (MJ-AMP2; Plant defensin) P25404 Belongs to the AMP family AMP2 Mirabilis jalapa (Garden four-o'clock) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found Function: Possesses antifungal activity and is also active on two tested Gram-positive bacteria: but is non-toxic for Gram-negative bacteria and cultured human cells. Tissue specificity: Found only in seeds. PTM: Contains three disulfide bonds 1-18; 8-22; Fungi: Alternaria brassicola (MIC=6 µg/ml), Ascochyta pisi (MIC=6 µg/ml), Botrytis cinerea (MIC=2 µg/ml), Cercospora beticola (MIC=2 µg/ml), Colletotrichum lindemuthianum (MIC=1 µg/ml), Fusarium culmorum (MIC=3 µg/ml), Fusarium oxysporum f.sp.pisi (MIC=5 µg/ml), Fusarium oxysporum f.sp.lycopersici (MIC=10 µg/ml), Nectria haematococca (MIC=0.5 µg/ml), Phoma betae (MIC=6 µg/ml), Pyrenophora tritici-repentis (MIC=20 µg/ml), Pyricularia oryzae (MIC=0.5 µg/ml), Rhizoctonia solani (MIC=15 µg/ml), Verticillium dahliae (MIC=0.5 µg/ml), Venturia inequalis (MIC=1 µg/ml).##Gram-positive bacteria: Bacillus megaterium (MIC=2 µg/ml), Sarcina lutea (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal Cys residue (forming a disulfide bond) Free There are three disulfide bonds between Cys1 and Cys18, Cys8 and Cys22, Cys17 and Cys33. L No cytotoxicity information found Not found 1733929##7647302 J Biol Chem. 1992 Feb 5;267(4):2228-2233.##Plant Mol Biol. 1995 Jul;28(4):713-721. Cammue BP, De Bolle MF, Terras FR, Proost P, Van Damme J, Rees SB, Vanderleyden J, Broekaert WF.##De Bolle MF, Eggermont K, Duncan RE, Osborn RW, Terras FR, Broekaert WF. Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds.##Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L. DRAMP01018 SIPCGESCVFIPCTVTALLGCSCKSKVCYKN 31 Cyclopsychotride-A (CPT; Plant defensin) P56872 Not found Not found Psychotria longipes Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has antibiotic activity. Inhibits the cytopathic effects and replication of the human immunodeficiency virus. Active against both Gram-positive and Gram-negative bacteria. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28." Gram-negative bacteria: Escherichia coli (MIC=1.55 µM), Pseudomonas aeruginosa (MIC=13.5 µM), Proteus vulgaris (MIC=13.2 µM), Klebsiella oxytoca (MIC=5.80 µM).##Gram-positive bacteria: Staphylococcus aureus (MIC=39.0 µM), Micrococcus luteus (MIC=48.0 µM).##Fungi: Candida albicans (MIC>500 µM), Candida kefyr (MIC=14.0 µM), Candida tropicalis (MIC=56.5 µM).##NOTE: Medium with 10 mM phosphate buffer. [Ref.10430870] HD50 = 405 μM against blood type A human erythrocytes. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) There are three disulfide bonds between Cys4 and Cys21, Cys8 and Cys23, Cys13 and Cys28 L [Ref.10430870] It caused 50% cell growth inhibition of mouse fibroblasts at 1850 μM. Not found 10430870##7714530 Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.##J Nat Prod. 1994 Dec;57(12):1619-1625. Tam JP, Lu YA, Yang JL, Chiu KW.##Witherup KM, Bogusky MJ, Anderson PS, Ramjit H, Ransom RW, Wood T, Sardana M. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.##Cyclopsychotride A, a biologically active, 31-residue cyclic peptide isolated from Psychotria longipes. DRAMP01061 SRSELIVHQR 10 Antifungal peptide (Cm-p1; Plants) B3EWI7 Not found Not found Cenchritis muricatus (Beaded periwinkle) Antimicrobial, Antifungal Protein level Not found Not found 2MP9 resolved by NMR. Function: The synthetic peptide has antifungal activity. Has no antibacterial or cytotoxic activity. Fungi: Botrytis cinerea (MIC=20 µM), Fusarium oxysporum (MIC=20 µM), Aspergillus niger (MIC=41 µM), Candida albicans 01U (MIC=13 µM), C. albicans 38U (MIC=7 µM), C. parapsilosis (MIC=105 µM), C. neoformans strain L26 (MIC=209 µM), C. neoformans strain L30 (MIC=209 µM), Trichophyton rubrum (MIC=3 µM). [Ref.22210491] At the highest evaluated dose (256 μg/mL), Cm-p1 showed no signs of toxicity against human red blood cells. Linear Free Free (very possibly) L [Ref.22210491] At the highest evaluated dose (256 μg/mL), Cm-p1 showed no signs of toxicity against RAW 264.7 cells. Not found 22210491 Biochimie. 2012 Apr;94(4):968-974. López-Abarrategui C, Alba A, Silva ON, Reyes-Acosta O, Vasconcelos IM, Oliveira JT, Migliolo L, Costa MP, Costa CR, Silva MR, Garay HE, Dias SC, Franco OL, Otero-González AJ. Functional characterization of a synthetic hydrophilic antifungal peptide derived from the marine snail Cenchritis muricatus. DRAMP18193 KRFKKFFKKVKKSVKKRLKKIFKKPMVIGVTIPF 34 Cathelicidin-related peptide crotalicidin U5KJM4 Belongs to the cathelicidin family. Not found Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found alpha helical Not found 2MWT resolved by NMR Function: Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane (By similarity). Hemolytic activities have been observed on mammalian cells. Expressed by the venom gland. [Ref.25100358]Gram-negative: E.coli ATCC 25922 (MIC=0.25 μg/mL),P.aeruginosa (MIC=1 μg/mL);##Gram-positive: E.faecalis (MIC=32 μg/mL), S.aureus (MIC=32 μg/mL). [Ref.25100358] Crotalicidin reached 10% hemolysis at 25 μM. Even so, extrapolation of existing data indicates that 50% hemolysis would be reached at near-millimolar values, which defines an adequate (~2 log) selectivity window. Cyclic Free Amidation L No cytotoxicity information found cell membrane 25100358 Amino Acids 46:2561-2571(2014) Falcao C.B., de La Torre B.G., Perez-Peinado C., Barron A.E.,Andreu D., Radis-Baptista G. Vipericidins: a novel family of cathelicidin-related peptides fromthe venom gland of South American pit vipers. DRAMP01064 AWKLFDDGV 9 Anticancerous peptide 1 (Cr-ACP1; Plants) B3EWE7 Not found Not found Cycas revoluta (Sago palm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Not found Not found Function: The synthetic peptide inhibits cell proliferation and induces apoptosis in cancer-derived cell lines Hep2 (IC50=1.5 mM) and HCT15 and, to a lesser extent, in non-cancerous NIH/3T3 cells. The mode of action is presumably an arrest in the G0/G1 phase. Antiproliferative, proapoptotic and DNA-binding activities are increased by acetylation at Ala-1 and Lys-3. Has a weak hemolytic activity against mouse erythrocytes. Has antibacterial activity. Antibacterial activity is decreased by acetylation. [Ref.21882228]Gram-positive bacteria: Staphylococcus epidermidis (MIC=60 µM), Bacillus subtilis (MIC=30 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=30 µM), EEscherichia coli strain ATCC 8739 (MIC=30 µM). [Ref.21882228] Hemocompatibility study revealed the effectiveness of both the peptides where it showed no significant lysis of normal RBC cells compare to positive control (Triton X-100). Cr-ACP1 induced hemolysis of 7% at the conentration of 1 mM. Linear Free Free L [Ref.21882228] IC50 = 1.5 mM in Hep2 (Human epidermoid cancer cells); IC50 = 0.9 mM in HCT15 (human colon carcinoma cells HCT15); Cr-ACP1 induced a cell viability of 66% at the concentration of 4 mM. DNA 21882228 J Cell Biochem. 2012 Jan;113(1):184-193. Mandal SM, Migliolo L, Das S, Mandal M, Franco OL, Hazra TK. Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties. DRAMP01066 PVVDTTGNNPLQQQEEYYV 19 Kunitz-type serine protease inhibitor 1 (Xb-KTI; Plants) P86930 Not found Not found Xanthosoma sagittifolium (Elephant's ear) (Arum sagittifolium) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Serine protease inhibitor. Displays antimicrobial activity against the Gram-negative bacterium S. typhimurium ATCC 14028. Displays a weak hemolytic activity. [Ref.21520894]Gram-negative bacterium: Salmonella typhimurium ATCC 14028 (MIC=10 µM). [Ref.21520894] No hemolytic activity was observed for Xb-KTI. The peptide induced a hemolysis of 12% at the highest concentration of 250 μg/mL. Values(OD540) were normalized against 100% lysed erythrocytes (0.1% Triton X-100) and PDB (untreated control) Linear Free Free L No cytotoxicity information found Not found 21520894 J Nat Prod. 2011 May 27;74(5):969-975. Lima TB, Silva ON, Migliolo L, Souza-Filho CR, Gonçalves EG, Vasconcelos IM, Oliveira JT, Amaral AC, Franco OL. A Kunitz proteinase inhibitor from corms of Xanthosoma blandum with bactericidal activity. DRAMP01081 GLKDIFKAGLGSLVKGIAAHVAN 23 Alyteserin-1a (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacterium Escherichia coli. The hemolytic activity against human erythrocytes of all peptides tested is relatively weak. Structural similarity: The alyteserin-1 peptides show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae." [Ref.19463738]Gram-negative bacterium: Escherichia coli (MIC=25 µM). [Ref:19463738] LC50 > 100 μM against human erthrocytes. Alyteserin-1a induced a hemolysis of 11% at the concentration of 100 μM. Linear Free α-Amidation L (to be determined) No cytotoxicity information found Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01082 ILGKLLSTAAGLLSNL 16 Alyteserin-2a (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Anti-Gram+, Cytotoxicity Not found Alpha helix It is helical in 50% TFE. "Function: The alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus. The hemolytic activity against human erythrocytes of all peptides tested is relatively weak. Structural similarity: Alyteserin-2a and alyteserin-2b and -2c show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae." [Ref.19463738]Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM). [Ref:19463738] LC50 = 135 μM against human erthrocytes. Linear Free α-Amidation L (to be determined) No cytotoxicity information found Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01083 GLKEIFKAGLGSLVKGIAAHVAN 23 Alyteserin-1b (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Amtimicrobial peptide. (By similarity) Gram-negative bacterium: Escherichia coli (MIC=25 µM). [Ref:19463738] LC50 = 210 μM against human erthrocytes. Linear Free α-Amidation L (to be determined) No cytotoxicity information found Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01085 GLKEIFKAGLGSLVKGIAAHVAS 23 Alyteserin-1c (toads, amphibians, animals) H0USY4 Not found Not found Alytes obstetricans (Common midwife toad) (Bufo obstetricans) Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21).(Ref.1) 2L5R resolved by NMR. Function: Alyteserin-1c shows selective growth-inhibitory activity against Gram-negative bacteria. Gram-negative bacterium: Escherichia coli (MIC=25 µM). [Ref:19463738] LC50 = 145 μM against human erthrocytes. Linear Free α-Amidation L (to be determined) No cytotoxicity information found Not found 21565166##19463738 Biochim Biophys Acta. 2011 Aug;1808(8):1975-1984.##Peptides. 2009 Jun;30(6):1069-1073. Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM.##Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.##The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01088 GFKEVLKADLGSLVKGIAAHVAN 23 Alyteserin-1Ma (toads, amphibians, animals) No entry found Not found Not found Alytes maurus (Midwife toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Alyteserin-1Ma has lower antimicrobial potencies (MIC>200 µM). Gram-negative bacterium: Escherichia coli NCTC 10418 (MIC=214 µM) and Gram-positive bacterium: Staphylococcus aureus NCTC 10788 (MIC=214 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 22800568 Toxicon. 2012 Nov;60(6):967-981. König E, Zhou M, Wang L, Chen T, Bininda-Emonds OR, Shaw C. Antimicrobial peptides and alytesin are co-secreted from the venom of the Midwife toad, Alytes maurus (Alytidae, Anura): Implications for the evolution of frog skin defensive secretions. DRAMP01089 GFKEVLKAGLGSLVKGIPAHVAN 23 Alyteserin-1Mb (toads, amphibians, animals) No entry found Not found Not found Alytes maurus (Midwife toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Alyteserin-2Ma has lower antimicrobial potencies (MIC>200 µM). Gram-negative bacterium: Escherichia coli NCTC 10418 (MIC=217 µM) and Gram-positive bacterium: Staphylococcus aureus NCTC 10788 (MIC=434 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 22800568 Toxicon. 2012 Nov;60(6):967-981. König E, Zhou M, Wang L, Chen T, Bininda-Emonds OR, Shaw C. Antimicrobial peptides and alytesin are co-secreted from the venom of the Midwife toad, Alytes maurus (Alytidae, Anura): Implications for the evolution of frog skin defensive secretions. DRAMP01090 FIGKLISAASGLLSHL 16 Alyteserin-2Ma (toads, amphibians, animals) No entry found Not found Not found Alytes maurus (Midwife toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli and Gram-positive bacteria S. aures. It only inhibits C. albicans at very high concentration of 150 microM. Gram-negative bacterium: Escherichia coli NCTC 10418 (MIC=38.4 µM) and Gram-positive bacterium: Staphylococcus aureus NCTC 10788 (MIC=9.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 22800568 Toxicon. 2012 Nov;60(6):967-981. König E, Zhou M, Wang L, Chen T, Bininda-Emonds OR, Shaw C. Antimicrobial peptides and alytesin are co-secreted from the venom of the Midwife toad, Alytes maurus (Alytidae, Anura): Implications for the evolution of frog skin defensive secretions. DRAMP01091 ILGAIIPLVSGLLSHL 16 Alyteserin-2Mb (toads, amphibians, animals) No entry found Not found Not found Alytes maurus (Midwife toad) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Function: Has antibacterial activity against the Gram-positive bacteria S. aures. It only inhibits C. albicans at very high concentration of 310 microM. Gram-positive bacterium: Staphylococcus aureus NCTC 10788 (MIC=19.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 22800568 Toxicon. 2012 Nov;60(6):967-981. König E, Zhou M, Wang L, Chen T, Bininda-Emonds OR, Shaw C. Antimicrobial peptides and alytesin are co-secreted from the venom of the Midwife toad, Alytes maurus (Alytidae, Anura): Implications for the evolution of frog skin defensive secretions. DRAMP01096 GIGSAILSAGKSALKGLAKGLAEHFAN 27 Bombinin-like peptide 2 (BLP-2; toads, amphibians, animals) P29003 Belongs to the bombinin family Not found Bombina orientalis (Oriental fire-bellied toad) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. Tissue specificity: Expressed by the skin glands." [Ref.1744108]Gram-negative bacterium: 58% inhibition Neisseria meningitidis 118V C (MIC=20 µg/ml), 98% inhibition Neisseria meningitidis 15240 IAI (MIC=20 µg/ml), 98% inhibition Neisseria meningitidis 126E IC1 (MIC=20 µg/ml), 97% inhibition Neisseria gonorrhoeoe F62 (MIC=20 µg/ml), 99% inhibition Neisseria Iactamica 15323 (MIC=20 µg/ml), 100% inhibition Neisseria Iactamica 15215A (MIC=20 µg/ml), 95% inhibition Neisseria cinerea 15461 (MIC=20 µg/ml). [Ref:1744108] No significant hemolytic activity was found which suggests a selectivity for prokaryotic over eukaryotic membranes. Cyclic Free Amidation L No cytotoxicity information found Not found 1744108 J. Biol. Chem. 1991; 266: 23103-23111. Gibson BW, Tang D, Mandrell R, Kelly M, Spindel ER. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. DRAMP03017 FMPIIGRLMSGSL 13 VESP-VB1 (Insects, animals) No entry found Not found Not found vespine wasps Vespa bicolor Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antimicrobial activities against standard strains and strong antimicrobial ability against drug-resistant strains. Among the tested drug-resistant strains, Pseudemonas aeruginosa and Staphylococcus aureus were the most sensitive for this kind of antimicrobial peptide. Has a little hemolytic activity. [Ref.18723059] Gram-negative bacterium: Escherichia coli ATCC25922(MIC=7.5μg/ml), Escherichia coli 23A(MIC=7.5μg/ml), Escherichia coli 27A(MIC=15.0μg/ml), Pseudemonas aeruginosa 3A(MIC=3.75μg/ml), Pseudemonas aeruginosa 7A(MIC=3.75μg/ml), ;## Gram-positive bacterium: Staphylococcus aureus ATCC2592(MIC=1.9μg/ml), Staphylococcus aureus 6A(MIC=3.75μg/ml), Staphylococcus aureus 15A(MIC=1.0μg/ml);## Fungus: Candida albicans ATCC2002(MIC=30.0μg/ml) [Ref.18723059] VESP-VB1 had a little hemolytic activity of 10.2% against rabbit red blood cells, and of 3.2% against human red blood cells with peptide concentration up to 200 μg/ml Linear Free Free L No cytotoxicity information found Not found 18723059 Peptides. 2008 Nov;29(11):1887-1892. Chen W, Yang X, Yang X, Zhai L, Lu Z, Liu J, Yu H. Antimicrobial peptides from the venoms of Vespa bicolor Fabricius. DRAMP01098 GIGAAILSAGKSALKGLAKGLAEHF 25 Bombinin-like peptide 3 (BLP-3; toads, amphibians, animals) P29004 Belongs to the bombinin family Not found Bombina orientalis (Oriental fire-bellied toad) Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix Not found "Function: Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. Tissue specificity: Expressed by the skin glands." [Ref.1744108]Gram-postive bacterium:Bacillus megaterium BmII (MIC=0.3 µM), Staphylococcus aureus Cowan1 (MIC=1.7 µM);##Gram-negative bacterium:59% inhibition Neisseria meningitidis 118V C (MIC=20 µg/ml), 99% inhibition Neisseria meningitidis 15240 IAI (MIC=20 µg/ml), 99% inhibition Neisseria meningitidis 126E IC1 (MIC=20 µg/ml), 99% inhibition Neisseria gonorrhoeoe F62 (MIC=20 µg/ml), 97% inhibitionNeisseria Iactamica 15323 (MIC=20 µg/ml), 100% inhibition Neisseria Iactamica 15215A (MIC=20 µg/ml), 97% inhibition Neisseria cinerea 15461 (MIC=20 µg/ml), Escherichia coli D21 (MIC=1.7 µM), Escherichia coli D22 (MIC=1.5 µM), Yersinia pseudotubercolosis (MIC=0.6 µM), Pseudomonas aeruginosa ATCC 15692 (MIC=9.2 µM);##Fungus:Candida albicans (MIC=0.4 µM). [Ref:1744108] No significant hemolytic activity was found which suggests a selectivity for prokaryotic over eukaryotic membranes. Cyclic Free Amidation L No cytotoxicity information found Not found 1744108 J Biol Chem. 1991 Dec 5;266(34):23103-23111. Gibson BW, Tang DZ, Mandrell R, Kelly M, Spindel ER. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. DRAMP01105 RSNKGFNFMVDMIQALSK 18 Maximin-S4 (chain of Maximins-S type B/C; toads, amphibians, animals) Q5GC92 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial Protein level Not found Not found Function: Maximin-S3 has an activity against mycoplasma but has no activity against common Gram-positive and Gram-negative bacteria nor fungi. Has no hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Lysine amide at position 18. [Ref.15649437]Mycoplasma humenis (MIC=46 µM), Ureaplasma urealyticum (MIC=46 µM). [Ref:15649437] Maximin S1 and S4 had no hemolytic activity. Linear Free Amidation L No cytotoxicity information found Not found 15649437 Biochem Biophys Res Commun. 2005 Feb 18;327(3):945-951. Wang T, Zhang J, Shen JH, Jin Y, Lee WH, Zhang Y. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima. DRAMP02090 FLPMLAGLAASMVPKFVCLITKKC 24 Brevinin-1Lb (Frogs, amphibians, animals) P82826 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=8 μM);##Gram-negative bacterium: Escherichia coli (MIC=16 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There is a disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02091 FLPFIAGMAAKFLPKIFCAISKKC 24 Brevinin-1Ba (Frogs, amphibians, animals) P82833 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01829 FLPILINLIHKGLL 14 Temporin-1Lc (Temporin 1Lc; Frogs, amphibians, animals) P82832 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 14. " [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=125 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01828 NFLGTLINLAKKIM 14 Temporin-1Lb (Temporin 1Lb; Frogs, amphibians, animals) P82831 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Methionine amide at position 14. " [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=48 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01518 GILSLFTGGIKALGKTLFKMAGKAGAEHLACKATNQC 37 Esculentin-2L (Frogs, amphibians, animals) P82827 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Great Basin spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=3 μM);##Gram-negative bacterium: Escherichia coli (MIC=6 μM).##Yeast: Candida albicans (MIC=53 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01827 VLPLISMALGKLL 13 Temporin-1La (Temporin 1La; Frogs, amphibians, animals) P82830 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. " [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=60 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free α-Amidation L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01517 GFSSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC 37 Esculentin-2P (Frogs, amphibians, animals) P82846 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram-, Antiviral Protein level Not found Not found "Function: Antibacterial activity against Gram-negative bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-negative bacterium: Escherichia coli (MIC=10 μM).##[Ref.11601906]Virus:##Frog Virus 3: 90% inhibition at 500 µM;##Channel Catfish Virus: 90% inhibition at 50 µM. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys31 and Cys37. L No cytotoxicity information found in the reference(s) presented Not found 11601906##10651828 Virology. 2001 Sep 30;288(2):351-7.##Eur J Biochem. 2000 Feb;267(3):894-900. Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L.##Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin.##Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01516 GLFSILRGAAKFASKGLGKDLTKLGVDLVACKISKQC 37 Esculentin-2B (Frogs, amphibians, animals) P82839 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=1 μM);##Gram-negative bacterium: Escherichia coli (MIC=1 μM).##Yeast: Candida albicans (MIC=29 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02077 FLPIIAGIAAKVFPKIFCAISKKC 24 Brevinin-1Pb (Frogs, amphibians, animals) Q8QFQ5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=5 μM);##Gram-negative bacterium: Escherichia coli (MIC=14 μM).##Yeast: Candida albicans (MIC=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 10651828##12413397 Eur J Biochem. 2000 Feb;267(3):894-900.##Biochem J. 2003 Apr 1;371(Pt 1):125-130. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM.##Chen T, Farragher S.M, Bjourson A.J, Orr D.F, Rao P, Shaw C. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens.##Granular gland transcriptomes in stimulated amphibian skin secretions. DRAMP01830 FLPIVGKLLSGLL 13 Temporin-1P (Temporin-1M; Temporin-1CSa; Frogs, amphibians, animals) P82848 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13." [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=110 µM). [Ref.17451843] LC50 = 75 μM against human erythrocytes. Cyclic Free α‐Amidation L No cytotoxicity information found Not found 10651828##17451843 Eur J Biochem. 2000 Feb;267(3):894-900.##Peptides 2007; 28: 1268-1274. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM.##Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens.##Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. DRAMP01151 GVGDLIRKAVSVIKNIV 17 Uperin-3.5 (toads, amphibians, animals) P82042 Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Lactococcus lactis (MIC=3 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12.5 µg/ml), Staphylococcus aureus (MIC=50 µg/ml), Staphylococcus epidermidis (MIC=12.5 µg/ml), Streptococcus uberis (MIC=12.5 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found Not found PubMed ID is not available##15203252 Aust. J. Chem. 1996; 49:475-484.##Peptides. 2004 Jun;25(6):1035-1054. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01152 GVIDAAKKVVNVLKNLP 17 Uperin-3.6 (toads, amphibians, animals) P82043 Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix In 50% (by vol.) trifluoroethanol, an NMR study and structure calculations indicate that uperin 3.6 adopts a well-defined amphipathic alpha-helix with distinct hydrophilic and hydrophobic faces.(Ref.1) Function: Shows antibacterial activity gaginst several Gram-positive bacteria. This peptide could inhibit HIV infection at a concentration that is also toxic to T cells (J Virol 2005; 79:11598-11606). Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Lactococcus lactis (MIC=3 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=25 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=12.5 µg/ml), Streptococcus uberis (MIC=12.5 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found Not found 10461748##15203252 J Pept Res. 1999 Aug;54(2):137-145.##Peptides. 2004 Jun;25(6):1035-1054. Chia BC, Carver JA, Mulhern TD, Bowie JH.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01153 GVIAAAKKVVNVLKNLF 17 Ala4-uperin 3.6 (toads, amphibians, animals) No entry found Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Shows antibacterial activity gaginst several Gram-positive bacteria. Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found Not found 10461748 J Pept Res. 1999 Aug;54(2):137-145. Chia BC, Carver JA, Mulhern TD, Bowie JH. The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii. DRAMP01154 GVIDAAAKVVNVLKNLF 17 Ala7-uperin 3.6 (toads, amphibians, animals) No entry found Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Shows antibacterial activity gaginst several Gram-positive bacteria. Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Streptococcus uberis (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found Not found 10461748 J Pept Res. 1999 Aug;54(2):137-145. Chia BC, Carver JA, Mulhern TD, Bowie JH. The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii. DRAMP01155 GVIDAAKKVVNVLANLF 17 Ala14-uperin 3.6 (toads, amphibians, animals) No entry found Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Shows antibacterial activity gaginst several Gram-positive bacteria. Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Streptococcus uberis (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found Not found 10461748 J Pept Res. 1999 Aug;54(2):137-145. Chia BC, Carver JA, Mulhern TD, Bowie JH. The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii. DRAMP01162 AGRGKQGGKVRAKAKTRSSRAGLQFPVGRVHRLLRKGNY 39 Buforin-1 (Buforin I; Fragment of Histone H2A; toads, amphibians, animals) P55897 Belongs to the histone H2A family Not found Bufo gargarizans (Asian toad) (Bufo bufo gargarizans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination of C-terminus gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties." Gram-positive bacteria: Bacillus subtilis (MIC=4 µg/ml), Staphylococcus aureus (MIC=4 µg/ml), Streptococcus mutans (MIC=8 µg/ml), Streptococcus pneumoniae (MIC=4 µg/ml), Pseudomonas putida (MIC=4 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=8 µg/ml), Salmonella typhimurium (MIC=4 µg/ml), Serratia sp. (MIC=8 µg/ml).##Fungi: Candida albicans (MIC=4 µg/ml), Cryptococcus neoformans (MIC=4 µg/ml), Saccharomyces cerevisiae (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free ①The residue at position 5 is N6-(2-hydroxyisobutyryl)lysine or N6-acetyllysine. ②The residue at position 9 is N6-(2-hydroxyisobutyryl)lysine or N6-lactoyllysine or N6-succinyllysine. ③The Lys13 has a interchain with G-Cter in ubiquitin. ④The Lys15 has a interchain with G-Cter in ubiquitin. ⑤The residue at position 36 is N6-(2-hydroxyisobutyryl)lysine. L No cytotoxicity information found DNA 8573171##8946958 Biochem Biophys Res Commun. 1996 Jan 5;218(1):408-413.##FEBS Lett. 1996 Nov 25;398(1):87-90. Park C.B, Kim M.S, Kim S.C.##Yi G.-S, Park C.B, Kim S.C, Cheong C. A novel antimicrobial peptide from Bufo bufo gargarizans.##Solution structure of an antimicrobial peptide buforin II. DRAMP01163 TRSSRAGLQFPVGRVHRLLRK 21 Buforin-2 (Buforin II; Fragment of Histone H2A; toads, amphibians, animals) P0DQL2 Belongs to the histone H2A family Not found Bufo gargarizans (Asian toad) (Bufo bufo gargarizans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Both buforin II and its derivative buforin IIb (sequence: RAGLQFPVGRLLRRLLRRLLR) showed selective anticancer activity against 62 cancer cell lines (Lee 2008 Cancer Lett 271: 47-51). Buforin II is more potent than buforin I. PTM: Monoubiquitination of C-terminus gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties." Gram-positive bacteria: Bacillus subtilis (MIC=2 µg/ml), Staphylococcus aureus (MIC=4 µg/ml), Streptococcus mutans (MIC=2 µg/ml), Streptococcus pneumoniae (MIC=4 µg/ml), Pseudomonas putida (MIC=2 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=1 µg/ml), Serratia sp. (MIC=4 µg/ml).##Fungi: Candida albicans (MIC=1 µg/ml), Cryptococcus neoformans (MIC=1 µg/ml), Saccharomyces cerevisiae (MIC=1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free ① The residue at position 21 is N6-(2-hydroxyisobutyryl)lysine L No cytotoxicity information found DNA 8573171##8946958 Biochem Biophys Res Commun. 1996 Jan 5;218(1):408-413.##FEBS Lett. 1996 Nov 25;398(1):87-90. Park C.B, Kim M.S, Kim S.C.##Yi G.-S, Park C.B, Kim S.C, Cheong C. A novel antimicrobial peptide from Bufo bufo gargarizans.##Solution structure of an antimicrobial peptide buforin II. DRAMP01164 GIGALSAKGALKGLAKGLAEHFAN 24 Bombinin (toads, amphibians, animals) P01505 Not found Not found Bombina variegata (Yellow-bellied toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial and hemolytic activities. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation. Caution: Residue 20 is assigned as E by similarity to other bombin sequences instead of Z (Glutamic acid or Gutamine) given " [Ref.8223491]Gram-negative bacterium: Escherichia coli D21 (MIC=3 µM);##Gram-positive bacterium: Staphylococcus aureus Cowan 1 (MIC=14 µM). [Ref.8223491] The lethal concentration (LC, the lowest concentration that inhibits growth) was over 50 μM Linear Free Amidation L No cytotoxicity information found Not found PubMed ID is not available##8223491 Monatsh. Chem. 1970;101:182-189.##EMBO J. 1993; 12:4829-4832. Csordas A, Michl H.##Mignogna G, Simmaco M, Kreil G, Barra D. Isolation and structural resolution of a haemolytically active polypeptide from the immune secretion of a European toad.##Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. DRAMP01165 FLPVILPVIGKLLNGILGK 19 Preprotemporin-1SKa (Frogs, amphibians, animals) No entry found Not found Not found Rana sakuraii (Japanese brown frog) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP01167 GILDAIKAIAKAAG 14 Hylaseptin-P1 (HSP1) P84292 Not found Not found Hyla punctata (Polka-dot tree frog) (Spotted tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Has antibacterial and antifungal activity. A weak hemolytic activity has been detected. [Ref.14715660]Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.1-8.0 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=48.8-64.0 µg/ml), Escherichia coli ATCC 25922 (MIC=24.4-32.0 µg/ml). [Ref.14715660] HSP1 MIC concentration (256 μg/mL = 195.2 μM) produced 4.7% hemolysis against human erythrocytes. Linear Free [Ref.11297740] Free / [Ref.32828849] Amidation L No cytotoxicity information found Not found 14715660##32828849 "J Biol Chem. 2004 Mar 26;279(13):13018-13026. ##Biochim Biophys Acta Biomembr . 2021 Jan 1;1863(1):183449. doi: 10.1016/j.bbamem.2020.183449. Epub 2020 Aug 21." Prates MV, Sfor§a ML, Regis WC, Leite JR, Silva LP, Pertinhez TA, Araºjo AL, Azevedo RB, Spisni A, Bloch C Jr.##Isabela P Gomes 1, Talita L Santos 1, Amanda N de Souza 1, Lúcio O Nunes, Gabriele A Cardoso, Carolina O Matos, Lívia M F Costa, Luciano M Lião, Jarbas M Resende, Rodrigo M Verly The NMR-derived solution structure of a new cationic antimicrobial peptide from the skin secretion of the anuran Hyla punctata.##Membrane interactions of the anuran antimicrobial peptide HSP1-NH 2: Different aspects of the association to anionic and zwitterionic biomimetic systems DRAMP01170 NLVSGLIEARKYLEQLHRKLKNCKV 25 Distinctin 2 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa distincta (Tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix (1 helices; 17 residues) Not found 1XKM resolved by NMR Comment: Distinctin is constituted of two different polypeptide chains connected by an intermolecular disulphide bridge. The entry is the chain 2 of Distinctin Note: Distinctin chain 2 links to Distinctin chain 1 to form a heterodimeric peptide to exert antibacterial function. ##Gram-positive bacteria: Enterococcus faecalis (MIC=14.5 µM), Staphylococcus aureus (MIC=28.0 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=28.0 µM), Escherichia coli (MIC=14.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free There is an intermolecular disulphide bridge between Distinctin chain 1 (Cys19) and Distinctin chain 2 (Cys22). L No cytotoxicity information found Not found 11297740 FEBS Lett. 2001 Apr 6;494(1-2):85-89. Batista CV, Scaloni A, Rigden DJ, Silva LR, Rodrigues Romero A, Dukor R, Sebben A, Talamo F, Bloch C. A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta. DRAMP01174 GLLDFVTGVGKDIFAQLIKQI 21 Ocellatin-4 (Frogs, amphibians, animals) P85090 Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes (HC50=14.3 µM). Has antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." [Ref.17884127]Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=64 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=64 µM). [Ref.17884127] HC50 = 14.3 μM against human O+ red blood cells Linear Free Amidation L No cytotoxicity information found Not found 17884127 Toxicon 2007; 50: 1095-1104. Nascimento A et al Castro MS. Purification, characterization and homology analysis of ocellatin 4, a cytolytic peptide from the skin secretion of the frog Leptodactylus ocellatus. DRAMP01177 GVVDILKGAAKDIAGHLASKVMNKL 25 Ocellatin-F1 (Fallaxin; Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus fallax (Mountain chicken frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found 5U9S##5U9Y##5UA8##5U9R##5U9X##5UA7##5U9Q##5U9V##5UA6 Function: Has low hemolytic activity of fallaxin (HC50>200 µM). [Ref.15544856]Gram-negative bacteria: Escherichia coli (MIC=40 µM), Pseudomonas aeruginosa (MIC=80 µM), Enterobacter cloacae (MIC=20 µM), Klebsiella pneumoniae (MIC=80 µM). [Ref:15544856]HC50>200 μM hemolytic activity of fallaxin Linear Free Amidation Free L [Ref.15544856]No cytotoxicity information found Not found 15544856 Regul Pept. 2005 Jan 15;124(1-3):173-178. Rollins-Smith LA, King JD, Nielsen PF, Sonnevend A, Conlon JM. An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae). DRAMP01182 GLLDTLKGAAKNVVGSLASKVMEKL 25 Ocellatin-P1 (Pentadactylin; Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus pentadactylus (South American bullfrog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=25 µM), Klebsiella pneumoniae KK3 9904 (MIC=100 µM), Enterobacter cloacae HNTCC 53001 (MIC=50 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=100 µM);##Gram-positive bacteria: Staphylococcus epidermidis RP62A (MIC=100 µM), Streptococcus Group B HNTCC 80130 (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16236555]No cytotoxicity information found Not found 16236555 Comp Biochem Physiol C Toxicol Pharmacol. 2005 Aug;141(4):393-397. King JD, Al-Ghaferi N, Abraham B, Sonnevend A, Leprince J, Nielsen PF, Conlon JM. Pentadactylin: an antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus. DRAMP01184 GVLDILKGAAKDLAGHVATKVI 22 SPX(1-22)(truncated peptide of Syphaxin; Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus syphax (Burgundy thin-toed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 29213 (MIC=14.6 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=40.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.17628627]No cytotoxicity information found Not found 17628627 Toxicon. 2007 Sep 15;50(4):572-580. Dourado F.S, Leite J.R.S.A, Silva L.P, Melo J.A.T, Bloch C. Jr, Schwartz E.F. Antimicrobial peptide from the skin secretion of the frog Leptodactylus syphax. DRAMP01185 GVLDILKGAAKDLAGH 16 SPX(1-16)(truncated peptide of Syphaxin; Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus syphax (Burgundy thin-toed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 29213 (MIC=40.5 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=10.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.17628627]No cytotoxicity information found Not found 17628627 Toxicon. 2007 Sep 15;50(4):572-580. Dourado F.S, Leite J.R.S.A, Silva L.P, Melo J.A.T, Bloch C. Jr, Schwartz E.F. Antimicrobial peptide from the skin secretion of the frog Leptodactylus syphax. DRAMP01188 LALKSGGWLRLFGLKDKKH 19 Chensinin-1ZHa (Frogs, amphibians, animals) No entry found Not found Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=17 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=35 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=9 µM).##Yeast: Candida albicans ATCC 2002 (MIC=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.22943378]No cytotoxicity information found Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01189 ATNIPFKVHFRCKAAFC 17 Andersonin-W1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=23.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC>47 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>47 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=47 µg/ml). [Ref:22029824] It has no hemolytic activity against human red blood cells Cyclic Free Cyclization (Cys12 and Cys17) Disulfide bond between Cys12 and Cys17. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01190 AVNIPFKVHFRCKAAFC 17 Andersonin-W2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=40.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10.1 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=20.2 µg/ml). [Ref:22029824] It has no hemolytic activity against human red blood cells Cyclic Free Cyclization (Cys12 and Cys17) Disulfide bond between Cys12 and Cys17. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01191 GLFSKFAGKGIVNFLIEGVE 20 Andersonin-X1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=15.3 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=15.3 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=30.5 µg/ml). [Ref:22029824]Not found Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01192 FLPKLFAKITKKNMAHIR 18 Andersonin-Y1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=3.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=1.6 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=1.6 µg/ml). [Ref:22029824]Not found Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01194 TSRCIFYRRKKCS 13 Andersonin-C1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Show hemolytic activity against human red blood cells and obvious insulin-stimulating activity at the concentration of 50 μg/mL. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=30 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>120 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=30 µg/ml). [Ref:22029824] It has 15.2±2.1% hemolytic activity at 50μg/ml against human red blood cells Cyclic Free Free Disulfide bond between Cys4 and Cys12. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01195 FIFPKKNIINSLFGR 15 Andersonin-D1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi. Andersonin-D1 showes obvious insulin-stimulating activity at the concentration of 50 μg/mL. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>126 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=16 µg/ml); ##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=16 µg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01199 RFIYMKGFGKPRFGKR 16 Hejiangin-A1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana hejiangensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Hejiangin-A1 showes killing effects against the tested strains. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=100 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=25 µg/ml); ##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=25 µg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01200 IPWKLPATFRPVERPFSKPFCRKD 24 Hejiangin-F1 (frog, amphibians, animals) No entry found Not found Not found Odorrana hejiangensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi and has no hemolytic activity under the test conditions. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>100 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=100 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=100 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=100 µg/ml). [Ref:22029824]Non-hemolytic activity against human red blood cells Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01201 AAPRGGKGFFCKLFKDC 17 Schmackerin-C1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana schmackeri Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Schmackerin-C1 showes killing effects against the tested strains. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=100 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=50 µg/ml); ##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=50 µg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys11 and Cys17) Disulfide bond between Cys11 and Cys17. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01202 GLLDFAKHVIGIASKLG 17 Fallaxidin 3.2 (Frogs, amphibians, animals) B5LUQ7, B5LUR0, B5LUR1, B5LUQ3 Not found Not found Litoria fallax (Eastern dwarf tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Fallaxidin-3.2 shows antibacterial activity against the Gram-positive bacteria. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Enterococcus faecalis (MIC=100 µM), Lactococcus lactis (MIC=500 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.18803332]No cytotoxicity information found Not found 18803332 Rapid Commun Mass Spectrom. 2008 Oct;22(20):3207-3216. Jackway RJ, Bowie JH, Bilusich D, Musgrave IF, Surinya-Johnson KH, Tyler MJ, Eichinger PC. The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins. DRAMP01203 GLLDLAKHVIGIASKL 16 Fallaxidin 3.1 (Frogs, amphibians, animals) B5LUQ8, B5LUQ3 Not found Not found Litoria fallax (Eastern dwarf tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Fallaxidin-3.1 shows antibacterial activity against the Gram-positive bacteria. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Enterococcus faecalis (MIC=100 µM), Lactococcus lactis (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.18803332]No cytotoxicity information found Not found 18803332 Rapid Commun Mass Spectrom. 2008 Oct;22(20):3207-3216. Jackway RJ, Bowie JH, Bilusich D, Musgrave IF, Surinya-Johnson KH, Tyler MJ, Eichinger PC. The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins. DRAMP01204 GLLSFLPKVIGVIGHLIHPPS 21 Fallaxidin 4.1 (Frogs, amphibians, animals) B5LUQ4 Not found Not found Litoria fallax (Eastern dwarf tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Fallaxidin-4.1 shows antibacterial activity against the Gram-positive bacteria. Inhibits the formation of NO by neuronal nitric oxide synthase (IC50=13.3 µM). Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Lactococcus lactis (MIC=12 µM), Micrococcus luteus (MIC=100 µM), Staphylococcus epidermidis (MIC=100 µM), Streptococcus uberis (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.18803332]No cytotoxicity information found Not found 18803332 Rapid Commun Mass Spectrom. 2008 Oct;22(20):3207-3216. Jackway RJ, Bowie JH, Bilusich D, Musgrave IF, Surinya-Johnson KH, Tyler MJ, Eichinger PC. The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins. DRAMP01208 SIITMTKEAKLPQLWKQIACRLYNTC 26 Pleurain-A1 (Pleurain A1; Frogs, amphibians, animals) A8DY01, A8DY00, A8DY02, A8DY03, A8DY04, A8DY09, A8DY10, A8DY15 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has little hemolytic activity on red blood cells. Tissue specificity: Expressed by the skin dorsal glands." [Ref.17764786]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=60 µg/ml), Helicobacter pylori NCTC 11637 (MIC=30 µg/ml);##Gram-positive bacteria: Bacillus dysenteriae (MIC=120 µg/ml), Staphylococcus aureus ATCC 2592 (MIC=15 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=30 µg/ml).. [Ref:17764786] It has little hemolytic activity on red blood cells even with peptide concentration up to 200 μg/ml Cyclic Free Cyclization (Cys20 and Cys26) Disulfide bond between Cys20 and Cys26. L No cytotoxicity information found Not found 17764786 Peptides. 2007 Oct;28(10):2069-2074. Wang X, Song Y, Li J, Liu H, Xu X, Lai R, Zhang K. A new family of antimicrobial peptides from skin secretions of Rana pleuraden DRAMP01209 SIITMTKEAKLPQSWKQIACRLYNTC 26 Pleurain-A2 (Pleurain A2; Frogs, amphibians, animals) A8B5P0 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has little hemolytic activity on red blood cells. Tissue specificity: Expressed by the skin dorsal glands." [Ref.17764786]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=60 µg/ml), Helicobacter pylori NCTC 11637 (MIC=30 µg/ml);##Gram-positive bacteria: Bacillus dysenteriae (MIC=60 µg/ml), Staphylococcus aureus ATCC 2592 (MIC=15 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=30 µg/ml). [Ref:17764786] It has little hemolytic activity on red blood cells even with peptide concentration up to 200 μg/ml Cyclic Free Cyclization (Cys20 and Cys26) Disulfide bond between Cys20 and Cys26. L No cytotoxicity information found Not found 17764786 Peptides. 2007 Oct;28(10):2069-2074. Wang X, Song Y, Li J, Liu H, Xu X, Lai R, Zhang K. A new family of antimicrobial peptides from skin secretions of Rana pleuraden. DRAMP01214 FLGAIAAALPHVINAVTNAL 20 Kassinatuerin-2Ma (Frogs, amphibians, animals) No entry found Not found Not found Kassina maculata (African hyperoliid frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix Secondary structure prediction analysis revealed that virtually the entire structure of each kassinatuerin-2 related peptide is composed of alpha-helix, the helix was not amphipathic like many other amphibian skin antimicrobial peptides, in which there is a hydrophobic face and a positively charged faces the latter presumably interacting with the negatively charged glycocalyx of cell membranes. Function: Natural kassinatuerin-2Ma and their synthetic replicates possessed relatively potent growth inhibitory activity against the Gram-positive bacterium, S. aureus, but were ineffective against the Gram-negative bacterium, E. coli at concentrations up to 200 µM and were relatively ineffective against the pathogenic yeast, C. albicans (120 µM). Also possessed hemolytic activity as demonstrated using horse erythrocytes. [Ref.19427345]Gram-positive bacterium: Staphylococcus aureus (NCTC 10788) (MIC=16 µM);##Gram-negative bacterium: Escherichia coli (NCTC 10418) (MIC>200 µM) (MIC=120 µM);##Yeast: Candida albicans (NCPF 1467) (MIC=120 µM). [Ref:19427345]18% hemolytic activity at 16 μM, 45–50% hemolytic activity at 120 μM against horse erythrocytes Linear Free Amidation Free L [Ref.19427345]No cytotoxicity information found Not found 19427345 Peptides. 2009 Aug;30(8):1428-1433. Wang L, Zhou M, McGrath S, Chen T, Gorman SP, Walker B, Shaw C. A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata. DRAMP01218 GFMKYIGPLIPHAVKAISDLI 21 Kassinatuerin-1 (Frogs, amphibians, animals) P0C010 Not found Not found Kassina senegalensis (Senegal running frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Shows broad-spectrum antimicrobial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-negative bacteria: Escherichia coli (MIC=6.25 µM), Klebsiella pneumoniae (MIC=25 µM), Enterobacter cloacae (MIC=6.25 µM), Pseudomonas aeruginosa (MIC=25 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.25 µM), Staphylococcus epidermidis (MIC=6.25 µM), Enterococcus faecalis (MIC=12.5 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15885852]Display cytotoxicity against L929 fibroblasts (LD50=12μM). Not found 10679222##15885852 Biochem Biophys Res Commun. 2000 Feb 16;268(2):433-436.##Peptides. 2005 Nov;26(11):2104-2110. Mattute B, Knoop FC, Conlon JM.##Conlon JM, Abraham B, Galadari S, Knoop FC, Sonnevend A, P¡l T. Kassinatuerin-1: a peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, Kassina senegalensis.##Antimicrobial and cytolytic properties of the frog skin peptide, kassinatuerin-1 and its L- and D-lysine-substituted derivatives. DRAMP01219 SLWENFKNAGKQFILNILDKIRCRVAGGCRT 31 Palustrin-2LTa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Has antibacterial avctivity. Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=1.7 µM), Bacillus licheniformis X39 (MIC=14 µM), Psychrobacter faecalis X29 (MIC=1.7 µM). [Ref.22426384] It has hemolytic activities (LD50=220μM) against human erythrocytes Cyclic Free Free Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01222 GFMDTAKNVAKNVAVTLIDKLRCKVTGGC 29 Palustrin-2AJ1 (PL2AJ1; Frogs, amphibians, animals) G3ETQ3 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Displays broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria. Has hemolytic activity, low cytotoxicity and low antioxidant activity. Tissue specificity: Expressed by the skin glands. PTM: One disulfide bond (C23-C29) and Cleavage on pair of basic residues." [Ref.21816202]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=20 µM), Enterococcus faecalis ATCC29212 (MIC=20 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=13 µM), Bacillus pyocyaneus CMCCB1010 (MIC=20 µM), Pseudomonas aeruginosa ATCC27853 (MIC=33 µM), Bacillus dysenteriae (MIC=50 µM). [Ref:21816202] IC50=135 μM against human and rabbit erythrocytes Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L [Ref.21816202] Cytotoxicity: the K562 (IC50=58μM) and HT29 mammalian cell lines(IC50=57μM). Not found 21816202 Biochimie. 2012 Feb;94(2):328-334. Chen Z, Yang X, Liu Z, Zeng L, Lee W, Zhang Y. Two novel families of antimicrobial peptides from skin secretions of the Chinese torrent frog, Amolops jingdongensis. DRAMP01227 ALFSILRGLKKLGNMGQAFVNCKIYKKC 28 Palustrin-1b (Frogs, amphibians, animals) P84275 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys22 and Cys28) Disulfide bond between Cys22 and Cys28. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01228 ALSILRGLEKLAKMGIALTNCKATKKC 27 Palustrin-1c (Frogs, amphibians, animals) P84276, A7WNV8 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial activity against Gram-negative bacteria E. coli. Possesses insulin-releasing activity. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=28 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys21 and Cys27) Disulfide bond between Cys21 and Cys27. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01229 ALSILKGLEKLAKMGIALTNCKATKKC 27 Palustrin-1d (Frogs, amphibians, animals) P84277 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=28 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys21 and Cys27) Disulfide bond between Cys21 and Cys27. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01231 GFFSTVKNLATNVAGTVIDTLKCKVTGGCRS 31 Palustrin-2b (Frogs, amphibians, animals) P84279, D3UA82 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=78 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01232 GFMDTAKNVAKNVAATLLDKLKCKITGGC 29 Palustrin-2ISc (Frogs, amphibians, animals) G3XHN9 Not found Not found Odorrana ishikawae (Ishikawa's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=25 µM), Bacillus subtilis (MIC=12.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21867685 Biochem Biophys Res Commun. 2011 Sep 9;412(4):673-677. Iwakoshi-Ukena E, Soga M, Okada G, Fujii T, Sumida M, Ukena K. Characterization of novel antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae by shotgun cDNA cloning. DRAMP01233 GFLSTVKNLATNVAGTVIDTLKCKVTGGCRS 31 Palustrin-2c (Frogs, amphibians, animals) P84280 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=120 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01234 GIFPKIIGKGIKTGIVNGIKSLVKGVGMKVFKAGLNNIGNTGCNEDEC 48 Palustrin-3a (Frogs, amphibians, animals) P84281 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys43 and Cys48) Disulfide bond between Cys43 and Cys48. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01235 GIFPKIIGKGIKTGIVNGIKSLVKGVGMKVFKAGLSNIGNTGCNEDEC 48 Palustrin-3b (Frogs, amphibians, animals) P84262 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys43 and Cys48) Disulfide bond between Cys43 and Cys48. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01237 GFMDTAKNVAKNVAVTLLDKLKCKITGGC 29 Palustrin-2ISa (Frogs, amphibians, animals) No entry found Not found Not found Odorrana ishikawae Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=25 µM), Staphylococcus aureus (MRSA) (MIC=100 µM), Bacillus subtilis (MIC=12.5 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01238 GLWNSIKIAGKKLFVNVLDKIRCKVAGGCKTSPDVE 36 Palustrin-2SIb (Frogs, amphibians, animals) No entry found Not found Not found Odorrana ishikawae Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=6.3 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 µM), S. aureus (MRSA) (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K.2011. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-2 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP01244 FFPIGVFCKIFKTC 14 Japonicin-1 (Frogs, amphibians, animals) P83305 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana japonica (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin dorsal glands. Gram-negative bacterium: Escherichia coli (MIC=30 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys8 and Cys14) Disulfide bond between Cys8 and Cys14. L No cytotoxicity information found Not found 11835990 Peptides. 2002;23:419-425 Isaacson T, Soto A, Iwamuro S, Knoop FC, Conlon JM. Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. DRAMP01245 FFPLALLCKVFKKC 14 Japonicin-1CDYa (Frogs, amphibians, animals) B3VZU2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Antimicrobial peptide. Lacks hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.19539775]Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacterium: Escherichia coli (MIC=25 µM). [Ref:19539775] HC50>300 μM against human red blood cells Cyclic Free Cyclization (Cys8 and Cys14) Disulfide bond between Cys8 and Cys14. L No cytotoxicity information found Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01246 FGLPMLSILPKALCILLKRKC 21 Japonicin-2 (Frogs, amphibians, animals) P83306 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana japonica (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli (MIC=12 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys14 and Cys21) Disulfide bond between Cys14 and Cys21. L No cytotoxicity information found Not found 11835990 Peptides. 2002;23:419-425. Isaacson T, Soto A, Iwamuro S, Knoop FC, Conlon JM. Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. DRAMP01248 FLIGMTHGLICLISRKC 17 Dybowskin-1 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Dybowskin-1 has low hemolytic activity against human red blood cells (hRBCs). [Ref.17698251]Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=12.5 µg/ml), Staphylococcus aureus KCTC3881 (MIC=25 µg/ml), Bacillus subtilis ATCC6633 (MIC=50 µg/ml), Staphylococcus epidermidis ATCC 12228 (MIC=60 µg/ml). [Ref:17698251] It has 0.99% hemolytic activity at 100 μg/ml against huamn red blood cells Cyclic Free Cyclization (Cys11 and Cys17) Disulfide bond between Cys11 and Cys17. L No cytotoxicity information found Not found 17698251 Peptides 2007; 28: 1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01249 FLIGMTQGLICLITRKC 17 Dybowskin-2 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Dybowskin-2 has hemolytic activity against human red blood cells (hRBCs). [Ref.17698251]Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=6.25 µg/ml), Staphylococcus aureus KCTC3881 (MIC=15 µg/ml), Bacillus subtilis ATCC6633 (MIC=25 µg/ml), Staphylococcus epidermidis ATCC12228 (MIC=25 µg/ml);##Gram-negative bacteria: Shigella dysenteriae ATCC9752 (MIC=50 µg/ml), Escherichia coli KCTC2433 (MIC=60 µg/ml), Klebsiella pneumoniae ATCC10031 (MIC=60 µg/ml), Proteus mirabilis ATCC25933 (MIC>100 µg/ml);##Yeast: Candida albicans ATCC36232 (MIC=100 µg/ml). [Ref:17698251] It has 10.99% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys11 and Cys17) Disulfide bond between Cys11 and Cys17. L No cytotoxicity information found Not found 17698251 Peptides 2007; 28: 1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01250 GLFDVVKGVLKGVGKNVAGSLLEQLKCKLSGGC 33 Dybowskin-3 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Dybowskin-3 has hemolytic activity against human red blood cells (hRBCs). [Ref.17698251]Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=39 µg/ml), Staphylococcus aureus KCTC3881 (MIC=50 µg/ml), Bacillus subtilis ATCC6633 (MIC=60 µg/ml), Staphylococcus epidermidis ATCC12228 (MIC=60 µg/ml);##Gram-negative bacteria: Shigella dysenteriae ATCC9752 (MIC=15 µg/ml), Escherichia coli KCTC2433 (MIC=15 µg/ml), Klebsiella pneumoniae ATCC10031 (MIC>100 µg/ml);##Yeast: Candida albicans ATCC36232 (MIC=100 µg/ml). [Ref:17698251] It has 1.86% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 17698251 Peptides 2007; 28: 1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01251 VWPLGLVICKALKIC 15 Dybowskin-4 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Dybowskin-4 has relatively greater hemolytic activity against human red blood cells (hRBCs). [Ref.17698251]Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=1.56 µg/ml), Staphylococcus aureus KCTC3881 (MIC=3.13 µg/ml), Bacillus subtilis ATCC6633 (MIC=6.25 µg/ml), Staphylococcus epidermidis ATCC12228 (MIC=6.25 µg/ml);##Gram-negative bacteria: Shigella dysenteriae ATCC9752 (MIC=30 µg/ml), Escherichia coli KCTC2433 (MIC=15 µg/ml), Klebsiella pneumoniae ATCC10031 (MIC=15 µg/ml);##Yeast: Candida albicans ATCC36232 (MIC=25 µg/ml). [Ref:17698251] It has 47.58% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys9 and Cys15) Disulfide bond between Cys9 and Cys15. L No cytotoxicity information found Not found 17698251 Peptides 2007; 28: 1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01252 GLFSVVTGVLKAVGKNVAKNVGGSLLEQLKCKKISGGC 38 Dybowskin-5 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Dybowskin-5 has hemolytic activity against human red blood cells (hRBCs). [Ref.17698251]Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=6.25 µg/ml), Staphylococcus aureus KCTC3881 (MIC=25 µg/ml), Bacillus subtilis ATCC6633 (MIC=50 µg/ml), Staphylococcus epidermidis ATCC12228 (MIC=50 µg/ml);##Gram-negative bacteria: Shigella dysenteriae ATCC9752 (MIC=50 µg/ml), Escherichia coli KCTC2433 (MIC=60 µg/ml), Klebsiella pneumoniae ATCC10031 (MIC=50 µg/ml);##Yeast: Candida albicans ATCC36232 (MIC=50 µg/ml). [Ref:17698251] It has 17.84% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 17698251 Peptides 2007; 28: 1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01253 FLPLLLAGLPLKLCFLFKKC 20 Dybowskin-6 (Frogs, amphibians, animals) No entry found Not found Not found Rana dybowskii (Korea brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Function: Dybowskin-6 has relatively greater hemolytic activity against human red blood cells (hRBCs). Gram-positive bacteria: Micrococcus luteus ATCC4698 (MIC=6.25 µg/ml), Staphylococcus aureus KCTC3881 (MIC=12.5 µg/ml), Bacillus subtilis ATCC6633 (MIC=50 µg/ml), Staphylococcus epidermidis ATCC12228 (MIC=50 µg/ml).##Yeast: Candida albicans (MIC=50 µg/ml). [Ref:17698251] It has 59.39% hemolytic activity at 100 μg/ml against huamn red blood cells Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found [Ref:17698251]59.39% hemolytic activity at 100 μg/ml against huamn red blood cells 17698251 Peptides. 2007 Aug;28(8):1532-1539. Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP01254 IIPLPLGYFAKKT 13 Dybowskin-1CDYa (Frogs, amphibians, animals) B5A9S9 Not found Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM);##Gram-negative bacterium: Escherichia coli (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.19539775]No cytotoxicity information found Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01255 SAVGRHGRRFGLRKHRKH 18 Dybowskin-2CDYa (Chensinin-1; Frogs, amphibians, animals) B5A9T1 Not found Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Antimicrobial peptide. Has activity against the Gram-positive bacteria: S. aureus and the Gram-negative bacteria E. coli. Lacks hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.19539775] Gram-negative bacterium: Escherichia coli (MIC=3 µM);##Gram-negative bacterium: Staphylococcus aureus (MIC=6 µM).##[Ref.19341344] Gram-positive bacteria: Staphylococcus aureus (MIC=14.4 µM), Bacillus cereus (MIC=14.4 µM), Streptococcus lactis (MIC=14.4 µM). [Ref:19539775]HC50>300 μM against human red blood cells Linear Free Free Free L [Ref.19539775]No cytotoxicity information found##[Ref.19341344]No cytotoxicity information found Not found 19539775##19341344 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178.##Zoolog Sci. 2009 Mar;26(3):220-226. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH.##Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii.##Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01257 GLWSKIKAAGKEAAKAAAKAAGKAALNAVSEAV 33 Dermadistinctin-K (DD K; Frogs, amphibians, animals) P83638 Not found Not found Phyllomedusa distincta (Monkey frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix Not found 2K9B, 2JX6 resolved by NMR. "Function: Also has antiprotozoal activity against Trypanosoma cruzi. Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus (MIC=4.7 µM), Enterococcus faecalis (MIC>19 µM);Gram-negative bacteria: Pseudomonas aeruginosa (MIC=2.4 µM), Escherichia coli (MIC=0.6 µM).##Fungi: Candida tropicalis (MIC=10.1 µM), Candida guilliermondii (MIC=20.3 µM), Candida albicans (MIC=20.3 µM), Candida albicans ATCC 1023 (MIC=10.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10477123]No cytotoxicity information found liposomes 10477123 Peptides. 1999;20(6):679-686. Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. DRAMP01258 ALWKTLLKNVGKAAGKAALNAVTDMVNQ 28 Dermadistinctin-L (DD L; Frogs, amphibians, animals) P83639 Not found Not found Phyllomedusa distincta (Monkey frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix Not found "Function: Also has antiprotozoal activity against Trypanosoma cruzi. Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes. Show little hemolytic activity against human red blood cells. Tissue specificity: Expressed by the skin glands." [Ref.10477123]Gram-positive bacteria: Staphylococcus aureus (MIC=1.3 µM), Enterococcus faecalis (MIC=10 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=40 µM), Escherichia coli (MIC=2.5 µM);##[Ref.17442605]Fungi: Candida tropicalis (MIC=10.9 µM), Candida guilliermondii (MIC=21.8 µM), Candida albicans (MIC=21.8 µM), Candida albicans ATCC 1023 (MIC=10.9 µM). [Ref:10477123]Show some hemolytic starting at 12.5 μM against human blood Linear Free Free Free L [Ref.10477123]No cytotoxicity information found liposomes 10477123##12379643##17409003##17442605 Peptides. 1999;20(6):679-686.##J Biol Chem. 2002 Dec 20;277(51):49332-49340.##Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):329-335.##Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):336-343. Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr.##Brand GD, Leite JR, Silva LP, Albuquerque S, Prates MV, Azevedo RB, Carregaro V, Silva JS, Sá VC, Brandão RA, Bloch C Jr.##Silva LP, Leite JR, Brand GD, Regis WB, Tedesco AC, Azevedo RB, Freitas SM, Bloch C Jr.##Leite JR, Brand GD, Silva LP, Kückelhaus SA, Bento WR, Araújo AL, Martins GR, Lazzari AM, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta.##Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells.##Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: liposomes fusion and/or lysis investigated by fluorescence and atomic force microscopy.##Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity. DRAMP01259 ALWKTMLKKLGTMALHAGKAAFGAAADTISQ 31 Dermadistinctin-M (DD M; Frogs, amphibians, animals) P83640 Not found Not found Phyllomedusa distincta (Monkey frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus (MIC=38 µM), Enterococcus faecalis (MIC>38 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=38 µM), Escherichia coli (MIC=9.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10477123]No cytotoxicity information found Not found 10477123 Peptides. 1999;20(6):679-686. Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. DRAMP01260 ALWKNMLKGIGKLAGQAALGAVKTLVGAES 30 Dermadistinctin-Q1 (DD Q1; Frogs, amphibians, animals) P83641 Not found Not found Phyllomedusa distincta (Monkey frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus (MIC=2.7 µM), Enterococcus faecalis (MIC=22 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=5.4 µM), Escherichia coli (MIC=1.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10477123]No cytotoxicity information found Not found 10477123 Peptides. 1999;20(6):679-686. Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. DRAMP01261 GLWSKIKEAAKTAGLMAMGFVNDMV 25 Dermadistinctin-Q2 (DD Q2; Frogs, amphibians, animals) P83642 Not found Not found Phyllomedusa distincta (Monkey frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus (MIC=22 µM), Enterococcus faecalis (MIC=11 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=22 µM), Escherichia coli (MIC=5.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10477123]To produce hemolysis more than 38 μM peptide concentrations was required. Not found 10477123 Peptides. 1999;20(6):679-686. Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. DRAMP01288 FLSLIPHIVSGVASIAKHF 19 Phylloseptin-1 (PSN-1; Frogs, amphibians, animals) E3PQH3 Not found PSN-1 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found Function: PSN-1 displayed broad-spectrum activity against a range of planktonic organisms. S. aureus (MIC=5 µM), Escherichia coli and Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.20451254]No cytotoxicity information found Not found 20451254 Mol Immunol. 2010 Jul;47(11-12):2030-2037. Zhang R, Zhou M, Wang L, McGrath S, Chen T, Chen X, Shaw C. Phylloseptin-1 (PSN-1) from Phyllomedusa sauvagei skin secretion: a novel broad-spectrum antimicrobial peptide with antibiofilm activity. DRAMP01301 FLSLIPHAINAVSAIAKHN 19 Phylloseptin-1 (PS-1; Frogs, amphibians, animals) P84566 Not found psn1 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix (1 helices; 14 residues) The antimicrobial phylloseptin peptides adopt alpha-helical conformations in membrane environments which are stabilized by electrostatic interactions of the helix dipole as well as other contributions such hydrophobic and capping interactions.(Ref.2) 2JQ0 resolved by NMR. "Function: Atomic force microscopy experiments indicated that the bacteriolytic properties of these peptides might be related to their disruptive action on the cell membrane. PS-1 did not exhibit significant hemolytic activity on human erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.15752569]Gram-positive bacteria: Staphylococcus aureus (MIC=7.9 µM), Enterococcus faecalis (MIC=4.0 µM);##Gram-negative bacteria: Escherichia coli (MIC=7.9 µM), Psecdomonas aeruginosa (MIC=4 µM), Psecdomonas aeruginosa wt (MIC=3 µM). [Ref:15752569]0.3% hemolytic activity at 4 μM, 0.57% hemolytic activity at 8 μM, 0.6% hemolytic activity at 16 μM, 0.98% hemolytic activity at 32 μM, 1.98% hemolytic activity at 64 μM against human red blood cells Linear Free Amidation Free L [REf.15752569]No cytotoxicity information found##[Ref.18656510]No cytotoxicity information found Cell membrane 15752569##18656510 Peptides. 2005 Apr;26(4):565-573.##Peptides. 2008 Oct;29(10):1633-1644. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr.##Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim NC, Valente AP, Bemquerer MP, Piló-Veloso D, Bechinger B. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus.##Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations. DRAMP01302 FLSLIPHAINAVSTLVHHF 19 Phylloseptin-2 (PS-2; Frogs, amphibians, animals) P85881, P84567, Q0VZ43 Not found psn2 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 14 residues) The antimicrobial phylloseptin peptides adopt alpha-helical conformations in membrane environments which are stabilized by electrostatic interactions of the helix dipole as well as other contributions such hydrophobic and capping interactions.(Ref.2) 2JPY resolved by NMR. "Function: Has antimicrobial activity. PS-2 did not exhibit significant hemolytic activity on human erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.18656510][ATCC Strains]: Gram-positive bacteria: S. aureus (MIC=15.1 µM);##Gram-negative bacteria: Escherichia coli (MIC=60.4 µM), Klebsiella pneumoniae (MIC=60.4 µM), Pseudomonas aeruginosa (MIC=60.4 µM);##[Wild Type]: Gram-positive bacteria: S. aureus (MIC=7.6 µM), S. agalactiae (MIC=1.9 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=60.4 µM), A. calcoaceticus (MIC=3.7 µM);##Fungi: Candida albicans (MIC=15.1 µM). [Ref:15752569]0.1% hemolytic activity at 4 μM, 0.28% hemolytic activity at 4 μM, 0.7% hemolytic activity at 8 μM, 0.8% hemolytic activity at 16 μM, 1.05% hemolytic activity at 32 μM, 2.05% hemolytic activity at 64 μM against human red blood cells Linear Free Amidation Free L [REf.15752569]No cytotoxicity information found##[Ref.18656510]No cytotoxicity information found Cell membrane 15752569##18656510 Peptides. 2005 Apr;26(4):565-573.##Peptides. 2008 Oct;29(10):1633-1644. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr.##Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim NC, Valente AP, Bemquerer MP, Piló-Veloso D, Bechinger B. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus.##Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations. DRAMP01303 FLSLIPHAINAVSALANHG 19 Phylloseptin-3 (PS-3; Frogs, amphibians, animals) P84568 Not found psn3 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 11 residues) The antimicrobial phylloseptin peptides adopt alpha-helical conformations in membrane environments which are stabilized by electrostatic interactions of the helix dipole as well as other contributions such hydrophobic and capping interactions.(Ref.2) 2JQ1 resolved by NMR. "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [ATCC Strains]: Gram-positive bacteria: S. aureus (MIC=32.9 µM);##Gram-negative bacteria: Escherichia coli (MIC=65.6 µM), Klebsiella pneumoniae (MIC=65.6 µM), Pseudomonas aeruginosa (MIC=65.6 µM). NOTE: Initial inoculum of 108 cells/Ml.##[Wild Type]: Gram-positive bacteria: S. aureus (MIC=8.2 µM), S. agalactiae (MIC=4.1 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=32.8 µM), A. calcoaceticus (MIC=4.1 µM).##Fungi: Candida albicans (MIC=8.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15752569]No cytotoxicity information found##[Ref.18656510]No cytotoxicity information found Cell membrane 15752569##18656510 Peptides. 2005 Apr;26(4):565-573.##Peptides. 2008 Oct;29(10):1633-1644. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr.##Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim NC, Valente AP, Bemquerer MP, Piló-Veloso D, Bechinger B. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus.##Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations. DRAMP01305 FLSLIPHAINAVSAIAKHFG 20 Phylloseptin-7 (PS-7; Frogs, amphibians, animals) P84572, Q0VZ42 Not found psn7 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-negative bacteria E. coli and P. aeruginosa, and the Gram-positive bacteria: S. aureus. No hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.16963159]Gram-negative bacteria: Escherichia coli (MIC=6 µM), Pseudomonas aeruginosa (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM) [Ref:16963159]Non-hemolytic activity at 6 μM against human erythrocytes Linear Free Amidation Free L [Ref.16713656]No cytotoxicity information found Not found 16963159##16713656 Peptides. 2006 Dec;27(12):3092-3999.##Peptides. 2006 Sep;27(9):2129-2136. Conceição K, Konno K, Richardson M, Antoniazzi MM, Jared C, Daffre S, Camargo AC, Pimenta DC.##Chen T, Zhou M, Gagliardo R, Walker B, Shaw C. Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis.##Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. DRAMP01306 FLSLIPHAINAVSAIAKHF 19 Phylloseptin-7 (PS-7; Frogs, amphibians, animals) P85882 Not found Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity but does not inhibit the growth of the fungus C. albicans. Tissue specificity: Expressed by the skin glands. PTM: Phenylalanine amide at F19." Gram-negative bacterium: Escherichia coli ATCC 11775 (MIC=7.2 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 12600 (MIC=3.6 µM), Micrococcus luteus ATCC 49732 (MIC=1.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16963159]No cytotoxicity information found##[Ref.17553595]No cytotoxicity information found Not found 17553595##16963159 Peptides. 2007 Jul;28(7):1331-1343.##Peptides. 2006 Dec;27(12):3092-3099. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S.##Conceição K, Konno K, Richardson M, Antoniazzi MM, Jared C, Daffre S, Camargo AC, Pimenta DC. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea.##Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis. DRAMP01314 FLSLLPSIVSGAVSLAKKLG 20 Phylloseptin 12 (PS-12; Frogs, amphibians, animals) Q17UY9 Not found psn-12 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium M. luteus. Does not inhibit the growth of the fungus C. albicans. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Gram-positive bacterium: Micrococcus luteus ATCC 49732 (MIC=1.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17553595]No cytotoxicity information found Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01319 RRSRRGRGGGRRGGSGGRGGRGGGGRSGAGSSIAGVGSRGGGGGRHYA 48 Cathelicidin-AL (Gly-rich; Frogs, amphibians, animals) No entry found Not found Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=6.25 µg/ml), Staphylococcus aureus ATCC43300 (MIC=6.25 µg/ml), Bacillus subtilis (MIC=100 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35P (MIC=25 µg/ml), Psecdomonas aeruginosa PA01 (MIC=12.5 µg/ml), Psecdomonas aeruginosa ATCC27853 (MIC=6.25 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.22009138]No cytotoxic against HUVEC or RMMCs at the concentration of 0.4 mg/ml. Not found 22009138 Amino Acids. 2012 Aug;43(2):677-685. Hao X, Yang H, Wei L, Yang S, Zhu W, Ma D, Yu H, Lai R. Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate. DRAMP01320 AAFRGCWTKNYSPKPCL 17 Ranacyclin-B-AL1 (Frogs, amphibians, animals) No entry found Not found Not found Amolops loloensis (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Has antibacterial activity. Gram-positive bacteria: Staphylococcus aureus (MIC=51 µM), Bacillus subtilis (MIC=26 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP01339 FLPIVGKLLSGLSGLL 16 Amolopin-2a (Frogs, amphibians, animals) No entry found Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus (MIC=2.00 µg/ml), Bacillus dysenteriae (MIC=1.50 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=3.00 µg/ml).##Candida albicans (MIC=6.50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17000029]Display cytotoxicity against HepG2(IC50=77 mg/ml). Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01341 FLPLAVSLAANFLPKLFCKITKKC 24 Amolopin-1b (Frogs, amphibians, animals) A0SN42 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus (MIC=5.50 µg/ml), Bacillus dysenteriae (MIC=2.20 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=6.50 µg/ml).##Yeast: Candida albicans (MIC=7.50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys18 and Cys24) Disulfide bridge between Cys18 and Cys24. L [Ref.17000029]Display cytotoxicity against HepG2(IC50=58 mg/ml). Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01346 VIGSILGALASGLPTLISWIKNR 23 Prepromelittin-related peptide (Frogs, amphibians, animals) A7BJK5 Not found prMRP Rana sakuraii (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM).##Yeast: Candida albicans (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17174009]No cytotoxicity information found##[Ref.17826868]No cytotoxicity information found Not found 17174009##17826868 Peptides. 2007;28(3):505-514.##Peptides. 2007 Oct;28(10):2061-2068. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM.##Suzuki H, Conlon JM, Iwamuro S. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii.##Evidence that the genes encoding the melittin-related peptides in the skins of the Japanese frogs Rana sakuraii and Rana tagoi are not orthologous to bee venom melittin genes: developmental- and tissue-dependent gene expression. DRAMP01347 AIGSILGALAKGLPTLISWIKNR 23 Prepromelittin-related peptide (Frogs, amphibians, animals) A7BJK6 Not found prMRP Rana tagoi (Tago frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Alpha helix Not found 6dst resolved by NMR (related PDB_ID) Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against C. albicans. [Ref.12804591]Gram-positive bacterium: Staphylococcus aureus (MIC=3.5 µM);##Gram-negative bacterium: Escherichia coli (MIC=20 µM).##Yeast: Candida albicans (MIC=19 µM).##EL4 T-lymphoma cells (MIC=14 µM).##[Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=6.25 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli (MIC=25 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=12.5 μM) [Ref.27271216] 100% hemolysis at 20 μM against human red blood cells Linear Free Amidation Free L [Ref.12804591]Display cytotoxic against L929 fibroblasts(LC50=20 μM);EL4 T-lymphoma cells(LC50=14 μM).##[Ref.27271216]L929 cells:Cell viability is approximately 10% at the concentration of 6.25 μM. Not found 12804591##17174009##27271216 Biochem Biophys Res Commun. 2003 Jun 27;306(2):496-500.##Peptides. 2007;28(3):505-514.##Sci Rep. 2016 Jun 8;6:27394. Conlon JM, Sonnevend A, Patel M, Camasamudram V, Nowotny N, Zilahi E, Iwamuro S, Nielsen PF, Pál T##Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM.##Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties##Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii##Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP01350 FCTMIPIPRCY 11 Tigerinin-1 (Frogs, amphibians, animals) P82651 Not found Not found Rana tigerina (Indian bull frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Bacillus subtilis (MIC=30 µg/ml), Staphylococcus aureus ATCC 8530 (MIC=30 µg/ml), Micrococcus luteus MT 166 (MIC=20 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=40 µg/ml), Pseudomonas putida NCIM 2102 (MIC=40 µg/ml).##Fungi: Saccharomyces cerevisiae ATCC 8530 (MIC=80 µg/ml). [Ref.11031261] It exhibits no hemolytic activity up to a concentration of 200 μg/ml against rat erythrocytes. Cyclic Free Amidation Disulfide bond between Cys2 and Cys10. L No cytotoxicity information found Cell membrane 11031261 J Biol Chem. 2001 Jan 26;276(4):2701-2707. Sai KP, Jagannadham MV, Vairamani M, Raju NP, Devi AS, Nagaraj R, Sitaram N. Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina. DRAMP01351 RVCFAIPLPICH 12 Tigerinin-2 (Frogs, amphibians, animals) P82652 Not found Not found Rana tigerina (Indian bull frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Bacillus subtilis (MIC=20 µg/ml), Staphylococcus aureus ATCC 8530 (MIC=40 µg/ml), Micrococcus luteus MT 166 (MIC=20 µg/ml).##Gram-negative bacteria: Pseudomonas putida NCIM 2102 (MIC=50 µg/ml), Escherichia coli (MIC=50 µg/ml).##Fungi: Saccharomyces cerevisiae ATCC 8530 (MIC=100 µg/ml). [Ref.11031261] It exhibits no hemolytic activity up to a concentration of 200 μg/ml against rat erythrocytes. Cyclic Free Amidation Disulfide bond between Cys3 and Cys11. L No cytotoxicity information found Cell membrane 11031261 J Biol Chem. 2001 Jan 26;276(4):2701-2707. Sai KP, Jagannadham MV, Vairamani M, Raju NP, Devi AS, Nagaraj R, Sitaram N. Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina. DRAMP01352 RVCYAIPLPICY 12 Tigerinin-3 (Frogs, amphibians, animals) P82653 Not found Not found Rana tigerina (Indian bull frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Bacillus subtilis (MIC=30 µg/ml), Staphylococcus aureus ATCC 8530 (MIC=30 µg/ml), Micrococcus luteus MT 166 (MIC=30 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=40 µg/ml), Pseudomonas putida NCIM 2102 (MIC=40 µg/ml).##Fungi: Saccharomyces cerevisiae ATCC 8530 (MIC=80 µg/ml). [Ref.11031261] It exhibits no hemolytic activity up to a concentration of 200 μg/ml against rat erythrocytes. Cyclic Free Amidation Disulfide bond between Cys3 and Cys11. L No cytotoxicity information found Cell membrane 11031261 J Biol Chem. 2001 Jan 26;276(4):2701-2707. Sai KP, Jagannadham MV, Vairamani M, Raju NP, Devi AS, Nagaraj R, Sitaram N. Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina. DRAMP01353 RVCYAIPLPIC 11 Tigerinin-4 (Frogs, amphibians, animals) P82654 Not found Not found Rana tigerina (Indian bull frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand-turn Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacterium: Staphylococcus aureus ATCC 8530 (MIC=50 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=60 µg/ml), Pseudomonas putida NCIM 2102 (MIC=60 µg/ml).##Fungi: Saccharomyces cerevisiae ATCC 8530 (MIC=100 µg/ml). [Ref.11031261] It exhibits no hemolytic activity up to a concentration of 200 μg/ml against rat erythrocytes. Cyclic Free Amidation;Cyclization (Cys3 and Cys11) Disulfide bond between Cys3 and Cys11. L No cytotoxicity information found Cell membrane 11031261 J Biol Chem. 2001 Jan 26;276(4):2701-2707. Sai KP, Jagannadham MV, Vairamani M, Raju NP, Devi AS, Nagaraj R, Sitaram N. Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina. DRAMP01354 LVRGCWTKSYPPKPCFVR 18 Peptide leucine arginine (pLR; Frogs, amphibians, animals) Q90WP7, P82110 Not found Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Mast cell degranulating peptide. Antiproliferative activity against human breast and ovarian tumor cell lines in vitro. Inhibits granulopoiesis in rat in vitro. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against Gram-positive bacteria: B.megaterium Bm11, S. lentus and M.luteus, and antifungal activity against C.tropicalis, C.guiller-mondii and P.nicotianae spores. Has hemolytic activity. The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores. [Ref.11099505]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=20 µM), Staphylococcus lentus (MIC=50 µM), Micrococcus luteus (MIC=10 µM);##Fungi: Candida tropicalis (MIC=11 µM), Candida guillermondii (MIC=6.6 µM), Phytophthora nicotianae spores (MIC=75 µM). [Ref:11099505] It has 2.5% hemolytic activity at 100 μM against human red blood Cyclic Free Free Disulfide bond between Cys5 and Cys15. L No cytotoxicity information found Not found 11099505 J. Biol. Chem. 2001;276:10145-10152. Salmon A.L, Cross L.J.M, Irvine A.E, Lappin T.R.J, Dathe M, Krause G, Canning P, Thim L, Beyermann M, Rothemund S, Bienert M, Shaw C. Peptide leucine arginine, a potent immunomodulatory peptide, isolated and structurally characterized from the skin of the Northern Leopard frog, Rana pipiens. DRAMP01355 FLGGLIKIVPAMICAVTKKC 20 Ranalexin (Frogs, amphibians, animals) P39084 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Potent microbicidal activity, active against S.aureus and E.coli. It acts as well as a membrane-disruptive agent at higher concentrations. Tissue specificity: Expressed by the skin dorsal glands. Developmental stage: Expression starts at metamorphosis and continues into adulthood. PTM: Contains one disulfide bond 14-20." Gram-positive bacterium: Staphylococcus aureus (MIC=4 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=32 µg/ml), Pseudomonas aeruginosa (MIC=128 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 8144672##9578480 J Biol Chem. 1994 Apr 8;269(14):10849-10855.##Eur J Biochem. 1998 Apr 1;253(1):221-228. Clark DP, Durell S, Maloy WL, Zasloff M.##Vignal E, Chavanieu A, Roch P, Chiche L, Grassy G, Calas B, Aumelas A. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin.##Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles. DRAMP03024 LKLKSIVSWAKKVL 14 Mastoparan B (MP-B; insects, arthropods, invertebrates, animals) P21654 Not found Not found Vespa basalis (Hornet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti Mammalian cells, Anti-cancer Not found Alpha helix Tryptophan residue in MP Function: Mast cell degranulating peptide. Activates G proteins that couple to phospholipase C. Has hemolytic activity. [Ref.10667861] Gram-positive bacteria: Staphylococcus epidermidis ATTC 12228 (MIC=25 µM), Bacillus subtilis PCI 219 (MIC=25 µM), Enterococcus faecium EFMY-28 (MIC=12.5 µM);##Gram-negative bacterium: Escherichia coli NIHJ JC-2 (MIC=50 µM) [Ref.10667861] 68.2% hemolysis at the peptide concentration of 100 µM is , 27.9% Hemolysis at 50 µM against human red blood cells. Linear Free Amidation Free L [Ref.10667861]No cytotoxicity information found##[Ref.8555423]No cytotoxicity information found Not found 10667861##8555423 J Pept Res. 2000 Jan;55(1):51-62.##Biopolymers. 1995 Dec;36(6):793-801 Yu K, Kang S, Park N, Shin J, Kim Y.##Park NG, Yamato Y, Lee S, Sugihara G1995 Relationship between the tertiary structures of mastoparan B and its analogs and their lytic activities studied by NMR spectroscopy.##Interaction of mastoparan-B from venom of a hornet in Taiwan with phospholipid bilayers and its antimicrobial activity DRAMP01358 FLGGLFKLVPSVICAVTKKC 20 Ranalexin-Vb (Frogs, amphibians, animals) No entry found Not found Not found Rana virgatipes (Ranidae) (Aquarana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 15996769 Regul Pept 2005; 131: 38-45. Conlon JM et al Bevier CR. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). DRAMP01359 FLGGLMKIIPAAFCAVTKKC 20 Ranalexin-1G (Frogs, amphibians, animals) No entry found Not found Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found Function: Has growth-inhibitory activity against the gram-positive bacterium Staphylococcus aureus, the gram-negative bacterium Escherichia coli and the yeast, Candida albicans. Gram-negative bacterium: Escherichia coli (MIC=9 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=18 µM).##Yeast: Candida albicans (MIC=70 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01360 GLLDALSGILGL 12 Frenatin-1 (Frogs, amphibians, animals) P82021 Not found Not found Litoria infrafrenata (Giant tree frog) (White-lipped tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." Gram-positive bacteria: Micrococcus luteus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.9225251]No cytotoxicity information found Not found 9225251 J Pept Sci. 1996 Mar-Apr;2(2):117-124. Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata. DRAMP01361 GLLGTLGNLLNGLGL 15 Frenatin-2 (Frogs, amphibians, animals) P82022 Not found Not found Litoria infrafrenata (Giant tree frog) (White-lipped tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." Gram-positive bacteria: Micrococcus luteus (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.9225251]No cytotoxicity information found Not found 9225251 J Pept Sci. 1996 Mar-Apr;2(2):117-124. Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata. DRAMP01362 GLMSVLGHAVGNVLGGLFKS 20 Frenatin-3 (Frogs, amphibians, animals) P56249 Not found Not found Litoria infrafrenata (Giant tree frog) (White-lipped tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." Gram-negative bacterium: Escherichia coli (MIC=50 µg/ml);##Gram-positive bacteria: Leuconostoc mesenteroides (MIC=25 µg/ml), Bacillus cereus (MIC=12.5 µg/ml), Micrococcus luteus (MIC=1.5 µg/ml), Pastewella haemolytica (MIC=0.8 µg/ml), Streptococcus uberis (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.9225251]No cytotoxicity information found Not found 9225251 J Pept Sci. 1996 Mar-Apr;2(2):117-124. Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata. DRAMP01364 GLFGVLAKVAAHVVPAIAEHF 21 Maculatin-1.1 (Frogs, amphibians, animals) P82066 Not found Not found Litoria genimaculata (Green-eyed tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Alpha helix Not found "Function: Maculatin-1.1 shows significant antibacterial activity against Gram-positive bacteria, less against Gram-negative bacteria. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Bacillus cereus (MIC=3 µg/ml), Listeria innocua (MIC=100 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=6 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=3 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=50 µg/ml). ##[Ref.16140737]Virus:HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=11.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L No cytotoxicity information found in the reference(s) presented Not found 16140737##9620615##15203252 J Virol. 2005 Sep;79(18):11598-606. ##J Pept Sci. 1998 Apr;4(2):111-115.##Peptides. 2004; 25: 1035-1054. VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D. ##Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.##The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01367 GLLGLLGSVVSHVLPAITQHL 21 Maculatin-1.4 (frog, amphibia, animals) No entry found Not found Not found Litoria eucnemis (Australian anurans) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found "Function: Shows antibacterial activity against the Gram-positive bacteria. PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Bacillus cereus (MIC=6 µg/ml), Listeria innocua (MIC=100 µg/ml), Micrococcus luteus (MIC=50 µg/ml), Staphylococcus aureus (MIC=50 µg/ml), Staphylococcus epidermidis (MIC=50 µg/ml), Streptococcus uberis (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252 Peptides. 2004 Jun; 25: 1035-1054. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01368 GFVDFLKKVAGTIANVVT 18 Maculatin-2.1 (Frogs, amphibians, animals) P82068 Not found Not found Litoria genimaculata (brown-spotted treefrog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows antibacterial activity against the Gram-positive bacteria. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Micrococcus luteus (MIC=100 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermidis (MIC=50 µg/ml), Streptococcus uberis (MIC=25 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found##[Ref.9620615]No cytotoxicity information found Not found 9620615##15203252 J Pept Sci. 1998 Apr;4(2):111-115.##Peptides. 2004; 25: 1035-1054. Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01370 MLCKLSMFGAVLGVPACAIDCLPMGKTGGSCEGGVCGCRKLTFKILWDKKFG 52 Oh-defensin (O. hainana defensin; spiders, animals) No entry found Not found Not found Ornithoctonus hainana (Venoms) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial and antifungal activities. Gram-positive bacteria: Staphylococcus aureus (MIC=1.25 µg/ml), Bacillus cereus (MIC=25 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=1.25 µg/ml), Bacillus dysenteriae (MIC=1.25 µg/ml), Pseudomonas aeruginosa (MIC=5 µg/ml).##Yeast: Candida albicans (MIC=1.25 µg/ml). [Ref.21538709] It has little hemolytic activity, inducing 7% hemolysis at the concentration up to 200 µg/ml (about 36 µM). Cyclic Free Free Has three disulfide bonds L No cytotoxicity information found Not found 21538709 J Pept Sci. 2011 Jul;17(7):540-544. Zhao H, Kong Y, Wang H, Yan T, Feng F, Bian J, Yang Y, Yu H. A defensin-like antimicrobial peptide from the venoms of spider, Ornithoctonus hainana. DRAMP01371 GLLSGILGAGKHIVCGLTGCAKA 23 Odorranain-NR (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Combine helix and strand structure Odorranain-NR has a large proportion of beta-sheet. In Tris HCl + SDS, odorranain-NR has a major conformation of beta-sheet (79.2%) and a minor conformation of beta-turn (1.3%). In Tris HCl, the beta-sheet has been decreased to 57.1% and the beta-turn has been increased to 10.5%. The beta-sheet has been decreased to 39.8% in water. "Function: Odorranain-NR exhibits antimicrobial activity against the tested strains except E. coli ATCC25922. Odorranain-NR has little hemolytic activity on red blood cells even with peptide concentration up to 100 mg/ml. PTM: Odorranain-NR has an intramolecular disulfide-bridged hexapeptide segment, which is a new type of disulfide-bridge motif in amphibian antimicrobial peptides." [Ref.18282640]Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=9.375 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>100 µg/ml), Bacillus dysenteriae (MIC=37.5 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=18.75 µg/ml). [Ref:18282640] It has little hemolytic activity at 100 μg/ml against rabbit red blood cells Cyclic Free Free Disulfide bond between Cys15 and Cys20. L No cytotoxicity information found Not found 18282640 Peptides. 2008 Apr;29(4):529-535. Che Q et al Lai R. A novel antimicrobial peptide from amphibian skin secretions of Odorrana grahami. DRAMP00931 TCSYTMEA 8 Antimicrobial peptide 3 (Cn-AMP3; Plant defensin) P86707 Not found Not found Cocos nucifera (Coconut palm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. Tissue specificity: Found in the liquid endosperm contained in green fruit of coconut palms, also known as coconut water (at protein level). Subunit structure: Monomer." [Ref.19111587] Gram-positive bacteria: Bacillus subtilis (MIC=257 μg/ml) and Staphylococcus aureus (MIC=274 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=302 μg/ml) and Pseudomonas aeruginosa (MIC=259 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.19111587]No cytotoxicity information found Not found 19111587 Peptides. 2009 Apr;30(4):633-637. Mandal SM, Dey S, Mandal M, Sarkar S, Maria-Neto S, Franco OL. Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water. DRAMP00930 TESYFVFSVGM 11 Antimicrobial peptide 2 (Cn-AMP2; Plant defensin) P86706 Not found Not found Cocos nucifera (Coconut palm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. Tissue specificity: Found in the liquid endosperm contained in green fruit of coconut palms, also known as coconut water (at protein level). Subunit structure: Monomer." [Ref.19111587] Gram-positive bacteria: Bacillus subtilis (MIC=150 μg/ml), Staphylococcus aureus (MIC=170 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=170 μg/ml), Pseudomonas aeruginosa (MIC=169 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.19111587]No cytotoxicity information found Not found 19111587 Peptides. 2009 Apr;30(4):633-637. Mandal SM, Dey S, Mandal M, Sarkar S, Maria-Neto S, Franco OL. Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water. DRAMP00929 SVAGRAQGM 9 Antimicrobial peptide 1 (Cn-AMP1; Plant defensin) P86705 Not found Not found Cocos nucifera (Coconut palm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Helix Not found 2N0V resolved by NMR. "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. Tissue specificity: Found in the liquid endosperm contained in green fruit of coconut palms, also known as coconut water (at protein level). Subunit structure: Monomer." [Ref.19111587] Gram-positive bacteria: Bacillus subtilis (MIC=76 μg/ml), Staphylococcus aureus (MIC=80 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=82 μg/ml), Pseudomonas aeruginosa (MIC=79 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.19111587]No cytotoxicity information found Not found 19111587 Peptides. 2009 Apr;30(4):633-637. Mandal SM, Dey S, Mandal M, Sarkar S, Maria-Neto S, Franco OL. Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water. DRAMP03542 HKTDSFVGLM 10 Neurokinin A (NKA; chicken, animals) P19851 Belongs to the tachykinin family. Not found Gallus gallus (Chicken) Antimicrobial, Antibacterial, Neuropeptide, Anti-Gram+, Anti-Gram- Protein level Not found Not found 1N6T resolved by NMR. "Function: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Antibacterial activity is very low. PTM: Methionine amide at position 10." [Ref.18603306] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>500 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC>500 μg/ml) ;## Gram-positive bacteria: Streptococcus mutans NCTC 10449 (MIC> 500 μg/ml), Lactobacillus acidophilus NCTC 1723 (MIC>500 μg/ml), Enterococcus faecalis NCTC 12697 (MIC>500 μg/ml), Staphylococcus aureus ATCC 25923 (MIC>500 μg/ml);## Yeast: Candida albicans NCTC 3179 (MIC>500 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.18603306]No cytotoxicity information found Not found 18603306 J Neuroimmunol. 2008 Aug 30;200(1-2):11-16. El Karim IA, Linden GJ, Orr DF, Lundy FT. Antimicrobial activity of neuropeptides against a range of micro-organisms from skin, oral, respiratory and gastrointestinal tract sites. DRAMP03310 FLPLILRKIVTAL 13 Crabrolin (Insects, animals) P01518 Not found Not found Vespa crabro (European hornet) Antimicrobial, Antibacterial, Anti Mammalian cells Protein level Helix Not found Function: Mast cell degranulating peptide. Induces the chemotaxis of neutrophils. Has antimicrobial and hemolytic activity. No MICs found in DRAMP database [Ref.6206053] Hemolysis is 20% of total at 10µg/ml against guinea pig red blood cell. Linear Free Amidation Free L [Ref.9273892]No cytotoxicity information found##[Ref.6206053]No cytotoxicity information found Not found 9273892##6206053 J Pept Res. 1997 Aug;50(2):88-93.##J Biol Chem. 1984 Aug 25;259(16):10106-10111. Krishnakumari V, Nagaraj R.##Argiolas A, Pisano JJ. Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogs.##Isolation and characterization of two new peptides, mastoparan C and crabrolin, from the venom of the European hornet, Vespa crabro. DRAMP02344 KVHGSLARAGK 11 40S ribosomal protein S30 (Fish, chordates, animals) P83328 Belongs to the eukaryotic ribosomal protein eS30 family. fau Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against Gram-positive bacteria and low activity against Gram-negative bacteria. [Ref.12147245] Gram-negetive bacteria: Escherichia coli (EC50>0.3 μM, MBC>0.3 μM), Listonella anguillarum (EC50>0.3 μM, MBC>0.3 μM) ;##Gram-positive bacteria: Bacillus subtilis (EC50=0.15–0.3 μM, MBC>0.3 μM), Planococcus citreus (EC50=0.02–0.04 μM, MBC=0.08 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.12147245]No cytotoxicity information found Not found 12147245 Biochem Biophys Res Commun. 2002 Aug 9;296(1):167-171. Fernandes JM, Smith VJ. A novel antimicrobial function for a ribosomal peptide from rainbow trout skin. DRAMP02993 YVPLPNVPQPGRRPFPTFPGQGPFNPKIKWPQGY 34 Abaecin (Pro-rich; insects, arthropods, invertebrates, animals) P15450? Not found Not found Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Rich The prolines are in repeated motifs. Function: This peptide has bactericidal activity. [Ref.2298215] Gram-negative bacteria: Agrobacterium tumefaciens Gembloux A (MIC=25-50 µg/ml), Erwinia salicis NCPPB 2530 (MIC=25-50 µg/ml), Escherichia coli NCTC 9001 (MIC=25-50 µg/ml), Escherichia coli K514 (MIC=10-25 µg/ml), Pseudomonas syringae pv.tomato NCPPB 1105 (MIC=25-50 µg/ml), Xanthomonas campestris pv. vesicatoria LMG 905 (MIC=5-10 µg/ml);##Gram-positive bacteria: Bacillus megateriurn QMB 1551 (MIC=10-25 µg/ml), Micrococcus lysodeikticus LMG 4050 (MIC=10-25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.2298215]No cytotoxicity information found##[Ref.7961803]No cytotoxicity information found Not found 2298215##7961803 Eur J Biochem. 1990 Jan 26;187(2):381-386.##J Biol Chem. 1994 Nov 18;269(46):28569-28575. Casteels P, Ampe C, Riviere L, Van Damme J, Elicone C, Fleming M, Jacobs F, Tempst P.##Casteels-Josson K, Zhang W, Capaci T, Casteels P, Tempst P. Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera).##Acute Transcriptional Response of the Honeybee Peptide-Antibiotics Gene Repertoire and Required Post-translational Conversion of the Precursor Structures. DRAMP02997 GNNRPVYIPQPRPPHPRL 18 Apidaecin-1B (Apidaecin IB; Insects, animals) P35581, Q06602, Q06601, Q8WSY8 Belongs to the apidaecin family Not found Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 4E81 resolved by X-ray. Function: Apidaecins have bactericidal activity; predominantly against Gram-negative bacteria. They seem to interfere with cell propagation. [Ref.2676519] Gram-negative bacteria: Agrobacterium tumefaciens (MIC=0.2 μg/ml), Erwinia salicis (MIC=0.02 μg/ml), Escherichia coli (MIC=0.1 μg/ml), Pseudomonas syringae (MIC=0.1 μg/ml), Rhizobium meliloti (MIC=0.02 μg/ml), Salmonella Newport (MIC=0.2 μg/ml), Salmonella typhimurium (MIC=0.1 μg/ml), Shigella flexneri (MIC=0.1 μg/ml);##Gram-positive bacteria: Corynebacterium insidiosum (MIC=50 μg/ml), Bacillus megaterium (MIC=100 μg/ml).##[Ref.2298215] Gram-negative bacteria: Agrobacterium tumefaciens Gembloux A (MIC≤1 µg/ml), Erwinia salicis NCPPB 2530 (MIC≤1 µg/ml), Escherichia coli NCTC 9001 (MIC≤1 µg/ml), Escherichia coli K514 (MIC=25-50 µg/ml), Pseudomonas syringae pv.tomato NCPPB 1105 (MIC≤1 µg/ml), Xanthomonas campestris pv. vesicatoria LMG 905 (MIC≥100 µg/ml);##Gram-positive bacteria: Bacillus megateriurn QMB 1551 (MIC=25-50 µg/ml), Bacillus alvei LMG 6922 (MIC=50-100 µg/ml),Micrococcus lysodeikticus LMG 4050 (MIC=25-50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.2298215]No cytotoxicity information found##[Ref.2676519]No cytotoxicity information found Not found 2676519##2298215 EMBO J. 1989 Aug;8(8):2387-2391.##Eur J Biochem. 1990 Jan 26;187(2):381-386. Casteels P, Ampe C, Jacobs F, Vaeck M, Tempst P.##Casteels P, Ampe C, Riviere L, Van Damme J, Elicone C, Fleming M, Jacobs F, Tempst P. Apidaecins: antibacterial peptides from honeybees.##Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). DRAMP18322 ITPATPFTPAIITEITAAVIA 21 Hominicin (Bacteriocin) No entry found Not found Not found Staphylococcus hominis MBBL 2-9 Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found NMR played a critical role in establishing the peptide primary structure. While the N-terminal residue is an N,N-dimethyl Ile (DmIle), the C-terminus is a N2, N2-dimethyl-1,2-propanediamine (Dmp). In addition, threonines are dehydrated into Dhb. In this sense, this peptide may be classified as a class I variant bacteriocin. Function: Hominicin exhibited heat stability up to 121 degrees C for 15min and activity under both acidic and basic conditions (from pH 2.0 to 10.0). Hominicin exhibited distinct structural and attractive biochemical characteristics with a high bactericidal activity against MRSA and VISA, heat-tolerance and pH stability. [Ref.20654578] Gram-positive bacteria: Staphylococcus aureus (MIC=0.06 µg/ml), MRSA (MIC=0.96 µg/ml), VISA (MIC=3.82 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free 1-DmIle(N,N-dimethyl Ile)-I; 2,5,8,15-DHB(dehydrated threonine)-T;21-Dmp(N2, N2-dimethyl-1,2-propanediamine)-A L [Ref.20654578]No cytotoxicity information found Not found 20654578 Biochem Biophys Res Commun. 2010 Aug 20;399(2):133-138. Kim PI, Sohng JK, Sung C, Joo HS, Kim EM, Yamaguchi T, Park D, Kim BG. Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2-9. DRAMP02840 FKCRRWQWRMKKLGAPSITCVRRAF 25 Lactoferricin B (Lfcin B; mammals, animals) P24627, E6YCQ7, B3VTM3, B9VPZ5, C7FE01, Q6LBN7, Q19KS1 Belongs to the transferrin family LTF Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand (4 strands; 8 residues) Residues 7-9 form beta1 and residues 17-19 form beta2 (in membrane). This contrasts with X-ray structure where residues 1-13 is helical. Thus, this peptide appears to be able to adopt a different conformation depending on environmental conditions. disulfide bond is not required for the antimicrobial potency. 1LFC resolved by NMR. "Function: Lactoferricin B function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. Activity regulation: Inhibited by PMSF and Pefabloc. PTM: Contains one disulfide bond 3-20" [Ref.8980754] Gram-negative bacteria: Escherichia coli L361 (MIC=4 µM or 12.5 µg/ml), Salmonella Salford (MIC=4 µM or 12.5 µg/ml), Escherichia coli O:9 (MIC=6 µM or 18.8 µg/ml), Pseudomonas fluorescens (MIC=10 µM or 31.3 µg/ml) ;##Gram-positive bacteria: Listeria monocytogenes (MIC=2 µM or 6.3 µg/ml), Staphylococcus aureus (MIC=6 µM or 18.8 µg/ml), Bacillus cereus (MIC=6 µM or 18.8 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys3 and Cys20. L No cytotoxicity information found Not found 8980754##9521752##1490908 "Antimicrob Agents Chemother. 1997 Jan;41(1):54-59. ##Biochemistry. 1998 Mar 24;37(12):4288-4298.## J Appl Bacteriol. 1992 Dec;73(6):472-9." Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. ##Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ. ##Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M.1992 "Antibacterial activity in bovine lactoferrin-derived peptides. ##Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. ## Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. " DRAMP02244 GLFLDTLKGAAKDVAGKLLEGLKCKIAGCKP 31 Ranatuerin-2Ca (Ranatuerin 2Ca; Frogs, amphibians, animals) P82878 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide has defense response to Gram-positive bacterium, defense response to Gram-negative bacterium, male-specific defense response to bacterium, antibacterial humoral response, antibacterial humoral response, induced systemic resistance, antifungal innate immune response, antifungal humoral response, defense response to fungus (incompatible interaction) in GO analysis. Tissue specificity: Expressed by the skin glands. PTM: Disulfide bond at position 24 and 29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys24 and Cys29. L No cytotoxicity information found Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP01821 FLPFLASLLTKVL 13 Temporin-1Cc (Temporin 1Cc; Frogs, amphibians, animals) P82882 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against the Gram-positive bacterium Staphylococcus aureus. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10822101]No cytotoxicity information found Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP01819 FLPFLAKILTGVL 13 Temporin-1Ca (Temporin 1Ca; Frogs, amphibians, animals) P82880 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against the Gram-positive bacterium Staphylococcus aureus. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10822101]No cytotoxicity information found Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP01357 FLGGLMKAFPAIICAVTKKC 20 Ranalexin-1Cb (Ranatuerin 1Cb; Frogs, amphibians, animals) P82877 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide has defense response to Gram-positive bacterium, defense response to Gram-negative bacterium, male-specific defense response to bacterium, antibacterial humoral response, antibacterial humoral response, induced systemic resistance, antifungal innate immune response, antifungal humoral response, defense response to fungus (incompatible interaction) in GO analysis. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP02246 SMLSVLKNLGKVGLGLVACKINKQC 25 Ranatuerin-1C (Ranatuerin 1C; Frogs, amphibians, animals) P82875 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=55 μM);##Gram-negative bacterium: Escherichia coli (MIC=1.5 μM).##Yeast: Candida albicans (MIC=58 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys19 and Cys25) Disulfide bond between Cys19 and Cys25. L No cytotoxicity information found Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP01394 GLLRASSVWGRKYYVDLAGCAKA 23 Odorranain-W2 (Frogs, amphibians, animals) A7YL71 Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Shows antibacterial and antifungal activities. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µg/ml), Bacillus dysenteriae (MIC=30 µg/ml), Helicobacter pylori NCTC 11637 (MIC=20 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=5 µg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.17698252]No cytotoxicity information found Not found 17698252 Peptides. 2007 Aug;28(8):1527-1531. Chen L, Li Y, Li J, Xu X, Lai R, Zou Q. An antimicrobial peptide with antimicrobial activity against Helicobacter pylori. DRAMP01395 VVKCSYRLGSPDSQCN 16 Odorranain-A-OA1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=35.2 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=35.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=17.6 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=17.6 µg/ml). [Ref:22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Free Disulfide bond between Cys4 and Cys15. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01396 GFMDTAKNVAKNMAGNLLDNLKCKITKAC 29 Odorranain-F-OA1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=10 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=2.5 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=2.5 µg/ml). [Ref:22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01397 GFMDTAKNVAKNMAVTLLDNLKCKITKAC 29 Odorranain-F-OA2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=7.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=7.5 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3.8 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=3.8 µg/ml). [Ref:22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01398 GFMDTAKNVAKNEAGNLLDNLKCKITKAC 29 Odorranain-F-OA3 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=12.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.3 µg/ml)；##Yeast: Candida albicans ATCC 2002 (MIC=6.3 µg/ml). [Ref:22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01399 GFMATAKNVAKNMDVTLLDNLKCKITKAC 29 Odorranain-F-OA4 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=4.1 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=4.1 µg/ml)；##Yeast: Candida albicans ATCC 2002 (MIC=4.1 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP18395 FFGHLFRGIINVGKHIHGLLSG 22 moroPC-NH2 (moronecidin-like peptide; fish, animals) No entry found Not found Not found Parachaenichthys charcoti Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against Gram- E. cloacae ATCC 13047 (MIC 25 uM), S. sonnei (ATCC 29930) (MIC 5 uM), Psychrobacter sp. (PAMC 25501) (MIC 2.5 uM), E. coli DH5alpha (MIC 5 uM), Gram+ E. faecalis (ATCC 29212) (MIC 25 uM), S. pyogenes (ATCC 19615) (MIC 2.5 uM), S. aureus (ATCC 33591), L. monocytogenes (ATCC 15313) (MIC 5 uM), and yeast C. tropicalis (ATCC 20115) (MIC 5 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.28122029]No cytotoxicity information found Not found 28122029 PLoS One. 2017 Jan 25;12(1):e0170821. Shin SC, Ahn IH, Ahn DH, Lee YM, Lee J, Lee JH, Kim HW, Park H Characterization of Two Antimicrobial Peptides from Antarctic Fishes (Notothenia coriiceps and Parachaenichthys charcoti) DRAMP01401 GFMNTAKNVAKNVAVTLLDNLKCKITGGC 29 Odorranain-F-OW1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana wuchuanensis (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=2 µM), Pseudomonas aeruginosa (MIC=4 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=4 µM).##Yeast: Candida albicans ATCC 2002 (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01402 GLFTLIKGAYKLDAPTVACN 20 Odorranain-J-OA1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=40.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=40.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=20.1 µg/ml)；##Yeast: Candida albicans ATCC 2002 (MIC=20.1 µg/ml). [Ref:22029824]Not found Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01403 GLFTLIKGAYKNDAPTVACN 20 Odorranain-J-OA2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Weakly active against bacteria and fungi. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=40.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=40.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=20.1 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=20.1 µg/ml). [Ref:22029824]Not found Linear Free Free Free L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01409 GILSGILGVGKKLVCGLSGLC 21 Nigrocin-OR1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana rotodora (Chinese odorous frogs) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=4 µM), Pseudomonas aeruginosa (MIC=7 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=2 µM).##Yeast: Candida albicans (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01410 GILSGILGVGKMLVCGLSGLC 21 Nigrocin-OR2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana rotodora (Chinese odorous frogs) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3 µM), Bacillus pyocyaneus CMCCB 10104 (MIC=5 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3 µM).##Yeast: Candida albicans ATCC 2002 (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01411 GILSGLLGVGKMLVCGLSGLC 21 Nigrocin-OR3 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana rotodora (Chinese odorous frogs) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3 µM), Bacillus pyocyaneus CMCCB 10104 (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6 µM).##Yeast: Candida albicans ATCC 2002 (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01412 GLLGSLFGAGKKVACALSGLC 21 Nigrocin-2HSa (Frogs, amphibians, animals) P0C8U0 Not found Not found Odorrana hosii (Hose's rock frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 15-21." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=56 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=28 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01413 GLLGSIFGAGKKIACALSGLC 21 Nigrocin-2HSb (Frogs, amphibians, animals) P0C8U1 Not found Not found Odorrana hosii (Hose's rock frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 15-21." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=28 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=14 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01414 GIFSTVFKAGKGIVCGLTGLC 21 Nigrocin-2ISa (Frogs, amphibians, animals) F1T156 Not found Not found Odorrana ishikawae (Ishikawa's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), Staphylococcus aureus (MRSA) (MIC=12.5 µM), Bacillus subtilis (MIC=12.5 µM).##Yeast: Candida albicans (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L [Ref.21193000]No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01415 GILGTVFKAGKGIVCGLTGLC 21 Nigrocin-2ISb (Frogs, amphibians, animals) F1T157 Not found Not found Odorrana ishikawae (Ishikawa's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), Staphylococcus aureus (MRSA) (MIC=12.5 µM), Bacillus subtilis (MIC=12.5 µM).##Yeast: Candida albicans (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01416 GILSTVFKAGKGIVCGLSGLC 21 Nigrocin-2ISc (Frogs, amphibians, animals) No entry found Not found Not found Odorrana ishikawae (Ishikawa's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=3 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 21867685 Biochem Biophys Res Commun. 2011 Sep 9;412(4):673-677. Iwakoshi-Ukena E, Soga M, Okada G, Fujii T, Sumida M, Ukena K. Characterization of novel antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae by shotgun cDNA cloning. DRAMP01417 GLLSGILGAGKHIVCGLSGLC 21 Nigrocin-2GRa (Frogs, amphibians, animals) No entry found Not found Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Has antibacterial against Gram-negative bacterium E. coli. Also has a weak hemolytic activity against human erythrocytes. [Ref.16621155]Gram-negative bacterium: Escherichia coli (MIC=25 µM). [Ref:16621155] LC50=295 μM against human erythrocytes Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 16621155 Peptides. 2006 Sep;27(9):2111-2117. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami. DRAMP01418 GLFGKILGVGKKVLCGLSGMC 21 Nigrocin-2GRb (Frogs, amphibians, animals) No entry found Not found Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial against the Gram-negative bacterium E. coli and the Gram-positive bacterium S. aureus. Also has a weak hemolytic activity against human erythrocytes. [Ref.16621155]Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 µM);##Gram-negative bacterium: Escherichia coli (MIC=3 µM);##Yeast: Candida albicans (MIC=50 µM). [Ref:16621155] LC50=40 μM against human erythrocytes Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 16621155 Peptides. 2006 Sep;27(9):2111-2117. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami. DRAMP01419 GLLSGILGAGKNIVCGLSGLC 21 Nigrocin-2GRc (Frogs, amphibians, animals) No entry found Not found Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Has antibacterial against Gram-negative bacterium E. coli. Also has a weak hemolytic activity against human erythrocytes. [Ref.16621155]Gram-negative bacterium: Escherichia coli (MIC=50 µM). [Ref:16621155] LC50>500 μM against human erythrocytes Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 16621155 Peptides. 2006 Sep;27(9):2111-2117. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami. DRAMP01420 GLLSGILGAGKHIICGLSGLC 21 Nigrocin-OG4 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC>100 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC>100 µg/ml), Bacillus subtilis (MIC>100 µg/ml).##Yeast: Candida albicans (MIC=1.10 µg/ml). [Ref.17272268] RCH=65.5 ± 7.7% against rabbit red blood cells at 50 μg/ml. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01421 GLLSGILGAGKQKVCGLSGLC 21 Nigrocin-OG5 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC=9.37 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=18.75 µg/ml), Bacillus subtilis (MIC=37.50 µg/ml).##Yeast: Candida albicans (MIC=4.68 µg/ml). [Ref.17272268] RCH=87.2 ± 2.6% against rabbit red blood cells at 50 μg/ml. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01422 GLLSGVLGVGKKVLCGLSGLC 21 Nigrosin-OG21 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC=4.68 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=9.37 µg/ml), Bacillus subtilis (MIC=18.75 µg/ml).##Yeast: Candida albicans (MIC=4.68 µg/ml). [Ref.17272268] RCH=100% against rabbit red blood cells at 50 μg/ml. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01423 GLLSGILGAGKHIVCGLSGLR 21 Nigrosin-OG13 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacterium: Escherichia coli (MIC=4.68 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=9.37 µg/ml), Bacillus subtilis (MIC=18.75 µg/ml).##Yeast: Candida albicans (MIC=1.10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.17272268]No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01426 GLLSGVLGVGKKIVCGLSGLC 21 Nigrocin-1-OA1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=10.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10.4 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=5.2 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01427 GIFGKILGVGKKTLCELSGMC 21 Nigrocin-1-OA2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.3 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=6.3 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.3 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=3.2 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01428 GIFLKVLGVGKKVLCGVSGLC 21 Nigrocin-1-OA3 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=21.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=5.4 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=10.8 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01429 GLISGILGVGKKLVCGLSGLC 21 Nigrocin-1-OR1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=23 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=5.8 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=11.5 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01430 GLISGILGVGKMLVCGLSGLC 21 Nigrocin-1-OR2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=17.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=8.6 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=8.6 µg/ml) [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01431 GLISGLLGVGKMLVCGLSGLC 21 Nigrocin-1-OR3 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=20.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=20.4 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=10.2 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01432 GILGNIVGMGKKIVCGLSGLC 21 Nigrocin-1-OW2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=12.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.2 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=3.1 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01433 GILGNIVGMGKKVVCGLSGLC 21 Nigrocin-1-OW3 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.3 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=22.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=11.3 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=6.7 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01434 GILSGVLGMGKKIVCGLRGLC 21 Nigrocin-1-OW4 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=7.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=14.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3.6 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=7.2 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01435 GILGNIVGMGKQVVCGLSGLC 21 Nigrocin-1-OW5 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=10.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=5.1 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=5.1 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP01436 GILSGVLGMGKKIVCGLSGLC 21 Nigrocin-1-OW1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4.4 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=8.8 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=8.8 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=4.4 µg/ml). [Ref:22029824] Not found in the literature Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. DRAMP18394 RLNTTFRPLNFKMLRFWGQNRNIMKHRGQKVHFSLILSDCKTNKDCPKLRRANVRCRKSYCVPI 64 NCR335 (nodule-specific cysteine-rich peptides; plants) No entry found Not found Not found Medicago truncatula Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against S. enterica (MIC 16 uM) and L. monocytogenes (MIC 32 uM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys40 and Cys61,Cys46 and Cys56. L [Ref.28167938]No cytotoxicity information found Not found 28167938 Front Microbiol. 2017 Jan 23;8:51. Farkas A, Mar Comparative Analysis of the Bacterial Membrane Disruption Effect of Two Natural Plant Antimicrobial Peptides. DRAMP01438 GIFGKILGAGKKVLCGLSGLC 21 Nigrocin-2JDa (Frogs, amphibians, animals) B3A0M6 Not found Not found Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Has hemolytic activity against rabbit erythrocytes. PTM: contains one disulfide bond 15-21. " [Ref.22917879]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=16 µM), Staphylococcus aureus CIB 85462 (MIC=8 µM);##Gram-negative bacteria: Escherichia coli ATCC 25992 (MIC=16 µM), Escherichia coli CIB 84492 (MIC=16 µM);##Yeast: Candida albicans (MIC=63 µM). [Ref:22917879] It has 80.3 ± 5.5% hemolytic activity at 128 μg/ml against rabbit red blood cells Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22917879 J Proteomics. 2012 Oct 22;75(18):5807-5821. Liu J, Jiang J, Wu Z, Xie F. Antimicrobial peptides from the skin of the Asian frog, Odorrana jingdongensis: De novo sequencing and analysis of tandem mass spectrometry data. DRAMP01439 GIFGKILGVGKKVLCGLSGMC 21 Nigrocin-2JDb (Odorranain-H2; Frogs, amphibians, animals) B3A0M7 Not found Not found Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Has hemolytic activity against rabbit erythrocytes. PTM: contains one disulfide bond 15-21. " [Ref.22917879]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=15 µM), Staphylococcus aureus CIB 85462 (MIC=15 µM);##Gram-negative bacteria: Escherichia coli ATCC 25992 (MIC=8 µM), Escherichia coli CIB 84492 (MIC=8 µM);##Yeast: Candida albicans (MIC=31 µM). [Ref:22917879] It has 88.4 ± 4.2% hemolytic activity at 128 μg/ml against rabbit red blood cells Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 22917879 J Proteomics. 2012 Oct 22;75(18):5807-5821. Liu J, Jiang J, Wu Z, Xie F. Antimicrobial peptides from the skin of the Asian frog, Odorrana jingdongensis: De novo sequencing and analysis of tandem mass spectrometry data. DRAMP01440 GILSGILGMGKKLVCGLSGLC 21 Nigrocin-2LVb (Frogs, amphibians, animals) No entry found Not found Not found Odorrana livida (Chinese Odorrana frogs) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM);##Gram-negative bacterium: Escherichia coli (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 20158520 FEBS J. 2010 Mar;277(6):1519-1531. Wang L, Evaristo G, Zhou M, Pinkse M, Wang M, Xu Y, Jiang X, Chen T, Rao P, Verhaert P, Shaw C. Nigrocin-2 peptides from Chinese Odorrana frogs--integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis. DRAMP01441 SILSGNFGVGKKIVCGLSGLC 21 Nigrocin-2VB (Frogs, amphibians, animals) No entry found Not found Not found Odorrana livida (Chinese Odorrana frogs) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity against the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 20158520 FEBS J. 2010 Mar;277(6):1519-1531. Wang L, Evaristo G, Zhou M, Pinkse M, Wang M, Xu Y, Jiang X, Chen T, Rao P, Verhaert P, Shaw C. Nigrocin-2 peptides from Chinese Odorrana frogs--integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis. DRAMP01442 GILSGILGAGKSLVCGLSGLC 21 Nigrocin-2SCa (Frogs, amphibians, animals) No entry found Not found Not found Odorrana schmackeri (Chinese Odorrana frogs) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity against the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 20158520 FEBS J. 2010 Mar;277(6):1519-1531. Wang L, Evaristo G, Zhou M, Pinkse M, Wang M, Xu Y, Jiang X, Chen T, Rao P, Verhaert P, Shaw C. Nigrocin-2 peptides from Chinese Odorrana frogs--integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis. DRAMP01443 GILSNVLGMGKKIVCGLSGLC 21 Nigrocin-2SCc (Frogs, amphibians, animals) No entry found Not found Not found Odorrana schmackeri (Chinese Odorrana frogs) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity against the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=70 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Not found 20158520 FEBS J. 2010 Mar;277(6):1519-1531. Wang L, Evaristo G, Zhou M, Pinkse M, Wang M, Xu Y, Jiang X, Chen T, Rao P, Verhaert P, Shaw C. Nigrocin-2 peptides from Chinese Odorrana frogs--integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis. DRAMP01447 GFSSIFRGVAKFASKGLGKDLAKLGVDLVACKISKQC 37 Esculentin-2CHa (Frogs, amphibians, animals) No entry found Not found Not found Lithobates chiricahuensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli (MIC=5 µM), K. pneumoniae (MIC=5 µM), P. aeruginosa (MIC=5 µM);##Gram-positive bacterium: S. aureus (MIC=5 µM).##Yeast: C. albicans (MIC=10 µM). [Ref.21262304] LC50=150 µM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 21262304 Peptides. 2011 Apr;32(4):664-669. Conlon JM, Mechkarska M, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona. DRAMP01452 RISFKKGKGSWIKNGLIKGIKGLGKEISLDVIRTGIDIAGCKIKGEC 47 Esculentin-1LTa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=0.6 µM), Bacillus licheniformis X39 (MIC=10 µM), Staphylococcus carnosus KHS (MIC=1.3 µM), Rhodococcus rhodochrous X15 (MIC=0.3 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=5 µM), Serratia rubidaea X01 (MIC=10 µM), Psychrobacter faecalis X29 (MIC=0.6 µM).##Yeast: Candida albicans ATCC2002 (MIC=80 µM). [Ref.22426384] LD50>480 μM against human erythrocytes Cyclic Free Cyclization (Cys41 and Cys47) Disulfide bond between Cys41 and Cys47. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01453 GIFSLFKAGAKFFGKHLLKQAGKAGAEHLACKATNQC 37 Esculentin-2LTa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=1.6 µM), Bacillus licheniformis X39 (MIC=3.2 µM), Staphylococcus carnosus KHS (MIC=3.2 µM), Rhodococcus rhodochrous X15 (MIC=0.8 µM);##Gram-negative bacterium: Psychrobacter faecalis X29 (MIC=1.6 µM). [Ref.22426384] LD50>600 μM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01454 GLFTLIKGAAKLIGKTVAKEAGKTGLELMACKITNQC 37 Esculentin-2JDa (Frogs, amphibians, animals) B3A0M8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against E. coli and S. aureus strains (Probable). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." Gram-negative bacteria: Escherichia coli (ATCC 25922) (MIC=34 µg/ml), Extended-spectrum ß-lactamases E. coli (ESBL) (MIC=34 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (ATCC 25923) (MIC=8 µg/ml), Methicillin-resistant S. aureus (MRSA) (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 22917879 J Proteomics. 2012 Oct 22;75(18):5807-5821. Liu J, Jiang J, Wu Z, Xie F. Antimicrobial peptides from the skin of the Asian frog, Odorrana jingdongensis: de novo sequencing and analysis of tandem mass spectrometry data. DRAMP01456 GLFSILKGVGKIALKGLAKNMGKMGLDLVSCKISKEC 37 Esculentin-2PLa (Frogs, amphibians, animals) A7WNV5, D3UA57 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against the Gram-negative bacterium E. coli, the Gram-positive bacterium: S. aureus and the yeast C. albicans. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." Gram-negative bacterium: Escherichia coli (MIC=1 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=10 µM).##Yeast: Candida albicans (MIC=49 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01457 GIFSKFAGKGIKDLIIKGVKGIAKEAGMDVIRTGIDIAGCKIKGEC 46 Esculentin-1V (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Chinese frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-positive bacterium: Staphylococcus aureus FDA 209P (MIC=4.9 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=3.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 16427248 Genomics. 2006 May;87(5):638-644. Chen T, Zhou M, Chen W, Lorimer J, Rao P, Walker B, Shaw C. Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. DRAMP01458 GIFTLFKGAAKLLGKTLAKEAGKTGLELMACKVTNQC 37 Esculentin-2V (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Chinese frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-positive bacterium: Staphylococcus aureus FDA 209P (MIC=4.4 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=2.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 16427248 Genomics. 2006 May;87(5):638-644. Chen T, Zhou M, Chen W, Lorimer J, Rao P, Walker B, Shaw C. Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. DRAMP01461 GLFSKFAGKGIKNMIIKGIKGIGKEVGMDVIRTGIDVAGCKIKGEC 46 Esculentin-1S (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana schmackeri (piebald odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-positive bacterium: Staphylococcus aureus FDA 209P (MIC=3 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=1.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 16427248 Genomics. 2006 May;87(5):638-644. Chen T, Zhou M, Chen W, Lorimer J, Rao P, Walker B, Shaw C. Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. DRAMP01462 GLFTLIKGAVKMIGKTVAKEAGKTGLELMACKVTNQC 37 Esculentin-2S (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana schmackeri (piebald odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-positive bacterium: Staphylococcus aureus FDA 209P (MIC=2.6 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=1.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 16427248 Genomics. 2006 May;87(5):638-644. Chen T, Zhou M, Chen W, Lorimer J, Rao P, Walker B, Shaw C. Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. DRAMP01469 GIFALIKTAAKFVGKNLLKQAGKAGLEHLACKANNQC 37 Esculentin-2-Ala (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Esculentin-2-Ala exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=2.5 µg/mL), Bacillus dysenteriae (MIC=7.5 µg/mL), Bacillus cereus (MIC=7.5 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=12.5 µg/mL), Bacillus pumilus (MIC=2.5 µg/mL), Acinetobacter calcoaceticus (MIC=25 µg/mL), Psecdomonas aeruginosa (MIC=50 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=2.5 µg/mL) [Ref:19843479] It has 22% hemolytic activity at 100 μg/mL against rabbit red blood cells Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloen. DRAMP01470 GIFSLIKTAAKFVGKNLLKQAGKAGVEHLACKANNQC 37 Esculentin-2-ALb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Esculentin-2-Alb exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=1.25 µg/mL), Bacillus pumilus (MIC=2.5 µg/mL), Bacillus cereus (MIC=7.5 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=12.5 µg/mL), Bacillus dysenteriae (MIC=7.5 µg/mL), Acinetobacter calcoaceticus (MIC=12.5 µg/mL), Psecdomonas aeruginosa (MIC=50 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=2.5 µg/mL). [Ref:19843479] It has 17% hemolytic activity at 100 μg/mL against rabbit red blood cells Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloen. DRAMP01471 GLFPKINKKKAKTGVFNIIKTVGKEAGMDLIRTGIDTIGCKIKGEC 46 Esculentin-1PLa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North American pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=1 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01472 GIFTKINKKKAKTGVFNIIKTIGKEAGMDVIRAGIDTISCKIKGEC 46 Esculentin-1PLb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North American pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=1 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP18393 AVKPKTAKPKTAKPKTA 17 VK6 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 3.6 uM) and S. aureus ATCC 25923 (EC50 3.3 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP01474 GIFSKINKKKAKTGLFNIIKTVGKEAGMDVIRAGIDTISCKIKGEC 46 Esculentin-1ARa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana areolata (crawfish frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Esculentin-1ARa has antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Also exhibits hemolytic activity against human erythrocytes (HC50=180 µM). [Ref.12429503]Gram-negative bacterium: Escherichia coli (MIC=2 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=13 µM). [Ref:12429503] HC50=180 µM against human erythrocytes Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 12429503 Biochim Biophys Acta. 2002 Nov 19;1601(1):55-63. Ali MF, Lips KR, Knoop FC, Fritzsch B, Miller C, Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. DRAMP01475 GLFPKFNKKKVKTGIFDIIKTVGKEAGMDVLRTGIDVIGCKIKGEC 46 Esculentin-1ARb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana areolata (crawfish frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Esculentin-1ARb has antibacterial against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Also exhibits hemolytic activity against human erythrocytes (HC50=120 µM). [Ref.12429503]Gram-negative bacterium: Escherichia coli (MIC=3 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=60 µM). [Ref:12429503] HC50=120 µM against human erythrocytes Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 12429503 Biochim Biophys Acta. 2002 Nov 19;1601(1):55-63. Ali MF, Lips KR, Knoop FC, Fritzsch B, Miller C, Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. DRAMP01476 GIFSLIKGAAQLIGKTVAKEAGKTGLELMACKVTKQC 37 Esculentin-2HSa (Frogs, amphibians, animals) P0C8T9 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hosii (Hose's rock frog) (Rana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 31-37." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=32 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01477 GIFSKFGGKAIKNLFIKGAKNIGKEVGMDVIRTGIDVAGCKIKGEC 46 Esculentin-1HSa (Frogs, amphibians, animals) P0C8T8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana hosii (Hose's rock frog) (Odorrana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 40-46." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01479 GLFSKLNKKKIKSGLIKIIKTAGKEAGLEALRTGIDVIGCKIKGEC 46 Esculentin-1CPa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (North American New World frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.19635516]Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM);##Yeast: Candida albicans (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP01480 GFFSLIKGVAKIATKGLAKNLGKMGLDLVGCKISKEC 37 Esculentin-2CPa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (North American New World frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Active against bacteria and fungi. [Ref.19635516]Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM);##Yeast: Candida albicans (MIC=25 µM) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP01482 GIFSKFAGKGIKNLLVKGVKNIGKEVGMDVIRTGIDIAGCKIKGEC 46 Esculentin-1ISa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Japanese Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial activity. Gram-negative bacterium: Escherichia coli (MC=6.3 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), Staphylococcus aureus (MRSA) (MIC=25 µM), Bacillus subtilis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01483 RIFSKIGGKAIKNLILKGIKNIGKEVGMDVIRTGIDVAGCKIKGEC 46 Esculentin-1ISb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Japanese Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity. Gram-negative bacterium: Escherichia coli (MC=3.1 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), Staphylococcus aureus (MRSA) (MIC=12.5 µM), Bacillus subtilis (MIC=12.5 µM).##Yeast: Candida albicans (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01484 GIFSLIKGAAKLITKTVAKEAGKTGLELMACKVTNQC 37 Esculentin-2ISa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Japanese Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity. Gram-negative bacterium: Escherichia coli (MC=12.5 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), Staphylococcus aureus (MRSA) (MIC=25 µM), Bacillus subtilis (MIC=6.3 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01486 GLFSKFAGKGIKNLIFKGVKHIGKEVGMDVIRTGIDVAGCKIKGEC 46 Esculentin-1GRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Odorrana andersonii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity, also activity against fungus C. albicans. Gram-negative bacterium: Escherichia coli (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 µM).##Yeast: Candida albicans (MIC>50 µM). [Ref.16621155] LC50=210 μM against human erythrocytes. Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 16621155 Peptides 2006; 27: 2111-2117. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H. Antimicrobial peptides from diverse families isolated from the skin of the Asia frog, Rana Grahami. DRAMP01490 GILSLVKGVAKLAGKGLAKEGGKFGLELIACKIAKQC 37 Esculentin-2A (Frogs, amphibians, animals) P40845 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European Edible frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species. [Ref.8163497]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.2 µM), Staphylococcus aureus Cowan 1 (MIC=0.8 µM);##Gram-negative bacteria: Escherichia coli D21 (MIC=0.4 µM), Pseudomonas aeruginosa ATCC15692 (MIC=3.5 µM). [Ref:8163497] Not found in the literature Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01491 GIFSKLAGKKLKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1B (Frogs, amphibians, animals) P40844 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European Edible frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli D21 (MIC=0.2 µM), Pseudomonas aeruginosa ATCC15692 (MIC=0.7 µM);##Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.1 µM), Staphylococcus aureus cowan I (MIC=0.4 µM).##Fungi: Candida albicans (MIC=0.5 µM), Saccharomyces cerevisiae (MIC=0.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.8163497]No cytotoxicity information found Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01493 GLFSKFVGKGIKNFLIKGVKHIGKEVGMDVIRVGIDVAGCKIKGVC 46 Esculentin-1-OA1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-positive bacteria: Bacillus pyocyaneus CMCCB 10104 (MIC=1.2 µg/mL), Staphylococcus aureus ATCC 25923 (MIC=1.2 µg/mL).##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=1.2 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=2.4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01494 GLFSKFSGKGIKNFLIKGVKHIGKEVGMDVIRTGIDVAGCKIKGEC 46 Esculentin-1-OA2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=2.5 µg/mL);##Gram-positive bacteria: Bacillus pyocyaneus CMCCB 10104 (MIC=2.5 µg/mL), Staphylococcus aureus ATCC 25923 (MIC=1.3 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=1.3 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01495 GLFSKFAGKGIKDLIFKGVKHIGKEVGMDVIRVGIDVAGCKIKGVC 46 Esculentin-1-OA3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=5.4 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=5.4 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=2.7 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=2.7 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01496 GLFTKFAGKGIKDLIFKGVKHIGKEVGMDVIRVGIDVAGCKIKGVC 46 Esculentin-1-OA4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=5.6 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2.8 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=2.8 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=5.6 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01497 GLFSKFAGKGIKNFLIKGVKHIGKEVGMDVIRVGIDVAGCKIKGVC 46 Esculentin-1-OA5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=3.4 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=1.7 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=3.4 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=1.7 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01499 GIFSKISGKAIKNLFIKGAKNVGKEVGMDVVRTGIDVVGCKIKGEC 46 Esculentin-1-OR1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=8.8 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4.4 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=17.6 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=8.8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01501 GIFSKISGKAIKNLFIKGAKNVGKRVGMDVVRTGMDVVGCKIKGEC 46 Esculentin-1-OR3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=5.5 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=11 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=11 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=11 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01502 GIFSKISGKAIKNLFIKGAENVGKHVGIDVVRTGIDVVGCKIKGEC 46 Esculentin-1-OR4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=8.6 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=8.6 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=8.6 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=8.6 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01503 GIFSKISGKAIKNLFIKGAKNVGKEVGIDVVRTGMDVVGCKIKGEC 46 Esculentin-1-OR5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=4.1 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4.1 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=8.2 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=2.1 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01504 GIFTLIKGAAKLIGKTVAKEAGKTGLELMACKITNQC 37 Esculentin-2-OA1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=8.5 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4.3 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=4.3 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=8.5 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01505 GLFTLIKGAAKLIGKTTAKEAGKTGKLEMACKITNQC 37 Esculentin-2-OA2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=10.8 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=21.6 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=21.6 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP18392 AKKPVAKKAAGGVKKPK 17 VK7 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 38.4 uM) and S. aureus ATCC 25923 (EC50 1.3 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP01507 GVFTLIKGATQLIGKTLGKELGKTGLELMACKITNQC 37 Esculentin-2-OR1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=10.8 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=21.6 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=21.6 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=10.8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01508 GVFTLIKGATQLIGKTLGKEVGKTGLELMACKITKQC 37 Esculentin-2-OR2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=8.1 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4.1 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=16.2 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=8.1 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01509 GVFTLLKGATQLIGKTLGKELGKTGLELMACKITNQC 37 Esculentin-2-OR3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=7.9 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=7.9 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=7.9 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=15.8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01510 GVFTLIKGATQLIGKTLGKELGKTGLELMACKITEQC 37 Esculentin-2-OR4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=3.6 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=3.6 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=3.6 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=3.6 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01511 GVFTLIKGATQLIGKTLGKELGKTGLEIMACKITKQC 37 Esculentin-2-OR5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=15.8 µg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=15.8 µg/mL), Bacillus pyocyaneus CMCCB 10104 (MIC=15.8 µg/mL).##Yeast: Candida albicans ATCC 2002 (MIC=7.9 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L [Ref.22029824]No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01513 GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1 (Frogs, amphibians, animals) P32414 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Has hemolytic activity. Gram-negative bacteria: Escherichia coli D21 (MIC=0.2 µM), Pseudomonas aeruginosaATCC15692 (MIC=0.7 µM);##Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.1 µM), Staphylococcus aureus Cowan1 (MIC=0.4 µM).##Fungi: Candida albicans (MIC=0.5 µM), Saccharomyces cerevisiae (MIC=0.9 µM). [Ref. 8163497] LC>100μM Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L [Ref.8508915]No cytotoxicity information found Not found 8508915 FEBS Lett. 1993 Jun 14;324(2):159-161. Simmaco M, Mignogna G, Barra D, Bossa F. Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta. DRAMP01520 GLLNTFKDWAISIAKGAGKGVLTTLSCKLDKSC 33 Rugosin-A (Frogs, amphibians, animals) P80954 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Glandirana rugosa (Japanese wrinkled frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacteria: Staphylococcus aureus 209P (MIC=6.25 µg/ml), Bacillus subtilis ATCC6633 (MIC=12.5 µg/ml), Micrococcus luteus ATCC9341 (MIC=25 µg/ml), Streptococcus pyogenes COOK (MIC=50 µg/ml);##Gram-negative bacteria: Escherichia coli NIHJ (MIC=100 µg/ml), Pseudomonas aeruginosa PAO-1 (MIC>100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L [Ref.7612013]No cytotoxicity information found Not found 7612013 Biochem Biophys Res Commun. 1995 Jul 6;212(1):249-254. Suzuki S, Ohe Y, Kagegawa T, Tatemoto K. Isolation and characterization of novel antimicrobial peptides, rugosins A, B and C, from the skin of the frog, Rana rugosa. DRAMP01521 SLFSLIKAGAKFLGKNLLKQGAQYAACKVSKEC 33 Rugosin-B (Frogs, amphibians, animals) P80955 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows antibacterial activity against both Gram-negative and Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacteria: Staphylococcus aureus 209P (MIC=6.25 µg/ml), Bacillus subtilis ATCC6633 (MIC=6.25 µg/ml), Micrococcus luteus ATCC9341 (MIC=1.56 µg/ml), Streptococcus pyogenes COOK (MIC=12.5 µg/ml);##Gram-negative bacteria: Escherichia coli NIHJ (MIC=12.5 µg/ml), Pseudomonas aeruginosa PAO-1 (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L [Ref.7612013]No cytotoxicity information found Not found 7612013 Biochem Biophys Res Commun. 1995 Jul 6;212(1):249-254. Suzuki S, Ohe Y, Kagegawa T, Tatemoto K. Isolation and characterization of novel antimicrobial peptides, rugosins A, B and C, from the skin of the frog, Rana rugosa. DRAMP01524 SIRDKIKTIAIDLAKSAGTGVLKTLICKLDKSC 33 Rugosin-RN1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has weak hemolytic activity gainst rabbit red cells. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=4.69 µg/ml), Bacillus subtilis (MIC=9.38 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=25.00 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=5.63 µg/ml) [Ref:19778602]Show weak hemolytic activity against rabbit red cells Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bridge between Cys27 and Cys33. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01525 SIRDKIKTIAIDLAKSAGMGILKTLICKLDKSC 33 Rugosin-RN3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=16.51 µg/ml), Bacillus subtilis (MIC=18.75 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=25.00 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=15.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bridge between Cys27 and Cys33. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01526 SIRDKIKTIAIDLAKSAGTGVLKTLICKLNKSC 33 Rugosin-RN5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=15.00 µg/ml), Staphylococcus aureus ATCC43300 (MRSA) (MIC=12.50 µg/ml), Bacillus subtilis (MIC=18.75 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=25.00 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=18.75 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bridge between Cys27 and Cys33. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01533 CVISAGWNHKIRCKLTGNC 19 Nigroain-B1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Bridge Not found PTM: Contains one disulfide bridge. Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=4.69 µg/ml), S. aureus ATCC43300 (MIC=50.00 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa PA01 (MIC=25.00 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=25.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys13 and Cys19) Disulfide bridge between Cys13 and Cys19. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01539 FKTWKRPPFQTSCWGIIKE 19 Nigroain-C2 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=27.50 µg/ml), S. aureus ATCC43300 (MIC=55.00 µg/ml), Bacillus subtilis (MIC=110.00 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35P (MIC=110.00 µg/ml), Pseudomonas aeruginosa PA01 (MIC=55.00 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=55.00 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=13.75 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01542 CVHWQTNTARTSCIGP 16 Nigroain-D3 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found PTM: Contains one disulfide bridge. Gram-positive bacterium: Bacillus subtilis (MIC=55 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=110 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (Cys1 and Cys13) Free Disulfide bridge between Cys1 and Cys13. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01543 DCTRWIIGINGRICRD 16 Nigroain-E1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Function: Has hemolytic activity against rabbit red cells. [Ref.19778602]Gram-positive bacterium: Staphylococcus aureus ATCC25923 (MIC=18.75 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=75 µg/ml). [Ref:19778602]7.62±1.6% hemolytic activity at 100 µg/ml against rabbit red cells Cyclic Free Free Disulfide bridge between Cys2 and Cys14. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01546 SLWETIKNAGKGFIQNLDKIR 21 Nigroain-K1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Also has hemolytic activity against rabbit red cells. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=9.38 µg/ml), Bacillus subtilis (MIC=21.88 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=37.50 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=32.74 µg/ml). [Ref:19778602]22.49 ± 4.8% hemolytic activity at 100 µg/ml against rabbit red cells Linear Free Free Free L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01547 SLWETIKNAGKGFILNILDKIRCKVAGGCKT 31 Nigroain-K2 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Also has hemolytic activity against rabbit red cells. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=11.25 µg/ml), Staphylococcus aureus ATCC43300 (MIC=9.38 µg/ml), Bacillus subtilis (MIC=9.38 µg/ml);##Gram-positive bacteria: Escherichia coli ML-35P (MIC=25.00 µg/ml), Pseudomonas aeruginosa PA01 (MIC=25.00 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=25.00 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=15.00 µg/ml) [Ref:19778602]85.52 ± 3.26% hemolytic activity at 50 µg/ml against rabbit red cells Cyclic Free Free Disulfide bridge between Cys23 and Cys29. L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01549 GLLSVLGSVAKHVLPHVVPVIAEHL 25 Caerin-1.1 (Frogs, amphibians, animals) P62568, P62569, Q800R2, P56226 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria splendida (Magnificent tree frog) (Litoria gilleni) (Litoria caerulea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Alpha helix The peptide adopts two well-defined helices from Leu2 to Lys11 and from Val17 to His24 separated by a region of less-defined helicity and greater flexibility. "Function: Antibacterial and antiviral peptides that adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Secreted by the skin parotoid and/or rostral glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility. Miscellaneous: Caerin 1.1 completely inhibits HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells (J Virol. 2005 Sep;79(18):11598-606). PTM: C-terminal amidation." [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=1.5 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12.5 µg/ml), Staphylococcus aureus (MIC=3-12 µg/ml), Staphylococcus epidermis (MIC=12.5 µg/ml), Streptococcus uberis (MIC=12.5 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml).##[Ref.16140737]Virus:HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=7.8 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=12.6 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L No cytotoxicity information found in the reference(s) presented Cell membrane 16140737##9266696##12709067##15203252 J Virol. 2005 Sep;79(18):11598-606. ##Eur J Biochem. 1997 Jul 15;247(2):545-557.##Eur J Biochem. 2003 May;270(9):2068-2081.##Peptides. 2004 Jun;25(6):1035-1054. VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D.##Wong H, Bowie JH, Carver JA.##Vanhoye D, Bruston F, Nicolas P, Amiche M.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.##The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.##Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01550 GLLGAMFKVASKVLPHVVPAITEHF 25 Caerin-1.11 (Frogs, amphibians, animals) Q800R9 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found "Function: Antibacterial and antiviral peptides that adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity (By similarity). PTM: C-terminal amidation." Gram-negative bacteria: Escherichia coli B (MIC=25 µM), Enterobacter cloacae (MIC=50 µM), Klebsiella pneumoniae (MIC=25 µM);##Gram-positive bacterium: Staphylococcus haemolyticus (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.12709067]No cytotoxicity information found##[Ref.22771617]No cytotoxicity information found Not found 12709067##22771617 Eur J Biochem. 2003 May;270(9):2068-2081.##Peptides. 2012 Sep;37(1):174-188. Vanhoye D, Bruston F, Nicolas P, Amiche M.##Bowie JH, Separovic F, Tyler MJ. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.##Host-defense peptides of Australian anurans. Part 2. Structure, activity, mechanism of action, and evolutionary significance. DRAMP01552 GLLSVLGSVAQHVLPHVVPVIAEHL 25 Caerin-1.3 (Frogs, amphibians, animals) P56228 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Australian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=25 µg/ml), Staphylococcus aureus (MIC=6-12 µg/ml), Staphylococcus epidermis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=50 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01553 GLLSSLSSVAKHVLPHVVPVIAEHL 25 Caerin-1.4 (Frogs, amphibians, animals) P62544, P56229, P62545, P56229 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) (also Litoria gilleni) (Centralian tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Listeria innocua (MIC=100 µg/ml), Micrococcus luteus (MIC=0.4 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=100 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=50 µg/ml), Pasteurella multocida (MIC=25 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01555 GLLSVLGSVVKHVIPHVVPVIAEHL 25 Caerin-1.5 (Frogs, amphibians, animals) P56230 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-,Antiviral Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation." [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=50 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml). ##[Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 12.5 µM. Not found 26026377##15203252##PubMed ID is not available Peptides. 2015 Sep;71:296-303. ##Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01560 GLFGVLGSIAKHVLPHVVPVIAEKL 25 Caerin-1.9 (Frogs, amphibians, animals) P81252 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria chloris (Blue-thighed frog) (frog skin active peptide family) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin dorsal glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation. Miscellaneous: Caerin 1.9 completely inhibited HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells (J Virol. 2005 Sep;79(18):11598-606)." [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=50 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=50 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=50 µg/ml). ##[Ref.16140737]Virus:HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=1.2 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=1.6 μM).##[Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 20 µM." Not found 26026377##16140737##15203252##9516047 Peptides. 2015 Sep;71:296-303. ##J Virol. 2005 Sep;79(18):11598-606. ##Peptides. 2004 Jun;25(6):1035-1054.##J Pept Res. 1998 Feb;51(2):121-126. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. DRAMP01562 GLVSSIGRALGGLLADVVKSKGQPA 25 Caerin-2.1 (Frogs, amphibians, animals) P56233, P86485 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria splendida (Magnificent tree frog) (Emerald spotted tree frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.15203252]No cytotoxicity information found##[Ref.19642086]No cytotoxicity information found Not found 15203252##19642086 Peptides. 2004 Jun;25(6):1035-1054.##Rapid Commun Mass Spectrom. 2009 Sep;23(17):2628-2636. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Bilusich D, Jackway RJ, Musgrave IF, Tyler MJ, Bowie JH. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides. DRAMP01563 GLVSSIGRALGGLLADVVKSKEQPA 25 Caerin-2.2 (Frogs, amphibians, animals) P62570, P62571, P56234 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gilleni (Centralian tree frog) (also Litoria caerulea) (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." Gram-positive bacterium: Micrococcus luteus (MIC=50 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01567 GLVSSIGKVLGGLLADVVKSKGQPA 25 Caerin-2.6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Caerin subfamily) Not found the skin secretions) (hybrid between female Litoria splendida; also male Litoria caerulea Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity (By similarity). PTM: C-terminal amidation." Gram-positive bacterium: Leuconostoc lactis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.16824041]No cytotoxicity information found Not found 16824041 FEBS J. 2006 Aug;273(15):3511-3519. Pukala TL, Bertozzi T, Donnellan SC, Bowie JH, Surinya-Johnson KH, Liu Y, Jackway RJ, Doyle JR, Llewellyn LE, Tyler MJ. Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea. DRAMP01568 GLVSSIGKALGGLLVDVVKSKGQPA 25 Caerin-2.7 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Caerin subfamily) Not found the skin secretions) (hybrid between female Litoria splendida; also male Litoria caerulea Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity (By similarity). PTM: C-terminal amidation." Gram-positive bacterium: Leuconostoc lactis (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.16824041]No cytotoxicity information found Not found 16824041 FEBS J. 2006 Aug;273(15):3511-3519. Pukala TL, Bertozzi T, Donnellan SC, Bowie JH, Surinya-Johnson KH, Liu Y, Jackway RJ, Doyle JR, Llewellyn LE, Tyler MJ. Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea. DRAMP01570 GLWEKIKEKASELVSGIVEGVK 22 Caerin-3.2 (Frogs, amphibians, animals) P56239 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." Gram-positive bacterium: Micrococcus luteus (MIC=3 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01573 GLWEKVKEKANELVSGIVEGVK 22 Caerin-3.5 (Frogs, amphibians, animals) P0C2A9 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gracilenta (Dainty green tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacterium: Leuconostoc lactis (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16554081]No cytotoxicity information found Not found 16554081 Toxicon. 2006 May;47(6):664-675. Maclean MJ, Brinkworth CS, Bilusich D, Bowie JH, Doyle JR, Llewellyn LE, Tyler MJ. New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry. DRAMP01574 GLWQKIKSAAGDLASGIVEGIKS 23 Caerin-4.1 (Frogs, amphibians, animals) P56242 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-,Antiviral Protein level Alpha helix Not found "PTM: adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." [Ref.15203252]Gram-positive bacterium: Micrococcus luteus (MIC=12 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01576 GLWQKIKNAAGDLASGIVEGIKS 23 Caerin-4.3 (Frogs, amphibians, animals) P56244 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." Gram-positive bacterium: Micrococcus luteus (MIC=25 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=50 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found Not found 15203252##PubMed ID is not available Peptides. 2004 Jun;25(6):1035-1054.##J. Chem. Res. 1993; 138: 910-936. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01577 GLLSVLGSVAKHVLPHVVPVIAEKL 25 Caerin-1.10 (Frogs, amphibians, animals) P86502, P82104 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria rothii (Roth's tree frog); also Litoria splendida (Magnificent tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-,Antiviral Protein level Not found Not found "Function: Antibacterial peptide with wide spectrum of activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.10601876]Gram-positive bacteria: Leuconostoc lactis (MIC=6 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=25 µg/ml), Streptococcus uberis (MIC=50 µg/ml), Staphylococcus epidermidis (MIC=100 µg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=100 µg/ml).##[Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 22 µM." Not found 26026377##16124032##10601876 Peptides. 2015 Sep;71:296-303. ##Rapid Commun Mass Spectrom. 2005;19(18):2716-2724.##Eur J Biochem. 2000 Jan;267(1):269-275. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Brinkworth CS, Bowie JH, Bilusich D, Tyler MJ.##Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC, Smith BP. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##The rothein peptides from the skin secretion of Roth's tree frog Litoria rothii. Sequence determination using positive and negative ion electrospray mass spectrometry.##Differences in the skin peptides of the male and female Australian tree frog Litoria splendida. The discovery of the aquatic male sex pheromone splendipherin, together with phe8 caerulein and a new antibiotic peptide caerin 1.10. DRAMP18389 AKKPVAKKAAGGVKKPKK 18 VK12 (histone derived; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 0.7 uM) and S. aureus ATCC 25923 (EC50 0.8 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP18390 AKAVKPKTAKPKTAKPKTAKA 21 VK11 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 2.8 uM) and S. aureus ATCC 25923 (EC50 4.7 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP18391 ARTKQTARKSTGGKAPRKQLAT 22 VK10 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found 2PY0, 2NQB, 2IO5, 2FJ7, 1ZLA, 1KX3, 1KX4, 1KX5,1HIO Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 1.3 uM) and S. aureus ATCC 25923 (EC50 2.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP01584 GLFSVLGSVAKHLLPHVAPIIAEKL 25 Caerin-1.17 (Frogs, amphibians, animals) P0C2A6 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gracilenta (Dainty green tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Caerin-1.17 shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus Strain ATCC 25923 (MIC=50 µg/ml), Staphylococcus aureus Strain ATCC 29213 (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml), Pasteurella multocida (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16554081]No cytotoxicity information found Not found 16554081 Toxicon. 2006 May;47(6):664-675. Maclean MJ, Brinkworth CS, Bilusich D, Bowie JH, Doyle JR, Llewellyn LE, Tyler MJ. New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry. DRAMP01585 GLFSVLGSVAKHLLPHVVPVIAEKL 25 Caerin-1.18 (Frogs, amphibians, animals) P0C2A7 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gracilenta (Dainty green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=25 µg/ml), Listeria innocua (MIC=12 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus ATCC 25923 (MIC=12 µg/ml), Staphylococcus aureus ATCC 29213 (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=25 µg/ml), Streptococcus uberis (MIC=25 µg/ml);##Gram-negative bacteria: Pasteurella multocida (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16554081]No cytotoxicity information found Not found 16554081 Toxicon. 2006 May;47(6):664-675. Maclean MJ, Brinkworth CS, Bilusich D, Bowie JH, Doyle JR, Llewellyn LE, Tyler MJ. New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry. DRAMP01586 GLFKVLGSVAKHLLPHVAPIIAEKL 25 Caerin-1.19 (Frogs, amphibians, animals) P0C2A8 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gracilenta (Dainty green tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-,Antiviral Protein level Not found Not found "Function: Caerin-1.19 shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." [Ref.16554081]Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=12 µg/ml), Micrococcus luteus (MIC=25 µg/ml), Staphylococcus aureus Strain ATCC 25923 (MIC=12 µg/ml), Staphylococcus aureus Strain ATCC 29213 (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml);##Gram-negative bacteria: Pasteurella multocida (MIC=50 µg/ml).##[Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L No cytotoxicity information found in the reference(s) presented Not found 26026377##16554081 Peptides. 2015 Sep;71:296-303. ##Toxicon. 2006 May;47(6):664-675. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Maclean MJ, Brinkworth CS, Bilusich D, Bowie JH, Doyle JR, Llewellyn LE, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry. DRAMP01587 GLFDVIKKVASVIGGL 16 Citropin-1.1 (Frogs, amphibians, animals) P81835, P81836, P81837 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found "Function: Bacteriostatic action for Gram-positive bacteria. Tissue specificity: Expressed by the dorsal and submental skin glands. PTM: C-terminal amidation." Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=6 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01588 GLFAVIKKVASVIGGL 16 Citropin-1.1 sm1 (Frogs, amphibians, animals) No entry found Not found Not found Synthesized modify Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Escherichia coli (MIC=100 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=12 µg/ml), Streptococcus uberis (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01589 GLFDVIAKVASVIGGL 16 Citropin-1.1 sm2 (Frogs, amphibians, animals) No entry found Not found Not found Synthesized modify Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=25 µg/ml), Micrococcus luteus (MIC=100 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermidis (MIC=100 µg/ml), Streptococcus uberis (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01590 GLFDVIAKVASVIKKL 16 Citropin 1.1 M14 (Frogs, amphibians, animals) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: E. coli (MIC=53 µM);##Gram-positive bacterium: S. aureus (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.20564028]No cytotoxicity information found Not found 20564028 Biopolymers. 2011;96(2):147-157. Chia CS, Gong Y, Bowie JH, Zuegg J, Cooper MA. Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin, and maculatin. DRAMP01591 GLFAVIKKVASVIKKL 16 Citropin 1.1 M15 (Frogs, amphibians, animals) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: E. coli (MIC=53 µM);##Gram-positive bacteria: S. aureus (MIC=3 µM), B. subtilis (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.20564028]No cytotoxicity information found Not found 20564028 Biopolymers. 2011;96(2):147-157. Chia CS, Gong Y, Bowie JH, Zuegg J, Cooper MA. Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin, and maculatin. DRAMP01594 GLFDIIKKVASVVGGL 16 Citropin-1.2 (Frogs, amphibians, animals) P81840, P81841, P81842, P81843 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=100 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=25 µg/ml), Streptococcus uberis (MIC=12 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found##[Ref.10504394]No cytotoxicity information found Not found 10504394##15203252 Eur J Biochem. 1999 Oct;265(2):627-637.##Peptides. 2004 Jun;25(6):1035-1054. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01600 GLFDIIKKVASVIGGL 16 Citropin-1.3 (Frogs, amphibians, animals) P81846 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacteria: Bacillus cereus (MIC=25 µg/ml), Leuconostoc lactis (MIC=6 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=25 µg/ml), Streptococcus uberis (MIC=25 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15203252]No cytotoxicity information found##[Ref.10504394]No cytotoxicity information found Not found 10504394##15203252 Eur J Biochem. 1999 Oct;265(2):627-637.##Peptides. 2004 Jun;25(6):1035-1054. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01601 GLIGSIGKALGGLLVDVLKPKL 22 Citropin-2.1 (Frogs, amphibians, animals) No entry found Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacterium: Leuconostoc lactis (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01602 GLIGSIGKALGGLLVDVLKPKLQAAS 26 Citropin-2.1.3 (Frogs, amphibians, animals) P81847, P81848, P81849, P81850 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacterium: Leuconostoc lactis (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01603 GLFDVIKKVASVIGLASP 18 Citropin 1.1.3 (Frogs, amphibians, animals) P81838 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." Gram-positive bacteria: Leuconostoc lactis (MIC=50 µg/ml), Streptococcus uberis (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10504394]No cytotoxicity information found Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01606 GLFDIIKKIAESI 13 Aurein-1.1 (Frogs, amphibians, animals) P82386 Not found Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Expressed by the skin dorsal glands. Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Lactococcus lactis (MIC=25 µg/ml), Listeria innocua (MIC=100 µg/ml), Streptococcus uberis (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191 Eur J Biochem. 2000 Sep;267(17):5330-5341. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. DRAMP01607 GLFDIIKKIAESF 13 Aurein-1.2 (Frogs, amphibians, animals) P82387 Not found Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Alpha helix (1 helices; 10 residues) Not found 1VM5 resolved by NMR. Function: Probably acts by disturbing membrane functions with its amphipathic structure. Aurein 1.2 is HIV active (Wang G et al. 2010 Antimicrob. Agents Chemother. (54) 1343-1346). Aurein 1.2 is also the smallest amphibian peptide to show both antibiotic and Anti-cancer activity. The aurein antibiotics show more activity towards Gram-positive than Gram-negative pathogens. Expressed by the skin dorsal glands. Gram-positive bacteria: Bacillus cereus (MIC=100 μg/ml), Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Streptococcus uberis (MIC=50 μg/ml), Staphylococcus aureus (MIC=8 μmol/L);##Gram-negative bacteria: Pasteurella multocida (MIC=100 μg/ml), Escherichia coli (MIC=8 μmol/L);##Fungi: Candida albicans (MIC=32 μmol/L) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found##[Ref.15572363]No cytotoxicity information found Cell membrane 10951191##15572363##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##J Biol Chem. 2005 Feb 18;280(7):5803-5811.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Wang G, Li Y, Li X.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01608 GLLDIVKKVVGAFGSL 16 Aurein-2.1 (Frogs, amphibians, animals) P69016, P69017, P82388 Not found Not found Litoria aurea (Green; also golden bell frog); also Litoria raniformis (Southern bell frog) Antimicrobial, Anti-cancer, Anti-Gram+ Protein level Not found Not found "Function:Antimicrobial activity against Gram-positive bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Bacillus cereus (MIC=50 μg/ml), Leuconostoc lactis (MIC=6 μg/ml), Listeria innocua (MIC=6 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Streptococcus uberis (MIC=100 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01612 GLFDIVKKVVGAFGSL 16 Aurein-2.5 (Frogs, amphibians, animals) P69018, P69019, P82392 Not found Not found Litoria raniformis (Southern bell frog); also Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." [Ref.10951191]Gram-positive bacteria: Bacillus cereus (MIC=50 μg/ml), Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=50 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=100 μg/ml), Staphylococcus aureus (MIC=50 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01613 GLFDIAKKVIGVIGSL 16 Aurein-2.6 (Frogs, amphibians, animals) P82393 Not found Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus (MIC=100 μg/ml), Leuconostoc lactis (MIC=6 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=25 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Staphylococcus aureus (MIC=50 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01614 GLFDIVKKIAGHIAGSI 17 Aurein-3.1 (Frogs, amphibians, animals) P69020, P69021, P82394 Not found Not found Litoria raniformis (Southern bell frog); also Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." [Ref.10951191]Gram-positive bacteria: Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=100 μg/ml), Streptococcus uberis (MIC=100 μg/ml), Staphylococcus aureus (MIC=50 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01617 GLFDIVKKIAGHIASSI 17 Aurein-3.2 (Frogs, amphibians, animals) P69022, P69023, P82395 Not found Not found Litoria aurea (green; also golden bell frog); also Litoria raniformis (blue-thighed treefrog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Leuconostoc lactis (MIC=6 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Streptococcus uberis (MIC=50 μg/ml), Staphylococcus aureus (MIC=50 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01618 GLFDIVKKIAGHIVSSI 17 Aurein-3.3 (Frogs, amphibians, animals) P82396 Not found Not found Litoria raniformis (blue-thighed treefrog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Leuconostoc lactis (MIC=12 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Streptococcus uberis (MIC=25 μg/ml), Staphylococcus aureus (MIC=100 μg/ml);##Gram-negative bacterium: Pasteurella multocida (MIC=100 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01620 GLMSSIGKALGGLIVDVLKPKTPAS 25 Aurein-5.2 (Frogs, amphibians, animals) P69030, P82402, P69031, P82402 Not found Not found Litoria raniformis (blue-thighed treefrog); also Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Leuconostoc lactis (MIC=100 μg/ml), Streptococcus uberis (MIC=50 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.10951191]No cytotoxicity information found Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01621 IIGPVLGMVGSALGGLLKKI 20 Bombinin-H1 (Frogs, amphibians, animals) P82282, P82283 Belongs to the bombinin family Not found Bombina variegata (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation and D-amino acid." [Ref.8223491]Gram-negative bacterium: Escherichia coli D21 (MIC=3.8 µM);##Gram-positive bacterium: Staphylococcus aureus Cowan 1 (MIC=2.1 µM). [Ref:8223491]Not determined hemolytic activity against human red blood cells. Linear Free Amidation Free L [Ref.8223491]No cytotoxicity information found Not found 8223491 EMBO J. 1993 Dec;12(12):4829-4832. Mignogna G, Simmaco M, Kreil G, Barra D. Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. DRAMP03722 IFGAIWNGIKSLF 13 Cytotoxic linear peptide IsCT2 Q8MTX2 Belongs to the scorpion NDBP 5 family Not found Opisthacanthus madagascariensis (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: IsCT2 showed broad activity spectra against microbes (Gram positive and negative bacteria as well as fungi). Has hemolytic activity. [Ref.12054688] Gram-negetive bacteria: P.aeroginosa ATCC 15442 (MIC>150 μM), P.aeroginosa ATCC 27853 (MIC=68.3 μM), E.coli CCT 1371 (MIC=3.4 μM), Escherichia coli ATCC 25922 (MIC=6.8 μM), P. mirabilis (MIC>150 μM);## Gram-positive bacteria: S.aureus ATCC 25293 (MIC=0.7 μM), S.aureus ATCC 6538 (MIC=3.4 μM), S.saprophyticus (MIC=0.7 μM), B.thuringensis (MIC=17.1 μM), B.subtilis CCT 2471 (MIC=6.8μM).##[Ref.28657596] Gram-positive bacterium:Staphylococcus aureus (MIC=50μg/mL), B. cereus (MIC=100μg/mL);##Gram-negative bacterium: S. typhimurium (MIC=100μg/mL), Escherichia coli (MIC=50μg/mL) [Ref.12054688] Showed relatively weak hemolytic activity against sheep red blood cells.##[Ref.28657596] 18% hemolysis at 10 μg/ml, 96% hemolysis at 50 μg/ml against human red blood cells. Linear Free Amidation Free L [Ref.12054688]No cytotoxicity information found##[Ref.28657596]No cytotoxicity information found Not found 12054688##28657596 Biochem Biophys Res Commun. 2002 May 24;293(5):1514-1522.##Antibiotics (Basel). 2017 Jun 28;6(3). pii: E13. Dai L, Corzo G, Naoki H, Andriantsiferana M, Nakajima T.##de la Salud Bea R, Petraglia AF, Ascuitto MR, Buck QM. Purification, structure-Function: analysis, and molecular characterization of novel linear peptides from scorpion Opisthacanthus madagascariensis.##Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides DRAMP01626 IIGPVLGLVGSALGGLLKKI 20 Bombinin-H5 (Frogs, amphibians, animals) P82285 Belongs to the bombinin family Not found Bombina variegata (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (1 helices; 16 residues) Not found 2AP7, 2AP8 resolved by NMR. "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation and D-amino acid." [Ref.8223491]Gram-negative bacterium: Escherichia coli D21 (MIC=5.0 µM);##Gram-positive bacterium: Staphylococcus aureus Cowan 1 (MIC=3.0 µM). [Ref:8223491]Not found Linear Free Amidation Free Mixed (2D-aIle(alloisoleucine)) [Ref.8223491]No cytotoxicity information found Not found 8223491##PubMed ID is not available EMBO J. 1993 Dec;12(12):4829-4832##TO BE PUBLISHED Mignogna G, Simmaco M, Kreil G, Barra D.##Zangger K, Jilek A, Khatai L. Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata.##Solution structure and orientation of bombinin H2 and H4 in a membrane-mimetic environment. DRAMP01627 YPPKPESPGEDASPEEMNKYLTALRHYINLVTRQRY 36 Skin peptide tyrosine-tyrosine (Skin-PYY; SPYY; Frogs, amphibians, animals) P80952 Belongs to the NPY family Not found Phyllomedusa bicolor (Two-colored leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows a broad spectrum of antibacterial activity against Gram-positive and Gram-negative bacteria, yeast and fungi. Tissue specificity: Skin. PTM: C-terminal amidation (By similarity)." Gram-negative bacteria: Aeromonas caviae (MIC=40 µg/ml), Escherichia coli (MIC=10 µg/ml);##Gram-positive bacteria: Enterococcus faecalis (MIC=10 µg/ml), Nocardia brasiliensis (MIC=20 µg/ml).##Fungi: Cryptococcus neoformans (MIC=20 µg/ml), Candida albicans (MIC=15 µg/ml), Microsporum canis (MIC=10 µg/ml), Tricophyton rubrum (MIC=15 µg/ml), Arthroderma simii (MIC=10 µg/ml), Aspergillus fumigatus (MIC=80 µg/ml), Aspergillus niger (MIC>100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.8601432]<20% cytotoxic against murine macrophages at the concentration up to 100μg/ml##[Ref.7937944]No cytotoxicity information found Cell membrane 7937944##8601432 Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10295-10299.##FEBS Lett. 1996 Feb 19;380(3):237-240. Mor A, Chartrel N, Vaudry H, Nicolas P.##Vouldoukis I, Shai Y, Nicolas P, Mor A. Skin peptide tyrosine-tyrosine, a member of the pancreatic polypeptide family: isolation, structure, synthesis, and endocrine activity.##Broad spectrum antibiotic activity of the skin-PYY. DRAMP01628 GWMSKIASGIGTFLSGMQQ 19 Phylloxin (Frogs, amphibians, animals) P81565, Q9PT74 Belongs to the frog skin active peptide family (Dermaseptin subfamily) PLX Phyllomedusa bicolor (Two-colored leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Antimicrobial peptide against the Gram-positive bacteria and the Gram-negative-bacteria. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Gram-negative bacteria: Acholeplasma laidlawii A-PG8 (MIC=12.5 µM), Spiroplasma melliferum BC3 (MIC=50 µM), Rhizobium meliloti 102F34 (MIC=12.5 µM), Escherichia coli K12 (MIC=10 µM);##Gram-positive bacteria: Bacillus megaterium KM (MIC=3.12 µM), Corynebacterium glutamicum ATCC 27853 (MIC=1.56 µM), Micrococcus luteus ATCC 27853 (MIC=3.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.10632707]No cytotoxicity information found Not found 10632707 Eur J Biochem. 2000 Jan;267(2):370-378. Pierre TN, Seon AA, Amiche M, Nicolas P. Phylloxin, a novel peptide antibiotic of the dermaseptin family of antimicrobial/opioid peptide precursors. DRAMP01638 GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS 32 Dermaseptin-L1 (Frogs, amphibians, animals) No entry found Not found Not found Hylomantis lemur (Lemur leaf frog) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=8 µM).##Fungi: Batrachochytrium dendrobatidis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.17561225]Displayed cytotoxic against HepG2 cells(LC50=45μM) Not found 17561225 Toxicon. 2007 Sep 15;50(4):498-506. Conlon JM, Woodhams DC, Raza H, Coquet L, Leprince J, Jouenne T, Vaudry H, Rollins-Smith LA. Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae). DRAMP01639 GLWSTIKNVGKEAAIAAGKAALGAL 25 Dermaseptin-1 (DShypo01, DPh-1; Frogs, amphibians, animals) P84596 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiprotozoal Protein level Not found Not found "Function: Has antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. Also has antiprotozoal activity against L. amazonensis. No hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.16963159]Gram-positive bacteria: Micrococcus luteus A270 (MIC=6 µM), Staphylococcus aureus ATCC 6538 (MIC=6 µM);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=6 µM), Pseudomonas aeruginosa ATCC 14502 (MIC=6.6 µM). [Ref:16844081]Non-hemolytic activity upto 53 μM against human red blood cells;##[Ref.16963159]Non-hemolytic activity at 6 μM against erythrocytes Linear Free Amidation Free L [Ref.16844081]No cytotoxicity information found##[Ref.16963159]No cytotoxicity information found Not found 16844081##16963159 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746.##Peptides. 2006 Dec;27(12):3092-3099. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr.##Conceição K, Konno K, Richardson M, Antoniazzi MM, Jared C, Daffre S, Camargo AC, Pimenta DC. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia).##Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis. DRAMP01643 GLWSTIKQKGKEAAIAAAKAAGQAALGAL 29 Dermaseptin-5 (DShypo05, DS 01; Frogs, amphibians, animals) P84600 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiprotozoal Protein level Not found Not found "Function: Has antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. Also has antiprotozoal activity against L. amazonensis. No hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Ref.8306981]Gram-negative bacterium: Escherichia coli (MIC=6.4 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=3.2 µM). [Ref:8306981]Non-hemolytic activity against rabbit red blood cells. Linear Free Amidation Free L [Ref.12379643]No cytotoxicity information found##[Ref.17442605]No cytotoxicity information found Not found 12379643##17442605 J Biol Chem. 2002 Dec 20;277(51):49332-49340. ##Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):336-343. Brand GD, Leite JR, Silva LP, Albuquerque S, Prates MV, Azevedo RB, Carregaro V, Silva JS, Sá VC, Brandão RA, Bloch C Jr. ##Leite JRSA, Brand GD, Silva LP, Kückelhaus SAS, Bento WRC, Araújo ALT, Martins GR, Lazzari AM, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. ##Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity. DRAMP01646 GLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAV 33 Adenoregulin (Dermaseptin BII; Dermaseptin B2; Frogs, amphibians, animals) P31107, P80283 Belongs to the frog skin active peptide family (Dermaseptin subfamily) ADR Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Fountion: Enhances binding of agonists to adenosine A1 receptors, adenosine A2a receptors, alpha-2 adrenergic receptors and 5-hydroxytryptamine 1A receptors. Enhances guanyl nucleotide exchange which may result in the conversion of receptors to a high affinity state complexed with guanyl nucleotide free G-protein. Affects human behavior eliciting profound malaise, followed by listlessness and then euphoria. Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Lack hemolytic activity. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation at V33 (Amidation in vitro increases antimicrobial activity against some microorganisms such as T. album and S. cerevisia)." [Ref.8306981]Fungi: Microsporum canis (IP 1194) (MIC=10 µg/ml), Tricophyton rubrum (IP 1400-82) (MIC=15 µg/ml), Arthroderma simii (IP 1063-74) (MIC=30 µg/ml), Aspergillus fumigatus IP (1025-70) (MIC=125 µg/ml), Aerornonas caviae (IP 67-16 T) (MIC=60 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neoformans (IP 962-67) (MIC=15 µg/ml), Candida albicans (IP 884-65) (MIC=15 µg/ml);##Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=15 µg/ml);##Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=30 µg/ml). [Ref:8306981]Lack hemolytic activity against rabbit red blood cells Linear Free Free Free L [Ref.8306981]No cytotoxicity information found##[Ref.1438301]No cytotoxicity information found##[Ref.7842473]No cytotoxicity information found##[Ref.8565049]No cytotoxicity information found Not found 8306981##1438301##7842473##8565049 Eur J Biochem 1994, 219 (1-2):145-154.##Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10960-10963.##Cell Mol Neurobiol. 1994 Apr;14(2):133-157.##Cell Mol Neurobiol. 1995 Aug;15(4):465-493. Mor, A, Nicolas, P.##Daly JW, Caceres J, Moni RW, Gusovsky F, Moos M Jr, Seamon KB, Milton K, Myers CW.##Shin Y, Moni RW, Lueders JE, Daly JW.##Moni RW, Romero FS, Daly JW. Isolation and structure of novel defensive peptides from frog skin.##Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor.##Effects of the amphiphilic peptides mastoparan and adenoregulin on receptor binding, G proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx.##The amphiphilic peptide adenoregulin enhances agonist binding to A1-adenosine receptors and [35S]GTP gamma S to brain membranes. DRAMP01647 FLSLIPHIVSGVAALAKHLG 20 DRP-PBN1 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa bicolor Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: S. aureus (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.15222751]No cytotoxicity information found Not found 15222751 Biochemistry. 2004 Jul 6;43(26):8391-8409. Vanhoye D, Bruston F, El Amri S, Ladram A, Amiche M, Nicolas P. Membrane association, electrostatic sequestration, and cytotoxicity of Gly-Leu-rich peptide orthologs with differing functions. DRAMP01648 GLVTSLIKGAGKLLGGLFGSVTGGQS 26 Dermaseptin-like PBN2 (DRP-PBN2; Plasticin-B1a; Frogs, amphibians, animals) Q800R4 Not found Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Possesses a potent antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and fungi. Probably acts by disturbing membrane functions with its amphipathic structure. Gram-negative bacteria: Escherichia coli B (MIC=1.5 µM), Salmonella typhimurium (MIC=3.1 µM), Salmonella enteritidis (MIC=1.5 µM), Enterobacter cloacae (MIC=12.5 µM), Klebsiella pneumoniae (MIC=0.8 µM);##Gram-positive bacteria: Aerococcus viridans (MIC=3.1 µM), Bacillus megaterium (MIC=0.8 µM), Staphylococcus aureus (MIC=3.1 µM), Staphylococcus haemolyticus (MIC=0.8 µM).##Fungi: Saccaromyces cerevisiae (MIC=3.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.12709067]No cytotoxicity information found##[Ref.15222751]No cytotoxicity information found Not found 12709067##15222751 Eur J Biochem. 2003 May;270(9):2068-2081.##Biochemistry. 2004 Jul 6;43(26):8391-8409. Vanhoye D, Bruston F, Nicolas P, Amiche M.##Vanhoye D, Bruston F, El Amri S, Ladram A, Amiche M, Nicolas P. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.##Membrane association, electrostatic sequestration, and cytotoxicity of Gly-Leu-rich peptide orthologs with differing functions. DRAMP01649 AMWKDVLKKIGTVALHAGKAALGAVADTISQ 31 Dermaseptin-BI (Dermaseptin B1; Frogs, amphibians, animals) P80282 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation (Potential)." Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=15 µg/ml);##Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=30 µg/ml).##Fungi: Tricophyton rubrum (IP 1400-82) (MIC=15 µg/ml), Microsporum canis (IP 1194) (MIC=10µg/ml), Arthroderma simii (IP 1063-74) (MIC=30 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neofonnans (IP 962-67) (MIC=15 µg/ml), Aspergillus fumigatus (IP 1025-70)(MIC=125 µg/ml), Aerornonas caviae (IP 67-16 T) (MIC=60 µg/ml), Candida albicans (IP 884-65) (MIC=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.8306981]No cytotoxicity information found##[Ref.8074751]No cytotoxicity information found Not found 8306981##8074751 Eur J Biochem. 1994 Jan 15;219(1-2):145-154.##J Biol Chem. 1994 Jul 8;269(27):17847-17852. Mor A, Nicolas P.##Amiche M, Ducancel F, Mor A, Boulain JC, Menez A, Nicolas P. Isolation and structure of novel defensive peptides from frog skin.##Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins. DRAMP01650 ALWKNMLKGIGKLAGQAALGAVKTLVGAE 29 Dermaseptin-B3 (Dermaseptin BIII; Frogs, amphibians, animals) P81485 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Possesses a potent antimicrobial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands." Gram-negative bacteria: Pseudomonas aeruginosa CIP A22 (MIC=2.3 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=5 µM), Escherichia coli ATCC 25922 (MIC=2.6 µM), E. coli 54127 (MIC=2.3 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25293 (MIC=1.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.9614066]No cytotoxicity information found Not found 9614066 J Biol Chem. 1998 Jun 12;273(24):14690-14697. Charpentier S, Amiche M, Mester J, Vouille V, Le Caer JP, Nicolas P, Delfour A. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. DRAMP01651 ALWKDILKNVGKAAGKAVLNTVTDMVNQ 28 Dermaseptin-B4 (Dermaseptin BIV; Frogs, amphibians, animals) P81486 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Possesses a potent antimicrobial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus ATCC 25293 (MIC=1.3 µM), S. aureus ATCC 25923 (MIC=3.0 µM);##Gram-negative bacteria: Pseudomonas aeruginosa CIP A22 (MIC=4.6 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=11.6 µM), Escherichia coli ATCC 25922 (MIC=5.0 µM), E. coli 54127 (MIC=2.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.9614066]No cytotoxicity information found Not found 9614066 J Biol Chem. 1998 Jun 12;273(24):14690-14697. Charpentier S, Amiche M, Mester J, Vouille V, Le Caer JP, Nicolas P, Delfour A. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. DRAMP01657 ALWKTIIKGAGKMIGSLAKNLLGSQAQPES 30 Dermaseptin DRG3 (Dermaseptin-3; Frogs, amphibians, animals) P81488, Q90ZK4 Belongs to the frog skin active peptide family (Dermaseptin subfamily) DRG3 Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial Transcript level Not found Not found MOA: This peptide is membranotropic and it efficiently depolarizes the plasma membrane. Several species of mollicutes (MIC=6.25-100 µM), firmicutes (MIC=6.25-100 µM), gracilicutes (MIC=6.25-100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.9540838] No cytotoxicity information found Not found 9540838 Biochim Biophys Acta. 1998 Mar 9;1396(2):228-236. Fleury Y, Vouille V, Beven L, Amiche M, Wróblewski H, Delfour A, Nicolas P. Synthesis, antimicrobial activity and gene structure of a novel member of the dermaseptin B family. DRAMP01668 ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ 34 Dermaseptin-1 (DS I; Dermaseptin-S1, DS1; Frogs, amphibians, animals) P24302, P80277 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix (CD) Not found "Function: Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. This peptide could also inhibit HIV infection at a concentration that is also toxic to T cells (J Virol 2005; 79:11598-11606). Tissue specificity: Expressed by the skin glands." Fungi: Microsporum canis (IP 1194) (MIC=50 µg/ml), Tricophyton rubrum (IP 1400-82) (MIC=100 µg/ml), Arthroderma simii (IP 1063-74) (MIC=100 µg/ml), Aspergillus fumigatus (IP 1025-70) (MIC=100 µg/ml), Aerornonas caviae IP (67-16) T (MIC=50 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neoformans (IP 962-67) (MIC=15 µg/ml), Candida albicans (IP 884-65) (MIC=60 µg/ml); ##Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=5 µg/ml);##Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=200 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.1909573]No cytotoxicity information found##[Ref.8306981]No cytotoxicity information found Cell membrane 1909573##8306981 Biochemistry. 1991 Sep 10;30(36):8824-8830.##Eur J Biochem. 1994 Jan 15;219(1-2):145-154. Mor A, Nguyen VH, Delfour A, Migliore-Samour D, Nicolas P.##Mor A, Nicolas P. Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.##Isolation and structure of novel defensive peptides from frog skin. DRAMP18386 SPKKTKPVKPKKVA 14 VK25 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 3.2 uM) and S. aureus ATCC 25923 (EC50 2.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML. Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP18387 KAAAAKKSPKKPKKPAAAKK 20 VK14 (histone derived;reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 0.6 uM) and S. aureus ATCC 25923 (EC50 1.2 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP18388 AAGGVKKPKKAAAAKKSPKKPKKPAAA 27 VK13 (histone derived; reptiles; animals) No entry found Not found Not found blood plasma, Komodo dragon, Varanus komodoensis Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against P. eruginosa ATCC9027 (EC50 0.9 uM) and S. aureus ATCC 25923 (EC50 1.0 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28164707]No cytotoxicity information found Not found 28164707 J Proteome Res. 2017 Apr 7;16(4):1470-1482. Bishop BM, Juba ML, Russo PS, Devine M, Barksdale SM, Scott S, Settlage R, Michalak P, Gupta K, Vliet K, Schnur JM, van Hoek ML Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo-Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry DRAMP18385 KKSCHTGLKKSAGWVIPIGTLVKNGIIVR 29 cOT2 (reptiles; animals) No entry found Not found Not found Siamese crocodile, Crocodylus siamensis Antimicrobial, Antibacterial Helix Not found Comment: No comments found on DRAMP database Active against E. coli ATCC 25922 (MIC 32 uM), V. cholerae (MIC 8 uM), Gram+ B. megaterium (MIC 8 uM) and B. pumilus TISTR 905 (MIC 16 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28159460]No cytotoxicity information found Not found 28159460 Biochim Biophys Acta Biomembr. 2017 May;1859(5):860-869. Prajanban BO, Jangpromma N, Araki T, Klaynongsruang S Antimicrobial effects of novel peptides cOT2 and sOT3 derived from Crocodylus siamensis and Pelodiscus sinensis ovotransferrins DRAMP01702 GLWSTIKNVGKEAAIAAGKAVLGSL 25 Dermaseptin-H5 (Dermaseptin-like peptide 5, DMS5; Frogs, amphibians, animals) Q1EJP4 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). Gram-negative bacterium: Escherichia coliEscherichia coli ATCC 11775 (MIC=0.5 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 12600 (MIC=0.5 µM), Micrococcus luteus ATCC 49732 (MIC=2.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17553595]No cytotoxicity information found Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01721 HFLGKLVNLAKKIL 14 [T5k]temporin-DRa (Frogs, amphibians, animals) No entry found Not found Not found Rana draytonii Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database Clinical isolates: Propionibacterium acnes strain ATCC 11828 (MIC=6 µM), P. acnes strain 32548 (MIC=6 µM), P. acnes strain 33257 (MIC=12.5 µM), P. acnes strain 50247 (MIC=3 µM), P. acnes strain 18380 (MIC=12.5 µM), P. acnes strain 15725 (MIC=6 µM), P. acnes strain 29903 (MIC=12.5 µM), P. acnes strain 31766 (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free Mixed (5D-Lys) [Ref.22374306]No cytotoxicity information found Not found 22374306 Peptides. 2012 Apr;34(2):275-282. Popovic S, Urbán E, Lukic M, Conlon JM. Peptides with antimicrobial and anti-inflammatory activities that have therapeutic potential for treatment of acne vulgaris. DRAMP02230 GFLDIINKLGKTFAGHMLDKIKCTIGTCPPSP 32 Ranatuerin-3 (Frogs, amphibians, animals) P82780 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found Function: Antibacterial activity against Gram-positive bacterium S.aureus. Has no detectable hemolytic activity. [Ref.9784389] Gram-positive bacterium: Staphylococcus aureus (MIC=60 µM). [Ref.9784389] Have no detectable hemolytic activity at aconcentration of 20µg/ml against human red blood cell. Cyclic Free Free Disulfide bridge between Cys23 and Cys28. L [Ref.9784389]No cytotoxicity information found Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02231 FLPFIARLAAKVFPSIICSVTKKC 24 Ranatuerin-4 (Frogs, amphibians, animals) P82819 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found Function: Antibacterial activity against Gram-positive bacterium S.aureus. Has no detectable hemolytic activity. [Ref.9784389] Gram-positive bacterium: Staphylococcus aureus (MIC=55 µM). [Ref.9784389] Have no detectable hemolytic activity at aconcentration of 20µg/ml against human red blood cell. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bridge between Cys18 and Cys24. L [Ref.9784389]No cytotoxicity information found Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP01731 FLPIAGKLLSGLSGLL 16 Temporin-ALd (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALd exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=1.25 µg/mL), Bacillus pumilus (MIC=2.5 µg/mL), Bacillus cereus (MIC=15 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=1.25 µg/mL), Bacillus dysenteriae (MIC=5 µg/mL), Acinetobacter calcoaceticus (MIC=15 µg/mL), Psecdomonas aeruginosa (MIC=5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=1.25 µg/mL). [Ref:19843479]12% hemolytic activity at 100 μg/mL against rabbit red blood cells Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01732 FFPIVGKLLFGLSGLL 16 Temporin-ALe (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALe exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=1.25 µg/mL), Bacillus pumilus (MIC=5 µg/mL), Bacillus cereus (MIC=15 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=1.25 µg/mL), Bacillus dysenteriae (MIC=5 µg/mL), Acinetobacter calcoaceticus (MIC=15 µg/mL), Psecdomonas aeruginosa (MIC=5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=1.25 µg/mL). [Ref:19843479]10% hemolytic activity at 100 μg/mL against rabbit red blood cells Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01733 FFPIVGKLLSGLSGLL 16 Temporin-ALf (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALf exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=2.5 µg/mL), Bacillus pumilus (MIC=5 µg/mL), Bacillus cereus (MIC=30 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=2.5 µg/mL), Bacillus dysenteriae (MIC=5 µg/mL), Acinetobacter calcoaceticus (MIC=30 µg/mL), Psecdomonas aeruginosa (MIC=5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=2.5 µg/mL). [Ref:19843479]7% hemolytic activity at 100 μg/mL against rabbit red blood cells. Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01734 FFPIVGKLLFGLFGLL 16 Temporin-ALg (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALg exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=2.5 µg/mL), Bacillus pumilus (MIC=2.5 µg/mL), Bacillus cereus (MIC=30 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=5 µg/mL), Bacillus dysenteriae (MIC=10 µg/mL), Acinetobacter calcoaceticus (MIC=30 µg/mL), Psecdomonas aeruginosa (MIC=7.5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=1.25 µg/mL). [Ref:19843479]16% hemolytic activity at 100 μg/mL against rabbit red blood cells. Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01735 FLPIVGKLLSGLSGLS 16 Temporin-ALh (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALh exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=2.5 µg/mL), Bacillus pumilus (MIC=7.5 µg/mL), Bacillus cereus (MIC=75 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=5 µg/mL), Bacillus dysenteriae (MIC=20 µg/mL), Acinetobacter calcoaceticus (MIC=60 µg/mL), Psecdomonas aeruginosa (MIC=2.5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=2.5 µg/mL). [Ref:19843479]13% hemolytic activity at 100 μg/mL against rabbit red blood cells. Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01736 FFPIVGKLLSGLL 13 Temporin-ALi (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALi exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=7.5 µg/mL), Bacillus pumilus (MIC=7.5 µg/mL), Bacillus cereus (MIC=75 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=7.5 µg/mL), Bacillus dysenteriae (MIC=20 µg/mL), Acinetobacter calcoaceticus (MIC=60 µg/mL), Psecdomonas aeruginosa (MIC=5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=5 µg/mL). [Ref:19843479]21% hemolytic activity at 100 μg/mL against rabbit red blood cells Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01737 FFPIVGKLLFGLL 13 Temporin-ALj (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALg exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=7.5 µg/mL), Bacillus pumilus (MIC=15 µg/mL), Bacillus cereus (MIC=75 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=15 µg/mL), Bacillus dysenteriae (MIC=30 µg/mL), Acinetobacter calcoaceticus (MIC=60 µg/mL), Psecdomonas aeruginosa (MIC=7.5 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=5 µg/mL). [Ref:19843479]19% hemolytic activity at 100 μg/mL against rabbit red blood cells. Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01738 FFPIVGKLLS 10 Temporin-ALk (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops loloensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Temporin-ALk exhibits hemolytic activity against rabbit red blood cells. [Ref.19843479]Gram-positive bacterium: Staphylococcus aureus ATCC2592 (MIC=15 µg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=30 µg/mL), Bacillus dysenteriae (MIC=60 µg/mL), Acinetobacter calcoaceticus (MIC=75 µg/mL), Psecdomonas aeruginosa (MIC=25 µg/mL);##Yeast: Candida albicans ATCC2002 (MIC=15 µg/mL). [Ref:19843479]25% hemolytic activity at 100 μg/mL against rabbit red blood cells. Linear Free Amidation Free L [Ref.19843479]No cytotoxicity information found Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP02229 GLFLDTLKGAAKDVAGKLEGLKCKITGCKLP 31 Ranatuerin-2 (Frogs, amphibians, animals) P82742 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found Function: Antibacterial activity against Gram-positive bacterium S.aureus. Has no detectable hemolytic activity. [Ref.9784389] Gram-positive bacterium: Staphylococcus aureus (MIC=60 µM). [Ref.9784389] It has no detectable hemolytic activity at aconcentration of 20µg/ml against human red blood cell. Cyclic Free Free Disulfide bond between Cys23 and Cys28. L No cytotoxicity information found Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP01750 FLPLVGKILSGLI 13 Temporin-1PLa (Frogs, amphibians, animals) A7WNV7 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Antimicrobial activity against the Gram-positive bacteria: S. aureus. Tissue specificity: Expressed by the skin glands. PTM: Isoleucine amide at position 13. Gram-positive bacterium: Staphylococcus aureus (MIC=70 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.11087945]No cytotoxicity information found Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01751 FLPGLIAGIAKML 13 Temporin-LT1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Temporin-LT1 shows hemolytic activities against rabbit red blood cells (LD50>100 µg/ml). [Ref.19340924]Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 µM), Bacillus subtilis (MIC=25 µM). [Ref:19340924]LD50>100 µg/ml against rabbit red blood cells Linear Free Amidation Free L [Ref.19340924]No cytotoxicity information found Not found 19340924 Biochimie. 2009 Apr;91(4):540-547. Wang H, Yan X, Yu H, Hu Y, Yu Z, Zheng H, Chen Z, Zhang Z, Liu J. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae). DRAMP01752 FLPIALKALGSIFPKIL 17 Temporin-LT2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Temporin-LT2 shows hemolytic activities against rabbit red blood cells (LD50>200 µg/ml). [Ref.19340924]Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 µM), Bacillus subtilis (MIC=50 µM). [Ref:19340924]LD50>200 µg/ml against rabbit red blood cells Linear Free Amidation Free L [Ref.19340924]No cytotoxicity information found Not found 19340924 Biochimie. 2009 Apr;91(4):540-547. Wang H, Yan X, Yu H, Hu Y, Yu Z, Zheng H, Chen Z, Zhang Z, Liu J. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae). DRAMP01753 FVDLKKIANIINSIFGK 17 Temporin-1CEa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix Not found Function: Temporin-1CEa exhibits the greatest ability to inhibit the growth of MCF-7 cells. Also temporin-1CEa shows hemolytic effect to human erythrocytes and has no significant cytotoxicity to normal HUVSMCs at concentrations showed potent antitumor activity. [Ref.21871946]Gram-positive bacteria: Staphylococcus aureus (MIC=14.4 µM), Bacillus cereus (MIC=14.4 µM), Streptococcus lactis (MIC=14.4 µM);##Gram-negative bacterium: Escherichia coli (MIC>100 µM). [Ref:21871946]LD50=99.08 μM against human erythrocytes Linear Free Amidation Free L [Ref.19341344]No cytotoxicity information found##[Ref.21871946]No determined cytotoxic against SMCs at the concentration between 20-60 μM. Not found 21871946##19341344 Biochimie. 2012 Feb;94(2):434-441.##Zoolog Sci. 2009 Mar;26(3):220-226. Wang C, Li HB, Li S, Tian LL, Shang DJ.##Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Antitumor effects and cell selectivity of temporin-1CEa, an antimicrobial peptide from the skin secretions of the Chinese brown frog (Rana chensinensis).##Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01754 ILPILSLIGGLLGK 14 Temporin-1CEb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (MIC=41 µM), Bacillus cereus (MIC=41 µM), Streptococcus lactis (MIC=41 µM);##Gram-negative bacterium: Escherichia coli (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19341344]No cytotoxicity information found Not found 19341344 Zoolog Sci. 2009 Mar;26(3):220-226. Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01755 FLGALAKIISGIF 13 Temporin-1TSa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana tsushimensis (Tsushima brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=4 µM);##Gram-negative bacterium: Escherichia coli (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16413829]No cytotoxicity information found Not found 16413829 Comp Biochem Physiol C Toxicol Pharmacol. 2006 May;143(1):42-49. Conlon JM, Al-Ghaferi N, Abraham B, Sonnevend A, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis. DRAMP01759 FLSAITSLLGKLL 13 Temporin-1SPb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.15556063]No cytotoxicity information found Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP01764 FLPILGKLLSGIL 13 Temporin-1TGa (Frogs, amphibians, animals) Q2PGA8 Belongs to the frog skin active peptide family (Brevinin subfamily) tmpTGa Rana tagoi (Tago frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=15 µM);##Gram-negative bacterium: Escherichia coli (MIC>100 µM).##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.12804591]No cytotoxicity information found##[Ref.16675060]No cytotoxicity information found Not found 12804591##16675060 Biochem Biophys Res Commun. 2003 Jun 27;306(2):496-500.##Peptides. 2006 Sep;27(9):2124-2128. Conlon JM, Sonnevend A, Patel M, Camasamudram V, Nowotny N, Zilahi E, Iwamuro S, Nielsen PF, Pál T.##Iwamuro S, Nakamura M, Ohnuma A, Conlon JM. A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties.##Molecular cloning and sequence analyses of preprotemporin mRNAs containing premature stop codons from extradermal tissues of Rana tagoi. DRAMP01765 AVDLAKIANKVLSSLF 16 Temporin-1TGb (Frogs, amphibians, animals) Q2PGA7 Belongs to the frog skin active peptide family (Brevinin subfamily) tmpTGb Rana tagoi (Tago frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC>150 µM);##Gram-negative bacterium: Escherichia coli (MIC=37.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16675060]No cytotoxicity information found Not found 16675060 Peptides. 2006 Sep;27(9):2124-2128. Iwamuro S, Nakamura M, Ohnuma A, Conlon JM. Molecular cloning and sequence analyses of preprotemporin mRNAs containing premature stop codons from extradermal tissues of Rana tagoi. DRAMP01766 FLPVILPVIGKLLSGIL 17 Temporin-1TGc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana tagoi (Tago's brown frog); also Rana sakuraii Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=37.5 µM);##Gram-negative bacterium: Escherichia coli (MIC>150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16675060]No cytotoxicity information found Not found 16675060 Peptides. 2006 Sep;27(9):2124-2128. Iwamuro S, Nakamura M, Ohnuma A, Conlon JM. Molecular cloning and sequence analyses of preprotemporin mRNAs containing premature stop codons from extradermal tissues of Rana tagoi. DRAMP01768 FLPVILPVIGKLLNGIL 17 Temporin-1SKa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sakuraii (stream brown frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC>50 µM);##Gram-negative bacteria: Staphylococcus aureus (MIC=25 µM).##Fungi: Candida albicans (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17174009]No cytotoxicity information found Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP18384 KKSCHTGLDRSAGWVIPIGTLVKKAILPWDRK 32 sOT2 (reptiles; animals) No entry found Not found Not found Chinese softshell turtle, Pelodiscus sinensis Antimicrobial, Antibacterial Helix Not found Comment: No comments found on DRAMP database Active against E. coli ATCC 25922 (MIC 28 uM), V. cholerae (MIC 7 uM), Gram+ B. megaterium (MIC 7 uM) and B. pumilus TISTR 905 (MIC 7 uM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L [Ref.28159460]No cytotoxicity information found Not found 28159460 Biochim Biophys Acta Biomembr. 2017 May;1859(5):860-869. Prajanban BO, Jangpromma N, Araki T, Klaynongsruang S Antimicrobial effects of novel peptides cOT2 and sOT2 derived from Crocodylus siamensis and Pelodiscus sinensis ovotransferrins DRAMP01771 FLPLLASLFSRLL 13 Temporin-1Oa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=70 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17147973]No cytotoxicity information found Not found 17147973 Peptides. 2007 Mar;28(3):524-532. Ohnuma A, Conlon JM, Yamaguchi K, Kawasaki H, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Japanese mountain brown frog Rana ornativentris: evidence for polymorphism among preprotemporin mRNAs. DRAMP01773 FLPLLASLFSRLF 13 Temporin-1Oc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17147973]No cytotoxicity information found Not found 17147973 Peptides. 2007 Mar;28(3):524-532. Ohnuma A, Conlon JM, Yamaguchi K, Kawasaki H, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Japanese mountain brown frog Rana ornativentris: evidence for polymorphism among preprotemporin mRNAs. DRAMP01775 FLSGIVGMLGKLFGK 15 Temporin-1Sa (Frogs, amphibians, animals) B3KYH4 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-1Sa Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Activity against Gram-positive and Gram-negative bacteria, and has hemolytic activity against human erythrocytes. [Ref.18584916]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=3 µM), Enterococcus faecalis ATCC 29212 (MIC=10 µM), Bacillus megaterium (MIC=2 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10 µM), Escherichia coli ATCC 35218 (MIC=10 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=31 µM);##Fungi: Candida albicans ATCC 90028 (MIC=16 µM), Candida parapsilosis ATCC 22019 (MIC=31 µM), Saccharomyces cerevisiae (MIC=8 µM). [Ref:18584916]LC50=25 μM against human erythrocytes Linear Free Amidation Free L [Ref.18584916]No cytotoxicity information found Not found 18584916 Peptides. 2008 Sep;29(9):1526-1523. Abbassi F, Oury B, Blasco T, Sereno D, Bolbach G, Nicolas P, Hani K, Amiche M, Ladram A Isolation, characterization and molecular cloning of new temporins from the skin of the North African ranid Pelophylax saharica. DRAMP01776 FLPIVTNLLSGLLGK 15 Temporin-1Sb (Temporin-SHb; Frogs, amphibians, animals) B3KYH5 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-1Sb Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Activity against Gram-positive and Gram-negative bacteria, and has strong hemolytic activity against human erythrocytes. [Ref.18584916]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=58 µM), Enterococcus faecalis ATCC 29212 (MIC>116 µM), Bacillus megaterium (MIC=46 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=231 µM), Escherichia coli ATCC 35218 (MIC>116 µM);##Fungi: Aspergillus flavus (MIC=58 µM). [Ref:18584916]LC50>116 μM against human erythrocytes Linear Free Amidation Free L [Ref.18584916]No cytotoxicity information found Not found 18584916 Peptides. 2008 Sep;29(9):1526-1523. Abbassi F, Oury B, Blasco T, Sereno D, Bolbach G, Nicolas P, Hani K, Amiche M, Ladram A Isolation, characterization and molecular cloning of new temporins from the skin of the North African ranid Pelophylax saharica. DRAMP01777 FLSHIAGFLSNLFGK 15 Temporin-1Sc (Temporin-SHc; Frogs, amphibians, animals) B3KYH6 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-1Sc Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Alpha helix Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria, and has hemolytic activity against human erythrocytes. [Ref.18584916]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=10 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>80 µg/ml), Bacillus megaterium (MIC=4 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=161 µg/ml), Escherichia coli ATCC 35218 (MIC>80 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC>161 µg/ml);##Fungi: Aspergillus flavus (MIC=10 µg/ml), Candida albicans ATCC 90028 (MIC=20 µg/ml), Candida parapsilosis ATCC 22019 (MIC=20 µg/ml), Saccharomyces cerevisiae (MIC=10 µg/ml). [Ref:18584916]LC50>80 μM against human erythrocytes Linear Free Amidation Free L [Ref.18584916]No cytotoxicity information found Not found 18584916 Peptides. 2008 Sep;29(9):1526-1523. Abbassi F, Oury B, Blasco T, Sereno D, Bolbach G, Nicolas P, Hani K, Amiche M, Ladram A Isolation, characterization and molecular cloning of new temporins from the skin of the North African ranid Pelophylax saharica. DRAMP01779 FFFLSRIFGK 10 Temporin-SHf (Frogs, amphibians, animals) D4YWD1 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-SHf Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 µM);##Gram-negative bacterium: Escherichia coli (MIC=25-200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.20308076]No cytotoxicity information found Not found 20308076 J Biol Chem. 2010 May 28;285(22):16880-16892. Abbassi F, Lequin O, Piesse C, Goasdoue N, Foulon T, Nicolas P, Ladram A. Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide. DRAMP01780 FLSGIVGMLGKLF 13 Temporin-SHa (Temporin-1Sa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax saharica (North Africa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (MIC=3 µM), Bacillus megaterium (MIC=2 µM);##Gram-negative bacterium: Escherichia coli (MIC=10 µM).##Yeast: Candida albicans (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.31614561]Display cytotoxic against human gastric cells(N87 cell:IC50=1558 ± 324μM) Not found 31614561 Biomolecules. 2019 Oct 11;9(10):598. Olleik H, Baydoun E, Perrier J, Hijazi A, Raymond J, Manzoni M, Dupuis L, Pauleau G, Goudard Y, Villéon B, Goin G, Sockeel P, Choudhary MI, Pasquale ED, Nadeem-Ul-Haque M, Ali H, Khan AI, Shaheen F, Maresca M. Temporin-SHa and Its Analogs as Potential Candidates for the Treatment of Helicobacter pylori. DRAMP01782 FFPLVLGALGSILPKIF 17 Temporin-LTa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (MIC=20 µg/ml) and Bacillus subtilis (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19022312]No cytotoxicity information found Cell membrance 19022312 Peptides. 2009 Feb;30(2):273-282. Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). DRAMP01783 FIITGLVRGLTKLF 14 Temporin-LTb (Frogs, amphibians, animals) B9UYA1 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+ Homology Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 µg/ml) and Bacillus subtilis (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19022312]No cytotoxicity information found Cell membrance 19022312 Peptides. 2009 Feb;30(2):273-282. Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). DRAMP01784 SLSRFLSFLKIVYPPAF 17 Temporin-LTc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Not found Not found Not found Comment: A mutant of the peptide is also HIV inhibitory (Wang G et al. 2010 Antimicrob. Agents Chemother. 54: 1343-1346). Gram-positive bacteria: Staphylococcus aureus (MIC=50 µg/ml), Bacillus subtilis (MIC=50 µg/ml);##Gram-negative bacterium: Pseudomonas fluorescens (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19022312]No cytotoxicity information found Not found 19022312 Peptides. 2009 Feb;30(2):273-282. Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). DRAMP01785 IPPFIKKVLTTVF 13 Temporin-CPa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (New World frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: For this series of peptides, there were not enough material for antimicrobial assays. It displayed hemolytic activity (human red blood cells) at LC50=220 uM. [Ref.19635516]Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=50 µM);##Yeast: Candida albicans ATCC 90028 (MIC=25 µM). [Ref:19635516]LC50=220 μM against human erythrocytes Linear Free Amidation Free L [Ref.19635516]No cytotoxicity information found Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP01787 AILTTLANWARKFL 14 Temporin-HN1 (Frogs, amphibians, animals) E7EKD0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Hainan odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has hemolytic activity against washed human erythrocytes (IC50=75 µM). [Ref.22450466]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=37.5 µM), Staphylococcus carnosus KHS (MIC=37.5 µM), Bacillus licheniformis X39 (MIC=19 µM), Rhodococcus rhodochrous X15 (MIC=4.8 µM);##Gram-negative bacteria: Psychrobacter faecalis X29 (MIC=75 µM);##Fungi: Slime mould 090223 (MIC=19 µM), Candida albicans ATCC2002 (MIC=75 µM). [Ref:22450466]IC50=75 µM against washed human erythrocytes Linear Free Amidation Free L [Ref.22450466]No cytotoxicity information found Not found 22450466 Peptides. 2012 Jun;35(2):285-290. Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP01788 NILNTIINLAKKIL 14 Temporin-HN2 (Frogs, amphibians, animals) E7EKD4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Hainan odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=4.8 µM), Staphylococcus carnosus KHS (MIC=19 µM), Bacillus licheniformis X39 (MIC=19 µM),Rhodococcus rhodochrous X15 (MIC=2.4 µM);##Gram-negative bacterium: Psychrobacter faecalis X29 (MIC=37.5 µM).##Fungi: Slime mould 090223 (MIC=9.5 µM) and Candida albicans ATCC2002 (MIC=9.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.22450466]No cytotoxicity information found Not found 22450466 Peptides. 2012 Jun;35(2):285-290. Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP01789 FLSSIGKILGNLL 13 Temporin-1Va (Temporin 1Va; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana virgatipes (Ranidae) (Aquarana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: It also has weak hemolytic activty. [Ref.15996769]Gram-positive bacteria: Staphylococcus aureus NCTC8325 (MIC=10 µM), S. aureus (MRSA) T7/20 (MIC=20 µM), S. epidermidis RP62A (MIC=20 µM), Enterococcus faecalis ATCC 29212 (MIC=40 µM), Streptococcus group B HNTCC 80130 (MIC=20 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=40 µM), Klebsiella pneumoniae KK3 9904 (MIC=80 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=160 µM), Enterobacter cloacae HNTCC 53001 (MIC=40 µM);##Yeast: Candida albicans ATCC 90028 (MIC=160 µM). [Ref:15996769]LD50=120 μM against washed human erythrocytes Linear Free Amidation Free L [Ref.15996769]No cytotoxicity information found Not found 15996769 Regul Pept. 2005 Nov;131(1-3):38-45. Conlon JM, Abraham B, Sonnevend A, Jouenne T, Cosette P, Leprince J, Vaudry H, Bevier CR. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). DRAMP01790 FLSIIAKVLGSLF 13 Temporin-1Vb (Temporin 1Vb; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana virgatipes (Ranidae) (Aquarana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: It also has weak hemolytic activty. [Ref.15996769]Gram-positive bacteria: Staphylococcus aureus NCTC8325 (MIC=5 µM), S. aureus (MRSA) T7/20 (MIC=10 µM), S. epidermidis RP62A (MIC=5 µM), Enterococcus faecalis ATCC 29212 (MIC=20 µM), Streptococcus group B HNTCC 80130 (MIC=20 µM). [Ref:15996769]LD50=30 μM against washed human erythrocytes Linear Free Amidation Free L [Ref.15996769]No cytotoxicity information found Not found 15996769 Regul Pept. 2005 Nov;131(1-3):38-45. Conlon JM, Abraham B, Sonnevend A, Jouenne T, Cosette P, Leprince J, Vaudry H, Bevier CR. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). DRAMP01791 FLPLVTMLLGKLF 13 Temporin-1Vc (Temporin 1Vc; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana virgatipes (Ranidae) (Aquarana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: It also has weak hemolytic activty. [Ref.15996769]Gram-positive bacteria: Staphylococcus aureus NCTC8325 (MIC=5 µM), S. aureus (MRSA) T7/20 (MIC=10 µM), S. epidermidis RP62A (MIC=10 µM), Enterococcus faecalis ATCC 29212 (MIC=40 µM), Streptococcus group B HNTCC 80130 (MIC=40 µM);##Gram-negative bacteria: Klebsiella pneumoniae KK3 9904 (MIC=80 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=160 µM), Enterobacter cloacae HNTCC 53001 (MIC=40 µM). [Ref:15996769]LD50=30 μM against washed human erythrocytes Linear Free Amidation Free L [Ref.15996769]No cytotoxicity information found Not found 15996769 Regul Pept. 2005 Nov;131(1-3):38-45. Conlon JM, Abraham B, Sonnevend A, Jouenne T, Cosette P, Leprince J, Vaudry H, Bevier CR. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). DRAMP01807 FLPLVLGALSGILPKIL 17 Temporin-RN1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=4.69 µg/ml);##Gram-negative bacterium: Pseudomonas aeruginosa PAO1 (MIC=4.7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01808 FFPLLFGALSSHLPKLF 17 Temporin-RN3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=3.75 µg/ml);##Gram-negative bacterium: Pseudomonas aeruginosa PAO1 (MIC=3.75 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.19778602]No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01811 FLKPLFNAALKLLP 14 Temporin-Ra (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (marsh frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found At 60 ug/ml, the peptide showed about 1.3% hemolysis. Gram-negative bacteria: Escherichia coli (MIC=24.2 µg/ml), Klebsiella pneumoniae PTCC 1388 (MIC=31.2 µg/ml);##Gram-positive bacteria: Streptococcus dysgalactiae PTCC 1074 (MIC=33.2 µg/ml), Streptococcus agalactiae PTCC 1365 (MIC=24.7 µg/ml) and Staphylococcus aureus PTCC 1431 (MIC=35.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.21956830]No cytotoxicity information found Not found 21956830 J Pept Sci. 2012 Jan;18(1):10-16. Asoodeh A, Zardini HZ, Chamani J. Identification and characterization of two novel antimicrobial peptides, temporin-Ra and temporin-Rb, from skin secretions of the marsh frog (Rana ridibunda). DRAMP01812 FLPVLAGVLSRA 12 Temporin-Rb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (marsh frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found At 60 ug/ml, the peptide showed about 1.1% hemolysis. Gram-positive bacteria: Streptococcus dysgalactiae PTCC 1074 (MIC=21.8 µg/ml), Streptococcus agalactiae PTCC 1365 (MIC=30.5 µg/ml), Staphylococcus aureus PTCC 1431 (MIC=42.1 µg/ml), Staphylococcus typhimurium (MIC=31.8 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=34.5 µg/ml), Klebsiella pneumoniae PTCC 1388 (MIC=35.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.21956830]No cytotoxicity information found Not found 21956830 J Pept Sci. 2012 Jan;18(1):10-16. Asoodeh A, Zardini HZ, Chamani J. Identification and characterization of two novel antimicrobial peptides, temporin-Ra and temporin-Rb, from skin secretions of the marsh frog (Rana ridibunda). DRAMP01815 FLPLLFGAISHLL 13 Temporin-GH (AMP-5; Frogs, amphibians, animals) P84858 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana guentheri (Gunther's frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Active against the Gram-positive bacteria S. aureus FDA209P and B. subtilis ATCC 6633, but not active against the Gram-negative bacteria E. coli or the fungus C. albicans. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13." Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=44.3 µg/ml), Bacillus subtilis ATCC 6633 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.16979798]No cytotoxicity information found Not found 16979798 Peptides. 2006 Dec;27(12):3077-3084 Zhou J, McClean S, Thompson A, Zhang Y, Shaw C, Rao P, Bjourson AJ. Purification and characterization of novel antimicrobial peptides from the skin secretion of Hylarana guentheri. DRAMP01816 FLPIIGKLLSGLL 13 Temporin-1CSb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana cascadae (Cascades frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=128 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17451843]No cytotoxicity information found Not found 17451843 Peptides 2007; 28: 1268-1274. Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. DRAMP01817 FLPLVTGLLSGLL 13 Temporin-1CSc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana cascadae (Cascades frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC>128 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=64 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17451843]No cytotoxicity information found Not found 17451843 Peptides 2007; 28: 1268-1274. Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. DRAMP01818 NFLGTLVNLAKKIL 14 Temporin-1CSd (Temporin-1DRb; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana cascadae (Cascades frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=64 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.17451843]No cytotoxicity information found Not found 17451843 Peptides 2007; 28: 1268-1274. Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. DRAMP03510 KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK 37 Cecropin A P01507 cecropin Not found Hyalophora cecropia Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha-helix Not found 1D9J Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.7140755] Gram-negative bacterium: Escherichia coli D21 (LC=0.19 µM), Escherichia coli D31 (LC=0.21 µM), Serratia marcescens Db11 (LC=4.2 µM), Serratia marcescens Db1108 (LC=2.5 µM), Serratia marcescens Db1121 (LC=4.4 µM), Serratia marcescens Strain 122 (LC=3.2 µM), Pseudomonas aeruginosa OT97 (LC=4.8 µM), Xenorhabdus nematophilus Xn21 (LC=1.4 µM).##[Ref.29925795]Gram-negative bacterium:Escherichia coli CVCC 245 (MIC=4.2 ± 0.35μg/mL);##Gram-positive bacteria:Staphylococcus aureus ATCC 25923 (MIC=198 ± 10.1μg/mL),L. mono. CVCC 1599 (MIC=64.5 ± 3.20μg/mL) [Ref.29925795] 50% hemolysis at 169 ± 8.20 μg/ml against sheep red blood cells. Linear Free Amidation Free L [Ref.29925795]No cytotoxicity information found##[Ref.7140755]No cytotoxicity information found Not found 7140755##29925795 Eur J Biochem. 1982 Sep;127(1):207-217.##Molecules. 2018 Jun 20;23(6):1491. Hultmark D, Engstr?m A, Bennich H, Kapur R, Boman HG.##Wei X, Wu R, Zhang L, Ahmad B, Si D, Zhang R. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae.##Expression, Purification, and Characterization of a Novel Hybrid Peptide with Potent Antibacterial Activity DRAMP01391 GCSRWIIGIHGQICRD 16 Odorranain-U1 (OdU1; Frogs, amphibians, animals) A6MBS4 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Odorranain-U1 adopts 60.2% Function: Odorranain-U1 exhibites moderate antimicrobial activities against all of the tested microbes. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC>100 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=75.00 μg/ml), Bacillus subtilis (MIC=9.37 μg/ml).##Yeast: Candida albicans (MIC=9.37 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01832 FLPGLLAGLL 10 Temporin-Eca (Frogs, amphibians, animals) C0HJB9 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Euphlyctis cyanophlyctis (Skittering frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Has no or very limited (<3%) hemolytic activity at concentrations of 15 µg/ml and 60 µg/ml, respectively. Tissue specificity: Expressed by the skin glands." [Swiss_Prot Entry C0HJB9]Gram-negative bacteria: Escherichia coli HP101BA (MIC=12.3 µM), Klebsiella pneumoniae PTCC1388 (MIC=9.8 µM);##Gram-positive bacteria: Micrococcus luteus PTCC1625 (MIC=8.3 µM), Staphylococcus aureus PTCC1431 (MIC=10.6 µM). [Ref.Int J Pept Res Ther(2012)18;107.]<3% hemolytic activity at 60 µg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Pept. Res. Ther. 2012;18:107-115. Asoodeh A, Ghorani-Azam A, Chamani JK. Identification and characterization of novel antibacterial peptides from skin secretions of Euphlyctis cyanophlyctis. DRAMP01833 RAGLKFPVGRVHRLLR 16 Buforin-EC (Frogs, amphibians, animals) C0HJB7 Belongs to the histone H2A family Not found Euphlyctis cyanophlyctis (Skittering frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Has no or very limited (<3%) hemolytic activity at concentrations of 15 µg/ml and 60 µg/ml, respectively. Tissue specificity: Expressed by the skin glands." [Swiss_Prot Entry C0HJB7]Gram-negative bacteria: Escherichia coli HP101BA (MIC=9.6 µM), Klebsiella pneumoniae PTCC1388 (MIC=10.6 µM);##Gram-positive bacteria: Micrococcus luteus PTCC1625 (MIC=6.0 µM), Staphylococcus aureus PTCC1431 (MIC=8.1 µM). [Ref.Int J Pept Res Ther(2012)18;107.]<3% hemolytic activity at 60 µg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Pept. Res. Ther. 2012;18:107-115. Asoodeh A, Ghorani-Azam A, Chamani JK. Identification and characterization of novel antibacterial peptides from skin secretions of Euphlyctis cyanophlyctis. DRAMP01834 FLNALKNFAKTAGKRLKSLLN 21 Cyanophlyctin (Frogs, amphibians, animals) C0HJB8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Euphlyctis cyanophlyctis (Skittering frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Has no or very limited (<3%) hemolytic activity at concentrations of 15 µg/ml and 60 µg/ml. Tissue specificity: Expressed by the skin glands." [Swiss_Prot Entry C0HJB8]Gram-negative bacteria: Escherichia coli HP101BA (MIC=6.4 µM), Klebsiella pneumoniae PTCC1388 (MIC=7.3 µM);##Gram-positive bacteria: Micrococcus luteus PTCC1625 (MIC=4.7 µM), Staphylococcus aureus PTCC1431 (MIC=5.3 µM). [Ref.Int J Pept Res Ther(2012)18;107.]<3% hemolytic activity at 60 µg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Pept. Res. Ther. 2012;18:107-115. oodeh A, Ghorani-Azam A, Chamani JK. Identification and characterization of novel antibacterial peptides from skin secretions of Euphlyctis cyanophlyctis. DRAMP01840 GFRDVLKGAAKAFVKTVAGHIAN 23 Ascaphin-1 (Frogs, amphibians, animals) P0CJ25 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Has a very weak hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: Asparagine amide at position 23. [Ref.15207717]Gram-negative bacterium: Escherichia coli (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>50 µM). [Ref.15207717]HC50>200 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01842 GFRDVLKGAAKAFVKTVAGHIANI 24 Ascaphin-3 (Frogs, amphibians, animals) P0CJ27 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Has a very weak hemolytic activity. Tissue specificity: Expressed by the skin glands. [Ref.15207717]Gram-negative bacterium: Escherichia coli (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>50 µM). [Ref.15207717]HC50>200 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01844 GIKDWIKGAAKKLIKTVASNIANQ 24 Ascaphin-5 (Frogs, amphibians, animals) P0CJ29 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. [Ref.15207717]Gram-negative bacteria: Escherichia coli (MIC=6 µM), Pseudomonas aeruginosa (MIC=13 µM), Enterobacter cloacae (MIC=6 µM), Klebsiella pneumoniae (MIC=13 µM), Proteus mirabilis (MIC>100 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=50 µM), Staphylococcus epidermidis (MIC=13 µM), Enterococcus faecalis (MIC>100 µM), Streptococcus Group B (MIC=6 µM);##Yeast: Candida albicans (MIC=100 µM). [Ref.15207717]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01846 GFKDWIKGAAKKLIKTVASSIANQ 24 Ascaphin-7 (Frogs, amphibians, animals) P0CJ31 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Has a very weak hemolytic activity. Tissue specificity: Expressed by the skin glands. [Ref.15207717]Gram-negative bacterium: Escherichia coli (MIC=3 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=25 µM). [Ref.15207717]HC50>200 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01847 GFKDLLKGAAKALVKTVLF 19 Ascaphin-8 (Frogs, amphibians, animals) P0CJ32 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Not found Not found Function: Antimicrobial peptide that shows similar potency against Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: Phenylalanine amide at position 19. [Ref.15207717]Gram-negative bacterium: Escherichia coli (MIC=6 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM). [Ref.15207717]HC50=50 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01849 DSMGAVKLAKLLIDKMKCEVTKAC 24 Jindongenin-1a (JD1a; Frogs, amphibians, animals) G3ETQ2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Displays broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria. Also displays antifungal activity against C. albicans ATCC 2002. Has hemolytic activity, low cytotoxicity and low antioxidant activity. [Ref.21816202]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=17 µM), Enterococcus faecalis ATCC29212 (MIC=60 µM), Staphylococcus aureus (IS 10#)(MIC=40 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=10 µM), Enterobacter cloacae ATCC13047 (MIC=40 µM), Klebsiella pneumoniae ATCC700603 (MIC=15 µM), Bacillus pyocyaneus CMCCB1010 (MIC=17 µM), Pseudomonas aeruginosa ATCC27853 (MIC=23 µM), Bacillus dysenteriae (MIC=40 µM);##Yeast: Candida albicans ATCC2002 (MIC=60 µM). [Ref.21816202] IC50=150 μM against washed human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L [Ref.21816202] Cytotoxicity: the K562 (IC50=46μM)and HT29 mammalian cell lines(IC50=40μM). Not found 21816202 Biochimie. 2012 Feb;94(2):328-334. Chen Z, Yang X, Liu Z, Zeng L, Lee W, Zhang Y. Two novel families of antimicrobial peptides from skin secretions of the Chinese torrent frog, Amolops jingdongensis. DRAMP01869 FFPIIAGMAAKLIPSLFCKITKKC 24 Brevinin-1SPa (Frogs, amphibians, animals) No entry found Not found Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has inhibitory activity towards reference strains of bacteria and an opportunistic yeast pathogen. Also has hemolytic activity against human erythrocytes. [Ref.15556063]Gram-negative bacterium: Escherichia coli (MIC=13 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM);##Yeast: Candida albicans (MIC=7 µM). [Ref.15556063]HC50=7 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP01870 FLPIIAGMAAKVICAITKKC 20 Brevinin-1SPb (Frogs, amphibians, animals) No entry found Not found Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has inhibitory activity towards reference strains of bacteria and an opportunistic yeast pathogen. Also has hemolytic activity against human erythrocytes (HC50=6 µM). [Ref.15556063]Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=13 µM);##Yeast: Candida albicans (MIC=25 µM). [Ref.15556063]HC50=25 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP01872 FFPIIAGMAAKVICAITKKC 20 Brevinin-1SPd (Frogs, amphibians, animals) No entry found Not found Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has inhibitory activity towards reference strains of bacteria and an opportunistic yeast pathogen. Also has hemolytic activity against human erythrocytes. [Ref.15556063]Gram-negative bacterium: Escherichia coli (MIC=13 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=3 µM);##Yeast: Candida albicans (MIC=8 µM). [Ref.15556063]HC50=8 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP01873 GIWDTIKSMGKVFAGKILQNL 21 Brevinin-2-related peptide (Frogs, amphibians, animals) No entry found Not found Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found "Function: Has inhibitory activity towards reference strains of bacteria and an opportunistic yeast pathogen. Also has hemolytic activity against human erythrocytes. Sequence similarity: This peptide shows limited structural similarity with the N-terminal region of brevinin-2 peptides previously isolated from R. temporaria skin but lacks the C-terminal cyclic heptapeptide domain associated with this family. PTM: C-terminal amidation." [Ref.15556063]Gram-negative bacterium: Escherichia coli (MIC=13 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=25 µM);##Yeast: Candida albicans (MIC=70 µM). [Ref.15556063]HC50=70 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP04213 KKLFKKILKYL 11 BP100 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix The peptide adopted with positively charged residues on one face and the hydrophobic residues on the opposite face of the helix Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.29750913] Gram-negative bacteria:Escherichia coli(ATCC 25922)(MIC=2 μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=2μM);Bacillus subtilis(PY79)(MIC=2μM) [Ref.29750913] 10% hemolysis at 64μM against human red blood cell Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29750913 Biochim Biophys Acta. 2018 Aug;1860(8):1502-1516. Carretero GPB, Saraiva GKV, Cauz ACG, Rodrigues MA, Kiyota S, Riske KA, Dos Santos AA, Pinatto-Botelho MF, Bemquerer MP, Gueiros-Filho FJ, Chaimovich H, Schreier S, Cuccovia IM. Synthesis, biophysical and functional studies of two BP100 analogues modified by a hydrophobic chain and a cyclic peptide. DRAMP03571 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 LL-37 P49913,Q71SN9 Belongs to the cathelicidin family CAMP Human lysosomes of polymorphonuclear leukocytes Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Alpha helix The peptide adopted 1 helices and 30 residues and a curved amphipathic helix-bend-helix motif spanning residues 2-31 followed by a disordered C-terminal tail. The helical bend is located between residues Gly-14 and Glu-16. 2K6O resolved by NMR Function:Antibacterial activity against the Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.29859288] Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=25 ± 0 μg/ml);ESBL-producing Escherichia coli(MIC=33.3 ± 14.4μg/ml);NDM-1 producing Acinetobacter baumannii(MIC=20.8 ± 7.2 μg/ml);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=133.3 ± 57.7μg/ml);##Fungi:Candida albicans (ATCC 90028)(MIC>400μg/ml) [Ref.29859288] 2.9 ± 0.7% Hemolysis at 500μg/ml against human red blood cell Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29859288 Gene. 2018 May 30. pii: S0378-1119(18)30617-6. Wanmakok M, Orrapin S, Intorasoot A, Intorasoot S. Expression in Escherichia coli of novel recombinant hybrid antimicrobial peptide AL32-P113 with enhanced antimicrobial activity in vitro. DRAMP01748 FFPIVGKRLYGLL 13 Temporin-AJ8 (Frogs, amphibians, animals) K7Z903 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops jingdongensis (torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Shows antimicrobial abilities against microorganisms including Gram-negative and Gram-positive bacteria, and fungi. Has hemolytic activity. [Ref.22828809] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=70 μg/ml), B. dysenteriae(MIC=18.75 μg/ml) ;## Gram-positive bacteria: Staphylococcus aureus ATCC 2592(MIC=4.7 μg/ml), Bacillus subtilis ATCC 6633(MIC=9.38 μg/ml);## Yeast: Candida albicans ATCC 2002(MIC=37.5 μg/ml). [Ref.22828809] 1.79% hemolysis at 25μg/ml, 5.22% hemolysis at 50μg/ml, 7.92% hemolysis at 100μg/ml, 10.85% hemolysis at 200μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Amino Acids. 2012 Jul 25. He X, Yang S, Wei L, Liu R, Lai R, Rong M. Antimicrobial peptide diversity in the skin of the torrent frog, Amolops jingdongensis. DRAMP01879 GAFGDLLKGVAKEAGMKLLNMAQCKLSGKC 30 Brevinin-2LTa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=2 µM), Bacillus licheniformis X39 (MIC=8 µM), Staphylococcus carnosus KHS (MIC=2 µM), Rhodococcus rhodochrous X15 (MIC=0.5 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=32.5 µM), Serratia rubidaea X01 (MIC=130 µM), Pseudomonas aeruginosa 1.50 (MIC=65 µM), Psychrobacter faecalis X29 (MIC=0.5 µM). [Ref.22426384] LD50=520 μM against human erythrocytes Cyclic Free Cyclization (Cys24 and Cys30) Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01880 SILDKIKNVALGVARGAGTGILKALLCKLDKSC 33 Brevinin-2LTb (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=3.8 µM), Bacillus licheniformis X39 (MIC=3.8 µM), Staphylococcus carnosus KHS (MIC=1.9 µM), Rhodococcus rhodochrous X15 (MIC=1.9 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=30 µM), Serratia rubidaea X01 (MIC=60 µM), Pseudomonas aeruginosa 1.50 (MIC=30 µM), Psychrobacter faecalis X29 (MIC=1.9 µM). [Ref.22426384] LD50=480 μM against human erythrocytes Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01881 GVLDTFKDVAIGVAKGAGTGVLKALLCKLDKSC 33 Brevinin-2LTc (Frogs, amphibians, animals) No entry found Not found Not found Hylarana latouchii (Broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=60 µM), Rhodococcus rhodochrous X15 (MIC=30 µM);##Gram-negative bacterium: Psychrobacter faecalis X29 (MIC=15 µM). [Ref.22426384] LD50>480 μM against human erythrocytes Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01885 FFGPLIKIATGVLPNLICKALGKC 24 Brevinin-1TEa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana temporalis (Indian bronzed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Showes higher antimicrobial activity against Gram-negative than against Gram-positive bacteria. Gram-negative bacteria: E. coli (NCLM 2064) (MIC=30 µg/ml), P. aeruginosa (ATCC 10145) (MIC=150 µg/ml), V. cholerae (PL 91) (MIC=150 µg/ml);##Gram-positive bacteria: B. cereus (NCLM 2156) (MIC=100 µg/ml), S. aureus (ATCC25923) (MIC>150 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21412958 J Pept Sci. 2011 May;17(5):342-347. Reshmy V, Preeji V, Parvin A, Santhoshkumar K, George S. Three novel antimicrobial peptides from the skin of the Indian bronzed frog Hylarana temporalis (Anura: Ranidae). DRAMP01886 GIGSMLLGLAKNVGMSLLNKAQCKISGKC 29 Brevinin-2TEa (Frogs, amphibians, animals) No entry found Not found Not found Hylarana temporalis (Indian bronzed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Showes higher antimicrobial activity against Gram-negative than against Gram-positive bacteria. Gram-negative bacteria: E. coli (NCLM 2064) (MIC=40 µg/ml), P. aeruginosa (ATCC 10145) (MIC=100 µg/ml), V. cholerae (PL 91) (MIC=150 µg/ml);##Gram-positive bacteria: B. cereus (NCLM 2156) (MIC>150 µg/ml), S. aureus (ATCC25923) (MIC>150 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21412958 J Pept Sci. 2011 May;17(5):342-347. Reshmy V, Preeji V, Parvin A, Santhoshkumar K, George S. Three novel antimicrobial peptides from the skin of the Indian bronzed frog Hylarana temporalis (Anura: Ranidae). DRAMP01887 GFMGDTLKGIARNAALALMNAAQCKLSGKC 30 Brevinin-2TEb (Frogs, amphibians, animals) No entry found Not found Not found Hylarana temporalis (Indian bronzed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Showes higher antimicrobial activity against Gram-negative than against Gram-positive bacteria. Gram-negative bacteria: E. coli (NCLM 2064) (MIC=20 µg/ml), P. aeruginosa (ATCC 10145) (MIC=40 µg/ml), V. cholerae (PL 91) (MIC=60 µg/ml);##Gram-positive bacteria: B. cereus (NCLM 2156) (MIC=150 µg/ml), S. aureus (ATCC25923) (MIC=40 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21412958 J Pept Sci. 2011 May;17(5):342-347. Reshmy V, Preeji V, Parvin A, Santhoshkumar K, George S. Three novel antimicrobial peptides from the skin of the Indian bronzed frog Hylarana temporalis (Anura: Ranidae). DRAMP01888 FFPTIAGLTKLFCAITKKC 19 Brevinin-1CHc (Frogs, amphibians, animals) No entry found Not found Not found Rana chiricahuensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: E. coli (MIC=80 µM);##Gram-positive bacterium: S. aureus (MIC=20 µM).##Yeast: C. albicans (MIC=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys13 and Cys19) Disulfide bond between Cys13 and Cys19. L No cytotoxicity information found Not found 21262304 Peptides. 2011 Apr;32(4):664-669. Conlon JM, Mechkarska M, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona. DRAMP01889 GIGSILGVIAKGLPTLISWIKNR 23 Brevinin-1TOa (Frogs, amphibians, animals) No entry found Not found Not found Rana tagoi okiensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: E. coli (MIC=20 µM);##Gram-positive bacterium: S. aureus (MIC=5 µM).##Yeast: C. albicans (MIC=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19799928 Toxicon. 2010 Feb-Mar;55(2-3):430-435. Conlon JM, Coquet L, Jouenne T, Leprince J, Vaudry H, Iwamuro S. Evidence from the primary structures of dermal antimicrobial peptides that Rana tagoi okiensis and Rana tagoi tagoi (Ranidae) are not conspecific subspecies. DRAMP01890 FLGAIAGVAAKFLPKVFCFITKKC 24 Brevinin-1VLa (Frogs, amphibians, animals) No entry found Not found Not found Rana vaillanti (Central American frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Brevinin-1VLa showes particularly high growth-inhibitory potency (MIC < or =3 microM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC(50)< or =8 microM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptide ia also active against a Gram-negative microorganism Escherichia coli (MIC< or =50 microM). Gram-negative bacterium: E. coli (MIC=25 µM);##Gram-positive bacterium: S. aureus (MIC=3 µM).##Yeast: C. albicans (MIC=3 µM). [Ref.19379837] LC50=8 mM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L [Ref.19379837] LC50=4mM against HepG2 hepatoma-derived cells Not found 19379837 Comp Biochem Physiol C Toxicol Pharmacol. 2009 Aug;150(2):150-154. Conlon JM, Raza H, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). DRAMP01891 FLPVIASVAAKVLPKVFCFITKKC 24 Brevinin-1VLc (Frogs, amphibians, animals) No entry found Not found Not found Rana vaillanti (Central American frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Brevinin-1VLc showes particularly high growth-inhibitory potency (MIC < or =3 microM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC(50)< or =8 microM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptide ia also active against a Gram-negative microorganism Escherichia coli (MIC< or =50 microM). Gram-negative bacterium: E. coli (MIC=50 µM);##Gram-positive bacterium: S. aureus (MIC=1.5 µM).##Yeast: C. albicans (MIC=3 µM). [Ref.19379837] LC50=7 mM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L [Ref.19379837] LC50=4mM against HepG2 hepatoma-derived cells Not found 19379837 Comp Biochem Physiol C Toxicol Pharmacol. 2009 Aug;150(2):150-154. Conlon JM, Raza H, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). DRAMP01892 FLPLIAGVAANFLPKIFCLISKKC 24 Brevinin-1VLd (Frogs, amphibians, animals) No entry found Not found Not found Rana vaillanti (Central American frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Inhibits the growth of reference strains of S. aureus, E. coli and C. albicans and to lyse human erythrocytes from a healthy donor and HepG2 human hepatoma-derived cells Gram-negative bacterium: E. coli (MIC>100 µM);##Gram-positive bacterium: S. aureus (MIC=3 µM).##Yeast: C. albicans (MIC=3 µM). [Ref.19379837] LC50=5 mM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L [Ref.19379837] LC50=6mM against HepG2 hepatoma-derived cells Not found 19379837 Comp Biochem Physiol C Toxicol Pharmacol. 2009 Aug;150(2):150-154. Conlon JM, Raza H, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). DRAMP01893 FLPLIAGVAASILPKIFCFITKKC 24 Brevinin-1VLe (Frogs, amphibians, animals) No entry found Not found Not found Rana vaillanti (Central American frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Inhibits the growth of reference strains of S. aureus, E. coli and C. albicans and to lyse human erythrocytes from a healthy donor and HepG2 human hepatoma-derived cells Gram-negative bacterium: E. coli (MIC>100 µM);##Gram-positive bacterium: S. aureus (MIC=3 µM).##Yeast: C. albicans (MIC=3 µM). [Ref.19379837] LC50=5 mM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L [Ref.19379837] LC50=7mM against HepG2 hepatoma-derived cells Not found 19379837 Comp Biochem Physiol C Toxicol Pharmacol. 2009 Aug;150(2):150-154. Conlon JM, Raza H, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). DRAMP01896 FLSTALKVAANVVPTLFCKITKKC 24 Brevinin-1CG1 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Rhodococcus rhodochrous X15 (MIC=9 µM), Bacillus licheniformis X39 (IS) (MIC=75 µM);##Gram-negative bacterium: Escherichia coli (ATCC 25922) (MIC=150 µM).##Fungi: Slime mold 090223 (IS) (MIC=75 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01897 FLPIVAGLAANFLPKIVCKITKKC 24 Brevinin-1CG2 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Rhodococcus rhodochrous X15 (MIC=9 µM), Bacillus licheniformis X39 (IS) (MIC=75 µM), Enterococcus faecalis 981 (MIC=19 µM), Staphylococcus carnosus KHS (IS) (MIC=9 µM), Staphylococcus aureus (ATCC 25923) (MIC=9 µM);##Gram-negative bacteria: Escherichia coli (ATCC 25922) (MIC=150 µM), Psychrobacter faecalis X29 (IS) (MIC=19 µM), Serratia rubidaea X01 (IS) (MIC=19 µM).##Fungi: Slime mold 090223 (IS) (MIC=4.5 µM), Candida albicans (ATCC 10231) (MIC=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01898 FLSTLLNVASNVVPTLICKITKKC 24 Brevinin-1CG3 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Primarily active against Gram-positive bacteria. Also highly active against Gram-negative P. faecalis X29 and S. rubidaea. Gram-positive bacteria: Rhodococcus rhodochrous X15 (MIC=2.3 µM), Bacillus licheniformis X39 (IS) (MIC=9 µM), Enterococcus faecalis 981 (MIC=75 µM), Staphylococcus carnosus KHS (IS) (MIC=19 µM), Staphylococcus aureus (ATCC 25923) (MIC=19 µM);##Gram-negative bacteria: Escherichia coli (ATCC 25922) (MIC=150 µM), Psychrobacter faecalis X29 (IS) (MIC=4.5 µM), Serratia rubidaea X01 (IS) (MIC=9 µM).##Fungi: Slime mold 090223 (IS) (MIC=9 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01899 FLSTLLNVASKVVPTLFCKITKKC 24 Brevinin-1CG4 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Rhodococcus rhodochrous X15 (MIC=2.3 µM), Bacillus licheniformis X39 (IS) (MIC=9 µM), Enterococcus faecalis 981 (MIC=9 µM), Staphylococcus carnosus KHS (IS) (MIC=9 µM), Staphylococcus aureus (ATCC 25923) (MIC=9 µM);##Gram-negative bacterium: Escherichia coli (ATCC 25922) (MIC=150 µM), Pseudomonas aeruginosa 11053 (IS) (MIC=75 µM), Psychrobacter faecalis X29 (IS) (MIC=9 µM), Serratia rubidaea X01 (IS) (MIC=9 µM).##Fungi: Slime mold 090223 (IS) (MIC=9 µM), Candida albicans (ATCC 10231) (MIC=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01900 FLPMLAGLAANFLPKIVCKITKKC 24 Brevinin-1CG5 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Primarily active against Gram-positive bacteria, escecially R. rhodochrous. Also highly active against Gram-negative P. faecalis X29 and S. rubidaea. Gram-positive bacteria: Rhodococcus rhodochrous X15 (MIC=0.6 µM), Bacillus licheniformis X39 (IS) (MIC=2.3 µM), Enterococcus faecalis 981 (MIC=9 µM), Staphylococcus carnosus KHS (IS) (MIC=1.2 µM), Staphylococcus aureus (ATCC 25923) (MIC=9 µM);##Gram-negative bacteria: Escherichia coli (ATCC 25922) (MIC=75 µM), Pseudomonas aeruginosa (CGMCC 1.50) (MIC=75 µM), Pseudomonas aeruginosa 11053 (IS) (MIC=75 µM), Klebsiella pneumoniae 08040724 (IS) (MIC=150 µM), Psychrobacter faecalis X29 (IS) (MIC=9 µM), Serratia rubidaea X01 (IS) (MIC=4.6 µM).##Fungi: Slime mold 090223 (IS) (MIC=4.5 µM), Candida albicans (ATCC 10231) (MIC=437.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01909 GFSSLFKAGAKYLLKSVGKAGAQQLACKAANNCA 34 Brevinin-2GHa (AMP-1; Frogs, amphibians, animals) P84860 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana guentheri (Gunther's frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 27-33. " Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=14.9 µg/ml), Bacillus subtilis ATCC 6633 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16979798 Peptides. 2006 Dec;27(12):3077-3084. Zhou J, McClean S, Thompson A, Zhang Y, Shaw C, Rao P, Bjourson AJ. Purification and characterization of novel antimicrobial peptides from the skin secretion of Hylarana guentheri. DRAMP01910 GVITDALKGAAKTVAAELLRKAHCKLTNSC 30 Brevinin-2GHb (AMP-2; Frogs, amphibians, animals) A0AEI5 Belongs to the frog skin active peptide family (Brevinin subfamily) br2GHb Rana guentheri (Gunther's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 24-30. " Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=16.5 µg/ml), Bacillus subtilis ATCC 6633 (MIC>64 µg/ml);##Gram-negative bacteria: Escherichia coli O111 (MIC=8.2 µg/ml), Escherichia coli ATCC 25922 (MIC=8.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys24 and Cys30) Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 16979798 Peptides. 2006 Dec;27(12):3077-3084. Zhou J, McClean S, Thompson A, Zhang Y, Shaw C, Rao P, Bjourson AJ. Purification and characterization of novel antimicrobial peptides from the skin secretion of Hylarana guentheri. DRAMP01911 SIWEGIKNAGKGFLVSILDKVRCKVAGGCNP 31 Brevinin-2GHc (AMP-4; Frogs, amphibians, animals) A0AEI6 Belongs to the frog skin active peptide family (Brevinin subfamily) br2GHc Rana guentheri (Gunther's frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 24-30. " Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=9.8 µg/ml), Bacillus subtilis ATCC 6633 (MIC>64 µg/ml);##Gram-negative bacteria: Escherichia coli O111 (MIC=19.6 µg/ml), Escherichia coli ATCC 25922 (MIC=9.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 16979798 Peptides. 2006 Dec;27(12):3077-3084. Zhou J, McClean S, Thompson A, Zhang Y, Shaw C, Rao P, Bjourson AJ. Purification and characterization of novel antimicrobial peptides from the skin secretion of Hylarana guentheri. DRAMP01913 FLPLLAGLAANFLPKIFCKITKKC 24 Brevinin-1GRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 16621155 Peptides. 2006 Sep;27(9):2111-2117. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami. DRAMP01914 GLLDTFKNLALNAAKSAGVSVLNSLSCKLSKTC 33 Brevinin-2GRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM).##Yeast: Candida albicans (MIC>100 µM). [Ref.16621155] LC50=140 μM against human erythrocytes. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16621155##17272268 Peptides. 2006 Sep;27(9):2111-2117.##Mol Cell Proteomics. 2007 May;6(5):882-894. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H.##Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami.##Anti-infection peptidomics of amphibian skin. DRAMP01918 FLPLIAGLAANFLPKIFCAITKKC 24 Brevinin-1PLb (Frogs, amphibians, animals) A7WNV3 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands." Gram-positive bacterium: Staphylococcus aureus (MIC=9 µM);##Gram-negative bacterium: Escherichia coli(MIC=26 µM).##Yeast: Candida albicans (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17698247##11087945 Peptides. 2007 Aug;28(8):1605-1610.##Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Zhou M, Wang L, Owens DE, Chen T, Walker B, Shaw C.##Basir YJ, Knoop FC, Dulka J, Conlon JM. Rapid identification of precursor cDNAs encoding five structural classes of antimicrobial peptides from pickerel frog (Rana palustris) skin secretion by single step shotgun cloning.##Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01919 FLPVIAGVAAKFLPKIFCAITKKC 24 Brevinin-1PLc (Frogs, amphibians, animals) A7WNV4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=4 µM);##Gram-negative bacterium: Escherichia coli(MIC=7 µM).##Yeast: Candida albicans (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17698247##11087945 Peptides. 2007 Aug;28(8):1605-1610.##Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Zhou M, Wang L, Owens DE, Chen T, Walker B, Shaw C.##Basir YJ, Knoop FC, Dulka J, Conlon JM. Rapid identification of precursor cDNAs encoding five structural classes of antimicrobial peptides from pickerel frog (Rana palustris) skin secretion by single step shotgun cloning.##Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01920 FLPILAGLAAKIVPKLFCLATKKC 24 Brevinin-1CSa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana cascadae (Cascades frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Brevinin-1CSa was strongly hemolytic against human erythrocytes. [Ref.17451843]Gram-negative bacterium: Escherichia coli (MIC=32 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=2 µM). [Ref.17451843] LD50=5 µM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 17451843 Peptides. 2007 Jun;28(6):1268-1274. Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. DRAMP18383 DEDLDE 6 XLAsp-P2 (X. laevis antibacterial peptide-P2; frog, amphibians, animals) No entry found Not found Not found skin, African clawed frog, Xenopus laevis, Africa Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28299865 J Pept Sci. 2017 Mar 16. in press. doi: 10.1002/psc. Zhang Y, Liu S, Li S, Cheng Y, Nie L, Wang G, Lv C, Wei W, Cheng C, Hou F, Hao L Novel short antimicrobial peptide isolated from Xenopus laevis skin DRAMP01922 GLFNVFKKVGKNVLKNVAGSLMDNLKCKVSGEC 33 Brevinin-2SKb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sakuraii (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=3 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP01933 GIMDTLKNLAKTAGKGALQSLVKMASCKLSGQC 33 Brevinin-2Ef (Frogs, amphibians, animals) P40842 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40842]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01934 GILSTIKDFAIKAGKGAAKGLLEMASCKLSGQC 33 Brevinin-2Ei (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans. Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01935 GIFLDKLKNFAKGVAQSLLNKASCKLSGQC 30 Brevinin-2Ej (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans. Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01937 GLGSILGKILNVAGKVGKTIGKVADAVGNKE 31 CPRF-Ea (caerulein precursor-related fragment; Frogs, amphibians, animals) No entry found Not found Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans. Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01938 GLGSFLKNAIKIAGKVGSTIGKVADAIGNKE 31 CPRF-Eb (caerulein precursor-related fragment; Frogs, amphibians, animals) No entry found Not found Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans. Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli (MIC=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01939 GLGSFFKNAIKIAGKVGSTIGKVADAIGNKE 31 CPRF-Ec (caerulein precursor-related fragment; Frogs, amphibians, animals) No entry found Not found Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans. Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01940 FLPIIAGVAAKVLPKLFCAITKKC 24 Brevinin-1CHa (Frogs, amphibians, animals) A7YJE2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chiricahuensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found PTM: Contains disulfide bond. Gram-negative bacteria: E. coli (MIC=10 µM), K. pneumoniae (MIC=40 µM), P. aeruginosa (MIC=20 µM);##Gram-positive bacterium: S. aureus (MIC=2.5 µM).##Yeast: C. albicans (MIC=2.5 µM).(Ref.2) [Ref.21262304] LC50=5 µM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 17938991##21262304 J Mol Evol. 2007 Nov;65(5):605-615.##Peptides. 2011 Apr;32(4):664-669. Tennessen JA, Blouin MS.##Conlon JM, Mechkarska M, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Selection for antimicrobial peptide diversity in frogs leads to gene duplication and low allelic variation.##Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona. DRAMP01941 FLPVIAGLAAKVLPKLFCAITKKC 24 Brevinin-1CHb (Frogs, amphibians, animals) A7YJE4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chiricahuensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found PTM: Contains disulfide bond. Gram-negative bacteria: E. coli (MIC=10 µM), K. pneumoniae (MIC=40 µM), P. aeruginosa (MIC=10 µM);##Gram-positive bacterium: S. aureus (MIC=2.5 µM).##Yeast: C. albicans (MIC=2.5 µM).(Ref.2) [Ref.21262304] LC50=5 µM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 17938991##21262304 J Mol Evol. 2007 Nov;65(5):605-615.##Peptides. 2011 Apr;32(4):664-669. Tennessen JA, Blouin MS.##Conlon JM, Mechkarska M, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Selection for antimicrobial peptide diversity in frogs leads to gene duplication and low allelic variation.##Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona. DRAMP01942 FLPAIVGAAGQFLPKIFCAISKKC 24 Brevinin-1Sa (Frogs, amphibians, animals) P82904 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sphenocephala (Southern leopard frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=55 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10604597 J Pept Res. 1999 Dec;54(6):522-527. Conlon JM, Halverson T, Dulka J, Platz JE, Knoop FC. Peptides with antimicrobial activity of the brevinin-1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala. DRAMP01943 FLPAIVGAAGKFLPKIFCAISKKC 24 Brevinin-1Sb (Frogs, amphibians, animals) P82905 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sphenocephala (Southern leopard frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=17 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10604597 J Pept Res. 1999 Dec;54(6):522-527. Conlon JM, Halverson T, Dulka J, Platz JE, Knoop FC. Peptides with antimicrobial activity of the brevinin-1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala. DRAMP01944 FFPIVAGVAGQVLKKIYCTISKKC 24 Brevinin-1Sc (Frogs, amphibians, animals) P82906 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sphenocephala (Southern leopard frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=14 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10604597 J Pept Res. 1999 Dec;54(6):522-527. Conlon JM, Halverson T, Dulka J, Platz JE, Knoop FC. Peptides with antimicrobial activity of the brevinin-1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala. DRAMP01949 FLPAVLRVAAKIVPTVFCAISKKC 24 Brevinin-1HSa (Frogs, amphibians, animals) P0C8S7 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana hosii (Hose's rock frog) (Odorrana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=24 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01950 FLPAVLRVAAQVVPTVFCAISKKC 24 Brevinin-1HSb (Brevinin-1JDb; Frogs, amphibians, animals) P0C8S8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana hosii (Hose's rock frog) (Odorrana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC>48 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01951 FMGGLIKAATKIVPAAYCAITKKC 24 Brevinin-1PTa (Frogs, amphibians, animals) P0C8T1 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=24 µM). Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01953 GLLDSLKNLAINAAKGAGQSVLNTLSCKLSKTC 33 Brevinin-2HSa (Frogs, amphibians, animals) P0C8S9 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hosii (Hose's rock frog) (Rana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=18 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=36 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01955 GAIKDALKGAAKTVAVELLKKAQCKLEKTC 30 Brevinin-2PTa (Frogs, amphibians, animals) P0C8T3 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 24-30." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=18 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=18 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys24 and Cys30) Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01956 GFKGAFKNVMFGIAKSAGKSALNALACKIDKSC 33 Brevinin-2PTb (Frogs, amphibians, animals) P0C8T4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=9 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=9 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01957 GLLDSFKNAMIGIAKSAGKTALNKIACKIDKTC 33 Brevinin-2PTc (Frogs, amphibians, animals) P0C8T5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>72 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=18 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01959 GFLDSFKNAMIGVAKSVGKTALSTLACKIDKSC 33 Brevinin-2PTe (Frogs, amphibians, animals) P0C8T7 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=36 µM);##Gram-negative bacterium: Escherichia coli ATCC 25726 (MIC=18 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01963 FLPAIVGAAAKFLPKIFCAISKKC 24 Brevinin-1BLa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates blairi (plains leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.19254736] Gram-positive bacteria : Staphylococcus aureus(MIC=1.5 μM);##Gram-negative bacteria : Escherichia coli(MIC=25 μM);##Fungi : Candida albicans(MIC=6 μM) [Ref.19254736] LC50=14 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01965 FLPIIAGIAAKFLPKIFCTISKKC 24 Brevinin-1BLc (Frogs, amphibians, animals) B6CPR0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates blairi (leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.19254736]Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=1.5 µM);##Yeast: Candida albicans (MIC=3 µM);##Cancer cells HepG2: (LC50=6 µM).. [Ref.19254736] LC50=9 μM against human red blood cells.##[Ref.14531844]Non-hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01968 FLPIIAGAAAKVVEKIFCAISKKC 24 Brevinin-1Yc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates yavapaiensis (North American leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.19254736] Gram-positive bacteria : Staphylococcus aureus(MIC=6 μM);##Gram-negative bacteria : Escherichia coli(MIC=100 μM);##Fungi : Candida albicans(MIC=6 μM)Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM).##Yeast: Candida albicans (MIC=6 µM).##cancer cells HepG2 (LC50=14 µM). [Ref.19254736] LC50=13 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01969 FLGSLIGAAIPAIKQLLGLKK 21 Brevinin-1Ja (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana japonica (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found It can produced cell death of mammalian COS7 cells (LD50=28 µM). Gram-positive bacterium: Staphylococcus aureus (MIC=15 µM);##Gram-negative bacterium: Escherichia coli (MIC=119 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18558801 Zoolog Sci 2008; 25: 487-491. Koyama T, Iwamuro S. Molecular cloning of a cDNA encoding atypical antimicrobial and cytotoxic brevinin-1Ja from the skin of the Japanese brown frog, Rana japonica. DRAMP01970 FLPFLLSALPKVFCFFSKKC 20 Brevinin-1ZHa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=8 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=32 µM).##Yeast: Candida albicans ATCC 2002 (MIC>43 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01971 FLPLLLSALPSFLCLVFKKC 20 Brevinin-1ZHb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=17 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=33 µM), Pseudomonas aeruginosa ATCC 9027 (MIC>44 µM).##Yeast: Candida albicans ATCC 2002 (MIC>44 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01974 GIMRVFKGVLKTAGKSVAKNVAGSFLDRLKCKISGGC 37 Brevinin-2ZHa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=1 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=5 µM).##Yeast: Candida albicans ATCC 2002 (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01986 SLLGTVKDLLIGAGKSAAQSVLKGLSCKLSKDC 33 Brevinin-2HS2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Huia schmackeri (Chinese piebald odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: It shows poor hemolycity activity (LC50=300 uM). Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=19 µM), Bacillus licheniformis X39 (MIC=39 µM), Rhodococcus rhodochrous X15 (MIC=9.5 µM);##Gram-negative bacterium: Psychrobacter faecalis X29 (MIC=9.5 µM).##Fungi: Slime mould 090223 (MIC=37.5 µM), Candida albicans ATCC2002 (MIC=19 µM). LC50=300µM against human erythrocytes Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18423796 Peptides. 2008 Aug;29(8):1456-1460. Quan Z, Zhou M, Chen W, Chen T, Walker B, Shaw C. Novel brevinins from Chinese piebald odorous frog (Huia schmackeri) skin deduced from cloned biosynthetic precursors. DRAMP01990 FMGSALRIAAKVLPAALCQIFKKC 24 Brevinin-1LT1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (Chinese broad-folded frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity against rabbit red blood cells. [Ref.19340924]Gram-positive bacteria: Staphylococcus aureus (MIC=6.25 µM), Bacillus subtilis (MIC=6.25 µM);##Gram-negative bacterium: Pseudomonas fluorescens (MIC=100 µM);##Yeast: Candida albicans (MIC=50 µM). [Ref.19340924]LC50>200 µg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19340924 Biochimie. 2009 Apr;91(4):540-547. Wang H, Yan X, Yu H, Hu Y, Yu Z, Zheng H, Chen Z, Zhang Z, Liu J. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae). DRAMP01994 SLLDTFKNLAVNAAKSAGVSVLNALSCKISRTC 33 Brevinin-2ISa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 µM), S. aureus (MRSA) (MIC=100 µM), Bacillus subtilis (MIC=12.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01995 SFLTTFKDLAIKAAKSAGQSVLSTLSCKLSNTC 33 Brevinin-2ISb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 µM), Bacillus subtilis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP01996 SVLGTVKDLLIGAGKSAAQSVLTTLSCKLSNSC 33 Brevinin-2ISc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana ishikawae (Endangered frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21193000 Peptides. 2011 Apr;32(4):670-676. Iwakoshi-Ukena E, Ukena K, Okimoto A, Soga M, Okada G, Sano N, Fujii T, Sugawara Y, Sumida M. Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae. DRAMP02001 FLPLIASLAANFVPKIFCKITKKC 24 Brevinin-1HN1 (Frogs, amphibians, animals) E7EKC4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Hainan odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria and fungi but has weak or no activity against a range of Gram-negative bacteria except P. faecalis. Has hemolytic activity against human erythrocytes (LC50=75 µM). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond." [Ref.22450466]Gram-positive bacteria: Enterococcus faecium 091299 (MIC=19 µM), Enterococcus faecalis 981 (MIC=19 µM), Staphylococcus aureus ATCC2592 (MIC=1.2 µM), Staphylococcus carnosus KHS (MIC=4.8 µM), Bacillus licheniformis X39 (MIC=2.4 µM), Rhodococcus rhodochrous X15 (MIC=1.2 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=150 µM), Psychrobacter faecalis X29 (MIC=4.8 µM);##Fungi: Slime mould 090223 (MIC=1.2 µM), Candida albicans ATCC2002 (MIC=2.4 µM). [Ref.22450466] LC50=75 µM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22450466 Peptides. 2012 Jun;35(2):285-290. Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP02004 FLPLIASVAANLVPKIFCKITKKC 24 Brevinin-1V (Frogs, amphibians, animals) Q2UXV8, E7EKC5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana versabilis (Chinese bamboo leaf odorous frog) (Rana versabilis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria and fungi but has weak or no activity against a range of Gram-negative bacteria except P. faecalis. Has hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond." [Ref.22450466]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=19 µM), Bacillus licheniformis X39 (MIC=37.5 µM), Rhodococcus rhodochrous X15 (MIC=9.5 µM), Enterococcus faecium 091299 (MIC=19 µM), E. faecalis 981 (MIC=19 µM);##Gram-negative bacterium: Psychrobacter faecalis X29 (MIC=9.5 µM);##Fungi: Slime mould 090223 (MIC=1.2 µM), Candida albicans ATCC2002 (MIC=19-37.5 µM). [Ref.22450466] LC50=75 µM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 16139929##22450466 Peptides. 2006 Jan;27(1):42-48.##Peptides. 2012 Jun;35(2):285-290. Chen T, Li L, Zhou M, Rao P, Walker B, Shaw C.##Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Amphibian skin peptides and their corresponding cDNAs from single lyophilized secretion samples: identification of novel brevinins from three species of Chinese frogs.##Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP02006 GIWDTLKNVGKAVLGKVLENV 21 Brevinin-2Va (Frogs, amphibians, animals) No entry found Not found Not found Rana virgatipes (Ranidae) (Aquarana) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15996769 Regul Pept. 2005 Nov;131(1-3):38-45. Conlon JM, Abraham B, Sonnevend A, Jouenne T, Cosette P, Leprince J, Vaudry H, Bevier CR. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). DRAMP02009 FLPVLAGIAAKVVPALFCKITKKC 24 Brevinin-1 (Frogs, amphibians, animals) P32423 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana brevipoda porsa (Japanese frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity. [Ref.1449472]Gram-positive bacterium: Staphylococcus aureus (MIC=8 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=34 µg/ml). [Ref.1449472] high hemolytic activity Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 1449472 Biochem Biophys Res Commun. 1992 Nov 30;189(1):184-190. Morikawa N, Hagiwara K, Nakajima T. Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. DRAMP02010 GLLDSLKGFAATAGKGVLQSLLSTASCKLAKTC 33 Brevinin-2 (Frogs, amphibians, animals) P32424 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana brevipoda porsa (Japanese frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity. [Ref.1449472]Gram-positive bacterium: Staphylococcus aureus (MIC=8 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=4 µg/ml). [Ref.1449472] high hemolytic activity Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 1449472 Biochem Biophys Res Commun. 1992 Nov 30;189(1):184-190. Morikawa N, Hagiwara K, Nakajima T. Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. DRAMP02019 GLFDVVKGVLKGAGKNVAGSLLEQLKCKLSGGC 33 Brevinin-2DYb (Frogs, amphibians, animals) P0C5X2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus (MIC=30 µM);##Gram-negative bacterium: Escherichia coli (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP18381 VVYALKRNGRTLYGF 15 H4-(86-100) (histone-derived) No entry found Not found Not found rat Antimicrobial, Antibacterial Not found Not found Fuction: ATP can enahnce its activity, implying its involvement in inhibiting the DNA gyrase activity. Active against E. coli (LD90 6.68 ug/ml), P. aeruginosa (LD90 4.8 ug/ml), B. subtilis (LD90 17 ug/ml), and S. aureus (14.7 ug.ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18803668 FEBS J. 2008 Nov;275(21):5286-97. Lemaire S, Trinh TT, Le HT, Tang SC, Hincke M, Wellman-Labadie O, Ziai S. Antimicrobial effects of H4-(86-100), histogranin and related compounds--possible involvement of DNA gyrase. DRAMP18382 VVYTLKRNGRTLYGF 15 HNr (histone-derived) No entry found Not found Not found rat Antimicrobial, Antibacterial Not found Not found Fuction: ATP can enahnce its activity, implying its involvement in inhibiting the DNA gyrase activity. Active against E. coli (LD90 10.3 ug/ml), P. aeruginosa LD90 8.7 ug/ml), and B. subtilis (LD90 14 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18803668 FEBS J. 2008 Nov;275(21):5286-97. Lemaire S, Trinh TT, Le HT, Tang SC, Hincke M, Wellman-Labadie O, Ziai S. Antimicrobial effects of H4-(86-100), histogranin and related compounds--possible involvement of DNA gyrase. DRAMP02023 GIFDVVKGVLKGVGKNVAGSLLEQLKCKLSGGC 33 Brevinin-2DYd (Frogs, amphibians, animals) P0C5X4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus (MIC=15 µM);##Gram-negative bacterium: Escherichia coli (MIC=15 µM).##NOTE: mixture of Brevinin-2DYc/2DYd No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP18380 SGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAQRVGAGAPVY 50 Acipensin 1 (Ac1) No entry found Not found Not found Leukocytes; the Russian Sturgeon, Acipenser gueldenstaedtii Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli ML35p (MIC 0.7 uM), L. monocytogenes EGD (MIC 1.1 uM), MRSA ATCC 33591 (MIC 0.9 uM), C. albicans 820 (MIC 1 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25558400 Acta Naturae. 2014 Oct;6(4):99-109 Shamova OV, Orlov DS, Balandin SV, Shramova EI, Tsvetkova EV, Panteleev PV, Leonova YF, Tagaev AA, Kokryakov VN, Ovchinnikova TV. Acipensins - Novel Antimicrobial Peptides from Leukocytes of the Russian Sturgeon Acipenser gueldenstaedtii DRAMP02025 GLFSVVTGVLKAVGKNVAKNVGGSLLEQLKCKISGGC 37 Brevinin-2DYe (Brevinin-2CDYa; Frogs, amphibians, animals) P0C5X5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Active against the Gram-positive bacteria: S. aureus and Gram-negative bacteria E. coli. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 31-37. Gram-positive bacterium: Staphylococcus aureus (MIC=15 µM);##Gram-negative bacterium: Escherichia coli (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 17688900##17698251 Toxicon. 2007 Nov;50(6):746-756.##Peptides. 2007 Aug;28(8):1532-1539. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S.##Kim SS, Shim MS, Chung J, Lim DY, Lee BJ. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii.##Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. DRAMP02026 LLSLALAALPKLFCLIFKKC 20 Brevinin-1CDYa (Frogs, amphibians, animals) B3VZU0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has low activity against the Gram-positive bacteria: S. aureus and Gram-negative bacteria E. coli. Has hemolytic activity against human erythrocytes (HC50=125 µM). Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 14-20." [Swiss_Prot Entry B3VZU0]Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 µM);##Gram-negative bacterium: Escherichia coli (MIC=25 µM) [Ref.19539775]HC50=125 μM against human red blood cells Cyclic Free Cyclization (Cys14 and Cys20) Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP18379 SGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLR 35 Acipensin 2 (Ac2) No entry found Not found Not found Leukocytes; the Russian Sturgeon, Acipenser gueldenstaedtii Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli ML35p (MIC 0.3 uM), L. monocytogenes EGD (MIC 1.0 uM), MRSA ATCC 33591 (MIC 0.6 uM), C. albicans 820 (MIC 0.9 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25558400 Acta Naturae. 2014 Oct;6(4):99-109. Shamova OV, Orlov DS, Balandin SV, Shramova EI, Tsvetkova EV, Panteleev PV, Leonova YF, Tagaev AA, Kokryakov VN, Ovchinnikova TV. Acipensins - Novel Antimicrobial Peptides from Leukocytes of the Russian Sturgeon Acipenser gueldenstaedtii. DRAMP02031 ILPLLLGKVVCAITKKC 17 Brevinin-1Da (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dalmatina (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "Sequence alignment suggests that the peptide is derived from brevinin-1 by multiple residue deletions (D for ""dalmatina"" and 'a' to denote the first isoform identified). " Gram-positive bacterium: Staphylococcus aureus (MIC=7 µM);##Gram-negative bacterium: Escherichia coli (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys11 and Cys17) Disulfide bond between Cys11 and Cys17. L No cytotoxicity information found Not found 15050930 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Feb;137(2):191-196. Conlon JM, Seidel B, Nielsen PF. An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina. DRAMP02032 FLGSIVGALASALPSLISKIRN 22 Brevinin-1TSa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana tsushimensis (Tsushima brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria, but hemolytic activity against human erythrocytes. [Ref.16413829]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=25 µM), Klebsiella pneumoniae KK3 9904 (MIC>100 µM), Enterobacter cloacae HNTCC 53001 (MIC=50 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=50 µM), Proteus mirabilis ATCC 25933 (MIC>100 µM);##Gram-positive bacteria: Staphylococcus aureus NCTC 8325 (MIC=25 µM), Methicillin-resistant Staphylococcus aureus T7/20 (MIC=25 µM), Staphylococcus epidermidis RP62A (MIC=12.5 µM), Enterococcus faecalis ATCC 29212 (MIC=50 µM), Streptococcus group B HNTCC 80130 (MIC=50 µM);##Yeast: Candida albicans ATCC 90028 (MIC=50 µM) [Ref.16413829]LD50=12 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16413829 Comp Biochem Physiol C Toxicol Pharmacol. 2006 May;143(1):42-49. Conlon JM, Al-Ghaferi N, Abraham B, Sonnevend A, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis. DRAMP02033 GIMSLFKGVLKTAGKHVAGSLVDQLKCKITGGC 33 Brevinin-2TSa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana tsushimensis (Tsushima brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria, but relatively low hemolytic activity against human erythrocytes. [Ref.16413829]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3 µM), Klebsiella pneumoniae KK3 9904 (MIC=6 µM), Enterobacter cloacae HNTCC 53001 (MIC=6 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=6 µM), Proteus mirabilis ATCC 25933 (MIC>100 µM);##Gram-positive bacteria: Staphylococcus aureus NCTC 8325 (MIC=12.5 µM), Methicillin-resistant Staphylococcus aureus T7/20 (MIC=25 µM), Staphylococcus epidermidis RP62A (MIC=12.5 µM), Enterococcus faecalis ATCC 29212 (MIC=25 µM);##Yeast: Candida albicans ATCC 90028 (MIC=100 µM). [Ref.16413829] LD50=100 μM against human erythrocytes Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16413829 Comp Biochem Physiol C Toxicol Pharmacol. 2006 May;143(1):42-49. Conlon JM, Al-Ghaferi N, Abraham B, Sonnevend A, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis. DRAMP02034 FLPILAGLAAKLVPKVFCSITKKC 24 Brevinin-1AUa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana aurora aurora (Northern red-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria, and also shows hemolytic. [Ref.15325526]Gram-negative bacteria: Escherichia coli (MIC=13 µM), Pseudomonas aeruginosa (MIC=25 µM), Enterobacter cloacae (MIC=13 µM), Klebsiella pneumoniae (MIC=50 µM), Proteus mirabilis (MIC>50 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3 µM), Staphylococcus epidermidis (MIC=6 µM), Enterococcus faecalis (MIC=13 µM), Streptococcus Group B (MIC=13 µM);##Yeast: Candida albicans (MIC>40 µM). [Ref.15325526] HC50=5 μM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 15325526 Dev Comp Immunol. 2005;29(1):83-90. Conlon JM, Sonnevend A, Davidson C, Demandt A, Jouenne T. Host-defense peptides isolated from the skin secretions of the Northern red-legged frog Rana aurora aurora. DRAMP02035 FLPILAGLAANILPKVFCSITKKC 24 Brevinin-1AUb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana aurora aurora (Northern red-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria, and also shows hemolytic activity. [Ref.15325526]Gram-negative bacteria: Escherichia coli (MIC=25 µM), Pseudomonas aeruginosa (MIC=25 µM), Enterobacter cloacae (MIC=25 µM), Klebsiella pneumoniae (MIC>50 µM), Proteus mirabilis (MIC>50 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3 µM), Staphylococcus epidermidis (MIC=6 µM), Enterococcus faecalis (MIC=6 µM), Streptococcus Group B (MIC=13 µM);##Yeast: Candida albicans (MIC=3 µM). [Ref.15325526] HC50=7 μM against human erythrocytes Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 15325526 Dev Comp Immunol. 2005;29(1):83-90. Conlon JM, Sonnevend A, Davidson C, Demandt A, Jouenne T. Host-defense peptides isolated from the skin secretions of the Northern red-legged frog Rana aurora aurora. DRAMP02036 GAFGNFLKGVAKKAGLKILSIAQCKLSGTC 30 Brevinin-2-RN1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Brevinin-2-RN1 and -RN2 could induce 17 and 21% Rabbit red blood cell hemolysis, respectively. Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=3.10 µg/ml), Staphylococcus aureus ATCC43300 (MIC=3.10 µg/ml), Bacillus subtilis (MIC=12.5 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35P (MIC=25 µg/ml), Pseudomonas aeruginosa PA01 (MIC=12.5 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=25 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=6.25 µg/ml). [Ref.21171145] It has 17% hemolysis at 100 µg/ml against rabbit red blood cell Cyclic Free Cyclization (Cys24 and Cys30) Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 21171145 J Pept Sci. 2011 Jan;17(1):68-72. Liu X, Liu R, Wei L, Yang H, Zhang K, Liu J, Lai R. Two novel antimicrobial peptides from skin secretions of the frog, Rana nigrovittata. DRAMP02037 GAFGNFLKGVAKKAGLKILSIAQCKLFGTC 30 Brevinin-2-RN2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Brevinin-2-RN1 and -RN2 could induce 17 and 21% Rabbit red blood cell hemolysis, respectively. Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=6.25 µg/ml), Staphylococcus aureus ATCC43300 (MIC=6.25 µg/ml), Bacillus subtilis (MIC=12.5 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35P (MIC=50 µg/ml), Pseudomonas aeruginosa PA01 (MIC=12.5 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=12.5 µg/ml). Yeast: Candida albicans ATCC2002 (MIC=3.1 µg/m). [Ref.21171145] It has 21% hemolysis at 100 µg/ml against rabbit red blood cell Cyclic Free Cyclization (Cys24 and Cys30) Disulfide bond between Cys24 and Cys30. L No cytotoxicity information found Not found 21171145 J Pept Sci. 2011 Jan;17(1):68-72. Liu X, Liu R, Wei L, Yang H, Zhang K, Liu J, Lai R. Two novel antimicrobial peptides from skin secretions of the frog, Rana nigrovittata. DRAMP02038 VIVFVASVAAEMMQHVYCAASKKC 24 Brevinin-1-OA1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12.4 µg/ml);##Gram-negative bacteria: Bacillus pyocyaneus CMCCB 10104 (MIC=12.4 µg/ml), Escherichia coli ATCC 25922 (MIC=6.2 µg/ml).##Yeast: Candida albicans (MIC=24.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP18378 ILELAGNAARDNKKTRIIPRHLQL 24 Acipensin 6 (Ac6) No entry found Not found Not found Leukocytes; the Russian Sturgeon, Acipenser gueldenstaedtii Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against E. coli ML35p (MIC 2.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25558400 Acta Naturae. 2014 Oct;6(4):99-109. Shamova OV, Orlov DS, Balandin SV, Shramova EI, Tsvetkova EV, Panteleev PV, Leonova YF, Tagaev AA, Kokryakov VN, Ovchinnikova TV. Acipensins - Novel Antimicrobial Peptides from Leukocytes of the Russian Sturgeon Acipenser gueldenstaedtii DRAMP02040 FLPAVIRVAANVLPTAFCAISKKC 24 Brevinin-1-OA12 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.6 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=13.2 µg/ml).##Yeast: Candida albicans (MIC=3.3 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02041 LPFVAGVAAEMMQHVYCAASKKC 23 Brevinin-1-OR1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.3 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=42.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10.6 µg/ml).##Yeast: Candida albicans (MIC=10.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys17 and Cys23) Disulfide bond between Cys17 and Cys23. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02042 IDPFVAGVAAEMMQHVYCAASKKC 24 Brevinin-1-OR3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=9.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=18.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=18.2 µg/ml).##Yeast: Candida albicans (MIC=18.2 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02043 INPFVAGVAAEMMQHVYCAASKKC 24 Brevinin-1-OR4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=8.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=8.6 µg/ml).##Yeast: Candida albicans (MIC=8.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02044 ILPFVAGVAAEMMKHVYCAASKKC 24 Brevinin-1-OR5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found It differs from AP1824 only at position 14: Q vs. K. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=30.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=15.2 µg/ml).##Yeast: Candida albicans (MIC=7.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02045 IIPFVAGVAAEMMEHVYCAASKKC 24 Brevinin-1-OR6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found It differs from AP1827 at two positions: 2: I vs. L and 14: K vs. E. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=22.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=22.2 µg/ml).##Yeast: Candida albicans (MIC=11.1 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02046 QLPFVAGVACEMCQCVYCAASKKC 24 Brevinin-1-OR7 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.7 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=5.7 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=11.4 µg/ml).##Yeast: Candida albicans (MIC=11.4 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02047 ILPFVAGVAAEMMEHVYCAASKKC 24 Brevinin-1-OR8 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=13.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=52.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=26.2 µg/ml).##Yeast: Candida albicans (MIC=13.1 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02048 ILPFVAGVAAMEMEHVYCAASKKC 24 Brevinin-1-OR9 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=9.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=9.8 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=4.9 µg/ml).##Yeast: Candida albicans (MIC=9.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02049 FLPAVLLVATHVLPTVFCAITRKC 24 Brevinin-1-OR10 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.4 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=27.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.8 µg/ml).##Yeast: Candida albicans (MIC=6.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02050 LAFVAGVAAEMMQHVYCAASKKC 23 Brevinin-1-OR11 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=12.4 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12.4 µg/ml).##Yeast: Candida albicans (MIC=12.4 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys17 and Cys23) Disulfide bond between Cys17 and Cys23. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02051 ILPFVAGVAAEMMQHVYCAASKKC 24 Lividin-1 (Brevinin-1-OR2; Frogs, amphibians, animals) Q2UXR4 Belongs to the frog skin active peptide family (Brevinin subfamily) lividin-1 Odorrana rotodora (Chinese odorous frog) (Odorrana livida) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains disulfide bond." Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=11.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=11.6 µg/ml).##Yeast: Candida albicans (MIC=5.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 16713657##22029824 Peptides. 2006 Sep;27(9):2118-2123.##J Proteome Res. 2012 Jan 1;11(1):306-319. Zhou M, Chen T, Walker B, Shaw C.##Yang X, Lee WH, Zhang Y. Lividins: novel antimicrobial peptide homologs from the skin secretion of the Chinese Large Odorous frog, Rana (Odorrana) livida. Identification by shotgun cDNA cloning and sequence analysis.##Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02052 SFLDTLKNLAISAAKGAGQSVLSTLSCKLSKTC 33 Lividin-2 (Brevinin-2-OR8; Frogs, amphibians, animals) Q2UXR3 Belongs to the frog skin active peptide family (Brevinin subfamily) lividin-2 Odorrana rotodora (Chinese odorous frog) (Odorrana livida) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains disulfide bond." Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=13.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=13.1 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=13.1 µg/ml).##Yeast: Candida albicans (MIC=13.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16713657##22029824 Peptides. 2006 Sep;27(9):2118-2123.##J Proteome Res. 2012 Jan 1;11(1):306-319. Zhou M, Chen T, Walker B, Shaw C.##Yang X, Lee WH, Zhang Y. Lividins: novel antimicrobial peptide homologs from the skin secretion of the Chinese Large Odorous frog, Rana (Odorrana) livida. Identification by shotgun cDNA cloning and sequence analysis.##Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02053 SVLGTVKDLLIGAGKSAAQSVLTALSCKLSNSC 33 Lividin-3 (Brevinin-2-OR1; Frogs, amphibians, animals) Q2UXR2 Belongs to the frog skin active peptide family (Brevinin subfamily) lividin-3 Odorrana rotodora (Chinese odorous frog) (Odorrana livida) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains disulfide bond." Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=22 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=11 µg/ml).##Yeast: Candida albicans (MIC=11 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16713657##22029824 Peptides. 2006 Sep;27(9):2118-2123.##J Proteome Res. 2012 Jan 1;11(1):306-319. Zhou M, Chen T, Walker B, Shaw C.##Yang X, Lee WH, Zhang Y. Lividins: novel antimicrobial peptide homologs from the skin secretion of the Chinese Large Odorous frog, Rana (Odorrana) livida. Identification by shotgun cDNA cloning and sequence analysis.##Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02054 GILDTFKNMALNAAKSAGVSVLNALSCKLSKTC 33 Brevinin-2-OA1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=12.1 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12.1 µg/ml).##Yeast: Candida albicans (MIC=6.0 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02055 GLLDTFKNMALNAAKSAGVSVLNALSCKLSKTC 33 Brevinin-2-OA2 (Brevinin-2E-OG1; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Found in multiple species. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=13.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=6.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.6 µg/ml).##Yeast: Candida albicans (MIC=6.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02056 GLLDTFKNMAINAAHGAGVSVLNALSCKLKKTC 33 Brevinin-2-OA3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.3 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=12.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6.3 µg/ml).##Yeast: Candida albicans (MIC=3.2 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02057 GLLDTFKNLAINAAESAGVSVLNSLSCKLSKTC 33 Brevinin-2-OA4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=20 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10 µg/ml).##Yeast: Candida albicans (MIC=10 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02058 GLLDGILNANFNAAKSAGTSVLNALSCKLSKTC 33 Brevinin-2-OA5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=30.6 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=30.6 µg/ml).##Yeast: Candida albicans (MIC=30.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02059 GVLATVKNLLIGTGDGAAQSVLKTLSCKLSNDC 33 Brevinin-2-OA6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=44.8 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=22.4 µg/ml).##Yeast: Candida albicans (MIC=11.2 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02060 GVLGTVKDLLIGAGKSAAQSTLKTLSCKISNDC 33 Brevinin-2-OA7 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=23.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=11.6 µg/ml).##Yeast: Candida albicans (MIC=5.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02061 GVLATVKNLLNGTGDGAAQSVLKTLSCKLSNDC 33 Brevinin-2-OA8 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=7.9 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=15.8 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=4.0 µg/ml).##Yeast: Candida albicans (MIC=4.0 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02062 GLLDTIKNMALNAAKSAGVSVLNSLSCKLSKTC 33 Brevinin-2-OR2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=6.0 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12.1 µg/ml).##Yeast: Candida albicans (MIC=12.1 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02063 GLIDTIKNMALNAAKSAGVSVLNTLSCKLSKTC 33 Brevinin-2-OR3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=41.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=20.6 µg/ml).##Yeast: Candida albicans (MIC=10.3 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02064 SVLGTVKDLLIGAGKSAAQSVLTANSCKLSNSC 33 Brevinin-2-OR4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=11.8 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=5.9 µg/ml).##Yeast: Candida albicans (MIC=11.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02065 SFLDTLKNLAISAAKGAGQSVLSTLSCKLSETC 33 Brevinin-2-OR5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=13.2 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=6.6 µg/ml).##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=6.6 µg/ml).##Fungi: Candida albicans (MIC=6.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02066 GLLDTIKNMALNAAKSAGVSVLNSLSCKDSKTC 33 Brevinin-2-OR6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=11.6 µg/ml).##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=5.8 µg/ml).##Fungi: Candida albicans (MIC=11.6 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02067 GLLDTIKNMALNAAKSAGVSVLNTLSCKLSKTC 33 Brevinin-2-OR7 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=8.6 µg/ml).##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=8.6 µg/ml).##Fungi: Candida albicans (MIC=17.2 µg/ml) [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02068 SFLSTFKELAINAAKNAGQSILHTLSCKLDKTC 33 Brevinin-2-OR9 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20.4 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=20.4 µg/ml).##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=10.2 µg/ml).##Fungi: Candida albicans (MIC=5.1 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02069 SFLSTFKELAINAAKNAGQSLLHTLSCKLDKTC 33 Brevinin-2-OR10 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: It differs from AP1850 only at position 21: L vs. I, so they are predicted to have essentially identical structure and activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15.8 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=7.9 µg/ml).##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=7.9 µg/ml).##Fungi: Candida albicans (MIC=15.8 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02070 SVMGTVKDLLIGAGKSAAQSVLKSLSCKISNDC 33 Brevinin-2-OW1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana wuchuanensis (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4.7 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=4.7 µg/ml).##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=9.4 µg/ml).##Fungi: Candida albicans (MIC=4.7 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02071 SVMGTVKDLLIGAGKSAAQSVLKSLSCKLSNDC 33 Brevinin-2-OW2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana wuchuanensis (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.6 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=6.6 µg/ml).##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=3.3 µg/ml).##Fungi: Candida albicans (MIC=3.3 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02072 SVMGTVKDLLIGAGKSAAQSVLKALSCKLSKDC 33 Brevinin-2-OW3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana wuchuanensis (Chinese odorous frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=21.0 µg/ml).##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10.5 µg/ml).##Fungi: Candida albicans (MIC=10.5 µg/ml). [Ref.22029824] It shows no hemolytic activity against human red blood cells at the concentration of 50 μg/mL. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP02073 FLPAVIRVAANVLPTVFCAISKKC 24 Brevinin-1JDa (Frogs, amphibians, animals) B3A0M4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial and antifungal activity. Has hemolytic activity against rabbit erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bonds." [Ref.22917879]Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), S. aureus (MRSA) (MIC=32 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=128 µg/ml);##Fungi: Candida albicans (MIC=128 µg/ml). [Ref.22917879] It has 79.2 ± 6.8% hemolytic activity at 128 μg/mL against rabbit red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22917879 J Proteomics. 2012 Oct 22;75(18):5807-5821. Liu J, Jiang J, Wu Z, Xie F. Antimicrobial peptides from the skin of the Asian frog, Odorrana jingdongensis: De novo sequencing and analysis of tandem mass spectrometry data. DRAMP02075 FLPAVLRVAAKVVPTVFCLISKKC 24 Brevinin-1JDc (Frogs, amphibians, animals) B3A0N0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial and antifungal activity. Has hemolytic activity against rabbit erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bonds." [Ref.22917879]Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), S. aureus (MRSA) (MIC=8 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=128 µg/ml). [Ref.22917879] It has 11.7 ± 3.2% hemolytic activity at 64 μg/mL and 88.4 ± 4.2% hemolytic activity at 128 μg/mL against rabbit red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 22917879 J Proteomics. 2012 Oct 22;75(18):5807-5821. Liu J, Jiang J, Wu Z, Xie F. Antimicrobial peptides from the skin of the Asian frog, Odorrana jingdongensis: De novo sequencing and analysis of tandem mass spectrometry data. DRAMP18376 GGGGGGHLVA 10 Peptide fraction II (Gly-rich; insects, arthropods, invertebrates, animals) No entry found Not found Not found Hemolymph, Antheraea mylitta Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against E. coli and P. aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28302399 Bioorg Med Chem Lett. 2017 Mar 3. in press. Dutta SR, Gauri SS, Ghosh T, Halder SK, DasMohapatra PK, Mondal KC, Ghosh AK. Elucidation of structural and functional integration of a novel antimicrobial peptide from Antheraea mylitta. DRAMP18377 MAGGKAGKDSGKAKAKAVSRSARAGLQFPVGRIHRHLK 38 Sphistin (histone-derived, Crustaceans, arthropods, invertebrates, animals) No entry found Not found Not found haemolymphs, Scylla paramamosain Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against G+ bacteria (S. aureus, C. glutamicum, B. subtilis, M. lysodeikticus, M. luteus) and G- bacteria (S. flexneri, P. stutzeri, and P. fluorescens) (MIC < 1.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25558400 Fish Shellfish Immunol. 2015 Dec;47(2):833-46. Chen B, Fan DQ, Zhu KX, Shan ZG, Chen FY, Hou L, Cai L, Wang KJ. Mechanism study on a new antimicrobial peptide Sphistin derived from the N-terminus of crab histone H2A identified in haemolymphs of Scylla paramamosain. DRAMP01745 LLPNLLKSLL 10 Temporin-K (Frogs, amphibians, animals) P56923 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Antibacterial activity against Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP01746 FVQWFSKFLGRIL 13 Temporin-L (Temporin-1Tl; temporin-Tl; TL; Frogs, amphibians, animals) P57104 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic, Anti-cancer Protein level Alpha helix Not found 6GS5 resolved by NMR. "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP02078 FLPVVAGLAAKVLPSIICAVTKKC 24 Brevinin-1SY (Frogs, amphibians, animals) P82871 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sylvatica (Wood frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=7 µM);##Gram-negative bacterium: Escherichia coli (MIC=45 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11042268 FEBS Lett. 2000 Oct 20;483(2-3):135-138. Matutte B, Storey KB, Knoop FC, Conlon JM. Induction: of synthesis of an antimicrobial peptide in the skin of the freeze-tolerant frog, Rana sylvatica, in response to environmental stimuli. DRAMP04238 FFHLHFHY 8 PL-101 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. [Ref.12569105] Gram-negative bacterium: Escherichia coli (MEC=7 μg/ml), Pseudomonas aeruginosa (MEC=10 μg/ml).;##Gram-positive bacteria: Staphylococcus aureus (MEC=3 μg/ml), MRSA (MEC=4 μg/ml) at PH 6.5. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12569105 J Biol Chem. 2003 Apr 11;278(15):13546-53. Tincu JA, Menzel LP, Azimov R, Sands J, Hong T, Waring AJ, Taylor SW, Lehrer RI. Plicatamide, an antimicrobial octapeptide from Styela plicata hemocytes. DRAMP02778 AHCLAIGRK 9 Defensin (Insects, animals) O96049 Belongs to the invertebrate defensin family (Type 1 subfamil Not found Oryctes rhinoceros (Coconut rhinoceros beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Shows very strong activity against Staphylococcus aureus. Has no hemolytic activity. [Ref.10561605] Gram-positive bacteria: Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus aureus (MRSA) (MIC>50 µg/ml);## Gram-negative bacteria: Escherichia coli (MIC=25 µg/ml), Pseudomonas aeruginosa (MIC>50 µg/ml). [Ref.10561605] Had no hemolytic activity against rabbit erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur. J. Biochem. 1999;266:616-623. Ishibashi J, Yang J, Saido-Sakanaka H, Nakazawa H, Yamamoto M, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP02084 GIMDTLKNLAKTAGKGALQSLLNKASCKLSGQC 33 Brevinin-2E (Frogs, amphibians, animals) P32413 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. [Ref.8508915]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.2 µM), Staphylococcus aureus Cowan 1 (MIC=2.0 µM);##Gram-negative bacteria: Escherichia coli D21 (MIC=0.5 µM), Pseudomonas aeruginosa ATCC 15692 (MIC>30 µM). [Ref.8163497]LC50>100 μM against human red blood cells Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 8508915 FEBS Lett. 1993 Jun 14;324(2):159-161. Simmaco M, Mignogna G, Barra D, Bossa F. Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta. DRAMP02101 FLPLLAGVVANFLPQIICKIARKC 24 Brevinin-1RTa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "Function: Brevinin-2RTb has antibacterial activity and hemolytic activity against rabbit red blood cells (LD50=100.0 µg/ml) in vitro. PTM: Contains one disulfide bond 27-33." [Ref.22100518]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=6.3 µg/ml), Bacillus licheniformis X39 (MIC=25.0 µg/ml), Rhodococcus rhodochrous X15 (MIC=3.1 µg/ml);##Gram-negative bacteria: Serratia rubidaea X01 (MIC=NA µg/ml), Pseudomonas aeruginosa 1.50 (MIC=NA µg/ml), Psychrobacter faecalis X29 (MIC=12.5 µg/ml). [Ref.22100518]LD50=100 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP02102 FLGSLLGLVGKVVPTLFCKISKKC 24 Brevinin-1RTb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "Function: Brevinin-2RTb has antibacterial activity and hemolytic activity against rabbit red blood cells (LD50=200.0 µg/ml) in vitro. PTM: Contains one disulfide bond 27-33." [Ref.22100518]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=3.1 µg/ml), Bacillus licheniformis X39 (MIC=25.0 µg/ml), Staphylococcus carnosus KHS (MIC=12.5 µg/ml), Rhodococcus rhodochrous X15 (MIC=3.1 µg/ml);##Gram-negative bacteria: Psychrobacter faecalis X29 (MIC=12.5 µg/ml) [Ref.22100518]LD50=200 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP02104 GLMSTLKDFGKTAAKEIAQSLLSTASCKLAKTC 33 Brevinin-2RTa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found "Function: Brevinin-2RTb has antibacterial activity and hemolytic activity against rabbit red blood cells in vitro. PTM: Contains one disulfide bond 27-33." [Ref.22100518]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=12.5 µg/ml), Bacillus licheniformis X39 (MIC=50.0 µg/ml), Staphylococcus carnosus KHS (MIC=6.3 µg/ml), Rhodococcus rhodochrous X15 (MIC=1.6 µg/ml);##Gram-negative bacteria: Serratia rubidaea X01 (MIC=100.0 µg/ml), Psychrobacter faecalis X29 (MIC=6.3 µg/ml). [Ref.22100518]LD50>400 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP02105 GILDTLKEFGKTAAKGIAQSLLSTASCKLAKTC 33 Brevinin-2RTb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "Function: Brevinin-2RTb has antibacterial activity and relatively low hemolytic activity (>400 µg/ml) against rabbit red blood cells in vitro. PTM: Contains one disulfide bond 27-33." [Ref.22100518]Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=50.0 µg/ml), Bacillus licheniformis X39 (MIC=200.0 µg/ml), Staphylococcus carnosus KHS (MIC=100.0 µg/ml), Rhodococcus rhodochrous X15 (MIC=12.5 µg/ml);##Gram-negative bacteria: Psychrobacter faecalis X29 (MIC=12.5 µg/ml). [Ref.22100518]LD50>400 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP02114 AWLDKLKSLGKVVGKVALGVAQNYLNPQQ 29 Raniseptin-1 (Rsp-1; Frogs, amphibians, animals) P86037 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against Gram-negative as well as Gram-positive bacteria. And has hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.18976634]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=10 µM), Xanthomonas citri (MIC<2 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 29313 (MIC=20 µM). [Ref.18976634]20% hemolytic activity at 80 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02125 IFGAILPLALGALKNLIK 18 Hylin-a1 (Hy-a1; Frogs, amphibians, animals) P85982 Not found Not found Hypsiboas albopunctatus (Spotted tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found 2N0O resolved by NMR. "Function: Has antibacterial activity against the Gram-positive bacteria and the Gram-negative bacteria. Has hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.19056441]Gram-positive bacteria: Staphylococcus aureus ATCC 25926 (MIC=8 µM), Enterococcus faecalis ATCC 29212 (MIC=16 µM), Bacillus subtilis ATCC 19659 (MIC=8 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=32 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=64 µM);##Fungi: Candida albicans ATCC 90028 (MIC=16.7 µM), C. krusei ATCC 6258 (MIC=16.7 µM), C. parapsilosis ATCC 22019 (MIC=67 µM), Cryptococcus neoformans ATCC 90012 (MIC=33.5 µM) [Ref.19056441]HC50=18 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19056441 Peptides. 2009 Feb;30(2):291-296. Castro MS, Ferreira TC, Cilli EM, Crusca E Jr, Mendes-Giannini MJ, Sebben A, Ricart CA, Sousa MV, Fontes W. Hylin a1, the first cytolytic peptide isolated from the arboreal South American frog Hypsiboas albopunctatus (spotted treefrog). DRAMP02127 GLLGGLLGPLLGGGGGGGGGLL 22 Leptoglycin (Gly-rich; Frogs, amphibians, animals) P86267 Not found Not found Leptodactylus pentadactylus (Smokey jungle frog) (Rana pentadactyla) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial protein. Has antibacterial activity but not against Gram-positive bacteria Staphylococcus aureus, Micrococcus luteus and Enterococcus faecalis, yeasts Candida albicans and Candida tropicalis and dermatophytes fungi Microsporum canis and Trichophyton rubrum. No hemolytic activity was observed at the 2-200 microM range concentration. Tissue specificity: Expressed by the skin glands." [Ref.19298834]Gram-negative bacteria: Escherichia coli ATCC 28922 (MIC=50 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=8 µM);##Fungi: Citrobacter freundii ATCC 8090 (MIC=75 µM) [Ref.19298834]Non-hemolytic activity was observed at 2-200 μM concentration Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19298834 Toxicon. 2009 Jul;54(1):23-32. Sousa JC, Berto RF, Gois EA, Fontenele-Cardi NC, Honório JE Jr, Konno K, Richardson M, Rocha MF, Camargo AA, Pimenta DC, Cardi BA, Carvalho KM. Leptoglycin: a new glycine/leucine-rich antimicrobial peptide isolated from the skin secretion of the South American frog Leptodactylus pentadactylus (Leptodactylidae). DRAMP02128 FLGGILNTITGLL 13 Kassorin-S (PreproKassorin-S; Frogs, amphibians, animals) E6ZBE2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Kassina senegalensis (Senegal running frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide. Has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Lacks ability to induce contraction of smooth muscle in isolated guinea pig urinary bladder. Elicits histamine release from rat peritoneal mast cells. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Gram-positive bacterium: Staphylococcus aureus (MIC=30 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21040978 Mol Immunol. 2011 Jan;48(4):442-451. Chen H, Wang L, Zeller M, Hornshaw M, Wu Y, Zhou M, Li J, Hang X, Cai J, Chen T, Shaw C. Kassorins: novel innate immune system peptides from skin secretions of the African hyperoliid frogs, Kassina maculata and Kassina senegalensis. DRAMP02129 FIKELLPHLSGIIDSVANAIK 21 Kasstasin (Frogs, amphibians, animals) G0LWV9 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Kassina maculata (African rhacophorid frog) (Hylambates maculatus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Peptide with potent vasoconstrictor properties. Has moderate antimicrobial activity. Not active against fungus C. albicans. Has hemolytic activity against horse erythrocytes. Tissue specificity: Expressed by the skin dorsal glands. Miscellaneous: Kasstasin is a derivation of Kassina, the taxon of origin, and the Ancient Greek word 'stasis' meaning 'stoppage of flow'." [Ref.21624426]Gram-positive bacterium: Staphylococcus aureus (MIC=55 µM);##Gram-negative bacterium: Escherichia coli (MIC=110 µM). [Ref.21624426]12.8% hemolytic activity at 125 μM against defibrinated horse blood Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21624426 Biochimie. 2011 Sep;93(9):1537-1542. Li X, Feng W, Zhou M, Ma C, Chen T, Zeller M, Hornshaw M, Wang L, Shaw C. Kasstasin: A novel potent vasoconstrictor peptide from the skin secretion of the African red-legged running frog, Kassina maculata. DRAMP02130 GFLGPLLKLAAKGVAKVIPHLIPSRQQ 27 Antimicrobial peptide 1 (XT-1; Frogs, amphibians, animals) P84387 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacterium S. aureus and Gram-negative bacterium E.coli and stronger activity against yeast C. albicans. Enhances the antibacterial activity of XT3. Has hemolytic activity against human red blood cells . Tissue specificity: Expressed by the skin glands." [Ref.11738090]Gram-positive bacteria: Staphylococcus aureus (MIC=5 µM);##Gram-negative bacteria: Escherichia coli (MIC=6 µM);##Fungi: Candida albicans (MIC=50 µM) [Ref.11738090]HC50=90 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02131 GVWSTVLGGLKKFAKGGLEAIVNPK 25 Antimicrobial peptide 2 (XT-2; Frogs, amphibians, animals) P84382 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has very strong antibacterial activity against Gram-positive bacterium S. aureus and very weak activity against Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacteria: Escherichia coli (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02133 GVFLDALKKFAKGGMNAVLNPK 22 Antimicrobial peptide 4 (XT-4; Frogs, amphibians, animals) P84384 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacterium S. aureus and yeast C. albicans, and very weak activity against Gram-negative bacterium E.coli. Has strong hemolytic activity against human red blood cells. Tissue specificity: Expressed by the skin glands." [Ref.11738090]Gram-positive bacteria: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacteria: Escherichia coli (MIC=18 µM);##Fungi: Candida albicans (MIC>100 µM). [Ref.11738090]HC50>150 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02135 GFLGSLLKTGLKVGSNLL 18 Antimicrobial peptide 6 (XT-6; Frogs, amphibians, animals) P84386 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacterium S. aureus and Gram-negative bacterium E.coli and strong activity against yeast C. albicans. Enhances the antibacterial activity of XT3. Has hemolytic activity against human red blood cells. Tissue specificity: Expressed by the skin glands." [Ref.11738090]Gram-positive bacterium: Staphylococcus aureus (MIC=5 µM);##Gram-negative bacterium: Escherichia coli (MIC=5 µM);##Yeast: Candida albicans (MIC=40 µM);##Clinical isolates: Staphylococcus aureus 8325 (MIC=6 µM), Staphylococcus aureus (MRSA) (MIC=7 µM), Staphylococcus epidermidis 1420129 (MIC=3 µM), S. saprophyticus 1950556 (MIC=13 µM), Escherichia coli 25922 (MIC=6 µM), Streptococcus group C 1541035 (MIC=3 µM), Shigella sonnei 1840187 (MIC=35 µM), Pseudomonas aeruginosa 0380972 (MIC=60 µM), Enterobacter cloacae 1441323 (MIC=35 µM) [Ref.11738090]HC50=70 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02136 GLLGPLLKIAAKVGSNLL 18 Antimicrobial peptide 7 (XT-7; Frogs, amphibians, animals) P84381 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has very strong antibacterial activity against many Gram-negative bacteria and the Gram-positive bacteria S.pneumoniae and Enterococcus sp. There is moderate antimicrobial activity against the Gram-negative bacterium P.aeruginosa and yeast C. albicans and weaker activity against the Streptococcal strains and E.coli. Has hemolytic activity against human red blood cells (HC50=70 µM). Seems to disrupt the membranes by adopting an alpha-helical conformation. Tissue specificity: Expressed by the skin glands. PTM: Amidation on Leu-18 is required to adopt an alpha-helical conformation in a hydrophobic solvent. The absence of amidation leads to a decrease in cationicity leading to a more than a 10-fold decrease in antimicrobial activities." Gram-positive bacterium: Staphylococcus aureus (MIC=5 µM);##Gram-negative bacterium: Escherichia coli (MIC=5 µM);##yeast Candida albicans (MIC=40 µM).##Clinical isolates: Staphylococcus aureus 8325 (MIC=6 µM), Staphylococcus aureus (MRSA) (MIC=7 µM), Staphylococcus epidermidis 1420129 (MIC=3 µM), S. saprophyticus 1950556 (MIC=13 µM), Escherichia coli 25922 (MIC=6 µM), Streptococcus group C 1541035 (MIC=3 µM), Shigella sonnei 1840187 (MIC=35 µM), Pseudomonas aeruginosa 0380972 (MIC=60 µM), Enterobacter cloacae 1441323 (MIC=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02142 GFLGPLLKLGLKGVAKVLPHLIPSRQQ 27 CPF-SP1 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Acinetobacter baumannii (MIC=12,5; Klebsiella pneumoniae=25 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP02219 GILSSFKGVAKGVAKNLAGKLLDELKCKITGC 32 Ranatuerin-2AUa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana aurora aurora (Northern red-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Activity against a range of Gram-positive and Gram-negative bacteria (minimum inhibitory concentrations<20 µM) but low hemolytic activity against human erythrocytes. [Ref.15325526]Gram-negative bacteria: Escherichia coli (MIC=5 µM), Pseudomonas aeruginosa (MIC=5 µM), Enterobacter cloacae (MIC=5 µM), Klebsiella pneumoniae (MIC=10 µM), P. mirabilis (MIC>40 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=20 µM), Staphylococcus epidermidis (MIC=20 µM), Enterococcus faecalis (MIC>40 µM), Streptococcus Group B (MIC=20 µM);##Yeast: Candida albicans (MIC>40 µM) [Ref.15325526]HC50=290 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15325526 Dev Comp Immunol. 2005;29(1):83-90. Conlon JM, Sonnevend A, Davidson C, Demandt A, Jouenne T. Host-defense peptides isolated from the skin secretions of the Northern red-legged frog Rana aurora aurora. DRAMP02220 GIMDTVKNVAKNLAGQLLDKLKCKITAC 28 Ranatuerin-2PLa (Frogs, amphibians, animals) A7WNV6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 23-28." Gram-negative bacterium: Escherichia coli (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP02221 GIMDTVKNAAKDLAGQLLDKLKCRITGC 28 Ranatuerin-2PLb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP02222 GLLDTIKNTAKNLAVGLLDKIKCKMTGC 28 Ranatuerin-2PLc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP02223 GIMDSVKNVAKNIAGQLLDKLKCKITGC 28 Ranatuerin-2PLd (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP02224 GIMDSVKNAAKNLAGQLLDTIKCKITAC 28 Ranatuerin-2PLe (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP02225 GIMDTVKNAAKDLAGQLDKLKCRITGC 27 Ranatuerin-2PLf (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (North America pickerel frog) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Not found Not found "Function: May have antimicrobial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli (MIC=23 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP18494 FIHHIIGGLFSAGKAIHRLIRRRRR 25 TP4 L0CKG3 Piscidin TP4 Oreochromis niloticus (Nile tilapia) (Tilapia nilotica) Antibacterial, Antifungal, anticancer, wound healing, Anti-Gram+, Anti-Gram-, Antimicrobial Protein level Alpha helix 1.0x sarkosyl can drive TP4 into a conformational change from a non-structure to an alpha-helical structure, and that LPS can also drive TP4 to an alpha-helical structure but with high hydrophobicity and low solubility. 5H2S Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. Has hemolytic activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=8 μg/ml; MBC=16 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=16 μg/ml; MBC=32 μg/ml);##Gram-negative bacterium: Pseudomonas aeruginosa (MIC=64 μg/ml; MBC=128 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 2% hemolysis at 0.78 μg/ml, 5% hemolysis at 1.56 μg/ml, 45% hemolysis at 3.13 μg/ml, 85% hemolysis at 6.25 μg/ml, 98% hemolysis at 12.50 μg/ml, 100% hemolysis at 25.00 μg/ml against mouse red blood cell Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet bacterial outer membrane target protein, OprI-binding 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP03002 GIGAVLKVLTTGLPALISWIKRKRQQ 26 Melittin (Allergen Api m 3; Allergen Api m III; Insects, animals) P01501,P01503 Belongs to the melittin family MELT Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found 2MLT, 3QRX, 1BH1 Function: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na+-K+-ATPase and the H+-K+-ATPase. It increases the permeability of cell membranes to ions, particularly Na+ and indirectly Ca2+, because of the Na+-Ca2+-exchange. It acts synergistically with phospholipase A2. [Ref.29783753] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2 μM), Listeria monocytogenes CMCC 54004 (MIC=1 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 μM), Escherichia coli UB 1005 (MIC=2 μM), Salmonella pullorum C7913 (MIC=8 μM), Salmonella enterica subsp enterica CMCC 50071 (MIC=2 μM) [Ref.29859288] MHC=1 μM against human red blood cell.##[Ref.2978375] 46.80% hemolysis at 2μM against human red blood cell##[Ref.20472009] Wild-type melittin:AVG ± S.D.(%)=0.077±0.002 (35) against human red blood cell. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (forms a transmembrane alpha-helix in the cell membrane.) 29859288##29783753##6309516##20472009##20403370##5300771 Gene. 2018 May 30. pii: S0378-1119(18)30617-6.##Molecules. 2018 May 19;23(5). pii: E1220. ##Eur J Biochem. 1983 Sep 1;135(1):123-126.##Peptides. 2010 Aug;31(8):1473-1479.##Toxicon. 2010 Sep 1;56(3):355-362.##Res Dev Tech Rep. 1967 Dec 5:1-13. Wanmakok M, Orrapin S, Intorasoot A, Intorasoot S.##Hou J, Liu Z, Cao S, Wang H, Jiang C, Hussain MA, Pang S.##Vlasak R, Unger-Ullmann C, Kreil G, Frischauf AM.##Sciani JM, Marques-Porto R, Louren?o Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC.##Ferreira Junior RS, Sciani JM, Marques-Porto R, Junior AL, Orsi Rde O, Barraviera B, Pimenta DC.##Fennell JF, Shipman WH, Cole LJ. Expression in Escherichia coli of novel recombinant hybrid antimicrobial peptide AL32-P113 with enhanced antimicrobial activity in vitro.##Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine AlphaS1-Casein.##Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin.##Identification of a novel melittin isoform from Africanized Apis mellifera venom.##Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of DRAMP02233 FISAIASMLGKFL 13 Ranatuerin-6 (Frogs, amphibians, animals) P82821 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+, Antiviral Protein level Not found Not found This peptide could inhibit HIV infection <10% at a concentration that is also toxic to T cells (J Virol 2005; 79:11598-11606). Gram-positive bacterium: Staphylococcus aureus (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02234 FLSAIASMLGKFL 13 Ranatuerin-7 (Frogs, amphibians, animals) P82822 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacterium S. aureus. Tissue specificity: Expressed by the skin glands." Gram-positive bacterium: Staphylococcus aureus (MIC=200 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02235 FISAIASFLGKFL 13 Ranatuerin-8 (Frogs, amphibians, animals) P82823 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacterium S. aureus. Tissue specificity: Expressed by the skin glands." Gram-positive bacterium: Staphylococcus aureus (MIC=130 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02236 FLFPLITSFLSKVL 14 Ranatuerin-9 (Frogs, amphibians, animals) P82824 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+, Antiviral Protein level Not found Not found This peptide was found to be HIV active, EC50= 16.7 uM (Wang, G et al., 2010 Antimicrob Agents Chemother 54: 1343). Gram-positive bacterium: Staphylococcus aureus (MIC=130 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02237 GLMDTIKGVAKTVAASWLDKLKCKITGC 28 Ranatuerin-2Ya (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Not found Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC(50)=20microM) than against erythrocytes (LC(50)>100microM). [Ref.19254736] Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM). [Ref.19254736] LC50>100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP02238 GLADYWRTAFRANFANLGPGIRCKSARC 28 Ranatuerin-2ZHa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=1 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=6 µM).##Yeast: Candida albicans ATCC 2002 (MIC>32 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP02239 SMISVLKNLGKVGLGFVACKVNKQC 25 Ranatuerin-1Ga (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=3.5 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=60 µM).##Yeast: Candida albicans (MIC=110 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP02241 GLLLDTLKGAAKDIAGIALEKLKCKITGCKP 31 Ranatuerin-2G (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=19 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01390 TSRCYIGYRRKVVCS 15 Odorranain-T1 (OdT1; Frogs, amphibians, animals) A6MBS1 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Odorranain-T1 adopts 28.2% turn structure in water solution. Function: Odorranain-T1 exhibites moderate antimicrobial activities against all of the tested microbes. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=17.50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=35.00 μg/ml), Bacillus subtilis (MIC=17.50 μg/ml).##Yeast: Candida albicans (MIC=8.75 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01389 FLPPSPWKETFRTS 14 Odorranain-S1 (OdS1; Frogs, amphibians, animals) A6MBS0, A6MBR9 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-S1 exhibites moderate antimicrobial activities against all of the tested microbes. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=42.50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=21.25 μg/ml), Bacillus subtilis (MIC=85.00 μg/ml).##Yeast: Candida albicans (MIC=21.25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP02251 GILSSFKGVAKGVAKDLAGKLLETLKCKITGC 32 Ranatuerin-2CSa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana cascadae (Cascades frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix (4 helices; 25 residues) In a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30), respectively. 2K10 resolved by NMR. Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has Hemolytic activity against human erythrocytes. [Ref.17451843]Gram-negative bacterium:Escherichia coli ATCC 25726 (MIC=5 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=10 µM) [Ref.17451843] LD50=150 μM against human erythrocytes Cyclic Free Cyclization (Cys27 and Cys32) Disulfide bond between Cys27 and Cys32. L No cytotoxicity information found Not found 17451843##18387372 Peptides. 2007 Jun;28(6):1268-1274.##Biochim Biophys Acta. 2008 Jun;1784(6):924-929. Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C.##Subasinghage AP, Conlon JM, Hewage CM. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group.##Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: identification of a full length helix-turn-helix motif. DRAMP02252 GLLDAIKDTAQNLFANVLDKIKCKFTKC 28 Ranatuerin 2SKa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sakuraii (Japanese brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=50 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>50 µM).##Yeast: Candida albicans (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys23 and Cys28) Disulfide bond between Cys23 and Cys28. L No cytotoxicity information found Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP01108 GIGTKILGGVKTALKGALKELASTYVN 27 Maximin-2 (Toads, amphibians, animals) P83081, P83086, Q58T49 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Maximins are linear cationic peptides and easy to form membrane pore and they may induce a detergent-type disruption of sperm membrane like in the case of magainins. "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has little hemolytic activity. Tissue specificity: Expressed by the skin glands." [Ref.11835991] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=19.5 µg/ml), Klebsiella pneumoniae (MIC=9 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=19.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=19.5 µg/ml), Bacillus megatherium (MIC=19.5 µg/ml), Bacillus dysenteriae (MIC=2.7 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=3 µg/ml). [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP03998 RKKWFW 6 PAF26 (Trp-rich; combinatorial library) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic Rich In general, positively charged residues (arginine or lysine) and residues with aromatic rings (tryptophan or phenylalanine) rendered antifungal activity. Function: Antibacterial against Gram-negative bacterium. The antifungal mixture is also antibacterial, with a predominance of basic and aromatic residues. [Ref.11976121] Gram-negative bacterium: Escherichia coli DH5α (MIC=160 µM, IC50>80 µM);##Fungi: Penicillium digitatum PHI-26 (MIC=20 µM, IC50=11 ± 1 µM), Penicillium italicum PHI-1 (MIC=40 µM, IC50=22 ± 3 µM), Botrytis cinerea CECT2100 (MIC=60 µM, IC50=38 ± 24 µM), Fusarium oxysporum CECT2866 (MIC=80 µM, IC50=45 ± 4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976121 Appl Environ Microbiol. 2002 May;68(5):2453-60. López-García B, Pérez-Payá E, Marcos JF. Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library. DRAMP01107 GIGTKILGGVKTALKGALKELASTYAN 27 Maximin-1 (Toads, amphibians, animals) P83080, Q58T87 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral, Anti-cancer Protein level Not found Maximins are linear cationic peptides and easy to form membrane pore and they may induce a detergent-type disruption of sperm membrane like in the case of magainins. 7OVZ "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has little hemolytic activity. Possess a significant cytotoxicity against tumor cell lines. Possess a significant anti-HIV activity. High spermicidal activity. Toxic dose: LD50 is 8.2 mg/kg by intraperitoneal injection into mice. Tissue specificity: Expressed by the skin glands." [Ref.11835991] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=19.5 µg/ml), Klebsiella pneumoniae (MIC=9 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=19.5 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=19.5 µg/ml), Bacillus megatherium (MIC=19.5 µg/ml), Bacillus dysenteriae (MIC=2.7 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=3 µg/ml);##Virus: HIV-1 (IC50=15.5 µg/ml, EC50=21.4 µg/ml);##Cancer cell lines: C8166 (IC50=15.3 µg/ml), Molt-4 (IC50=24.3 µg/ml), BIU-87 (IC50=20.5 µg/ml), T24 (IC50=35.4 µg/ml). [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP02268 GWASKIGQTLGKIAKVGLKELIQPK 25 Xenopsin precursor fragment (XPF; Frogs, amphibians, animals) P07198 Belongs to the magainin family Not found Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: XPF has antimicrobial activity. Tissue specificity: XPF is synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa, it is stored as active, processed peptides in large granules within the granular gland secretions of the skin." Gram-negative bacteria: Escherichia coli (MIC=16-31 µg/ml), K. Pneumonae (MIC=62-125 µg/ml), Pseudomonas aeruginosa (MIC=125-250 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=250-500 µg/ml), Streptococcus faecalis (MIC=250-500 µg/ml).##Yeast: Candida albicans (MIC=250-500 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1717472 J Biol Chem. 1991 Oct 15;266(29):19851-19857. Moore KS, Bevins CL, Brasseur MM, Tomassini N, Turner K, Eck H, Zasloff M. Antimicrobial peptides in the stomach of Xenopus laevis. DRAMP02269 GVLSNVIGYLKKLGTGALNAVLKQ 24 Antimicrobial peptide PGQ (PGQ; Frogs, amphibians, animals) P39080 Belongs to the magainin family pgq Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix(potential) Not found "Function: Antimicrobial peptide. Tissue specificity: Is synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin." Gram-negative bacteria: Escherichia coli (MIC=62-250 µg/ml), K. Pneumonae (MIC=125-250 µg/ml), Pseudomonas aeruginosa (MIC=250-500 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=250-500 µg/ml), Streptococcus faecalis (MIC=250-500 µg/ml).##Yeast: Candida albicans (MIC=250-500 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1717472 J Biol Chem. 1991 Oct 15;266(29):19851-19857. Moore KS, Bevins CL, Brasseur MM, Tomassini N, Turner K, Eck H, Zasloff M. Antimicrobial peptides in the stomach of Xenopus laevis. DRAMP02271 GIGKFLHSAKKFGKAFVGEIMNS 23 Magainin-2 (Magainin II; chain of Magainins; Frogs, amphibians, animals) C0HKN6 Belongs to the gastrin/cholecystokinin family. Magainin subfamily. Xenopus ruwenzoriensis (Uganda clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix The secondary structure is shown to be helical in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. 2MAG, 2LSA resolved by NMR. "Function: Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents. Tissue specificity: Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin." Gram-negative bacteria: Escherichia coli D31 (MIC=5 µg/ml), Klebsiella pneumoniae (MIC=10 µg/ml), Escherichia coli (MIC=50 µg/ml), Pseudomonas putida (MIC=10 µg/ml), Citrobacter freundii (MIC=30 µg/ml), Enterobacter cloacae (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Serratia marcescens (MIC=100 µg/ml), Proteus mirabilis (MIC>100 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis (MIC=10 µg/ml), Staphylococcus aureus (MIC=50 µg/ml), Streptococcus fecalis (MIC>100 µg/ml).##Protozoa: Paramecium caudatum (MIC=10 µg/ml).##Yeast: Candida albicans (MIC=80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3299384##9090128##PubMed ID is not available Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-5453.##J Biomol NMR. 1997 Feb;9(2):127-135.##To be Published. Zasloff M.##Gesell J, Zasloff M, Opella SJ.##Vermeer LS, Kozlowska J, Lorenz CD, Mason JA. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.##Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.##All Atom Simulations of the Initial Binding of Magainin and Pleurocidin to Membranes Comprising a Mixture of Anionic and Zwitterionic DRAMP02272 GMASKAGAIAGKIAKVALKAL 21 PGLa (chain of PYLa/PGLa A; Frogs, amphibians, animals) Q99134, B7ZSG6, Q91826 Belongs to the gastrin/cholecystokinin family (Magainin subfamily) pgla-a AND pgla-b Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: PGLa display a broad-spectrum of antibacterial activity against a range of Gram-positive and Gram-negative bacteria. PGLa also displays antifungal activity against C. albicans ATCC 14053. Tissue specificity: Expressed by the skin glands. Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. Stored as active, processed peptides in large granules within the granular gland secretions of the skin. PTM: Leucine amide at position 21." Gram-negative bacteria: Escherichia coli 25922 (MIC=62-125 µg/ml), Klebsiella pneumoniae 13883 (MIC=250-500 µg/ml), Pseudomonas aeruginosa 27853 (MIC=250-500 µg/ml);##Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=125-500 µg/ml), Strepococcus faecalis (MIC>500 µg/ml).##Yeast: Candida albicans 14053 (MIC=250-500 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3606567##1717472 Biochem J. 1987 Apr 1;243(1):113-120.##J Biol Chem. 1991 Oct 15;266(29):19851-19857. Giovannini MG, Poulter L, Gibson BW, Williams DH.##Moore KS, Bevins CL, Brasseur MM, Tomassini N, Turner K, Eck H, Zasloff M. Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones.##Antimicrobial peptides in the stomach of Xenopus laevis. DRAMP02273 KIAKVALKAL 10 PGLa-H (chain of PYLa/PGLa A; Frogs, amphibians, animals) Q99134, B7ZSG6, Q91826 Belongs to the gastrin/cholecystokinin family (Magainin subfamily) pgla-a AND pgla-b Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: PGLa-H display a broad-spectrum of antibacterial activity against a range of Gram-positive and Gram-negative bacteria. PGLa-H shows moderate antibacterial activity against the multidrug-resistant methicillin-resistant S. aureus (MRSA) but exhibits hemolytic activity. Tissue specificity: Expressed by the skin glands. Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. Stored as active, processed peptides in large granules within the granular gland secretions of the skin. PTM: Leucine amide at position 10." [Ref.22014884]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=8.7 µg/ml), Bacillus subtilis (MIC=14.4 µg/ml), Staphylococcus aureus (MRSA) (MIC=67.8 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=23.6 µg/ml) [Ref.22014884]3.15% hemolytic activity at 100 μg/mL, 7.95% hemolytic activity at 200 μg/mL against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22014884##1717472 Int J Antimicrob Agents. 2011 Dec;38(6):510-515.##J Biol Chem. 1991 Oct 15;266(29):19851-19857. Hou F, Li J, Pan P, Xu J, Liu L, Liu W, Song B, Li N, Wan J, Gao H.##Moore KS, Bevins CL, Brasseur MM, Tomassini N, Turner K, Eck H, Zasloff M. Isolation and characterisation of a new antimicrobial peptide from the skin of Xenopus laevis.##Antimicrobial peptides in the stomach of Xenopus laevis. DRAMP02274 SAPRGCWTKSYPPKPCK 17 Ranacyclin-E (Frogs, amphibians, animals) P83663 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial activity. The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores. Has hemolytic activity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores. Tissue specificity: Expressed by the skin granular glands." [Ref.14636071]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3 µM), Staphylococcus lentus (MIC=7 µM), Micrococcus luteus (MIC=5 µM);##Gram-negative bacteria: Yersinia pseudotuberculosis YP III (MIC=9 µM), Pseudomonas syringae pv tabaci (MIC=80 µM);##Fungi: Candida tropicalis (MIC=7.4 µM), C. guillermondii (MIC=3.4 µM), Phytophthora nicotianae spores (MIC=32 µM). [Ref.14636071] It has 55% hemolytic activity at 100 μM against human erythrocytes Cyclic Free Amidation Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Cell membrane 14636071 Biochemistry. 2003 Dec 2;42(47):14023-14035. Mangoni ML, Papo N, Mignogna G, Andreu D, Shai Y, Barra D, Simmaco M. Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity. DRAMP02275 GALRGCWTKSYPPKPCK 17 Ranacyclin-T (Frogs, amphibians, animals) P83719 Belongs to the frog skin active peptide family (Brevinin subfamily) RNCT Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found MOA: The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores. Has hemolytic activity. [Ref.14636071]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3 µM), Staphylococcus lentus (MIC=10 µM), Micrococcus luteus (MIC=8 µM);##Gram-negative bacteria: Escherichia coli D21 (MIC=30 µM), Yersinia pseudotuberculosis YP III (MIC=5 µM), Pseudomonas syringae pv tabaci (MIC=16 µM);##Fungi: Candida albicans ATCC 10231 (MIC=22 µM), Candida tropicalis (MIC=14 µM), C. guillermondii (MIC=1 µM), Phytophthora nicotianae spores (MIC=16 µM). [Ref.14636071] It has 20% hemolytic activity at 100 μM against human erythrocytes Cyclic Free Amidation Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Cell membrane 14636071 Biochemistry. 2003 Dec 2;42(47):14023-14035. Mangoni ML, Papo N, Mignogna G, Andreu D, Shai Y, Barra D, Simmaco M. Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity. DRAMP02276 AALKGCWTKSIPPKPCSGKR 20 Ranacyclin B3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana grahami (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=11.7 µM).##Yeast: Candida albicans (MIC=23.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02277 AALRGCWTKSIPPKPCSGKR 20 Ranacyclin B5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana grahami (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=5.8 µM).##Yeast: Candida albicans (MIC=23.1 µM) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02278 AALRGCWTKSIPPKPCPGKR 20 Ranacyclin-B-RL1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana livida (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (MIC=5.8 µM), Bacillus subtilis (MIC=46.2 µM);##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02279 SALVGCWTKSYPPKPCFGR 19 Ranacyclin-B-RN1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana nigrovittata (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02280 SALVGCGTKSYPPKPCFGR 19 Ranacyclin-B-RN2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana nigrovittata (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=12.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02281 SALVGCWTKSYPPNPCFGRG 20 Ranacyclin-B-RN6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana nigrovittata (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=11.7 µM).##Yeast: Candida albicans (MIC=46.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02282 SALVGCWTKSWPPKPCFGRG 20 Ranacyclin-B-LK1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana nigrovittata (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=23 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02283 SALVGCWTKSWPPKPCFGR 19 Ranacyclin-B-LK2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana nigrovittata (Ranidae frogs) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MIC=11.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys16. L No cytotoxicity information found Not found 21927839 Amino Acids. 2012 Jul;43(1):309-316. Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins. DRAMP02288 FIGPVLKIAAGILPTAICKIFKKC 24 Gaegurin-RN1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has hemolytic activity against rabbit red cells.. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=2.34 µg/ml), Staphylococcus aureus ATCC43300 (MIC=9.38 µg/ml), Bacillus subtilis (MIC=4.69 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=18.75 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=4.69 µg/ml) [Ref.19778602] It has 46.13 ± 1.49% hemolytic activity at 100 μg/ml against rabbit red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02289 FVGPVLKIAAGILPTAICKIYKKC 24 Gaegurin-RN4 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Function: Has hemolytic activity against rabbit red cells. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=1.17 µg/ml), Staphylococcus aureus ATCC43300 (MIC=9.38 µg/ml), Bacillus subtilis (MIC=2.34 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=2.34 µg/ml). [Ref.19778602] It has 18.64 ± 0.25% hemolytic activity at 100 μg/ml against rabbit red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02290 FLGPIIKIATGILPTAICKFLKKC 24 Gaegurin-RN5 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has hemolytic activity against rabbit red cells. [Ref.19778602]Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=3.75 µg/ml), Staphylococcus aureus ATCC43300 (MIC=62.50 µg/ml), Bacillus subtilis (MIC=4.69 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35P (MIC=37.50 µg/ml);##Yeast: Candida albicans ATCC2002 (MIC=4.69 µg/ml). [Ref.19778602] It has no detectable hemolysis at the concentration up to 100 μg/ml Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02291 SLFSLIKAGAKFLGKNLLKQGACYAACKASKQC 33 Gaegurin-1 (Gaegurin 1; GGN1; Frogs, amphibians, animals) P80395 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN1 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has hemolytic activity against rabbit red cells. [Ref.7999137]Gram-positive bacteria: Micrococcus luteus (MIC=5 µg/ml), Staphylococcus epidermidis (MIC=50 µg/ml), Bacillus subtilis (MIC=50 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=100 µg/ml), Shigella dysentariae (MIC=25 µg/ml), Pseudomonas putida (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml), Eshchericia coli (MIC=25 µg/ml). [Ref.7999137] It has 0.04% hemolytic activity at 0.1 μg/ml, 0.14% hemolytic activity at 1 μg/ml, 0.51% hemolytic activity at 10 μg/ml, 0.59% hemolytic activity at 100 μg/ml against human red blood cells. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 7999137 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954. Park JM, Jung J-E, Lee BJ.1994 Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. DRAMP02292 GIMSIVKDVAKNAAKEAAKGALSTLSCKLAKTC 33 Gaegurin-2 (Gaegurin 2; GGN2; Frogs, amphibians, animals) P80396 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN2 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=25 µg/ml), Shigella dysentariae (MIC=25 µg/ml), Pseudomonas putida (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml), Eshchericia coli (MIC=75 µg/ml).##Fungi: Saccharomyces cerevisiae (MIC=150 µg/ml), Candida albicans (MIC=150 µg/ml), Salmonella typhimurium (MIC=150 µg/ml), Proteus mirabilis (MIC>200 µg/ml), Serratia marcescens (MIC>200 µg/ml). [Ref.7999137] It has 0.19% hemolytic activity at 0.1 μg/ml, 0.16% hemolytic activity at 1 μg/ml, 0.31% hemolytic activity at 10 μg/ml, 0.82% hemolytic activity at 100 μg/ml against human red blood cells. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 7999137 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954. Park JM, Jung JE, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. DRAMP02293 GIMSIVKDVAKTAAKEAAKGALSTLSCKLAKTC 33 Gaegurin-3 (Gaegurin 3; GGN3; Frogs, amphibians, animals) P80397 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN3 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=25 µg/ml), Shigella dysentariae (MIC=25 µg/ml), Pseudomonas putida (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml), Eshchericia coli (MIC=75 µg/ml).##Fungi: Saccharomyces cerevisiae (MIC>200 µg/ml), Candida albicans (MIC>200 µg/ml), Salmonella typhimurium (MIC=150 µg/ml), Proteus mirabilis (MIC>200 µg/ml), Serratia marcescens (MIC>200 µg/ml). [Ref.7999137] It has 0.11% hemolytic activity at 0.1 μg/ml, 0.12% hemolytic activity at 1 μg/ml, 0.35% hemolytic activity at 10 μg/ml, 1.20% hemolytic activity at 100 μg/ml against human red blood cells. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 7999137 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954. Park JM, Jung JE, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. DRAMP02294 GILDTLKQFAKGVGKDLVKGAAQGVLSTVSCKLAKTC 37 Gaegurin-4 (Gaegurin 4; GGN4; Frogs, amphibians, animals) P80398, Q91328, Q98TA6 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN4 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Alpha helix (3 helices; 22 residues) In 100% H2O, Gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34 (Ref.2). 2G9L resolved by NMR. "Function: Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. Has hemolytic activity against rabbit red cells. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." [Ref.7999137]Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=25 µg/ml), Shigella dysentariae (MIC=25 µg/ml), Pseudomonas putida (MIC=100 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Eshchericia coli (MIC=75 µg/ml);##Fungi: Saccharomyces cerevisiae (MIC=200 µg/ml), Candida albicans (MIC=200 µg/ml), Salmonella typhimurium (MIC=200 µg/ml), Proteus mirabilis (MIC>200 µg/ml), Serratia marcescens (MIC>200 µg/ml). [Ref.7999137] It has 0.50% hemolytic activity at 0.1 μg/ml, 0.74% hemolytic activity at 1 μg/ml, 0.78% hemolytic activity at 10 μg/ml, 1.67% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 7999137##17141187##11004488 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954.##Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-597.##Biochim Biophys Acta. 2000 Jun 21;1492(1):185-190. Park JM, Jung JE, Lee BJ.##Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH.##Kwon SY, Carlson BA, Park JM, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa.##Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.##Structural organization and expression of the gaegurin 4 gene of Rana rugosa. DRAMP02295 FLGALFKVASKVLPSVFCAITKKC 24 Gaegurin-5 (Gaegurin 5; GGN5; Brevinin-1EMa; Frogs, amphibians, animals) P80399, Q91329 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN5 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal Protein level Not found Not found Function: Has low hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. PTM: Problely contains one disulfide bond 18-24. [Ref.7999137]Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=50 µg/ml), Shigella dysentariae (MIC=50 µg/ml), Pseudomonas putida (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Eshchericia coli (MIC=50 µg/ml);##Fungi: Saccharomyces cerevisiae (MIC=50 µg/ml), Candida albicans (MIC=50 µg/ml), Salmonella typhimurium (MIC=200 µg/ml), Proteus mirabilis (MIC>200 µg/ml). [Ref.7999137] It has 0.19% hemolytic activity at 0.1 μg/ml, 0.31% hemolytic activity at 1 μg/ml, 0.78% hemolytic activity at 10 μg/ml, 1.01% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 7999137 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954. Park JM, Jung JE, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. DRAMP02296 FLPLLAGLAANFLPTIICKISYKC 24 Gaegurin-6 (Gaegurin 6; GGN6; Frogs, amphibians, animals) P80400 Belongs to the frog skin active peptide family (Brevinin subfamily) GGN6 Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has low hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. PTM: Problely contains one disulfide bond 18-24. [Ref.7999137]Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=50 µg/ml), Shigella dysentariae (MIC=50 µg/ml), Pseudomonas putida (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Eshchericia coli (MIC=50 µg/ml);##Fungi: Saccharomyces cerevisiae (MIC=50 µg/ml), Candida albicans (MIC=50 µg/ml), Salmonella typhimurium (MIC=200 µg/ml), Proteus mirabilis (MIC>200 µg/ml), Serratia marcescens (MIC>200 µg/ml). [Ref.7999137] It has 0.39% hemolytic activity at 0.1 μg/ml, 0.62% hemolytic activity at 1 μg/ml, 0.78% hemolytic activity at 10 μg/ml, 0.86% hemolytic activity at 100 μg/ml against human red blood cells Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 7999137 Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954. Park JM, Jung JE, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. DRAMP02300 VIDDLKKVAKKVRRELLCKKHHKKLN 26 Guentherin (AMP-3; Frogs, amphibians, animals) P84859 Not found Not found Rana guentheri (Gunther's frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antimicrobial peptide. Active against the Gram-positive bacteria. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=35.5 µg/ml), Bacillus subtilis (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16979798 Peptides. 2006 Dec;27(12):3077-3084. Zhou J, McClean S, Thompson A, Zhang Y, Shaw C, Rao P, Bjourson AJ. Purification and characterization of novel antimicrobial peptides from the skin secretion of Hylarana guentheri. DRAMP02306 IIEKLVNTALGLLSGL 16 Riparin-2.1 (Frogs, amphibians, animals) P86127 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity. Lacks antibacterial activity against the Gram-negative bacteria E. cloacae and E. coli, and against the Gram-positive bacteria B. cereus, E. faecalis, L. innocua, M. luteus, S. aureus, S. epidermidis and S. uberis. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Tissue specificity: Expressed by the skin glands." Gram-positive bacterium: Lactococcus lactis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16470724 Rapid Commun Mass Spectrom. 2006;20(5):797-803. Maselli VM, Bilusich D, Bowie JH, Tyler MJ. Host-defence skin peptides of the Australian streambank froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry. DRAMP02307 GLADFLNKAVGKVVDFVKS 19 Deserticolin-1 (Frogs, amphibians, animals) P86136 Not found Not found Crinia deserticola (Desert froglet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacteria. Inhibits the formation of NO by neuronal nitric oxide synthase with an IC50 of 2.4 µM. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Leuconostoc lactis (MIC=25 µM), Streptococcus uberis (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18601958 Regul Pept. 2008 Nov 29;151(1-3):80-87. Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02308 IIGHLIKTALGMLGL 15 Signiferin-2.1 (Frogs, amphibians, animals) P86131 Not found Not found Crinia signifera (Common eastern froglet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against a wide spectrum of Gram-positive bacteria. Lacks antibacterial activity against the Gram-negative bacteria E. cloacae and E. coli. Inhibits the formation of NO by neuronal nitric oxide synthase with an IC50 of 12.4 µM. Tissue specificity: Expressed by the skin glands." Gram-positive bacteria: Bacillus cereus (MIC=25 µM), Enterococcus faecalis ATCC 29212 (MIC=100 µM), Leuconostoc lactis (MIC=12 µM), Listeria innocua (MIC=50 µM), Micrococcus luteus ATCC 9341 (MIC=25 µM), Staphylococcus aureus ATCC 29213 (MIC=12 µM), Staphylococcus epidermidis ATCC14990 (MIC=25 µM), Streptococcus uberis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15317042##16470724##18601958 Rapid Commun Mass Spectrom. 2004;18(18):2155-2161.##Rapid Commun Mass Spectrom. 2006;20(5):797-803.##Regul Pept. 2008 Nov 29;151(1-3):80-87. Maselli VM, Brinkworth CS, Bowie JH, Tyler MJ.##Maselli VM, Bilusich D, Bowie JH, Tyler MJ.##Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Host-defence skin peptides of the Australian Common Froglet Crinia signifera: sequence determination using positive and negative ion electrospray mass spectra.##Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry.##Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02312 SGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAHRVGAGAPVYL 51 Hipposin (fish, chordates, animals) P59890 Belongs to the histone H2A family Not found Hippoglossus hippoglossus (Atlantic halibut) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database Gram+ (MIC=0.3 µM);##Gram- (MIC=0.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12637028 Biochim Biophys Acta. 2003 Mar 21;1646(1-2):207-215. Birkemo GA, Luders T, Andersen O, Nes IF, Nissen-Meyer J Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.). DRAMP02314 RCRFCCRCCPRMRGCGICCRF 21 Hepcidin (fish, chordates, animals) A1Z0M0 Belongs to the hepcidin family hamp Larimichthys crocea (Croceine croaker) (Pseudosciaena crocea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. Tissue specificity: Expressed in all tissues tested, with highest levels of expression in kidney and lowest levels in liver. Intra-peritoneal injection of lipopolysaccharide results in increased expression in heart, spleen and stomach, but not in kidney or liver. PTM: Contains four disulfide bonds 2-19; 5-8; 6-15; 9-18." Gram-negative bacteria: Vibrio alginolyticus(MIC=24 µM), V. fluvialis, V. harveyis (MIC=12 µM) and Vibrio parahaemolyticus (MIC=6 µM), Aeromonas hydrophila (MIC=6 µM), Escherichia coli (MIC=24 µM), Escherichia coli BL21(DE3)plysS (MIC=6 µM);##Gram-positive bacteria: Bacillus cereus (MIC=24 µM), Bacillus subtilis (MIC=6 µM), C. glutamicum (MIC=3 µM), Micrococcus luteus (MIC=3 µM), M. lysodeikticus, Staphylococcus aureus (MIC=6 µM) and S.epidermis (MIC=12 µM).##Fungi: Aspergillus niger (MIC=24 µM), F;##Graminearum (MIC=24 µM) and Fusarium solani (MIC=24 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys2 and Cys19; Cys5 and Cys8; Cys6 and Cys15,Cys9 and Cys18. L No cytotoxicity information found Not found 19150638##19344770 Peptides. 2009 Apr;30(4):638-646.##Fish Shellfish Immunol. 2009 Jun;26(6):864-870. Wang KJ, Cai JJ, Cai L, Qu HD, Yang M, Zhang M.##Zhang J, Yan Q, Ji R, Zou W, Guo G. Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide.##Isolation and characterization of a hepcidin peptide from the head kidney of large yellow croaker, Pseudosciaena crocea. DRAMP02315 FFGWLIKGAIHAGKAIHGLIHRRRH 25 Chrysophsin-1 (fish, chordates, animals) P83545 Belongs to the pleurocidin family Not found Chrysophrys major (Red sea bream) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Shows hemolytic activity human red blood cells. [Ref.12581207]Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=0.25 µM), Lactococcus garvieae ATCC 49156 (MIC=10 µM), S.iniae F-8502 (MIC=2.5 µM);##Gram-negative bacteria: Escherichia coli WT-2 (MIC=0.25 µM), Vibrio anguillarum ATCC 19264 (MIC=2.5 µM), Vibriopenaeicida KHA (MIC=10 µM), V. harveyi ATCC 14126 (MIC=2.5 µM), V. vulnificus ATCC 33148 (MIC=5 µM), Aeromonas salmonicida NCMB 1102 (MIC=10 µM), Pseudomonas putida ATCC 12633 (MIC=40 µM). [Ref.12581207]10% hemolytic activity at 0.25 μM, 80% hemolytic activity at 1 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12581207 Eur J Biochem. 2003 Feb;270(4):675-686. Iijima N, Tanimoto N, Emoto Y, Morita Y, Uematsu K, Murakami T, Nakai T. Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major. DRAMP02316 FFGWLIRGAIHAGKAIHGLIHRRRH 25 Chrysophsin-2 (fish, chordates, animals) P83546 Belongs to the pleurocidin family Not found Chrysophrys major (Red sea bream) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Shows hemolytic activity human red blood cells. [Ref.12581207]Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=0.25 µM), Lactococcus garvieae ATCC 49156 (MIC=5 µM), S.iniae F-8502 (MIC=1.5 µM);##Gram-negative bacteria: Escherichia coli WT-2 (MIC=0.25 µM), Vibrio anguillarum ATCC 19264 (MIC=1.25 µM), Vibriopenaeicida KHA (MIC=5 µM), V. harveyi ATCC 14126 (MIC=5 µM), V. vulnificus ATCC 33148 (MIC=2.5 µM). [Ref.12581207]10% hemolytic activity at 0.25 μM, 70% hemolytic activity at 1 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12581207 Eur J Biochem. 2003 Feb;270(4):675-686. Iijima N, Tanimoto N, Emoto Y, Morita Y, Uematsu K, Murakami T, Nakai T. Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major. DRAMP02317 FIGLLISAGKAIHDLIRRRH 20 Chrysophsin-3 (fish, chordates, animals) P83547 Belongs to the pleurocidin family Not found Chrysophrys major (Red sea bream) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Shows hemolytic activity human red blood cells. [Ref.12581207]Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=0.25 µM), Lactococcus garvieae ATCC 49156 (MIC=10 µM), S.iniae F-8502 (MIC=10 µM);##Gram-negative bacteria: Escherichia coli WT-2 (MIC=0.25 µM), Vibrio anguillarum ATCC 19264 (MIC=10 µM), Vibriopenaeicida KHA (MIC=10 µM), V. harveyi ATCC 14126 (MIC=5 µM), V. vulnificus ATCC 33148 (MIC=10 µM), Aeromonas salmonicida NCMB 1102 (MIC=10 µM), Pseudomonas putida ATCC 12633 (MIC=40 µM). [Ref.12581207]0% hemolytic activity at 0.25 μM, 10% hemolytic activity at 1 μM against human erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12581207 Eur J Biochem. 2003 Feb;270(4):675-686. Iijima N, Tanimoto N, Emoto Y, Morita Y, Uematsu K, Murakami T, Nakai T. Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major. DRAMP02318 FIGGIISFFKRLF 13 Grammistin Pp1 (Group II grammistin; fish, chordates, animals) P69842 Belongs to the grammistin family (Group 2 subfamily) Not found Pogonoperca punctata (Clown grouper) (Bearded grouper) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=3.13 µg/ml), Staphylococcus aureus IAM 1011 (MIC=3.13 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=50 µg/ml), Escherichia coli JCM 1649 (MIC>50 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=6.25 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=6.25 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=12.5 µg/ml), Vibrio parahaemolyticus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Fish. Sci. 2001 Oct;67:928-933. Yokota H, Nagashima Y, Shiomi K. Interaction of grammistins with lipids and their antibacterial activity. DRAMP02320 FIGGIISFIKKLF 13 Grammistin PpIIb (Group II grammistin; fish, chordates, animals) P69844 Belongs to the grammistin family (Group 2 subfamily) Not found Pogonoperca punctata (Clown grouper) (Bearded grouper) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activities. [Ref.Fish. Sci. 2001 Feb;67:163-169.]Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=6.25 µg/ml), Staphylococcus aureus IAM 1011 (MIC=3.13 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC>50 µg/ml), Escherichia coli JCM 1649 (MIC=50 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=12.5 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=6.25 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=12.5 µg/ml), Vibrio parahaemolyticus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phospholipids PubMed ID is not available Fish. Sci. 2001 Feb;67:163-169. Shiomi K, Yokota H, Nagashima Y, Ishida M. Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata. DRAMP02321 NWRKILGQIASVGAGLLGSLLAGYE 25 Grammistin Pp3 (Group III grammistin; fish, chordates, animals) P69847 Belongs to the grammistin family (Group 3 subfamily) Not found Pogonoperca punctata (Clown grouper) (Bearded grouper) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has hemolytic activity. Thanks to its abundant amphiphilic alpha-helices, it may integrate into membrane phospholipids, leading to lysis of the membrane. [Ref.Fish. Sci. 2001 Oct;67:928-933.]Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=50 µg/ml), Staphylococcus aureus IAM 1011 (MIC=50 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=50 µg/ml), Escherichia coli JCM 1649 (MIC>50 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=25 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=12.5 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=50 µg/ml), Vibrio parahaemolyticus (MIC=50 µg/ml). [Ref.Fish. Sci. 2001 Oct;67:928-933.]75 HU/mg hemolytic activity against horse erythrocytes(1 HU was defined as the amount of peptide causing 50% hemolysis) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Fish. Sci. 2001 Oct;67:928-933. Yokota H, Nagashima Y, Shiomi K. Interaction of grammistins with lipids and their antibacterial activity. DRAMP02324 AEVAPAPAAAAPAKAPKKKAAAKPKKAGPS 30 SAMP H1 (fish, chordates, animals) P84408, Q5GMQ6 Belongs to the histone H1/H5 family Not found Salmo salar (Atlantic salmon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=2 µM), Aeromonas salmonicida subsp salmonicida (MIC=4 µM), Vibrio anguillarum (MIC=1 µM) Salmonella typhimurium (MIC=4 µM);##Gram-positive bacteria: Bacillus subtilis (MIC=2 µM), Listeria ivanovii (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15917539 Antimicrob Agents Chemother. 2005 Jun;49(6):2399-2406. Luders T, Birkemo G.A, Nissen-Meyer J, Andersen O, Nes I.F. Proline conformation-dependent antimicrobial activity of a proline-rich histone H1 N-terminal peptide fragment isolated from the skin mucus of Atlantic salmon. DRAMP02330 FFHHIFRGIVHVGKTIHRLVTG 22 Piscidin-1 (Pis-1; Piscidin 1; fish, chordates, animals) Q8UUG0 Belongs to the pleurocidin family Not found Morone saxatilis (Striped bass) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found 2JOS, 2OJM resolved by NMR. Function: Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria. Also has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores. [Ref.11713517]Gram-positive bacteria: Enterococcus faecalis VRE (MIC=5-10 µM), E. faecalis (MIC=2.5-5 µM), Listeria monocytogenes (MIC=2.5-5 µM), Micrococcus luteus (MIC=10-20 µM), Staphylococcus aureus MRSA (MIC=1.25-2.5 µM), S. epidermitis (MIC=5-10 µM), S. saprophiticus (MIC=5-10 µM), Staphylococcus xylosus (MIC>20 µM), S. agalactiae (MIC=1.25-2.5 µM), S. bovis (MIC=1.25-2.5 µM), S. equisimilis (MIC=2.5-5 µM), S. mitis (MIC=1.25-2.5 µM), S. Pneumonae (MIC=1.25-2.5 µM), S. pyrogenes (MIC=1.25-2.5 µM), Streptococcus iniae KST740 ak (MIC=1.25-2.5 µM), S. iniae KSTSi 6P (MIC=1.25-2.5 µM);##Gram-negative bacteria: Aeromonas hydrophila (MIC>20 µM), Burkholderia cepacia (MIC>20 µM), Vibrio Cholera (MIC=2.5-5 µM), Escherichia coli (MIC=5-10 µM), Enterobacter cloacae (MIC=10-20 µM), E. Aerogenes (MIC=10-20 µM), Klebsiella pneumoniae (MIC=2.5-5 µM), K. oxytoca (MIC=5-10 µM), Salmonella choleraesuis (MIC=10-20 µM), S. typhimurium (MIC=10-20 µM), S. arizonae (MIC=10-20 µM), Serratia marcescens (MIC>20 µM), Shigella flexneri (MIC=2.5-5 µM), S. sonnei (MIC=5-10 µM), Yersinia enterocolitica (MIC=2.5-5 µM); Fungi: Neurospora crassa (MIC=1.56-3.12 µM), A. fumigatus (MIC=50-100 µM), F. axysporum (MIC=0.78-1.56 µM), F. culmorum (MIC=0.39-0.78 µM), C. ablicans (MIC=10-20 µM), C. glabrata (MIC=10-20 µM), C. lusitania (MIC=10-20 µM), C. tropacalis (MIC=10-20 µM). [Ref.11713517]10% hemolytic activity at 5 μg/mL, 60% hemolytic activity at 10 μg/mL, 100% hemolytic activity at 50 μg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11713517 Nature. 2001 Nov 15;414(6861):268-269. Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. DRAMP02331 FFHHIFRGIVHVGKTIHKLVTG 22 Piscidin-2 (Pis-2; fish, chordates, animals) Q8UUG2 Belongs to the pleurocidin family Not found Morone chrysops (White bass) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Seems to disrupt the membranes by adopting an alpha helical conformation. Tissue specificity: Expressed in gill, skin, intestine, spleen, anterior kidney, and blood cells." Gram-positive bacteria: Enterococcus faecalis (MIC=5-10 µM), E. faecalis (MIC=2.5-5 µM), Listeria monocytogenes (MIC=2.5-5 µM), Micrococcus luteus (MIC=10-20 µM), Staphylococcus aureus (MIC=1.25-2.5 µM), S. epidermidis (MIC=5-10 µM), S. saprophiticus (MIC=5-10 µM), S. xylosus (MIC>20 µM), Streptococcus agalactiae (MIC=1.25-2.5 µM), S. bovis (MIC=1.25-2.5 µM), S. equisimilis (MIC=2.5-5 µM), S. mitis (MIC=1.25-2.5 µM), Streptococcus pneumoniae (MIC=1.25-2.5 µM), Streptococcus pyogenes (MIC=1.25-2.5 µM), S. iniae KST740ak (MIC=1.25-2.5 µM), S. iniae KSTSi 6P (MIC=1.25-2.5 µM);##Gram-negative bacteria: Aeromonas hydrophila (MIC>20 µM), Burkholderia cepacia (MIC>20 µM), Vibrio cholera (MIC=2.5-5 µM), Escherichia coli (MIC=5-10 µM), Moraxella catarrhalis (MIC=2.5-5 µM), Neisseria gonorrhoeae (MIC>20 µM), Pseudomonas aeruginosa (MIC=5-10 µM), Enterobacter cloacae (MIC=10-20 µM), E. aerogenes (MIC=10-20 µM), Klebsiella pneumoniae (MIC=2.5-5 µM), K. oxytoca (MIC=5-10 µM), Salmonella choleraesuis (MIC=10-20 µM), Salmonella typhimurium (MIC=10-20 µM), S. arizonae (MIC=10-20 µM), Serratia marcescens (MIC>20 µM), Shigella flexneri (MIC=2.5-5 µM), S. sonnei (MIC=5-10 µM), Yersinia enterocolitica (MIC=2.5-5 µM).##Fungi: Neurospora crassa (MIC=1.56-3.12 µM), Aspergillus fumigatus (MIC=50-100 µM), Fusarium oxysporum (MIC=0.78-1.56 µM), F. culmorum (MIC=0.39-0.78 µM), Candida albicans (MIC=10-20 µM), C. glabrata (MIC=10-20 µM), C. lusitania (MIC=10-20 µM), C. tropicalis (MIC=10-20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02336 KAVAAKKSPKKAKKPATPKKAAKSPKKVKKPAAAAKKAAKSPKKATKAAKPKAAKPKAAKAKKAAPKKK 69 Oncorhyncin II (Oncorhyncin 2; fish, chordates, animals) P06350, P83374 Belongs to the histone H1/H5 family Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Potentially important role in mucosal defense. Gram-positive bacteria: Planococcus citreus (MIC=0.2-0.4 µM), Micrococcus luteus (MIC=0.2-0.4 µM);##Gram-negative bacteria: Escherichia coli (MIC=0.4-0.8 µM), Listonella anguillarum (MIC=0.4-0.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12969798 Dev Comp Immunol. 2004 Feb;28(2):127-138. Fernandes JM, Molle G, Kemp GD, Smith VJ. Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss. DRAMP02337 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAG 66 Oncorhyncin III (Oncorhyncin 3; fish, chordates, animals) P02315, P83338 Belongs to the HMGN family Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Plays a role in mucosal innate host defence. Gram-positive bacteria: Aerococcus viridans (MIC=0.06-0.12 µM), Bacillus subtilis (MIC=0.25-0.5 µM), Micrococcus luteus (MIC=0.12-0.25 µM), Planococcus citreus (MIC=0.06-0.12 µM);##Gram-negative bacteria: Aeromonas hydrophila (MIC>0.5 µM), Aeromonas salmonicida 004 (MIC>0.5 µM), Escherichia coli (MIC=0.25-0.5 µM), Listonella anguillarum (MIC=0.25-0.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet DNA 12713443 Biochem J. 2003 Jul 15;373(Pt 2):621-628. Fernandes J.M.O, Saint N, Kemp G.D, Smith V.J. Oncorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss. DRAMP02347 GKGRWLERIGKAGGIIIGGALDHL 24 NRC-1 (fish, chordates, animals) No entry found Not found Not found Pseudopleuronectes americanus (Winter flounder 1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found C-terminal NH2, this NRC seris of peptides was identified by gene analysis and biological activity verified using synthetic peptides. Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=64 µg/ml), Aeromonas salmonicida 97-4 (MIC=64 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=16 µg/ml), Salmonella enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=32 µg/ml), Escherichia coli CGSC 4908 (MIC=32 µg/ml), Escherichia coli UB1005 (MIC=32 µg/ml), Escherichia coli DC2 (MIC=32 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC>64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC>64 µg/ml).##Yeast: Candida albicans C627 (MIC=64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02348 WLRRIGKGVKIIGGAALDHL 20 NRC-2 (fish, chordates, animals) No entry found Not found Not found Pseudopleuronectes americanus (Winter flounder 1a) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC>128 µg/ml), Aeromonas salmonicida 97-4 (MIC=128 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=64 µg/ml), S. enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC=64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=32 µg/ml), Escherichia coli CGSC 4908 (MIC=64 µg/ml), E. coli UB1005 (MIC=64 µg/ml), E. coli DC2 (MIC=64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC>64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC>64 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02349 GRRKRKWLRRIGKGVKIIGGAALDHL 26 NRC-3 (fish, chordates, animals) No entry found Not found Not found Pseudopleuronectes americanus (Winter flounder 1a-1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found 6RY9##6RYQ Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=2 µg/ml), Aeromonas salmonicida 97-4 (MIC=4 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=2 µg/ml), Salmonella enterica serovar Typhimurium 14028s (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=2 µg/ml), Pseudomonas aeruginosa Z61 (MIC=1 µg/ml), Escherichia coli CGSC 4908 (MIC=2 µg/ml), Escherichia coli UB1005 (MIC=8 µg/ml), Escherichia coli DC2 (MIC=2 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=8 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=8 µg/ml).##Yeast: Candida albicans C627 (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02350 GWGSFFKKAAHVGKHVGKAALTHYL 25 Pleurocidin (NRC-4; fish, chordates, animals) P81941, P81619, Q9PRJ9, Q90ZY0, Q90VW6 Belongs to the pleurocidin family ple1 AND ple2 Pseudopleuronectes americanus (Winter flounder 2-2.1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 19 residues) From NMR structural studies with the uniformly (15)N-labeled peptide, a structure of pleurocidin is determined to be in a random coil conformation in aqueous solution whereas it assumes an alpha-helical structure in TFE and in dodecylphosphocholine (DPC) micelles.(Ref.2) 1Z64 resolved by NMR. May play a role in innate host defense. Gram-negative bacteria: Escherichia coli (MIC=2.2-3.3 µM), Leucothrix mucor (MIC>35.0 µM), Serratia marcescens (MIC>35.0 µM), Pseudomonas aeruginosa (MIC>35.0 µM), Aeromonas salmonicida (MIC=17.7-35.0 µM), Cytophaga aquatilis (MIC=2.2-4.4 µM), Pasteurella haemolytica (MIC=4.4-8.8 µM), Salmonella typhimurium I (MIC=8.8-17.7 µM), Salmonella typhimurium II (MIC=8.8-17.7 µM);##Gram-positive bacteria: Bacillus subtilis (MIC=1.1-2.2 µM), Staphylococcus aureus (MIC=17.7-35.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9115266 J Biol Chem. 1997 May 2;272(18):12008-12013. Cole A.M, Weis P, Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. DRAMP02351 FFRLLFHGVHHVGKIKPRA 19 NRC-10 (fish, chordates, animals) No entry found Not found Not found Pseudopleuronectes americanus (Winter flounder Z) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC>64 µg/ml), Aeromonas salmonicida 97-4 (MIC=32 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=16 µg/ml), Salmonella enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), Pseudomonas aeruginosa Z61 (MIC=8 µg/ml), Escherichia coli CGSC 4908 (MIC=32 µg/ml), Escherichia coli UB1005 (MIC=32 µg/ml), Escherichia coli DC2 (MIC=32 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=32 µg/ml), Staphylococcus aureus C623 (MRSA) (MIC=64 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02352 GWKKWLRKGAKHLGQAAIK 19 NRC-16 (fish, chordates, animals) No entry found Not found Not found Glyptocephalus cynoglossus (Witch flounder GC3.8-t) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=2 µg/ml), A. salmonicida 97-4 (MIC=1 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=0.5 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=16 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Pseudomonas aeruginosa Z61 (MIC=1 µg/ml), Escherichia coli CGSC 4908 (MIC=1 µg/ml), E. coli UB1005 (MIC=2 µg/ml), E. coli DC2 (MIC=0.5 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=16 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=32 µg/ml).##Yeast: Candida albicans C627 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02354 FFRLLFHGVHHGGGYLNAA 19 Pleurocidin-like peptide WFY (fish, chordates, animals) No entry found Not found Not found Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida A449 field isolate (MIC>64 µg/ml), A. salmonicida 97-4 field isolate (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=64 µg/ml), Escherichia coli CGSC4908 triple (MIC=64 µg/ml), Salmonella typhimurium 14028s (MIC>64 µg/ml), Salmonella typhimurium MS7953s (MIC=64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis (human clinical isolates) (MIC>64 µg/ml), Staphylococcus aureus (MRSA) (MIC>64 µg/ml).##Fungi: Candida albica (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12950255 Eur J Biochem. 2003 Sep;270(18):3720-3730. Douglas SE, Patrzykat A, Pytyck J, Gallant JW. Identification, structure and differential expression of novel pleurocidins clustered on the genome of the winter flounder, Pseudopleuronectes americanus (Walbaum). DRAMP02357 FLGALIKGAIHGGRFIHGMIQNHH 24 Pleurocidin-like peptide WF3 (NRC-5; fish, chordates, animals) Q90VW7 Belongs to the pleurocidin family ple3 Pseudopleuronectes americanus (Winter flounder 3) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC>64 µg/ml), A. salmonicida 97-4 (MIC>64 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=64 µg/ml), Salmonella enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=32 µg/ml), Escherichia coli CGSC 4908 (MIC=64 µg/ml), Escherichia coli UB1005 (MIC=64 µg/ml), Escherichia coli DC2 (MIC>64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=32 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=32 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506##11113283 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470.##Dev Comp Immunol. 2001 Mar;25(2):137-147. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE.##Douglas SE, Gallant JW, Gong Z, Hew C. Novel antimicrobial peptides derived from flatfish genes.##Cloning and developmental expression of a family of pleurocidin-like antimicrobial peptides from winter flounder, Pleuronectes americanus (Walbaum). DRAMP02358 GWGSIFKHGRHAAKHIGHAAVNHYL 25 Pleurocidin-like peptide WF4 (NRC-6; fish, chordates, animals) Q90ZX8, Q90ZX9 Belongs to the pleurocidin family ple4 Pseudopleuronectes americanus (Winter flounder 4-1.1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found 6RZC Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=4 µg/ml), A. salmonicida 97-4 (MIC=4 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=4 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=64 µg/ml), Pseudomonas aeruginosa K799 (MIC=16 µg/ml), Pseudomonas aeruginosa Z61 (MIC=4 µg/ml), Escherichia coli CGSC 4908 (MIC=4 µg/ml), E. coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=2 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC>64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=32 µg/ml).##Yeast: Candida albicans C627 (MIC=32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506##11113283 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470.##Dev Comp Immunol. 2001 Mar;25(2):137-147. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE.##Douglas SE, Gallant JW, Gong Z, Hew C. Novel antimicrobial peptides derived from flatfish genes.##Cloning and developmental expression of a family of pleurocidin-like antimicrobial peptides from winter flounder, Pleuronectes americanus (Walbaum). DRAMP02359 RWGKWFKKATHVGKHVGKAALTAYL 25 Pleurocidin-like peptide YT2 (NRC-7; fish, chordates, animals; Predicted) Q7SZH1 Not found ple Limanda ferruginea (Yellowtail flounder YT2) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=4 µg/ml), A. salmonicida 97-4 (MIC=2 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=2 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Pseudomonas aeruginosa Z61 (MIC=2 µg/ml), Escherichia coli CGSC 4908 (MIC=4 µg/ml), E. coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=64 µg/ml).##Yeast: Candida albicans C627 (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02360 GWKSVFRKAKKVGKTVGGLALDHYLG 26 Pleurocidin-like peptide AP1 (NRC-11; fish, chordates, animals; Predicted) Q7SZH4 Not found ple Hippoglossoides platessoides (American plaice AP1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=8 µg/ml), A. salmonicida 97-4 (MIC=8 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=4 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=32 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), Pseudomonas aeruginosa Z61 (MIC=4 µg/ml), Escherichia coli CGSC 4908 (MIC=4 µg/ml), E. coli UB1005 (MIC=16µg/ml), E. coli DC2 (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC>64 µg/ml).##Yeast: Candida albicans C627 (MIC=32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02361 GWKKWFNRAKKVGKTVGGLAVDHYLG 26 Pleurocidin-like peptide AP2 (NRC-12; fish, chordates, animals; Predicted) Q7SZH3 Not found ple Hippoglossoides platessoides (American plaice AP2) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=2 µg/ml), A. salmonicida 97-4 (MIC=2 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=2 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=8µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Pseudomonas aeruginosa Z61 (MIC=1 µg/ml), Escherichia coli CGSC 4908 (MIC=2 µg/ml), E. coli UB1005 (MIC=8 µg/ml), E. coli DC2 (MIC=2 µg/ml);##Gram-positive bacteria: S. epidermidis C621 (MIC=8 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=16 µg/ml).##Yeast: Candida albicans C627 (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02362 GWRTLLKKAEVKTVGKLALKHYL 23 Pleurocidin-like peptide AP3 (NRC-13; fish, chordates, animals; Predicted) Q7SZH2 Not found ple Hippoglossoides platessoides (American plaice AP3) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=4 µg/ml), A. salmonicida 97-4 (MIC=2 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=2 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Pseudomonas aeruginosa Z61 (MIC=1 µg/ml), Escherichia coli CGSC 4908 (MIC=2 µg/ml), E. coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=2 µg/ml).##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=4 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=4 µg/ml).##Yeast: Candida albicans C627 (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02363 AGWGSIFKHIFKAGKFIHGAIQAHND 26 Pleurocidin-like peptide GcSc4C5 (NRC-14; fish, chordates, animals) Q7SZH0 Not found ple Glyptocephalus cynoglossus (Witch flounder GcSc4C5) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=32 µg/ml), A. salmonicida 97-4 (MIC=16 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=16 µg/ml), S. enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), Pseudomonas aeruginosa Z61 (MIC=8 µg/ml), Escherichia coli CGSC 4908 (MIC=16 µg/ml), E. coli UB1005 (MIC=16 µg/ml), E. coli DC2 (MIC=16 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=16 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=16 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02364 GFWGKLFKLGLHGIGLLHLHL 21 Pleurocidin-like peptide GcSc4B7 (NRC-15; fish, chordates, animals; Predicted) Q7SZG9 Not found ple Glyptocephalus cynoglossus (Witch flounder GcSc4B7) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=8 µg/ml), A. salmonicida 97-4 (MIC=16 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=4 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=16 µg/ml), Pseudomonas aeruginosa K799 (MIC=8 µg/ml), Pseudomonas aeruginosa Z61 (MIC=4 µg/ml), Escherichia coli CGSC 4908 (MIC=8 µg/ml), E. coli UB1005 (MIC=8 µg/ml), E. coli DC2 (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=4 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=4 µg/ml).##Yeast: Candida albicans C627 (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02365 GWKKWLRKGAKHLGQAAIKGLAS 23 Pleurocidin-like peptide GC3.8 (NRC-17; fish, chordates, animals; Predicted) Q7SZG8 Not found ple Glyptocephalus cynoglossus (Witch flounder GC3.8) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=2 µg/ml), A. salmonicida 97-4 (MIC=1 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=1 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Pseudomonas aeruginosa Z61 (MIC=2 µg/ml), Escherichia coli CGSC 4908 (MIC=1 µg/ml), E. coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=1 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=32 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=16 µg/ml).##Yeast: Candida albicans C627 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02366 GWKKWFTKGERLSQRHFA 18 Pleurocidin-like peptide GC3.2 (NRC-18; fish, chordates, animals; Predicted) Q7SZG7 Not found ple Glyptocephalus cynoglossus (Witch flounder GC3.2) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC>64 µg/ml), A. salmonicida 97-4 (MIC=128 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=32 µg/ml), S. enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=64 µg/ml), Escherichia coli CGSC 4908 (MIC=64 µg/ml), E. coli UB1005 (MIC=64 µg/ml), E. coli DC2 (MIC=64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC>64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC>64 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02367 FLGLLFHGVHHVGKWIHGLIHGHH 24 Pleurocidin-like peptide Hb26 (NRC-19; fish, chordates, animals; Predicted) Q7SZG6 Not found ple Hippoglossus hippoglossus (Halibut Hb26) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC=64 µg/ml), A. salmonicida 97-4 (MIC>64 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC=16 µg/ml), S. enterica serovar Typhimurium 14028s (MIC=64 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), Pseudomonas aeruginosa Z61 (MIC=8 µg/ml), Escherichia coli CGSC 4908 (MIC=32 µg/ml), E. coli UB1005 (MIC=16 µg/ml), E. coli DC2 (MIC=32 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC=8 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC=8 µg/ml).##Yeast: Candida albicans C627 (MIC=64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02368 GFLGILFHGVHHGRKKALHMNSERRS 26 Pleurocidin-like peptide Hb18 (NRC-20; fish, chordates, animals; Predicted) Q7SZG5 Not found ple Hippoglossus hippoglossus (Halibut Hb18) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Aeromonas salmonicida 99-1 (MIC>64 µg/ml), A. salmonicida 97-4 (MIC>64 µg/ml), Salmonella enterica serovar Typhimurium MS7953s (MIC>64 µg/ml), S. enterica serovar Typhimurium 14028s (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC=64 µg/ml), Escherichia coli CGSC 4908 (MIC>64 µg/ml), E. coli UB1005 (MIC>64 µg/ml), E. coli DC2 (MIC>64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis C621 (MIC>64 µg/ml), Staphylococcus aureus (MRSA) C623 (MIC>64 µg/ml).##Yeast: Candida albicans C627 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878506 Antimicrob Agents Chemother. 2003 Aug;47(8):2464-2470. Patrzykat A, Gallant JW, Seo JK, Pytyck J, Douglas SE. Novel antimicrobial peptides derived from flatfish genes. DRAMP02374 GCRFCCNCCPNMSGCGVCCRF 21 Bass hepcidin (fish, chordates, animals) P82951 Belongs to the hepcidin family hamp Morone chrysops x Morone saxatilis (white bass x striped sea-bass) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Beta strand (2 strands; 6 residues) Solution structure by NMR indicates that bass hepcidin is very similar to that of human hepcidin, including the presence of an antiparallel beta-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond. 1S6W resolved by NMR. "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity). Synthetic bass hepcidin is active in vitro against Gram-negative pathogens and fungi but showes no activity against key Gram-positive pathogens and a single yeast strain tested. Tissue specificity: Predominantly expressed in liver. Induction: By bacterial challenge. PTM: Contains four disulfide bonds 2-19; 5-8; 6-15; 9-18." Gram-negative bacteria: Escherichia coli ATCC 25,922,351,50 (MIC=22 µM), Escherichia coli ATCC D31K (MIC=11 µM), Klebsiella pneumoniae ATCC 10,031 (MIC=22 µM), P. shigelloides ATCC KST (MIC=11 µM), S. flexneri ATCC 12,022 (MIC=22 µM), Shigella sonnei ATCC 9290 (MIC=44 µM), Y. enterocolitica ATCC 23,715 (MIC=22 µM).##Fungi: Aspergillus niger (MIC=44 µM). [Ref.15546886] It displays essentially no hemolytic activity toward HSB erythrocytes Cyclic Free Free Disulfide bonds between Cys2 and Cys19; Cys5 and Cys8; Cys6 and Cys15,Cys9 and Cys18. L No cytotoxicity information found Not found 11985602##15546886 Eur J Biochem. 2002 Apr;269(8):2232-2237.##J Biol Chem. 2005 Mar 11;280(10):9272-9282. Shike H, Lauth X, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Shimizu C, Bulet P, Burns JC.##Lauth X, Babon JJ, Stannard JA, Singh S, Nizet V, Carlberg JM, Ostland VE, Pennington MW, Norton RS, Westerman ME. Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge.##Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections. DRAMP02376 LFGFLIKLIPSLFGALSNIGRNRNQ 25 Grammistin Gs 1 (Grammistin Gs F; Group I grammistin; soapfish, chordates, animals) P69835 Belongs to the grammistin family (Group 1 subfamily) Not found Grammistes sexlineatus (Sixline soapfish) (Golden stripe soapfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=25 µg/ml), Staphylococcus aureus IAM 1011 (MIC=6.25 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=50 µg/ml), Escherichia coli JCM 1649 (MIC=50 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=12.5 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=12.5 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=50 µg/ml), Vibrio parahaemolyticus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Fish. Sci. 2001 Oct;67:928-933. Yokota H, Nagashima Y, Shiomi K. Interaction of grammistins with lipids and their antibacterial activity. DRAMP02377 LFGFLIPLLPHIIGAIPQVIGAIR 24 Grammistin Gs 2 (Grammistin Gs G; Group I grammistin; soapfish, chordates, animals) P69836 Belongs to the grammistin family (Group 1 subfamily) Not found Grammistes sexlineatus (Sixline soapfish) (Golden stripe soapfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=12.5 µg/ml), Staphylococcus aureus IAM 1011 (MIC=6.25 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=50 µg/ml), Escherichia coli JCM 1649 (MIC=50 µg/ml), Photobacterium damselae subsp. Piscicida Sp 9587 (MIC=6.25 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=6.25 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=25 µg/ml), Vibrio parahaemolyticus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Fish. Sci. 2001 Oct;67:928-933. Yokota H, Nagashima Y, Shiomi K. Interaction of grammistins with lipids and their antibacterial activity. DRAMP02378 WWRELLKKLAFTAAGHLGSVLAAKQSGW 28 Grammistin Gs A (Group III grammistin; soapfish, chordates, animals) P69845 Belongs to the grammistin family (Group 3 subfamily) Not found Grammistes sexlineatus (Sixline soapfish) (Golden stripe soapfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=25 µg/ml), Staphylococcus aureus IAM 1011 (MIC=12.5 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=25 µg/ml), Escherichia coli JCM 1649 (MIC=50 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=25 µg/ml), Salmonella typhimurium S1 (MIC>50 µg/ml), S. putrefaciens IAM 1509 (MIC=6.25 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=50 µg/ml), Vibrio parahaemolyticus (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15777955 Toxicon. 2005 Apr;45(5):595-601. Sugiyama N, Araki M, Ishida M, Nagashima Y, Shiomi K. Further isolation and characterization of grammistins from the skin secretion of the soapfish Grammistes sexlineatus. DRAMP02379 IGGIISFFKRLF 12 Grammistin Gs B (Group II grammistin; soapfish, chordates, animals) P69839 Belongs to the grammistin family (Group 2 subfamily) Not found Grammistes sexlineatus (Sixline soapfish) (Golden stripe soapfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=6.25 µg/ml), Staphylococcus aureus IAM 1011 (MIC=6.25 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=25 µg/ml), Escherichia coli JCM 1649 (MIC=12.5 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=6.25 µg/ml), Salmonella typhimurium S1 (MIC=12.5 µg/ml), S. putrefaciens IAM 1509 (MIC=3.13 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=6.25 µg/ml), Vibrio parahaemolyticus (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15777955 Toxicon. 2005 Apr;45(5):595-601. Sugiyama N, Araki M, Ishida M, Nagashima Y, Shiomi K. Further isolation and characterization of grammistins from the skin secretion of the soapfish Grammistes sexlineatus. DRAMP02380 NWRKILGKIAKVAAGLLGSMLAGYQV 26 Grammistin Gs C (Group III grammistin; soapfish, chordates, animals) P69846 Belongs to the grammistin family (Group 3 subfamily) Not found Grammistes sexlineatus (Sixline soapfish) (Golden stripe soapfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found MOA: Thanks to its amphiphilic alpha-helice(s), it may integrate into membrane phospholipids, leading to lysis of the membrane. Gram-positive bacteria: Bacillus subtilis IAM 1026 (MIC=6.25 µg/ml), Staphylococcus aureus IAM 1011 (MIC=12.5 µg/ml);##Gram-negative bacteria: Aeromonas salmonicida NCIBM 1102 (MIC=25 µg/ml), Escherichia coli JCM 1649 (MIC=12.5 µg/ml), P. dameselae subsp. Piscicida Sp 9587 (MIC=6.25 µg/ml), Salmonella typhimurium S1 (MIC=12.5 µg/ml), S. putrefaciens IAM 1509 (MIC=6.25 µg/ml), Vibrio anguillarum NCIBM 829 (MIC=12.5 µg/ml), Vibrio parahaemolyticus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15777955 Toxicon. 2005 Apr;45(5):595-601. Sugiyama N, Araki M, Ishida M, Nagashima Y, Shiomi K. Further isolation and characterization of grammistins from the skin secretion of the soapfish Grammistes sexlineatus. DRAMP18375 GLDFSQPFPSGEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFLCCRQRI 51 hBD-5 (human beta-defensin 5) No entry found Belongs to the beta-defensin family. Not found Homo sapiens Antimicrobial, Antibacterial bridge Not found PTM: There are 7 cysteines, making it likely to form an intermolecular S-S bond. Active against E. coli K12. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12193721 J Immunol. 2002 Sep 1;169(5):2516-23. Yamaguchi Y, Nagase T, Makita R, Fukuhara S, Tomita T, Tominaga T, Kurihara H, Ouchi Y. Identification of multiple novel epididymis-specific beta-defensin isoforms in humans and mice. DRAMP18373 CMSYGGSCQRSCNGGFRLGGHCGHPKIRCCRRK 33 mBD-6 (Murine beta-defensin 6) No entry found Belongs to the beta-defensin family. Not found Mus musculus Antimicrobial, Antibacterial, Anti-Gram- bridge Not found Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11408484 J Biol Chem. 2001 Aug 24;276(34):31510-4 Yamaguchi Y, Fukuhara S, Nagase T, Tomita T, Hitomi S, Kimura S, Kurihara H, Ouchi Y. A novel mouse beta-defensin, mBD-6, predominantly expressed in skeletal muscle. DRAMP18374 FFDEKCNKLKGTCKNNCGKNEELIALCQKSLKCCRTIQPSGSIID 45 hBD-6 (human beta-defensin 6) No entry found Belongs to the beta-defensin family. Not found Homo sapiens Antimicrobial, Antibacterial, Anti-Gram-, Chemotactic beta Not found 2LWL Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli K12. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12193721 J Immunol. 2002 Sep 1;169(5):2516-23 Yamaguchi Y, Nagase T, Makita R, Fukuhara S, Tomita T, Tominaga T, Kurihara H, Ouchi Y. Identification of multiple novel epididymis-specific beta-defensin isoforms in humans and mice. DRAMP02386 KGRGKQGGKVRAKAKTRSS 19 Parasin I (histone-H2A-derived; catfishes, chordates, animals) No entry found Not found Not found Parasilurus asotus (Amur catfish) Antimicrobial, Antibacterial Not found Alpha helix Not found Comment: No comments found on DRAMP database Aeromonas salmonicida (MIC=10 µg/ml), Cytophaga aquatilis (MIC=5 µg/ml), Yersinia rukeri (MIC=15 µg/ml), Edwardsiella ictaluri (MIC=10 µg/ml), Lactococcus garvieae (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 9824303 FEBS Lett 1998; 437: 258-262. Park IY, Park CB, Kim MS, Kim SC. Parasin I, an antimicrobial peptide derived from histon H2A in the catfish, Parasilurus asotus. DRAMP02390 RPRPNYRPRPIYRP 14 Astacidin 2 (crayfish, Arthropods, animals) Q0PJU7 Not found Not found Pacifastacus leniusculus (signal crayfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Rich Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Shigella flexneri ATCC 203 (MIC=0.98 µg/ml), Proteus vulgaris OX19 ATCC 6380 (MIC=7.8 µg/ml), Escherichia coli D21 (MIC=3.9 µg/ml), Psedomonas aeruginosa OT 97 (MIC=7.8 µg/ml).##Gram-positive bacteria: Bacillus megateriun B11 (MIC=1.9 µg/ml), Bacillus subtilis ATCC 6633 (MIC=1.95 µg/ml), Staphylococcus aureus JC-1 (MIC=7.8 µg/ml), Micrococcus luteus Ml 11 (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17049601 Dev Comp Immunol. 2007;31(5):441-455. Jiravanichpaisal P, Lee SY, Kim YA, Andrén T, Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern. DRAMP02391 GWFKKAWRKVKHAGRRVLDTAKGVGRHYLNNWLNRYRG 38 Hematopoietic antimicrobial peptide-37 (MgCath37; hagfishes, chordates, animals) Q71MD7 Not found CATH37 Myxine glutinosa (Atlantic hagfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Propionibacterium acnes ATCC 11827 and 33179 (MIC=2 µg/ml), Staphylococcus epidermidi (MIC=2-4 µg/ml), Streptococcus pyogenes (MIC=4 µg/ml), Enterococcus faecium (MIC=4-8 µg/ml), Staphylococcus aureus ATCC 29213 (MIC=8 µg/ml), Clostridium perfringens ATCC 9081 and 13124 (MIC=4-32 µg/ml), Enterococcus faecalis (MIC=32 µg/ml);##Gram-negative bacteria: Bacteroides spp. ATCC 29771, 43935, 12290 (MIC=0.5-4 µg/ml), Shigella sonnei (MIC=2-4 µg/ml), Xanthomonas maltophilia (MIC=2-8 µg/ml), Salmonella Group B (MIC=4-8 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/ml), Acinetobacter baumannii (MIC=8-16 µg/ml), Escherichia coli ATCC 25922 (MIC=8 µg/ml), Enterobacter aerogenes (MIC=8-16 µg/ml), Enterobacter cloacae (MIC=8-16 µg/ml), Klebsiella pneumoniae (MIC=8-16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019197 Peptides. 2003 Nov;24(11):1655-1667. Uzzell T, Stolzenberg ED, Shinnar AE, Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. DRAMP02393 GFFKKAWRKVKHAGRRVLDTAKGVGRHYVNNWLNRYRZ 38 HFIAP-1 (HFIAP-2; hagfishes, chordates, animals) No entry found Not found Not found Myxine glutinosa (Atlantic hagfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found "Function: Has antibacterial against a bank of Gram-negative and Gram-positive bacteria as well as a representative fungal species. Sequence similarity: Sequences for HFIAP-1 and -2 are identical, but HFIAP-2 is brominated only at residue 7; they differ from MgCath37 by conservative replacements." Gram-positive bacteria: Propionibacterium acnes ATCC 11827/33179 (MIC=2 µg/ml), Staphylococcus epidermidi (MIC=2-4 µg/ml), Streptococcus pyogenes (MIC=4 µg/ml), Enterococcus faecium (MIC=4-8 µg/ml), Staphylococcus aureus ATCC 29213 (MIC=8 µg/ml), Clostridium perfringens ATCC 9081/13124 (MIC=4-32 µg/ml), Enterococcus faecalis (MIC=32 µg/ml);##Gram-negative bacteria: Bacteroides spp. ATCC 29771/43935/12290 (MIC=0.5-4 µg/ml), Shigella sonnei (MIC=2-4 µg/ml), Xanthomonas maltophilia (MIC=2-8 µg/ml), Salmonella Group B (MIC=4-8 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/ml), Acinetobacter baumannii (MIC=8-16 µg/ml), Escherichia coli ATCC 25922 (MIC=8 µg/ml), Enterobacter aerogenes (MIC=8-16 µg/ml), Enterobacter cloacae (MIC=8-16 µg/ml), Klebsiella pneumoniae (MIC=8-16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019197 Peptides. 2003 Nov;24(11):1655-1667. Uzzell T, Stolzenberg ED, Shinnar AE, Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. DRAMP02394 GWFKKAWRKVKNAGRRVLKGVGIHYGVGLIZ 31 HFIAP-3 (hagfishes, chordates, animals) No entry found Not found Not found Myxine glutinosa (Atlantic hagfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial against a bank of Gram-negative and Gram-positive bacteria as well as a representative fungal species. HFIAP-1 and HFIAP-3 exhibit similar inhibitory activity. Gram-positive bacteria: Propionibacterium acnes ATCC 11827/33179 (MIC=2 µg/ml), Staphylococcus epidermidi (MIC=2-4 µg/ml), Streptococcus pyogenes (MIC=4 µg/ml), Enterococcus faecium (MIC=4-8 µg/ml), Staphylococcus aureus ATCC 29213 (MIC=8 µg/ml), Clostridium perfringens ATCC 9081/13124 (MIC=4-32 µg/ml), Enterococcus faecalis (MIC=32 µg/ml);##Gram-negative bacteria: Bacteroides spp. ATCC 29771/43935/12290 (MIC=0.5-4 µg/ml), Shigella sonnei (MIC=2-4 µg/ml), Xanthomonas maltophilia (MIC=2-8 µg/ml), Salmonella Group B (MIC=4-8 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/ml), Acinetobacter baumannii (MIC=8-16 µg/ml), Escherichia coli ATCC 25922 (MIC=8 µg/ml), Enterobacter aerogenes (MIC=8-16 µg/ml), Enterobacter cloacae (MIC=8-16 µg/ml), Klebsiella pneumoniae (MIC=8-16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019197 Peptides. 2003 Nov;24(11):1655-1667. Uzzell T, Stolzenberg ED, Shinnar AE, Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. DRAMP02395 AACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC 40 Aurelin (jellyfish, chordates, animals) Q0MWV8, P84891 Belongs to ShKT domain family Not found Aurelia aurita (Moon jellyfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Not found 2LG4 resolved by NMR. "Function: Antimicrobial peptide exhibits activity against Gram-positive and Gram-negative bacteria. Domian: Contains 1 ShKT domain. PTM: Contains three disulfide bonds (By similarity)." Gram-positive bacterium: Listeria monocytogenes EGD (MIC=22.64 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35p (MIC=7.66 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys19 and Cys40) Disulfide bonds between Cys3 and Cys33; Cys12 and Cys37; Cys19 and Cys40. L No cytotoxicity information found Not found 16890198##PubMed ID is not available Biochem Biophys Res Commun. 2006 Sep 22;348(2):514-523.##To be Published. Ovchinnikova TV, Balandin SV, Aleshina GM, Tagaev AA, Leonova YF, Krasnodembsky ED, Men'shenin AV, Kokryakov VN.##Shenkarev Z, Altukhov D, Gizatullina A, Arseniev A, Ovchinnikova T. Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins.##Solution structure of aurelin, a novel antimicrobial peptide. DRAMP02397 AVPDVAFNAYG 11 Big defensin (RPD-1) P86316 Belongs to the big defensin family Not found Venerupis philippinarum (Japanese carpet shell) (Tapes japonica) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Not found Not found Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro. Has antibacterial activity. Gram-positive bacteria: Staphylococcus aureus (MIC=9.6 mg/L), Bacillus subtilis (MIC=76.8 mg/L), Micrococcus tetragenus (MIC=38.4 mg/L);##Gram-negative bacteria: Escherichia coli (MIC=76.8 mg/L), Vibrio parahaemolyticus (MIC=19.2 mg/L), Vibrio anguillarum (MIC=19.2 mg/L). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14673509 Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Dec;35(12):1145-8. Wei YX, Guo DS, Li RG, Chen HW, Chen PX. Purification of a big defensin from Ruditapes philippinesis and its antibacterial activity. DRAMP02402 FLPKMSTKLRVPYRRGTKDYH 21 Antimicrobial peptide scolopin-1 P0CH48 Not found Not found Scolopendra mutilans (Chinese red-headed centipede) (Scolopendrasubspinipes mutilans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide against both Gram-positive, Gram-positive and yeast. Also induces histamine release by mast cells and shows hemolytic activities against both human and rabbit red cells. Tissue specificity: Expressed by the venom gland." [Ref.19716842]Gram-negative bacteria: Escherichia coli standard strain (MIC=12.5 µg/ml), E. coli drug-resistant strain (MIC=15 µg/ml);##Gram-positive bacteria: Staphylococcus aureus standard strain (MIC=1.2 µg/ml), S. aureus drug-resistant strain (MIC=5.0 µg/ml), Bacillus dysenteriae standard and drug-resistant strains (MIC=7.5 µg/ml);##Yeast: Candida albicans (MIC=15 µg/ml). [Ref.19716842]25 ± 2% hemolytic activity at 50 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19716842 Toxicon. 2010 Feb-Mar;55(2-3):274-279. Peng K, Kong Y, Zhai L, Wu X, Jia P, Liu J, Yu H. Two novel antimicrobial peptides from centipede venoms. DRAMP02403 GILKKFMLHRGTKVYKMRTLSKRSH 25 Antimicrobial peptide scolopin-2 P0CH49 Not found Not found Scolopendra mutilans (Chinese red-headed centipede) (Scolopendrasubspinipes mutilans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide against both Gram-positive, -negative and yeast. Also induces histamine release by mast cells and shows hemolytic activities against both human and rabbit red cells. Tissue specificity: Expressed by the venom gland." [Ref.19716842]Gram-negative bacteria: Escherichia coli standard and drug-resistant strains (MIC=5.0 µg/ml);##Gram-positive bacteria: Staphylococcus aureus standard strain (MIC=0.5 µg/ml), S. aureus drug-resistant strain (MIC=1.0 µg/ml), Bacillus dysenteriae standard strain (MIC=2.5 µg/ml), B. dysenteriae drug-resistant strain (MIC=5.0 µg/ml);##Yeast: Candida albicans (MIC=7.5 µg/ml). [Ref.19716842]32 ± 7% hemolytic activity at 50 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19716842 Toxicon. 2010 Feb-Mar;55(2-3):274-279. Peng K, Kong Y, Zhai L, Wu X, Jia P, Liu J, Yu H. Two novel antimicrobial peptides from centipede venoms. DRAMP02409 GCLEFWWKCNPNDDKCCRPKLKCSKLFKLCNFSF 34 M-theraphotoxin-Gr1a (M-TRTX-Gr1a; GsMTx-4) Q7YT39, Q7M3T1 Belongs to the huwentoxin-1 family Not found Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand (5 strands; 9 residues) Not found 1LU8, 1TYK resolved by NMR. "Function: This cationic hydrophobic peptide inhibits a lot of different channels and has an antimicrobial activity. It blocks mechanosensitive ion channels (also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. Acts by partitioning into the membrane and perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. Inhibits atrial fibrillation as well as the membrane motor of outer hair cells at low doses. GsMTx-4 exhibites antimicrobial properties and was more active against Gram-positive than Gram-negative bacteria. Tissue specificity: Expressed by the venom gland. Miscellaneous: This toxin does not inhibit potassium channels Kv1.1/KCNA1 (IC50>85 µM), Kv1.4/KCNA4 (IC50>85 µM) and Kv11.3/KCNH7 (IC50=53 µM). PTM: Contains three disulfide bonds." Gram-positive bacteria: Bacillus subtilis (MIC=0.5 µM), Staphylococcus aureus (MIC=2-4 µM), Staphylococcus epidermidis (MIC=4-8 µM);##Gram-negative bacteria: Salmonella typhimurium (MIC=32.64 µM), Pseudomonas aeruginosa (MIC=8-16 µM), Escherichia coli (MIC=8-16 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys2 and Cys17,Cys9 and Cys23,Cys16 and Cys30. L No cytotoxicity information found Not found PubMed ID is not available##12082099##10779316##163768 Submitted (MAY-2002) to the PDB data bank##J Biol Chem. 2002 Sep 13;277(37):34443-50.##J Gen Physiol. 2000 May;115(5):583-598.##Biochem Biophys Res Commun. 2006 Feb 10;340(2):633-638. Jung HJ, Lee CW, Earm YE, Kim JI.##Oswald RE, Suchyna TM, McFeeters R, Gottlieb P, Sachs F.##Suchyna TM, Johnson JH, Hamer K, Leykam JF, Gage DA, Clemo HF, Baumgarten CM, Sachs F.##Jung HJ, Kim PI, Lee SK, Lee CW, Eu YJ, Lee DG, Earm YE, Kim JI. Solution structure of GsMTx-4, a peptide blocker of cation-selective stretch-activated channels.##Solution structure of peptide toxins that block mechanosensitive ion channels.##Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels.##Lipid membrane interaction and antimicrobial activity of GsMTx-4, an inhibitor of mechanosensitive channel. DRAMP02410 FSKYERQKDKRPYSERKNQYTGPQFLYPPERIPPQKVIKWNEEGLPIYEIPGEGGHAEPAAA 62 Antimicrobial peptide lumbricin-1 O96447 Not found Not found Lumbricus rubellus (Humus earthworm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Displays antimicrobial activity and weak hemolytic activity. Developmental stage: Adult-specific. Not detected in eggs or 1-week-old worms but abundant in 6-month-old worms. Induction: Constitutively expressed. Not induced by bacterial infection." [Ref.9784609]Gram-positive bacteria: Bacillus subtilis ATCC 62037 (MIC=12 µg/ml), Staphylococcus aureus ATCC 15752 (MIC=16 µg/ml), Streptococcus mutans ATCC 25175 (MIC=30 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 27325 (MIC=12 µg/ml), Pseudomonas putidaATCC 17426 (MIC=16 µg/ml), Serratia sp. ATCC 21074 (MIC=16 µg/ml);##Fungi: Candida albicans ATCC 10231 (MIC=16 µg/ml), Cryptococcus neoformance ATCC 34881 (MIC=25 µg/ml), Saccharomyces cerevisiae ATCC 44774 (MIC=12 µg/ml).##NOTE: Minimal inhibitory concentrations were determined by incubating approximately 104–105 CFU/ml of cells with serial dilutions of each peptide in a 96-well microtiter plate. [Ref.9784609]0.02% hemolytic activity at 5 μg/ml, 0.06% hemolytic activity at 10 μg/ml, 0.14% hemolytic activity at 25 μg/ml, 0.19% hemolytic activity at 50 μg/ml, 0.23% hemolytic activity at 100 μg/ml against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784609 Biochim Biophys Acta. 1998 Oct 22;1408(1):67-76. Cho JH, Park CB, Yoon YG, Kim SC. Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization. DRAMP02411 GHLGRPYIGGGGGFNRGGGFHRGGGFHRGGGFHSGGGFHRGGGFHSGGSFGYR 53 Armadillidin (Glyc-rich) Q64HC7 Not found Not found Armadillidium vulgare (Pillbug) (Pill woodlouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium B. megaterium LM101. Tissue specificity: Expressed in hemocytes and at very low levels in ovary. Not expressed in adipose tissue, brain, caecum, gut, heart and nervous chain. PTM C-terminal amidation." Gram-positive bacteria: Bacillus megaterium LM101 (MIC=0.5-1.25 µM), Enterococcus faecalis LM002, Micrococcus luteus LM610, Listeria ivanovii BUG496;##Gram-negative bacteria: Escherichia coli JM83, Salmonella thyphimurium LM122, Enterobacter cloacae LM111, Citrobacter freundii LM457.##NOTE: Because of the low amount of the purified peptide, this minimal concentration activity is only tested on B. megaterium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752546 Dev Comp Immunol. 2005;29(6):489-499. Herbinière J, Braquart-Varnier C, Grève P, Strub JM, Frère J, Van Dorsselaer A, Martin G. Armadillidin: a novel glycine-rich antibacterial peptide directed against Gram-positive bacteria in the woodlouse Armadillidium vulgare (terrestrial isopod, crustacean). DRAMP02412 SYVGDCGSNGGSCVSSYCPYGNRLNYFCPLGRTCCRHAYV 40 Panusin (Defensin-like peptide 7, PaD7) F6KSI8 Belongs to the beta-defensin family Not found Panulirus argus (Caribbean spiny lobster) (Palinurus argus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Has antibacterial activity. PTM: Contains two disulfide bonds (By similarity)." Gram-positive bacterium: Staphylococcus aureus ATCC 29737 (MIC=3.46 µM);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=4.8 µM). [Ref.27616720] It shows no hemolytic effect on human red blood cells Cyclic Free Free Disulfide bonds between Cys6 and Cys28,Cys13 and Cys34,Cys18 and Cys35. L No cytotoxicity information found Not found 22885029##PubMed ID is not available Fish Shellfish Immunol. 2012 Oct;33(4):872-879.##Submitted (FEB-2012) to UniProtKB Montero-Alejo V, Acosta-Alba J, Perdomo-Morales R, Perera E, Hernández-Rodríguez EW, Estrada MP, Porto-Verdecia M.##Montero-Alejo V, Pacios-Michelena A, Perdomo-Morales R, Crozo G, Vega-Hurtado Y. Defensin like peptide from Panulirus argus relates structurally with beta defensin from vertebrates.##Panusin, a new defensin-like antimicrobial peptide from the hemocytes of spiny lobster Panulirus argus. DRAMP02419 YENPYGCPTDEGKCFDRCNDSEFEGGYCGGSYRATCVCYRT 41 Amblyomma defensin peptide 2 (ADP-2; Ticks, Arthropods, animals) No entry found Not found Not found Amblyomma hebraeum (Tick) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Escherichia coli (MIC=30 µM) and Staphylococcus aureus (MIC=7.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Has three disulfide bonds l No cytotoxicity information found Not found 14705963 Biochem J. 2004 May 1;379(Pt 3):681-685. Lai R, Lomas LO, Jonczy J, Turner PC, Rees HH. Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, Amblyomma hebraeum. DRAMP02421 ACHAHCQSVGRRGGYCGNFRMTCYCY 26 Hlgut-defensin (H. longicornis midgut defensin; Ticks, Arthropods, animals) A4GUC3 Not found Not found Haemaphysalis longicornis (Bush tick) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found "Function: Both Hlgut-defensin and Hlsal-defensin sequences have antibactrrial activity against a variety of Gram-positive and Gram-negative bacteria. Induction: By a lipopolysaccharide (LPS) injection." Gram-positive bacterium: Staphylococcus aureus (MIC=5-25 mg/mL);##Gram-negative bacterium: Escherichia coli (MIC=10-25 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17521774 Peptides. 2007 Jun;28(6):1304-1310. Zhou J, Liao M, Ueda M, Gong H, Xuan X, Fujisaki K. Sequence characterization and expression patterns of two defensin-like antimicrobial peptides from the tick Haemaphysalis longicornis. DRAMP02422 NCIQQCVSKGAQGGYCTNEKCTCY 24 Hlsal-defensin (H. longicornis salivary gland defensin; Ticks, Arthropods, animals) A4GUC4 Not found Not found Haemaphysalis longicornis (Bush tick) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found "Function: Both Hlgut-defensin and Hlsal-defensin sequences have antibactrrial activity against a variety of Gram-positive and Gram-negative bacteria. Induction: By a lipopolysaccharide (LPS) injection." Gram-positive bacterium: Staphylococcus aureus (MIC=5-25 mg/mL);##Gram-negative bacterium: Escherichia coli (MIC=10-25 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17521774 Peptides. 2007 Jun;28(6):1304-1310. Zhou J, Liao M, Ueda M, Gong H, Xuan X, Fujisaki K. Sequence characterization and expression patterns of two defensin-like antimicrobial peptides from the tick Haemaphysalis longicornis. DRAMP02423 DFGCARGMIFVCMRRCARMYPGSTGYCQGFRCMCDTMIPIRRPPFIMG 48 HlMS-defensin (Ticks, Arthropods, animals) No entry found Not found Not found Haemaphysalis longicornis (Tick) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus ATCC2592 (MIC=18.8 µg/ml), Bacillus licheniformis (MIC=9.4 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=28.1 µg/ml), Pseudomonas aeruginosa ATCC27853 (MIC=37.5 µg/ml), Serratia rubidaea (MIC=28.1 µg/ml), Psychrobacter faecalis (MIC=2.3 µg/ml).##Fungi: Candida albicans ATCC2002 (MIC=18.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22033149 Dev Comp Immunol. 2012 May;37(1):207-211. Zheng H, Zhou L, Yang X, Wang D, Liu J. Cloning and characterization of a male-specific defensin-like antimicrobial peptide from the tick Haemaphysalis longicornis. DRAMP02425 QLKVDLWGTRSGIQPEQHSSGKSDVRRWRSRY 32 Ixosin-B (Ticks, Arthropods, animals) A7UDM9 Not found Not found Ixodes sinensis (Hard tick) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antifungal and antibacterial activity. Ixosin-B has little hemolytic activity on red blood cells even with peptide concentrations up to 200 µg/mL." [Ref.18295522]Gram-positive bacterium: Staphylococcus aureus (MIC=2.5 µg/mL);##Gram-negative bacterium: Escherichia coli (MIC=15 µg/mL);##Yeast: Candida albicans (MIC=7.5 µg/mL). [Ref.18295522]Little hemolytic activity on rabbit red blood cells up to 200 μg/mL Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18295522 Comp Biochem Physiol B Biochem Mol Biol. 2008 Apr;149(4):557-561. Liu Z, Liu H, Liu X, Wu X. Purification and cloning of a novel antimicrobial peptide from salivary glands of the hard tick, Ixodes sinensis. DRAMP02427 GGYYCPFFQDKCHRHCRSFGRKAGYCGGFLKKTCICV 37 Ixodes ricinus defensin def1 (Ticks, Arthropods, animals) No entry found Not found def1 Ixodes ricinus (European tick) Antimicrobial, Antibacterial, Anti-Gram+ Not found Bridge Not found Function: Has antibacterial activity against Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis (MIC=1.5 µM), Micrococcus luteus(MIC=0.75 µM), Staphylococcus aureus (MRSA) (MIC=50 µM). [Ref.21504572] It has 2.9% and 75% hemolysis at concentrations of 12.5 μM and 100 μM against human erythrocytes . Cyclic Free Free Disulfide bonds between Cys5 and Cys26,Cys12 and Cys34,Cys16 and Cys36. L No cytotoxicity information found Not found 21504572 Parasit Vectors. 2011 Apr 19;4(1):63. Chrudimska T, Slaninova J, Ruzek D, Rudenko N, Grubhoffer L. Functional characterization of two defensin isoforms of the hard tick Ixodes ricinus. DRAMP02428 GGYYCPFRQDKCHRHCRSFGRKAGYCGGFLKKTCICV 37 Ixodes ricinus defensin def2 (Ticks, Arthropods, animals) No entry found Not found def2 Ixodes ricinus (European tick) Antimicrobial, Antibacterial, Anti-Gram+ Not found Bridge Not found Function: Has antibacterial activity against Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis (MIC=0.75 µM), Micrococcus luteus(MIC=0.37 µM), Staphylococcus aureus (MRSA) (MIC=25 µM). [Ref.21504572] It has 2.0% and 64.6% hemolysis at concentrations of 12.5 μM and 100 μM against human erythrocytes . Cyclic Free Free Disulfide bonds between Cys5 and Cys26,Cys12 and Cys34,Cys16 and Cys36. L No cytotoxicity information found Not found 21504572 Parasit Vectors. 2011 Apr 19;4(1):63. Chrudimska T, Slaninova J, Ruzek D, Rudenko N, Grubhoffer L. Functional characterization of two defensin isoforms of the hard tick Ixodes ricinus. DRAMP02429 QRGSRGQRCGPGEVFNQCGSACPRVCGRPPAQACTLQCVSGCFCRRGYIRTQRGGCIPERQCHQR 65 Chymotrypsin-elastase inhibitor ixodidin (Ticks, Arthropods, animals) P83516 Not found Not found Boophilus microplus (Cattle tick) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Inhibits chymotrypsin and elastase. Has antibacterial activity against Gram-positive bacterium M.luteus and the Gram-negative bacterium E. coli. PTM: Contains five disulfide bonds." Escherichia coli (20% inhibition at 1mM), Micrococcus luteus(MIC=0.12-0.24 mM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic pyroglutamic acid Free Disulfide bonds between Cys9 and Cys34,Cys18 and Cys42,Cys22 and Cys38,Cys26 and Cys62,Cys44 and Cys56. L No cytotoxicity information found Not found 16191451 Peptides. 2006 Apr;27(4):667-74. Fogaça AC, Almeida IC, Eberlin MN, Tanaka AS, Bulet P, Daffre S. Ixodidin, a novel antimicrobial peptide from the hemocytes of the cattle tick Boophilus microplus with inhibitory activity against serine proteinases. DRAMP02430 GLHKVMREVLGYERNSYKKFFLR 23 Ixosin (Ticks, Arthropods, animals) Q2LKX9 Not found Not found Ixodes sinensis (Hard tick) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antifungal activity against C. albicans. Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacterium E. coli. Little hemolytic activity against rabbit erythrocytes. [Ref.16087274]Gram-postive bacteria: Staphylococcus aureus (MIC=3.7 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=30 µg/ml);##Fungi: Candida albicans (MIC=7.5 µg/ml). [Ref.16087274]Little hemolytic activity on rabbit red blood cells up to 50 μg/mL Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16087274 Peptides. 2006 Jan;27(1):31-5. Yu D, Sheng Z, Xu X, Li J, Yang H, Liu Z, Rees HH, Lai R. A novel antimicrobial peptide from salivary glands of the hard tick, Ixodes sinensis. DRAMP02432 PDPGQPWQVKAGRPPCYSIPCRKHDECRVGSCSRCNNGLWGDRTCR 46 Antimicrobial peptide ISAMP (Ticks, Arthropods, animals) Q8MVA6 Not found Not found Ixodes scapularis (Black-legged tick) (Deer tick) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial activity and weak hemolytic. Tissue specificity: Expressed in the fat body, hemocytes and salivary glands of partially-fed female ticks. Not expressed in the midgut." [Ref.19852941]Gram-positive bacteria: Bacillus cereus (MIC=5.8 µg/ml), Bacillus subtilis (MIC=12.3 µg/ml), Staphylococcus aureus (MIC=10.4 µg/ml);##Gram-negative bacteria: Escherichia coli Edl 933 (MIC=3.2 µg/ml), E. coli MG/655 (MIC=4.2 µg/ml). [Ref.19852941]Insignificant hemolytic activity even up to 150 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12177149##19852941 J Exp Biol. 2002 Sep;205(Pt 18):2843-2864.##Biochem Biophys Res Commun. 2009 Dec 18;390(3):511-515. Valenzuela JG, Francischetti IM, Pham VM, Garfield MK, Mather TN, Ribeiro JM.##Pichu S, Ribeiro JM, Mather TN. Exploring the sialome of the tick Ixodes scapularis.##Purification and characterization of a novel salivary antimicrobial peptide from the tick, Ixodes scapularis. DRAMP02433 HHQELCTKGDDALVTELECIRLRISPETNAAFDNAVQQLNCLNRACAYRKMCATNNLEQAMSVYFTNEQIKEIHDAATACDPEAHHEHDH 90 Antimicrobial peptide microplusin (Microplusin; Ticks, Arthropods, animals) Q86LE5 Not found Not found Boophilus microplus (Cattle tick) Antimicrobial, Antifungal, Antibacterial Protein level Alpha helix Microplusin consists of five alpha-helices: alpha1 (residues Gly-9 to Arg-21), alpha2 (residues Glu-27 to Asn-40), alpha3 (residues Arg-44 to Thr-54), alpha4 (residues Leu-57 to Tyr-64), and alpha5 (residues Asn-67 to Cys-80). The N and C termini are disordered. 2KNJ resolved by NMR. "Function: Has bacteriostatic activity against the Gram-positive bacterium M.luteus. Has fungistatic activity against C.neoformans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus. Tissue specificity: Expressed in the hemocytes, fat body and ovaries. PTM: Contains three disulfide bonds 6-52; 19-80; 41-46." Micrococcus luteus (MIC=0.38-0.76 µM), Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys52,Cys19 and Cys80,Cys41 and Cys46. L No cytotoxicity information found Metal-binding: copper II and iron II 14642886##19828445 Dev Comp Immunol. 2004 Mar;28(3):191-200.##J Biol Chem. 2009 Dec 11;284(50):34735-34746. Fogaça AC, Lorenzini DM, Kaku LM, Esteves E, Bulet P, Daffre S.##Silva FD, Rezende CA, Rossi DC, Esteves E, Dyszy FH, Schreier S, Gueiros-Filho F, Campos CB, Pires JR, Daffre S. Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile.##Structure and mode of action of microplusin, a copper II-chelating antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus) microplus. DRAMP02434 FSRYARMRDSRPWSDRKNNYSGPQFTYPPEKAPPEKLIKWNNEGSPIFEMPAEGGHIEP 59 Antimicrobial peptide lumbricin-PG (Lumbricin-PG) P86929 Not found Not found Pheretima guillelmi (Earthworm) (Metaphire guillelmi) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Displays stronger activity against P. aeruginosa and S. aureus than E. coli. At the concentration of 200 g/ml, it induces 1.5 and 2.1% hemolysis of human and rabbit red blood cells, respectively. Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=5 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=2.5 µg/m).##Fungi: Candida albicans ATCC 2002. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21539875 Peptides. 2011 Jun;32(6):1146-1150. Li W, Li S, Zhong J, Zhu Z, Liu J, Wang W. A novel antimicrobial peptide from skin secretions of the earthworm, Pheretima guillelmi (Michaelsen). DRAMP02439 FTCAISCDIKVNGKPCKGSGEKKCSGGWSCKFNVCVKV 38 U-theraphotoxin-Aju1a (U-TRTX-Aju1a; Juruin) B3EWQ0 Belongs to the huwentoxin-2 family Not found Avicularia juruensis (Yellow-banded pinktoe) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has strong antifungal activity. Has no hemolytic activity against human erythrocytes. Probable ion channel inhibitor (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds 3-24; 7-30; 16-35." [Ref. Front.Microbiol.2012 Sep;3:324-324.]Fungi: Candida albicans MDM8, C. albicans IOC 45588 (MIC=2.5-5 µM), C. krusei IOC 4559 (MIC=2.5-5 µM), C. glabrata IOC 45658 (MIC=2.5-5 µM), C. parapsilosis IOC 456416 (MIC=2.5-5 µM), C. tropicalis IOC 45608 (MIC=2.5-5 µM), C. guilliermondii IOC 455716 (MIC=2.5-5 µM) and Aspergillus niger (MIC=5-10 µM) [Ref. 22973266] It has no hemolytic activity at 10μM against human human erythrocytes Cyclic Free Free Disulfide bonds between Cys3 and Cys24,Cys7 and Cys30,Cys16 and Cys35. L No cytotoxicity information found Not found PubMed ID is not available Front. Microbiol. 2012 Sep;3:324-324. Ayroza G, Ferreira ILC, Sayegh RSR, Tashima AK, Silva jr PI. Juruin: an antifungal juruentoxin peptide from the venom of the amazonian pink toe spider, Avicularia juruensis, which contains the inhibitory cystine knot motif. DRAMP02445 LYKLVKVVLNM 11 Antimicrobial protein BL-A60 B3EWC5 Not found Not found Brevibacillus laterosporus (Bacillus laterosporus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial and antifungal activity. In P.capsici, inhibits mycelial growth (EC50=7.89 µg/ml), formation of sporangia (EC50=0.6 µg/ml) and cytospore germination (EC50=21.96 µg/ml). PTM: Contains a choline moiety at the N-terminus and a tenuazonic acid moiety at the C-terminus. Biophysicochemical properties: pH dependence (Active between pH 3 and 11); Temperature dependence (Retains >80% activity after 15 min at 100 degrees Celsius)." Gram-negative bacterium: Pseudomonas solanacearum (MIC=10 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=5 µM).##Fungi: Phytophthora capsici (MIC=15 µM), Botrytis cinerea (MIC=25 µM), Verticillium dahliae (MIC=200 µM), Fusarium oxysporum (MIC=50 µM), Xerocomus vesicolor (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22244810 Peptides. 2012 Feb;33(2):206-211. Zhao J, Guo L, Zeng H, Yang X, Yuan J, Shi H, Xiong Y, Chen M, Han L, Qiu D. Purification and characterization of a novel antimicrobial peptide from Brevibacillus laterosporus strain A60. DRAMP02446 YSKSLPLSVLNP 12 Antimicrobial protein 1 (Antimicrobial protein AN5-1) B3EWQ6 Not found Not found Paenibacillus alvei (Bacillus alvei) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has a broad inhibitory spectrum against both Gram-positive and -negative bacterial strains. Miscellaneous: A synthetic peptide has no antibacterial activity against S. agalactiae ATCC 12386, S. epidermidis, P. aeruginosa and methicillin-resistant S. aureus (MRSA). Biophysicochemical properties: pH dependence (Active between pH 2 and 12); Temperature dependence (Active between 37 and 90 degrees Celsius. Activity is reduced at 100 degrees Celsius and absent at 110 degrees Celsius. Activity is unaffected by storage at -20 degrees Celsius)." Gram-positive bacteria: Lactobacillus plantarum strain ATCC 8014 (MIC=32 µg/ml), Lactococcus lactis ATCC 11454 (MIC>128 µg/ml), Bacillus cereus strain ATCC 14579 (MIC=64 µg/ml), Staphylococcus aureus (MIC=64 µg/ml), Bacillus subtilis (MIC=32 µg/ml), Bacillus anthracis (MIC=128 µg/ml) and Bacillus licheniformis (MIC>128 µg/ml), Bacillus flexus (MIC=32 µg/ml);##Gram-negative bacteria: Escherichia coli strain ATCC 13076 (MIC=8 µg/ml), Salmonella enteritidis ATCC 13076 (MIC=4 µg/ml), Enterobacter spp. (MIC=16 µg/ml), Serratia marcescens (MIC=32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23508455 J Ind Microbiol Biotechnol. 2013 Jun;40(6):571-579. Alkotaini B, Anuar N, Kadhum AA, Sani AA. Detection of secreted antimicrobial peptides isolated from cell-free culture supernatant of Paenibacillus alvei AN5. DRAMP02449 TGVAWRIT 8 Lectin P86922 Not found Not found Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has metal-independent hemagglutinating activity against erythrocytes from human, sheep, goat, rat, rabbit and chicken. Hemagglutinating activity is inhibited by glycoproteins fetuin, asialo-fetuin, fibrinogen, asialo-fibrinogen, thyroglobulin, bovine (BSM) as well as porcine submaxillary mucin and asialo-BSM but not by sugars alpha-L-fucose, D-glucose, D-galactose, D-glucosamine, D-galactosamine, lactose, D-melibiose, D/L-mannose, D-mannosamine, D-raffinose, L-rhamnose, xylose, glacaturonic acid or N-acetylglucosamine. Has antifungal activity. Biophysicochemical properties: pH dependence (Hemagglutinating activity is stable from pH 4 to pH 9 but drops sharply below pH 4 and above pH 9); Temperature dependence (Hemagglutinating activity is stable below 60 degrees Celsius but drops sharply to about 20% at 80 degrees Celsius)." Fungi: Fusarium oxysporum (MIC=20 µg/ml), Penicillium chrysogenum (MIC=35 µg/ml), Aspergillus niger (MIC=50 µg/ml), Cladosporium musae (MIC=60 µg/ml), Botrytis cinerea (MIC=65 µg/ml), Trichophyton rubrum (MIC=65 µg/ml), T. tonsurans (MIC=20 µg/ml), T. interdigitale (MIC=20 µg/ml), Epidermophyton floccosum (MIC=15 µg/ml), Microsporum canis (MIC=70 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21728991 Protein Pept Lett. 2011 Nov;18(11):1150-1157. U Girjal V, Neelagund S, Krishnappa M. Ganoderma lucidum: A source for novel bioactive lectin. DRAMP02456 DGVCSNRRQCNKEVCGSSYDVAIVGA 26 L-amino-acid oxidase (LAAO; LAO; Dactylomelin-P) P86163 Belongs to the flavin monoamine oxidase family Not found Aplysia dactylomela (Spotted sea hare) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Catalyzes the oxidative deamination of positively charged L-amino acids L-Lys and L-Arg but not of amino acids L-His, L-Asp or L-Glu. Has antibacterial activity. This antibacterial activity is bacteriostatic in the absence of amino acids L-Lys or L-Arg but bactericidal in their presence. The antibacterial effect is largely dependent on H2O2 produced in the oxidative deamination of substrates. Has hemagglutinating activity towards rabbit erythrocytes. Hemagglutinating activity is inhibited by the glycoprotein fetuin, but not by glucose, mannose, galactose, N-acetylglucosamine, N-acetylgalactosamine or sialic acid. Tissue specificity: Expressed by the ink gland. Biophysicochemical properties: Kinetic parameters (KM=0.22 mM for L-Lys; KM=0.015 mM for L-Arg); pH dependence (Optimum pH is 8. More than 50% activity is retained between pH 3 and 12. Inactive at pH 2); Temperature dependence (Activity remains stable after 30 min at 55 degrees Celsius)." Gram-positive bacterium: S. aureus (MIC=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10758276 Toxicon. 2000 Oct;38(10):1415-1427. Melo VM, Duarte AB, Carvalho AF, Siebra EA, Vasconcelos IM. Purification of a novel antibacterial and haemagglutinating protein from the purple gland of the sea hare, Aplysia dactylomela rang, 1828. DRAMP02470 SCTTCECCCSCS 12 Nosiheptide (NOS; Antibiotic 9671-RP) C6FX52 Belongs to the thiocillin family nosM Streptomyces actuosus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Inhibits bacterial protein biosynthesis by binding to ribosomes. Specifically, binds to the complex of 23S rRNA and ribosomal protein L11 (RPLK) in the 50S ribosomal subunit. While allowing a weak binding of elongation factor G (EF-G) to the ribosome and subsequent GTP-hydrolysis, probably impairs conformational changes in both the ribosome and EF-G which are necessary for translocation. In vitro, inhibits a variety of Gram-positive bacteria and inhibits Gram-negative bacterium P. multocida strain A125 (MIC=0.0024 µg/ml). Does not inhibit Gram-negative bacterium E. coli strain ATCC 9637 but does inhibit purified ribosomes from E. coli. In vivo, has no systemic effect in mice infected with staphylococci or streptococci when applied orally or subcutaneously. Has a local effect in mice infected subcutaneously or intraperitoneally with staphylococci when applied immediately afterwards. Is not toxic to mice. Miscellaneous: The mature peptide is identical to multhiomycin from S. antibioticus strain 8446CC1 (PMID 681244). Used as an antibiotic growth promotant in poultry and pig farming in parts of Asia." Gram-positive bacteria: Staphylococcus aureus strain 209P (MIC=0.0009 µg/ml), S. aureus strain 133 (MIC=0.0019 µg/ml), S. aureus strain B3 (MIC=0.003 µg/ml), S. aureus strain Hb (MIC=0.003 µg/ml), Micrococcus citreus strain ATCC 8411 (MIC=0.0038 µg/ml), M. lysodeikticus strain ATCC 4698 (MIC=0.003 µg/ml), Sarcina Lutea strain ATCC 9341 (MIC=0.0011 µg/ml), Streptococcus faecalis strain ATCC 9790 (MIC=0.0007 µg/ml), S. viridans (MIC=0.0065 µg/ml), Streptococcus pyogenes hemolyticus strain Dig7 (MIC=0.00028 µg/ml), Diplococcus pneumoniae strain Til (MIC=0.00015 µg/ml), N. catrrhalis (MIC=0.0017 µg/ml), Lactobacillus casei strain ATCC 6633 (MIC=0.003 µg/ml), Bacillus cereus ATCC 6630 (MIC=0.0071 µg/ml) and various isolates of Listeria monocytogenes.##Gram-negative bacterium: P. multocida strain A125 (MIC=0.0024 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19678698##18406324 ACS Chem Biol. 2009 Oct 16;4(10):855-864.##Mol Cell. 2008 Apr 11;30(1):26-38. Yu Y, Duan L, Zhang Q, Liao R, Ding Y, Pan H, Wendt-Pienkowski E, Tang G, Shen B, Liu W.##Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P. Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework.##Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. DRAMP02473 KFFRKLKKSVKKRAKEFFKKPRVIGVSIPF 30 Cathelicidin-BF (Cathelicidin-related protein; Snakes, reptiles, animals) B6D434 Not found Not found Bungarus fasciatus (Banded krait) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells. Tissue specificity: Expressed by the venom gland, stomach, trachea, skin, muscle, heart, kidney, lung, brain, intestine, spleen, liver, and ovary. Miscellaneous: A predicted cleavage site is located at position Val-157-158-Lys, giving a peptide of 34 residues instead of the 30 residues found for the purified protein. The 30 residues cathelicidin-BF could result from a further processing." [Ref.18795096]Gram-negative bacteria: Pseudomonas aeruginosa ATCC27853 (MIC=1.2 µg/ml), P. aeruginosa IS/DR (MIC=2.3 µg/ml), P. aeruginosa 08031205 IS/DR (MIC=9.4 µg/ml), P. aeruginosa 08031014 IS/DR (MIC=18.7 µg/ml), Escherichia coli ATCC25922 (MIC=2.3 µg/ml), E. coli 08A852 IS/DR (MIC=1.2 µg/ml), E. coli 08A866 IS/DR (MIC=0.6 µg/ml), E. coli 08031017 IS/DR (MIC=2.3 µg/ml), E. coli 08032813 IS/DR (MIC=2.3 µg/ml), E. coli 08040726 IS/DR (MIC=0.6 µg/ml), E. coli 08040722 IS/DR (MIC=0.6 µg/ml), Klebsiella pneumoniae IS/DR (MIC=4.7 µg/ml), K. pneumoniae 08031012 IS/DR (MIC=9.4 µg/ml), K. pneumoniae 08040202 IS/DR (MIC=0.6 µg/ml), K. pneumoniae 08040724 IS/DR (MIC=0.3 µg/ml), Pseudomonas luteola (MIC=1.2 µg/ml), Salmonella Typhi IS/DR (MIC=1.2 µg/ml), Acinetobacter calcoaceticus (MIC=2.3 µg/ml), Sphingobacterium siyangense (MIC=9.4 µg/ml), Saccharibacillus kuerlensis (MIC=4.7 µg/ml);##Gram-positive bacteria: Bacillus subtilis (MIC=9.4 µg/ml), B. pumilus (MIC=9.4 µg/ml), B. cereus (MIC=1.2 µg/ml), Staphylococcus aureus ATCC2592 (MIC=4.7 µg/ml), S. aureus 08A875 IS/DR (MIC=75 µg/ml), S. aureus 08031002 IS/DR (MIC>100 µg/ml), S. aureus 08031013 IS/DR (MIC>100 µg/ml), S. aureus 08032706 IS/DR (MIC>100 µg/ml), S. aureus 08032712 IS/DR (MIC>100 µg/ml), S. aureus 08032810 IS/DR (MIC>100 µg/ml), Enterococcus faecium IS/DR (MIC=150 µg/ml);##Fungi: Aspergillus terreus GIM3.34 (MIC=18.7 µg/ml), Aspergillus nidulans (MIC=18.7 µg/ml), Candida albicans ATCC2002 (MIC=4.7 µg/ml), Pichia pastoris (MIC=0.3 µg/ml). [Ref.18795096]Non-hemolytic activity at 400 µg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18795096##18620012 PLoS One. 2008 Sep 16;3(9):e3217.##Peptides. 2008 Oct;29(10):1685-1691. Wang Y, Hong J, Liu X, Yang H, Liu R, Wu J, Wang A, Lin D, Lai R.##Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics.##Identification and characterization of novel reptile cathelicidins from elapid snakes. DRAMP02474 KFFRKLKKSVKKRAK 15 cathelicidin-BF15 (Snakes, reptiles, animals) B6D434 Not found Not found Bungarus fasciatus (Banded krait) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Pseudomonas aeruginosa ATCC27853 (MIC=4.7 µg/ml), P. aeruginosa IS/DR (MIC=37.5 µg/ml), P. aeruginosa 08031205 IS/DR (MIC=18.7 µg/ml), P. aeruginosa 08031014 IS/DR (MIC=75 µg/ml), Escherichia coli ATCC25922 (MIC=18.7 µg/ml), E. coli 08A852 IS/DR (MIC=18.7 µg/ml), E. coli 08A866 IS/DR (MIC=18.7 µg/ml), E. coli 08031017 IS/DR (MIC=37.5 µg/ml), E. coli 08040722 IS/DR (MIC=9.4 µg/ml), K. pneumoniae 08040202 IS/DR (MIC=75 µg/ml), Salmonella Typhi IS/DR (MIC=1.2 µg/ml), Saccharibacillus kuerlensis (MIC=4.7 µg/ml).##Gram-positive bacteria: Bacillus subtilis (MIC=75 µg/ml), Staphylococcus aureus ATCC2592 (MIC=75 µg/ml), S. aureus 08A875 IS/DR (MIC=75 µg/ml), S. aureus 08031002 IS/DR (MIC>100 µg/ml).##Fungi: Candida albicans ATCC2002 (MIC=18.7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18795096 PLoS One. 2008 Sep 16;3(9):e3217. Wang Y, Hong J, Liu X, Yang H, Liu R, Wu J, Wang A, Lin D, Lai R. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. DRAMP02478 IKFEPPLPPKKAHKKFWEDDGIYYPPNHNFP 31 L-amino-acid oxidase (Bm-LAO; LAAO; LAO; Snakes, reptiles, animals) B3EWI9 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothropoides matogrossensis (Pitviper) (Bothrops neuwiedimatogrossensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). Tissue specificity: Expressed by the venom gland." Gram-positive bacteria: Bacillus subtilis strain ATCC 6633 (MIC=32 µM), Enterococcus faecalis strain ATCC 12953 (MIC=32 µM), Staphylococcus aureus strain ATCC 29213 (MIC=32 µM), Streptococcus pyogenes strain ATCC 19615 (MIC=8 µM);##Gram-negative bacteria: Escherichia coli strain ATCC 8739 (MIC=4 µM), Klebsiella pneumoniaee strain ATCC 13885 (MIC=2 µM), Proteus mirabilis strain ATCC 25933 (MIC=2 µM), Pseudomonas aeruginosa strain ATCC 15442 (MIC=8 µM), Salmonella typhimurium strain ATCC 14028 (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22438972 PLoS One. 2012;7(3):e33639. Okubo BM, Silva ON, Migliolo L, Gomes DG, Porto WF, Batista CL, Ramos CS, Holanda HH, Dias SC, Franco OL, Moreno SE. Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom. DRAMP02520 KRFKKFFKKLKNSVKKRAKKFFKKPRVIGVSIPF 34 OH-CATH (Snakes, reptiles, animals) No entry found Not found Not found Ophiophagus hannah (King cobra) (Naja hannah) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8 µg/ml), E. coli ML-35P (MIC=6 µg/ml), E. coli clinic strain (MIC=20 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µg/ml), Pseudomonas aeruginosa PA 01 (MIC=2 µg/ml), Pseudomonas aeruginosa clinic strain (MIC=2 µg/ml), Enterobacter aerogenes clinic strain (MIC=2 µg/ml), E. cloacae clinic strain (MIC=1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18620012 Peptides. 2008 Oct;29(10):1685-1691. Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y. Identification and characterization of novel reptile cathelicidins from elapid snakes. DRAMP02522 HVINLEESFQEPEYENHLA 19 L-amino-acid oxidase (LAAO, LAO, Oh-LAAO; Snakes, reptiles, animals) P81383, A8QL50 Not found Not found Ophiophagus hannah (King cobra) (Naja hannah) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 5 mg/kg by intravenous injection into mice. Temperature dependence: Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing." Gram-negative bacteria: Klebsiella pneumonia (MIC=0.4 µM), Pseudomonas aeruginosa (MIC=0.2 µM), Escherichia coli (MIC=0.4 µM), Escherichia coli ATCC 25922 (MIC=0.8 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=0.006 µM), S. epidermidis (MIC=0.012 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Bacterial cell 9304806##2619759##2044840##7886693##21059402 Int J Biochem Cell Biol. 1997 Jun;29(6):911-919.##Biochem Int. 1989 Oct;19(4):937-944.##Int J Biochem. 1991;23(3):323-327.##Toxicon. 1994 Nov;32(11):1349-1358.##Comp Biochem Physiol C Toxicol Pharmacol. 2011 M Ahn MY, Lee BM, Kim YS.##Tan NH, Saifuddin MN.##Tan NH, Saifuddin MN.##Li ZY, Yu TF, Lian EC.##Lee ML, Tan NH, Fung SY, Sekaran SD. Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).##Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom.##Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase.##Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation.##Antibacterial action of a heat-stabl DRAMP02573 QVYKGGYTRPIPRPPPFVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYS 62 Penaeidin-3a (Pen-3a; shrimps, Arthropods, animals) P81058 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Tissue specificity: Higher expression in hemocytes and to a lesser extent in heart, testis, gills, intestine, lymphonoid organ and hepatopancreas. Traces in eyes and subcuticular epithelium. Not present in the brain. Developmental stage: Expression decreases 3 hours after microbial challenge to return to control levels after 12 hours and slightly increases after 24 hours. PTM: C-terminal amidation and contains three disulfide bonds 32-47; 36-54; 48-55." Gram-positive bacteria: Aerococcus viridans (MIC=0.3-0.6 µM), Micrococcus luteus (MIC=1.25-2.5 µM), Bacillus megaterium (MIC=2.5-5 µM), Enterococcus fecalis (MIC>20 µM), Saphylococcus aureus (MIC>40 µM);##Gram-negative bacteria: Escherichia coli 363 (MI=10-20 µM), Vibrio vulnificus (MIC>20 µM), Salmonella thyphimurium (MIC>40 µM), Klebsiella pneumoniae (MIC>40 µM).##Fungi: Fusarium oxysporum (MIC=5-10 µM), Botrytis cinerea (MIC=5-10 µM), Neurospora crassa (MIC=1.25-2.5 µM), Aspergillus fumigatus (MIC>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic pyroglutamic acid Amidation Disulfide bonds between Cys32 and Cys47,Cys36 and Cys54,Cys48 and Cys55. O-glycosylated on Thr8 L No cytotoxicity information found Chitin-binding 9353298##10561573##12842879 J Biol Chem. 1997 Nov 7;272(45):28398-28406.##Eur J Biochem. 1999 Dec;266(2):335-346.##J Biol Chem. 2003 Sep 19;278(38):36859-36867. Destoumieux D, Bulet P, Loew D, Van Dorsselaer A, Rodriguez J, Bachère E.##Destoumieux D, Bulet P, Strub JM, Van Dorsselaer A, Bachère E.##Yang Y, Poncet J, Garnier J, Zatylny C, Bachère E, Aumelas A. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda).##Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp.##Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. DRAMP02574 QVYKGGYARPIPRPPPFVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYSG 63 [T8A]-Penaeidin-3a ([T8A]-Pen-3a; shrimps, Arthropods, animals) P81058 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 11 residues) [T8A]-Pen-3a structure consists of an unconstrained and a constrained part, which roughly match with the proline-rich (1-28 residues) and the cysteine-rich (29-58 residues) domains, respectively. The proline-rich domain does not adopt a constrained structure, whereas the cysteine-rich domain adopts a well-defined structure that consists of a helix (41-50 residues) tightly bound to the upstream (27-40 residues) and the downstream (51-63 1UEO resolved by NMR. "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. PTM: Contains three disulfide bonds." Gram-positive bacteria: Aerococcus viridans (MIC=0.4-0.8 µM), Micrococcus luteus (MIC=0.8-1.6 µM), Bacillus megaterium (MIC=3.12-6.25 µM);##Gram-negative bacteria: Escherichia coli 363 (MI=3.12-6.25 µM), Vibrio vulnificus (MIC>50 µM), Salmonella thyphimurium (MIC>50 µM), Klebsiella pneumoniae (MIC>50 µM).##Fungi: Fusarium oxysporum (MIC=3.12-6.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic pyroglutamic acid Amidation Disulfide bonds between Cys32 and Cys47,Cys36 and Cys54,Cys48 and Cys55. O-glycosylated on Thr8 L No cytotoxicity information found Not found 12842879 J Biol Chem. 2003 Sep 19;278(38):36859-36867. Yang Y, Poncet J, Garnier J, Zatylny C, Bachère E, Aumelas A. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. DRAMP18370 RERSKGSKYLYVG 13 Crinicepsin-2 (insects, arthropods, invertebrates, animals) No entry found Not found Not found working ants, Trichomyrmex criniceps Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: S. aureus (MIC 62 ug/ml), and weakly active against E. coli and V. cholerae (MIC 125 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28346717 Arch Insect Biochem Physiol. 2017 Mar 27. in press. Bhagavathula N, Meedidoddi V, Bourque S, Vimaladevi R, Kesavakurup S, Selvadurai D, Shrivastava S, Krishnappa C. Characterization of two novel antimicrobial peptides from the cuticular extracts of the ant Trichomyrmex criniceps (Mayr), (Hymenoptera: Formicidae). DRAMP18371 VGVGGGFGR 9 Crinicepsin-1 (insects, arthropods, invertebrates, animals) No entry found Not found Not found working ants, Trichomyrmex criniceps Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: S. aureus (MIC 125 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28346717 Arch Insect Biochem Physiol. 2017 Mar 27. in press. Bhagavathula N, Meedidoddi V, Bourque S, Vimaladevi R, Kesavakurup S, Selvadurai D, Shrivastava S, Krishnappa C. Characterization of two novel antimicrobial peptides from the cuticular extracts of the ant Trichomyrmex criniceps (Mayr), (Hymenoptera: Formicidae). DRAMP18372 CHTNGGYCVRAICPPSARRPGSCFPEKNPCCKYM 34 mBD-2 (Murine beta-defensin 2a) No entry found Belongs to the beta-defensin family. Not found Mus musculus Anti-cancer bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10922379 J Biol Chem. 2000 Oct 27;275(43):33314-20. Jia HP, Wowk SA, Schutte BC, Lee SK, Vivado A, Tack BF, Bevins CL, McCray PB Jr. A novel murine beta -defensin expressed in tongue, esophagus, and trachea Cancer cells. DRAMP02584 HSSGYTRPLPKPSRPIFIRPIGCDVCYGIPSSTARLCCFRYGDCCHR 47 Penaeidin-4a (Pen-4a; shrimps, Arthropods, animals) Q95NT0 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity (By similarity). PTM: Contains three disulfide bonds 23-37; 26-44; 38-45 and C-terminal amidation." Gram-positive bacteria: Aerococcus viridans (MIC=1.9-2.92 µM), Micrococcus luteus (MIC=1.9-2.92 µM), Bacillus megaterium (MIC>50 µM), Saphylococcus aureus (MIC>50 µM);##Gram-negative bacteria: Escherichia coli 363 (MIC=22-33 µM), Vibrio vulnificus (MIC>50 µM), Salmonella thyphimurium (MIC>50 µM), Klebsiella pneumoniae (MIC>50 µM).##Fungi: Fusarium oxysporum (MIC=0.84-1.26 µM), Botrytis cinerea (MIC=4.38-6.57 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bonds between Cys23 and Cys37,Cys26 and Cys44,Cys38 and Cys45. L No cytotoxicity information found Chitin-binding 12242595##15084144 Immunogenetics. 2002 Sep;54(6):442-445.##Biochem J. 2004 Jul 1;381(Pt 1):79-86. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS.##Cuthbertson BJ, Bullesbach EE, Fievet J, Bachère E, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species.##A new class (penaeidin class 4) of antimicrobial peptides from the Atlantic white shrimp (Litopenaeus setiferus) exhibits target specificity and an independent proline-rich-domain function. DRAMP02586 QRGGFTGPIPRPPPHGRPPLGPICNACYRLSFSDVRICCNFLGKCCHLVK 50 Penaeidin-2d (Pen-2d; shrimps, Arthropods, animals) Q962A9 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found "Function: Antibacterial and antifungal activity. Presents chitin-binding activity (By similarity). Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser." Gram-positive bacteria: Aerococcus viridans (MIC=1.25-2.5 µM), Micrococcus luteus (MIC=2.5-5 µM), Bacillus megaterium (MIC=2.5-5 µM), Enterococcus fecalis (MIC>20 µM), Saphylococcus aureus (MIC>20 µM);##Gram-negative bacteria: Escherichia coli 363 (MIC>40 µM), Vibrio vulnificus (MIC>20 µM), Salmonella thyphimurium (MIC>20 µM), Klebsiella pneumoniae (MIC>20 µM).##Fungi: Fusarium oxysporum (MIC=5-10 µM), Botrytis cinerea (MIC=5-10 µM), Neurospora crassa (MIC=2.5-5 µM), Aspergillus fumigatus (MIC>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595##10561573 Immunogenetics. 2002 Sep;54(6):442-445.##Eur J Biochem. 1999 Dec;266(2):335-346. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS.##Destoumieux D, Bulet P, Strub JM, Van Dorsselaer A, Bachère E. Diversity of the penaeidin antimicrobial peptides in two shrimp species.##Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. DRAMP02591 HSSGYTRPLRKPSRPIFIRPIGCDVCYGIPSSTARLCCFRYGDCCHL 47 Penaeidin-4d (Pen-4d; shrimps, Arthropods, animals) Q962A7 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix (1 helices; 9 residues) Calculation of PEN4 three-dimensional structure reveales that the PEN4 structure consisted of an unconstrained and a constrained part, which roughly match with the PRD (residues 1-17) and the CRD (residues 18-47), respectively. The global fold of the CRD mainly consisted of a helix (residues 31-41), two turns of type IV (Cys23-Cys26 and Gly42-Cys45 residues), and one loop spanning 27-30 residues (Ref.2). 1XV3 resolved by NMR. "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity (By similarity). PTM: Contains three disulfide bonds 23-37; 26-44; 38-45." Fungi: Fusarium oxysporum (MIC=0.84-1.26 µM), Botrytis cinerea (MIC=4.38-6.57 µM), Penicillium crustosum (MIC=1.26-1.9 µM).## Gram-positive bacteria: Aerococcus viridans (MIC=1.9-2.92 µM), Bacillus megaterium (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595##15699044 Immunogenetics. 2002 Sep;54(6):442-445.##J Biol Chem. 2005 Apr 22;280(16):16009-18. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS.##Cuthbertson BJ, Yang Y, Bachère E, Büllesbach EE, Gross PS, Aumelas A. Diversity of the penaeidin antimicrobial peptides in two shrimp species.##Solution structure of synthetic penaeidin-4 with structural and functional comparisons with penaeidin-3. DRAMP02603 AALRGALRAVARVGKAILPHVAIANPYVRTPYVHNNP 37 Putative antimicrobial peptide A Northern Europe Heligoland (chordates, animals) No entry found Not found Not found Ciona intestinalis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus megaterium (MIC=0.1 µM), Bacillus subtilis (MIC=3.1 µM), Staphylococcus aureus (MIC>25 µM), Staphylococcus epidermidis (MIC=25 µM).##Gram-negative bacteria: Escherichia coli K12 D31 (MIC=0.8 µM), Y. enterocolitica (MIC=3.1 µM), Klebsiella pneumoniae (MIC>25µM), Pseudomonas aeruginosa (MIC=12.5 µM), Serratia marcescens(MIC>25 µM).##Fungi: Candida albicans ATCC 10261 (MIC=6.3 µM), Candida albicans SC 5314 (MIC=6.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17658598 Dev Comp Immunol. 2008;32(3):286-298. Fedders H, Leippe M. A reverse search for antimicrobial peptides in Ciona intestinalis: identification of a gene family expressed in hemocytes and evaluation of activity. DRAMP02609 RLGDILQKAREKIEGGLKKLVQKIKDFFGKFAPRTES 37 CjaRL-37 (cathelicidin; primates, mammals, animals) No entry found Not found Not found Platyrrhini (New World monkeys) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Has antibacterial activity. In 20% TSB in SPB medium: Escherichia coli (MIC=4 µM), Pseudomonas aeruginosa (MIC>32 µM); Staphylococcus aureus (MIC=32 µM), Enterococcus faecalis (MIC>32 µM).##In 20% SAB in SPB medium: Candida albicans (MIC>32 µM). In 5% SAB in SPB Candida albicans (MIC>32 µM). In 20% SAB in PIL Candida albicans (MIC>32 µM).##In 5% TSB in SPB Escherichia coli (MIC=1 µM), Pseudomonas aeruginosa (MIC=2 µM), Staphylococcus aureus (MIC=8-16 µM).##In 20% TSB in PIL Escherichia coli (MIC>32 µM), Pseudomonas aeruginosa (MIC>32 µM); Staphylococcus aureus (MIC=16 µM), Enterococcus faecalis (MIC>32 µM).##In 50% MH in SPB medium Escherichia coli (MIC>32 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02650 APIIRRIPYYPEVESDLRIVDCKRSEGFCQEYCNYLETQVGYCSKKKDACCLH 53 Sperm associated antigen 11 isoform C (primates, mammals, animals) No entry found Not found Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=50-100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15229135 Biol Reprod. 2004 Nov;71(5):1453-1460. Avellar MC, Honda L, Hamil KG, Yenugu S, Grossman G, Petrusz P, French FS, Hall SH. Differential expression and antibacterial activity of epididymis protein 2 isoforms in the male reproductive tract of human and rhesus monkey (Macaca mulatta). DRAMP02727 SLGNFFRKARKKIGEEFKRIVQRIKDFLQHLIPRTEA 37 HmdSL-37 (cathelicidin; primates, mammals, animals) No entry found Not found Not found Hylobates sp. (Gibbon) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Has antibacterial activity. In 20% TSB in SPB medium Escherichia coli (MIC=2 µM), Pseudomonas aeruginosa (MIC=8 µM), Staphylococcus aureus (MIC>32 µM), Enterococcus faecalis (MIC=8 µM).##In 20% SAB in SPB Candida albicans (MIC>32 µM). In 5% SAB in SPB Candida albicans (MIC=8 µM). In 20% SAB in PIL Candida albicans (MIC>32 µM).##In 5% TSB in SPB Escherichia coli (MIC=1 µM), Pseudomonas aeruginosa (MIC=2 µM), Staphylococcus aureus (MIC=2 µM).##In 20% TSB in PIL Escherichia coli (MIC>32 µM), Pseudomonas aeruginosa (MIC=16-32 µM); Staphylococcus aureus (MIC=8-16 µM), Enterococcus faecalis (MIC>32 µM).##In 50% MH in SPB medium Escherichia coli (MIC>32 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP18369 VSFPWSCAALSGVCRQGACLPSELYFGPLGCGKGSLCCVSYFL 43 ccBD(channel catfish beta defensin) No entry found Belongs to the beta-defensin family. Not found skin, Ictalurus punctatus Antimicrobial, Antibacterial bridge Not found Comment: No comments found on DRAMP database Active against Gram- E. coli, E. ictaluri, Y. ruckeri, A. hydrophila, A. veronii, Gram+ S. aureus, S. iniae, and S. agalactiae (MIC 12.5-25 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys7 and Cys37,Cys14 and Cys31,Cys19 and Cys38. L No cytotoxicity information found Not found 28340427 Mol Immunol. 2017 Mar 21;85:256-264. Zhu J, Wang H, Wang J, Wang X, Peng S, Geng Y, Wang K, Ouyang P, Li Z, Huang X, Chen D. Identification and characterization of a DRAMP02740 YDLSKNCRLRGGICYIGKCPRRFFRSGSCSRGNVCCLRFG 40 TBD-1 (Turtle beta-defensin 1; Reptiles, animals) P86253 Belongs to the beta-defensin family Not found Emys orbicularis (European pond turtle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacteria methicillin-resistant S. aureus ATCC 33591 and L. monocytogenes EGD, the Gram-negative bacterium E. coli ML53p and the yeast C. albicans 820. Has no hemolytic activity towards human erythrocytes. PTM: Contains three disulfide bonds 7-35; 14-29; 19-36." [Ref.19253295]Gram-negative bacterium (LS, HS): Escherichia coli ML35p (MIC=0.65, >20 µmol/L);##Gram-positive bacteria: (LS, HS): Listeria monocytogenes EGD (MIC=0.65, >20 µmol/L), Methicillin-resistant Staphylococcus aureus ATCC 33591 (MIC=5.6, >20 µmol/L).##Yeast: Candida albicans (MIC=5.2, >20 µmol/L).##NOTE: LS (low salt): 10 mmol/L sodium phosphate buffer (pH 7.4) and HS (high salt): 10 mmol/L sodium-phosphate buffer (pH 7.4), 0.1 mol/L sodium chloride. [Ref.19253295] It has no hemolytic activity against human erythrocytes up to 25 mmol/L Cyclic Free Free Disulfide bonds between Cys7 and Cys35; Cys14 and Cys29; Cys19 and Cys36. L No cytotoxicity information found Not found 19253295 Proteomics. 2009 Mar;9(5):1364-1373. Stegemann C, Kolobov A Jr, Leonova YF, Knappe D, Shamova O, Ovchinnikova TV, Kokryakov VN, Hoffmann R. Isolation, purification and de novo sequencing of TBD-1, the first beta-defensin from leukocytes of reptiles. DRAMP02768 GLGSVFGRLARILGRVIPKVAKKLGPKVAKVLPKVMKEAIPMAVEMAKSQEEQQPQ 56 Pilosulin-1 (Myr b I; ants, insects, animals) Q07932, Q9TWC1 Belongs to the pilosulin family Not found Myrmecia banksi (Jack jumper ant) (Australian jumper ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has strong cytotoxic and hemolytic activities. Is more potent against mononuclear leukocytes than against granulocytes. The synthesized peptide 57-76 shows a potent and broad spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria, and also against the fungus C. albicans. Adopts an alpha-helical structure. Tissue specificity: Expressed by the venom gland. Allergenic properties: Causes an allergic reaction in human." [Ref.9813247]Gram-positive bacteria: Micrococcus luteus (MIC=0.5 µM), Enterococcus spp.I-11305b (MIC=2 µM), Enterococcus spp. I-11054 (MIC=2 µM), Staphylococcus simulans 22 (MIC=2 µM), S. haemolyticus I-10925 (MIC=2 µM), S. epidermidis LT1324 (MIC=2 µM), S. aureuss 5185 (MI=2 µM), S. aureuss methicillin-sensitive I-11574 (MIC=2 µM), S. aureuss (MRSA) LT1338 (MIC=3 µM), S. aureuss (MRSA) LT1334 (MIC=1.5 µM);##Gram-negative bacteria: Citrobacter freundii I-11090 (MIC=2 µM), Klebsiella pneumoniae I-10910 (MIC=2 µM), Escherichia coli I-11276b (MIC=4 µM), E. coli O-19592 (MIC=2 µM), Stenotrophomonas maltophilia O-16451 (MIC=2 µM), S. maltophila I-10717 (MIC=2 µM), Pseudomonas aeruginosa 4991 (MIC=4 µM), Pseudomonas aeruginosa I-10968 (MIC=4 µM);##Fungi: Candida albicans I-11301 (MIC=4 µM), Candida albicans I-11134 (MIC>4 µM). [Ref.9813247]Complete lysis in the presence of pilosulin 1 was obtained at a concentration of 40 μM with evidence of partial lysis visible down to 1.25 μM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 9813247##9701394##15639237##8866004 Arch Biochem Biophys. 2005 Feb 15;434(2):358-364.##Cytometry. 1998 Aug 1;32(4):268-273.##Arch Biochem Biophys. 2005 Feb 15;434(2):358-364.##Biochem Mol Biol Int. 1996 Aug;39(5):877-885. Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A.##King MA, Wu QX, Donovan GR, Baldo BA.##Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A.##Donovan GR, Street MD, Tetaz T, Smith AI, Alewood D, Alewood P, Sutherland SK, Baldo BA. Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin.##Flow cytometric analysis of cell killing by the jumper ant venom peptide pilosulin 1.##Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin.##Expression of jumper ant (Myrmecia pilosula) venom allergens: post-translational processing of allergen gene products. DRAMP02774 CIKNGNGCQPDGSQGNCCSRYCHKEPGWVAGYCR 34 Antimicrobial peptide Alo-1 (Alo-1; knottin-type peptide; Insects, animals) P83651 Belongs to the AMP family Not found Acrocinus longimanus (Giant harlequin beetle) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Has antifungal activity against C. glabrata. Domain: The presence of a disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds 1-18; 8-22; 17-33." Fungi: Candida glabrata patient 1 (MIC>64 µg/mL), C. albicans IHEM 8060 (MIC=64 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys1 and Cys18; Cys8 and Cys22; Cys17 and Cys33. L No cytotoxicity information found Not found 14661954 Biochemistry. 2003 Dec 16;42(49):14434-14442. Barbault F, Landon C, Guenneugues M, Meyer JP, Schott V, Dimarcq JL, Vovelle F. Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus. DRAMP02776 CIKNGNGCQPNGSQGNCCSGYCHKQPGWVAGYCRRK 36 Antimicrobial peptide Alo-3 (Alo-3; knottin-type peptide; Insects, animals) P83653 belongs to the inhibitor cystine-knot family Not found Acrocinus longimanus (Giant harlequin beetle) Antimicrobial, Antifungal Protein level Beta strand (3 strands; 8 residues) Alo-3 contains six cysteine residues forming three disulfide bridges. It exhibits all the structural features characteristic of the knottin fold, namely, a triple-stranded antiparallel beta-sheet with a long flexible loop connecting the first strand to the second strand and a series of turns. 1Q3J resolved by NMR. "Function: Alo-3 shows a level of activity significantly higher against C. glabrata than Alo-1 or Alo-2. Domain: The presence of a disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds 1-18; 8-22; 17-33." Fungi: Candida glabrata patient 1 (MIC=8 µg/mL), C. glabrata ATCC 90030 (MIC=16 µg/mL), C. albicans IHEM 8060 (MIC=16 µg/mL), C. albicans ATCC 36082 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys1 and Cys18; Cys8 and Cys22; Cys17 and Cys33. L No cytotoxicity information found Not found 14661954 Biochemistry. 2003 Dec 16;42(49):14434-14442. Barbault F, Landon C, Guenneugues M, Meyer JP, Schott V, Dimarcq JL, Vovelle F. Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus. DRAMP02777 SLQPGAPNFPMPGSQLPTSITSNIEKQGPNTAATINAQHKTDRYDVGATWSKVIRGPGRSKPNWSIGGTYRW 72 Rhinocerosin (Insects, animals) O76145 Belongs to the coleoptericin family Not found Oryctes rhinoceros (Coconut rhinoceros beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has strong antibacterial activity against Escherichia coli, Streptococcus pyogenes, Staphylococcus aureus but not against Pseudomonas aeruginosa. Gram-positive bacteria: Staphylococcus aureus (MIC=1 µg/ml), Streptococcus pyogenes (MIC=1 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9738915 Eur J Biochem. 1998 Aug 1;255(3):734-738. Yang J, Yamamoto M, Ishibashi J, Taniai K, Yamakawa M. Isolation, cDNA cloning and gene expression of an antibacterial protein from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP01623 LIGPVLGLVGSALGGLLKKI 20 Bombinin-H4 (bombinin H isomers; Frogs, amphibians, animals) P82284 Belongs to the bombinin family Not found Bombina variegata (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, hemolytic against mammalian cells, Antifungal Protein level Alpha helix The epimerization reaction is incomplete, or, after racemization, the peptides still containing the L-amino acid in position 2 are partly degraded. Function: Have antimicrobial activity. Have some hemolytic activity. [Ref.8223491] Gram-negative bacterium: Escherichia coli D21 (MIC=4.8 µM);##Gram-positive bacterium: Staphylococcus aureus Cowan 1 (MIC=3.3 µM). [Ref.8223491] Lethal concentration is 14.6 µM against human red blood cell. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8223491 EMBO J. 1993; 12:4829-4832. Mignogna G, Simmaco M, Kreil G, Barra D.1993 Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. DRAMP02779 VTCDLLSFEAKGFAANHSICAAHCLAIGRKGGSCQNGVCVCRN 43 Defensin-A (Defensin A; Insects, animals) P83669 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Anomala cuprea (Cupreous chafer beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Strong activity against the Gram-positive bacteria M.luteus, B.megaterium and S. aureus. Reduced activity against Gram-positive bacterium B.subtilis and weak activity against Gram-negative bacterium X.japonicus. PTM: Problely contains three disulfide bonds 3-34; 20-39; 24-41." Gram-positive bacteria: Bacillus megaterium (MIC=1.2-2.5 µM), Bacillus subtilis (MIC>40 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Staphylococcus aureus (MIC=2.5-5 µM).##Gram-negative bacteria: Enterobacter asbriae (MIC>40 µM), Escherichia coli (MIC>40 µM), Pseudomonas aeruginosa (MIC>40 µM), Serratia marcescens (MIC>40 µM), Xenorhabdus japonicus (MIC>40 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys34; Cys20 and Cys39; Cys24 and Cys41. L No cytotoxicity information found Not found 11719071 Insect Biochem Mol Biol. 2001 Dec;32(1):75-84. Yamauchi H. Two novel insect defensins from larvae of the cupreous chafer, Anomala cuprea: purification, amino acid sequences and antibacterial activity. DRAMP02780 VTCDLLSFEAKGFAANHSICAAHCLVIGRKGGACQNGVCVCRN 43 Defensin-B (Defensin B; Insects, animals) P83668 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Anomala cuprea (Cupreous chafer beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has antibacterial activity against Gram-positive bacteria and the Gram-negative bacterium X. japonicus. PTM: Problely contains three disulfide bonds 3-34; 20-39; 24-41." Gram-positive bacteria: Bacillus megaterium (MIC=1.2-2.5 µM), Bacillus subtilis (MIC=20-40 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Staphylococcus aureus (MIC=2.5-5 µM);##Gram-negative bacterium: X. japonicus (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys34; Cys20 and Cys39; Cys24 and Cys41. L No cytotoxicity information found Not found 11719071 Insect Biochem Mol Biol. 2001 Dec;32(1):75-84. Yamauchi H. Two novel insect defensins from larvae of the cupreous chafer, Anomala cuprea: purification, amino acid sequences and antibacterial activity. DRAMP02802 AREASKSLIGTASCTCRRAWICRWGERHSGKCIDQKGSTYRLCCRR 46 Paneth cell-specific alpha-defensin 1 (DEFA1; horse defensin; houses, mammals, animals A6YB85 Not found DEFA1 Equus caballus (Horse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found 2MXQ resolved by NMR. Function: Membrane permeabilization is at least an essential part of the peptide's mode of action. Gram-negative bacteria: Escherichia coli [ATCC 11775 (MBC=0.4 µM); ATCC 25922 (MBC=0.4 µM); ATCC 35218 (MBC=0.4 µM)], E. coli D31 (MBC=0.8 µM), Pseudomonas aeruginosa ATCC 11440 (MBC=3 µM);##Gram-positive bacteria: Staphylococcus aureus [ATCC 6538 (MBC=0.8 µM); ATCC 12600 (MBC=1.5 µM)], Staphylococcus epidermidis ATCC 14990 (MBC=1.5 µM), Enterococcus faecalis ATCC 29212 (MBC=6.1 µM), E. faecalis PEG 205 (wild-type) (MBC=3 µM), Streptococcus pyogenes ATCC 12344 (MBC=0.8 µM), Bacillus megaterium ATCC 14581 (MBC=0.2 µM).##Yeast: Candida albicans ATCC 24433 (MIC=0.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys14 and Cys44; Cys16 and Cys32; Cys22 and Cys43. L No cytotoxicity information found Not found 17620056 Biochem J. 2007 Oct 15;407(2):267-276. Bruhn O, Regenhard P, Michalek M, Paul S, Gelhaus C, Jung S, Thaller G, Podschun R, Leippe M, Grötzinger J, Kalm E. A novel horse alpha-defensin: gene transcription, recombinant expression and characterization of the structure and function. DRAMP02809 HPHVCTSYYCSKFCGTAGCTRYGCRNLHRGKLCFCLHCSR 40 Myticin-B (Myt B; Cys-rich; molluscas, animals) P82102 Not found Not found Mytilus galloprovincialis (Mediterranean mussel) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Rich Not found "Function: Bacteriolytic activity against Gram-positive bacteria and Gram-negative bacteria. Also possesses antifungal activity against F. oxysporum. PTM: contains four disulfide bonds." Gram-positive bacteria: Micrococcus luteus (MBC=1-2 µM), Bacillus megaterium (MBC=1-2 µM), Aerococcus viridans (MBC=2-4 µM).##Gram-negative bacteria: Escherichia coli D31 (MBC=20-10 µM).##Fungi: Fusarium oxysporum (MIC=5-10 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free contains four disulfide bonds. L No cytotoxicity information found Not found 10491159 Eur J Biochem. 1999 Oct 1;265(1):71-78. Mitta G, Hubert F, Noël T, Roch P. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. DRAMP02811 GFGCPNNYQCHRHCKSIPGRCGGYCGGWHRLRCTCYRC 38 Defensin MGD-1 (molluscas, animals) P80571, Q9Y0B0 Not found FH3 Mytilus galloprovincialis (Mediterranean mussel) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure The three-dimensional solution structure of MGD-1 has been established using (1)H NMR and mainly consists of a helical part (Asn7-Ser16) and two antiparallel beta-strands (Arg20-Cys25 and Cys33-Arg37), together giving rise to the common cystine-stabilized alpha-beta motif frequently observed in scorpion toxins. In MGD-1, the cystine-stabilized alpha-beta motif is stabilized by four disulfide bonds (Cys4-Cys25, Cys10-Cys33, Cys14-Cys35, 1FJN resolved by NMR. "Function: Active against both Gram-positive and Gram-negative bacteria but is not cytotoxic towards human erythrocytes or protozoa. Transgenic plants: expression of this peptide in tobacco improves resistance to pathogens. PTM: Contains four disulfide bonds 4-25; 10-33; 14-35; 21-38." Gram-positive bacteria: Micrococcus luteus (MIC=0.4 µM)&(MBC=1.5 µM), Bacillus megaterium (MIC=0.8 µM)&(MBC=1.5 µM), Staphylococcus aureus (MIC=0.6 µM)&(MBC=1.2 µM), Staphylococcus epidermidis (MIC=3.1 µM)&(MBC=6.2 µM), Enterococcus fecalis (MIC=0.6 µM)&(MBC=1.2 µM), Aerococcus viridans (MIC=0.4 µM)&(MBC=1.5 µM);##Gram-negative bacteria: Escherichia coli D31 (MIC=1.2 µM)&(MBC=1.2 µM), E. coli 363 (MIC=1.2 µM)&(MBC=1.2 µM), Salmonella newport (MIC>100 µM)&(MBC>100 µM), Vibrio alginolyticus (MIC=50 µM)&(MBC>100 µM), Vibrio harveyi (MIC=50 µM)&(MBC=100 µM), Vibrio metshnikovii (MIC>100 µM)&(MBC>100 µM).##NOTE: MIC=minimal inhibitory concentration; MBC = minimal bactericidal concentration. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys4 and Cys25, Cys10 and Cys33, Cys14 and Cys35,Cys21 and Cys38. L No cytotoxicity information found Not found 10564642##8925841##11087396 J. Cell Sci. 1999;112:4233-4242.##Eur. J. Biochem. 1996;240:302-306.##Biochemistry 2000 Nov 28;39(47):14436-47. Mitta G, Vandenbulcke F, Hubert F, Roch P.##Hubert F, Noeel T, Roch P.##Yang YS, Mitta G, Chavanieu A, Calas B, Sanchez JF, Roch P, Aumelas A. Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge.##A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis).##Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). DRAMP02813 FHPSLWVLIPQYIQLIRKILKSG 23 Conolysin-Mt1 P0C8S6 Not found Not found Conus mustelinus (Weasel cone) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: This cytolytic peptide has ability to disrupt the integrity of cell membranes from both prokaryotes and eukaryotes. It permeabilizes both negatively charged prokaryotic (PE:PG) and zwitterionic eukaryotic (PC:cholesterol) model membranes. It has potent hemolytic activity on human erythrocytes and exhibits low antimicrobial activity against the Gram-negative bacterium E. coli and the Gram-positive bacterium S. aureus. Intracranial injection causes mice to shuffle backward until the encounter an obstacle, at which time the mouse jump into the air. The backward shuffle is reminiscent to the signature dance 'moonwalk' that gained widespread popularity after being performed by Michael Jackson. Tissue specificity: Expressed by the venom duct. Miscellaneous: The mature peptide does not contain cysteine residue. Mt1 and Mt2 peptides are found in a ratio of 1:4. Mt1 is more active when intracranially injected." [Ref.17927208]Gram-positive bacterium: Staphylococcus aureus (MIC=25-50 µM);##Gram-positive bacterium: Escherichia coli (MIC>50 µM). [Ref.17927208]95% hemolytic activity at 25 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17927208 Biochemistry. 2007 Nov 6;46(44):12586-12593. Biggs J.S, Rosenfeld Y, Shai Y, Olivera B.M. Conolysin-Mt: a conus peptide that disrupts cellular membranes. DRAMP02817 VDKGSYLPRPTPPRPIYNRN 20 Pyrrhocoricin P37362, P80307 Belongs to the drosocin family Not found Pyrrhocoris apterus (Sap sucking bug) (Cimex apterus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Not found 4EZN resolved by X-ray. Function: Antibacterial peptide. Affects Gram-negative bacteria E.coli 1106, P.aeruginosa, E.coli D22 and E.cloacae and Gram-positive bacteria M.luteus and B.subtilis. Gram-positive bacteria: Micrococcus luteus (MIC>80 µM in L.B, P.B), Bacillus megaterium (MIC>80 µM in L.B, P.B);##Gram-negative bacteria: Escherichia coliD22 (MIC=0.3 µM in L.B, P.B), A.tumefaciens (MIC=1.25 µM in LB and 3 µM in PB), Salmonella typhimurium (MIC=5 µM in L.B and 10 µM in P.B). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10076062##8002963##23562829 Biochim Biophys Acta. 1999 Feb 2;1426(3):459-467.##Biochem J. 1994 Jun 1;300 (Pt 2):567-575.##J Mol Biol. 2013 Jul 24;425(14):2463-2479. Hoffmann R, Bulet P, Urge L, Otvös L Jr.##Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru C, Hoffmann JA, Bulet P.##Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Sträter N. Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects.##Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus.##Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK. DRAMP02835 FAEPLPSEEEGESYSKEVPEMEKRYGGFM 29 Enkelytin (one chain of Proenkephalin-A; mammals, animals) P01211, Q2T9T4 Belongs to the opioid neuropeptide precursor family PENK Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus (MIC=0.2-0.4 µM), Bacillus megaterium (MIC=0.2-0.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6952189##8654396 Proc Natl Acad Sci U S A. 1982 Jan;79(2):360-364.##Eur J Biochem. 1996 Feb 1;235(3):516-525. Comb M, Herbert E, Crea R.##Goumon Y, Strub JM, Moniatte M, Nullans G, Poteur L, Hubert P, Van Dorsselaer A, Aunis D, Metz-Boutigue MH. Partial characterization of the mRNA that codes for enkephalins in bovine adrenal medulla and human pheochromocytoma.##The C-terminal bisphosphorylated proenkephalin-A-(209-237)-peptide from adrenal medullary chromaffin granules possesses antibacterial activity. DRAMP01381 GLFTLIKGAAKLIGKTVPKKQARLGMNLWLVKLPTNVKT 39 Odorranain-K1 (OdK1; Frogs, amphibians, animals) A6MBN8 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-K1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=4.68 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=4.68 μg/ml), Bacillus subtilis (MIC=1.10 μg/ml).##Yeast: Candida albicans (MIC=1.10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01383 ATAWDFGPHGLLPIRPIRIRPLCGKDKS 28 Odorranain-M1 (OdM1; Frogs, amphibians, animals) A6MBP6 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-M1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=9.37 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=4.68 μg/ml), Bacillus subtilis (MIC=75 μg/ml).##Yeast: Candida albicans (MIC=18.75 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP02841 RQKDKRPYSERKNQYTGPQFLYPPERIPPQKVIK 34 Lumbricin I(6–34) O96447 Not found Not found Synthetic construct (derived from residues 6–34 of lumbricin I) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Lumbricin I(6-34) has marginally stronger antimicrobial activities than lumbricin I. Has weak hemolytic activity when tested against human erythrocytes. [Ref.9784609]Gram-positive bacteria: Bacillus subtilis ATCC 62037 (MIC=8 µg/ml), Staphylococcus aureus ATCC 15752 (MIC=12 µg/ml), Streptococcus mutans ATCC 25175 (MIC=20 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 27325 (MIC=8 µg/ml), Pseudomonas putidaATCC 17426 (MIC=12 µg/ml), Serratia sp. ATCC 21074 (MIC=12 µg/ml).##Fungi: Candida albicans ATCC 10231 (MIC=12 µg/ml), Cryptococcus neoformance ATCC 34881 (MIC=16 µg/ml), Saccharomyces cerevisiae ATCC 44774 (MIC=8 µg/ml).##NOTE: Minimal inhibitory concentrations were determined by incubating approximately 104–105 CFU/ml of cells with serial dilutions of each peptide in a 96-well microtiter plate.. [Ref.9784609]0.03% hemolytic activity at 5 μg/ml, 0.07% hemolytic activity at 10 μg/ml, 0.13% hemolytic activity at 25 μg/ml, 0.17% hemolytic activity at 50 μg/ml, 0.21% hemolytic activity at 100 μg/ml against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784609 Biochim Biophys Acta. 1998 Oct 22;1408(1):67-76. Cho JH, Park CB, Yoon YG, Kim SC. Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization. DRAMP02843 ILKKWPWWPWRRKX 14 chain a, Structure Of An Indolicidin Peptide Derivative With No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Non helix or strand structure Not found 1QXQ resolved by NMR. Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=8 µg/ml), Pseudomonas aeruginosa (MIC=16 µg/ml), Salmonella typhimurium (MIC=64 µg/ml), S. typhimurium defensin sensitive (MIC=2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Staphylococcus aureus (MRSA) (MIC=16 µg/ml), S. epidermidis (MIC=4 µg/ml), Enterococcus faecalis (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11123901 Biochemistry. 2000 Dec 26;39(51):15765-15774. Rozek A, Friedrich CL, Hancock RE. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. DRAMP02844 ILAWKWAWWAWRR 13 CP10A (Indolicidin peptide derivative; mammals, animals) P33046 Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 8 residues) The structure of CP10A in DPC micelles determined from NMR data is mainly a-helical with elements of 310 helical geometry. 1HR1 resolved by NMR. "Function: A derivative of indolicidin, CP10A, has alanine residues substituted for proline residues and has improved activity against Gram-positive organisms. Chemical modification: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4 µg/ml), S. aureus SAP0017 MRSA (MIC=4 µg/ml), Staphylococcus haemolyticus Clinical isolate (MIC=2 µg/ml), S. haemolyticus Vancomycin-resistant isolate (MIC=1 µg/ml), Staphylococcus epidermidis Clinical isolate (MIC=2 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=8 µg/ml), Listeria monocytogenes NCTC 7973 (MIC=1 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=1 µg/ml), Corynebacterium xerosis Lab strain (MIC=1 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11294848 Antimicrob. Agents Chemother. 1999,43:1542-1548. Friedrich, C, M. G. Scott, N. Karunaratne, H. Yan, and R. E. Hancock. "Salt-resistant alpha-helical cationic antimicrobial peptides.##Antibacterial Action of Structurally Diverse Cationic Peptides on Gram-Positive Bacteria." DRAMP02845 ICLKKWPWWPWRRCKX 16 CP-11 (cathelicidin; mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Non helix or strand structure Not found 1QX9 resolved by NMR. Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=16 µg/ml), Pseudomonas aeruginosa (MIC=64 µg/ml), Salmonella typhimurium(MIC=64 µg/ml), S. typhimurium defensin sensitive (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Staphylococcus aureus (MRSA) (MIC=16 µg/ml), S. epidermidis(MIC=8 µg/ml), Enterococcus faecalis (MIC=64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11123901##14640680 Biochemistry. 2000 Dec 26;39(51):15765-15774.##Biochemistry. 2003 Dec 9;42(48):14130-14138. Rozek A, Friedrich CL, Hancock RE.##Rozek, A.; Powers, JP.; Friedrich, CL.; Hancock, RE. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.##Structure-based design of an indolicidin peptide analogue with increased protease stability. DRAMP02849 RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPPFRPPLRFP 42 Bactenecin 5 (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Salmonella typhimurium (MIC=2-10 µM), Klebsiella pneumoniae, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2229048 J Biol Chem. 1990 Nov 5;265(31):18871-18874. Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. DRAMP02851 RLCRIVVIRVCR 12 Cathelicidin-1 (Bactenecin-1, Bac1; Cyclic dodecapeptide; mammals, animals) P22226, A5PJA3, Q24JY5 Belongs to the cathelicidin family CATHL1 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Three disulfide bonds. "Function: Potent microbicidal activity; active against S.aureus and E.coli. Tissue specificity: Large granules of neutrophils. PTM: Contains three disulfide bonds." Gram-positive bacterium: Staphylococcus aureus (MIC=1-8 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=8-25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys3 and Cys11. L No cytotoxicity information found Not found 3290210 J Biol Chem. 1988 Jul 15;263(20):9573-9575. Romeo D, Skerlavaj B, Bolognesi M, Gennaro R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. DRAMP02854 GGLRSLGRKILRAWKKYGPIIVPIIRIG 28 Cathelicidin-5 (Antibacterial peptide BMAP-28; Myeloid antib P54229, A5PJ96, B9UKL6 Belongs to the cathelicidin family CATHL5 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found 2NDC "Function: Exerts a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus, and fungi. PTM: Contains two disulfide bonds. (By similarity)" Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µM), E. coli ML35 (MIC=2 µM), E. coli D21 (MIC=0.5 µM), Salmonella typhimurium ATCC 14028 (MIC=1 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=1 µM), Serratia marcescens ATCC 8100 (MIC=2 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µM), Staphylococcus aureus Cowan 1 (MIC=1 µM), Staphylococcus aureus (MRSA) (MIC=4 µM), Staphylococcus epidermidis ATCC 12228 (MIC=1 µM), Bacillus megaterium Bm11 (MIC=2 µM).##Fungi: Candida albicans (MIC=8 µM), Cryptococcus neoformans (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8910461##8706679 J Biol Chem. 1996 Nov 8;271(45):28375-28381.##Eur J Biochem. 1996 Jun 15;238(3):769-776. Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M.##Storici P, Tossi A, Lenarcic B, Romeo D. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities.##Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. DRAMP02855 GRFKRFRKKFKKLFKKLSPVIPLLHLG 27 Cathelicidin-6 (Antibacterial peptide BMAP-27, Myeloid antib P54228, B9UKM5 Belongs to the cathelicidin family CATHL6 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (2 helices; 19 residues) Not found 2KET resolved by NMR. "Function: Exerts a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus, and fungi. PTM: Contains two disulfide bonds. (By similarity)" Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=1 µg/ml), E. coli ML35 (MIC=1 µg/ml), E. coli D21 (MIC=0.25 µg/ml), Salmonella typhimurium ATCC 14028 (MIC=1 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=1 µg/ml), Serratia marcescens ATCC 8100 (MIC=2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µg/ml), Staphylococcus aureus Cowan 1 (MIC=2 µg/ml), Staphylococcus aureus (MRSA) (MIC=4 µg/ml), S. epidermidis ATCC 12228 (MIC=1 µg/ml), Bacillus megaterium Bm11 (MIC=2 µg/ml).##Fungi: Candida albicans (MIC=8 µg/ml), Cryptococcus neoformans (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8910461##19136450##PubMed ID is not available J. Biol. Chem. 1996;271:28375-28381.##J. Hered. 2009;100:241-245.##To be Published Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M.##Gillenwaters EN, Seabury CM, Elliott JS, Womack JE.##Yang S, Jung H, Kim J. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities.##Sequence analysis and polymorphism discovery in 4 members of the bovine cathelicidin gene family.##solution structure of BMAP-27. DRAMP02858 DFASCHTNGGICLPNRCPGHMIQIGICFRPRVKCCRSW 38 Bovine Beta-defensin 1 (bBD-1; BNBD-1; BNDB-1; mammals, animals) P46159 Belongs to the beta-defensin family DEFB1 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 but not against S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. (By similarity)" Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16777238 Vet Immunol Immunopathol. 2006 Sep 15;113(1-2):181-190. Aono S, Li C, Zhang G, Kemppainen RJ, Gard J, Lu W, Hu X, Schwartz DD, Morrison EE, Dykstra C, Shi J. Molecular and functional characterization of bovine beta-defensin-1. DRAMP02859 VRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKCCRSW 40 Bovine Beta-defensin 2 (bBD-2; BNBD-2; BNDB-2; mammals, animals) P46160 Belongs to the beta-defensin family DEFB2 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 7-36; 14-29; 19-37. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of Beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02860 EGVRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKCCRSW 42 Bovine Beta-defensin 3 (bBD-3; BNBD-3; BNDB-3; mammals, animals) P46161 Belongs to the beta-defensin family DEFB3 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635##9488394 J Biol Chem. 1993 Mar 25;268(9):6641-6648.##Infect Immun. 1998 Mar;66(3):1045-1056. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS.##Tarver AP, Clark DP, Diamond G, Russell JP, Erdjument-Bromage H, Tempst P, Cohen KS, Jones DE, Sweeney RW, Wines M, Hwang S, Bevins CL. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils.##Enteric beta-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection. DRAMP02861 QRVRNPQSCRWNMGVCIPFLCRVGMRQIGTCFGPRVPCCRR 41 Bovine Beta-defensin 4 (bBD-4; BNBD-4; BNDB-4; mammals, animals) P46162 Belongs to the beta-defensin family DEFB4 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 520A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##8454635 Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.##J Biol Chem. 1993 Mar 25;268(9):6641-6648. Yount N.Y, Yuan J, Diamond G, Tarver A, McGuire P.A, McCullough C, Cullor J.S, Bevins C.L, Selsted M.E.##Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Molecular cloning and expression of an antimicrobial beta-defensin from bovine neutrophils. Characterization of BNBD-4 cDNA and genomic sequences and localization of the peptide to large granules of mature neutrophils.##Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02862 QVVRNPQSCRWNMGVCIPISCPGNMRQIGTCFGPRVPCCRRW 42 Bovine Beta-defensin 5 (bBD-5; BNBD-5; BNDB-5; mammals, animals) P46163, O97533 Belongs to the beta-defensin family DEFB5 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 but not against S. aureus 502A. Tissue specificity: Neutrophilic granules. Alveolar macrophages. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02863 QGVRNHVTCRIYGGFCVPIRCPGRTRQIGTCFGRPVKCCRRW 42 Bovine Beta-defensin 6 (bBD-6; BNBD-6; BNDB-6; mammals, animals) P46164 Belongs to the beta-defensin family DEFB6 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02865 VRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPQIKCCR 38 Bovine Beta-defensin 8 (bBD-8; BNBD-8; BNDB-8; mammals, animals) P46166 Belongs to the beta-defensin family DEFB8 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 7-36; 14-29; 19-37. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of Beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02866 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTCLAPQIKCCR 40 Bovine Beta-defensin 9 (bBD-9; BNBD-9; BNDB-9; mammals, animals) P46167, O18814 Belongs to the beta-defensin family DEFB9 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-301 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635##9488394 J Biol Chem. 1993 Mar 25;268(9):6641-6648.##Infect Immun. 1998 Mar;66(3):1045-1056. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS.##Tarver AP, Clark DP, Diamond G, Russell JP, Erdjument-Bromage H, Tempst P, Cohen KS, Jones DE, Sweeney RW, Wines M, Hwang S, Bevins CL. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils.##Enteric beta-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection. DRAMP02867 QGVRSYLSCWGNRGICLLNRCPGRMRQIGTCLAPRVKCCR 40 Bovine Beta-defensin 10 (bBD-10; BNBD-10; BNDB-10; mammals, animals) P46168, Q5W5G8 Belongs to the beta-defensin family DEFB10 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635##15520886 J Biol Chem. 1993 Mar 25;268(9):6641-6648.##Mamm Genome. 2004 Oct;15(10):834-842. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS.##Roosen S, Exner K, Paul S, Schröder JM, Kalm E, Looft C. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils.##Bovine beta-defensins: identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue. DRAMP02868 GPLSCRRNGGVCIPIRCPGPMRQIGTCFGRPVKCCRSW 38 Bovine Beta-defensin 11 (bBD-11; BNBD-11; BNDB-11; mammals, animals) P46169, Q5W5G7 Belongs to the beta-defensin family DEFB11 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635##15520886 J Biol Chem. 1993 Mar 25;268(9):6641-6648.##Mamm Genome. 2004 Oct;15(10):834-842. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS.##Roosen S, Exner K, Paul S, Schröder JM, Kalm E, Looft C. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils.##Bovine beta-defensins: identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue. DRAMP02869 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW 38 Bovine Beta-defensin 12 (bBD-12; BNBD-12; BNDB-12; mammals, animals) P46170 Belongs to the beta-defensin family DEFB12 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand Not found 1BNB resolved by NMR. "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli ML35 (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635##8454636 J Biol Chem. 1993 Mar 25;268(9):6641-6648.##J Biol Chem. 1993 Mar 25;268(9):6649-6653. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS.##Tang YQ, Selsted ME. Purification, primary structures, and antibacterial activities of Beta-defensins, a new family of antimicrobial peptides from bovine neutrophils.##Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils. DRAMP02870 SGISGPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW 42 Bovine Beta-defensin 13 (bBD-13; BNBD-13; BNDB-13; mammals, animals) P46171 Belongs to the beta-defensin family DEFB13 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found 1BNB "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus (MIC=10-300 µg/ml);##Gram-negative bacterium: Escherichia coli (MIC=10-300 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of Beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02872 GRFKRFRKKFKKLFKKLS 18 Myeloid antimicrobial peptide BMAP-27 (1-18) (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Also has antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µM), Escherichia coli ML35 (MIC=4 µM), Escherichia coli D21 (MIC=4 µM), Salmonella typhimurium ATCC 14028 (MIC=4 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=1 µM), Serratia marcescens ATCC 8100 (MIC=2 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µM), Staphylococcus aureus Cowan 1 (MIC=2 µM), Staphylococcus aureus (MRSA) (MIC=4 µM), Staphylococcus epidermidis ATCC 12228 (MIC=1 µM), Bacillus megaterium Bm11 (MIC=2 µM).##Fungi: Candida albicans (MIC=16 µM), Cryptococcus neoformans (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8910461 J Biol Chem. 1996 Nov 8;271(45):28375-28381. Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. DRAMP02873 GGLRSLGRKILRAWKKYG 18 Myeloid antimicrobial peptide BMAP-28 (1-18) (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Also has antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli ML35 (MIC=0.5 µM), Escherichia coli D21 (MIC=0.5 µM), Salmonella typhimurium ATCC14028 (MIC=2 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=1 µM), Serratia marcescens ATCC 8100 (MIC=2 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µM), Staphylococcus aureus Cowan 1 (MIC=1 µM), Staphylococcus aureus (MIC=4 µM), Staphylococcus epidermidis ATCC 12228 (MIC=1 µM), Bacillus megaterium Bm11 (MIC=2 µM).##Fungi: Candida albicans (MIC=16 µM), Cryptococcus neoformans (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8910461 J Biol Chem. 1996 Nov 8;271(45):28375-28381. Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. DRAMP02875 LPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQ 76 Vasostatin-1 (VS-1; N-terminal fragment of Chromogranin-A; mammals, animals) P05059, P79392, Q2KJ52 Belongs to the chromogranin/secretogranin protein family CHGA Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found 6R2X "Function: Vasostatin-1 has antibacterial activity against Gram-positive bacteria M. luteus, B. megaterium. Possesses antifungal activity against N. crassa, A. fumigatus, A. brassicicola, N. hematococca, F. culmorum and F. oxyporum and against the yeast S. cerevisiae and C. albicans. Miscellaneous: Binds calcium with a low-affinity." Gram-positive bacteria: Micrococcus luteus (MIC=2 µM), Bacillus megaterium (MIC=0.2 µM).##Fungi: Neurospora crassa (MIC=3 µM), Aspergillus fumigatus (MIC=5 µM), Alternaria brassicicola (MIC=3 µM), Nectria haematococca (MIC=1 µM), Fusarium culmorum (MIC=1 µM), F. oxyporum (MIC=10 µM), Saccharomyces cerevisiae (MIC=10 µM), Candida albicans (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binds calcium with a low-affinity. 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP02877 GGLRSLGRKILRAWKKYGPQATPATRQ 27 mBMAP28 (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found 2NDC Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli ML35 (MIC=0.5 µM), Salmonella typhimurium ATCC 14028 (MIC=1 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=0.5 µM), Serratia marcescens ATCC 8100 (MIC=4 µM).##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=8 µM), Staphylococcus aureus (MRSA) (MIC>64 µM), Staphylococcus epidermidis ATCC 12228 (MIC=2 µM), Bacillus megaterium Bm11 (MIC=2 µM).##Fungi: Candida albicans (MIC=8 µM), Cryptococcus neoformans (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8910461 J. Biol. Chem. 1996; 271:28375-28381 Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M.1996 Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. DRAMP02878 NPVSCVRNKGICVPIRCPGSMKQIGTCVGRAVKCCRKK 38 Tracheal antimicrobial peptide (TAP; mammals, animals) P25068, O97532 Belongs to the beta-defensin family (LAP/TAP subfamily) Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial activity in vitro. In addition, the peptide is active against Candida albicans, indicating a broad spectrum of activity. Tissue specificity: Tracheal epithelium. PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. (By similarity)" Gram-negative bacteria: Escherichia coli D31 (MIC=12-25 µg/ml), Klebsiella pneumoniae 13883 (MIC=12-25 µg/ml), Pseudomonas aeruginosa 27853 (MIC=25-50 µg/ml).##Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=25-50 µg/ml).##Fungi: Candida ablicans (MIC=6-12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2023943##8506305 Proc Natl Acad Sci U S A. 1991 May 1;88(9):3952-3956.##Proc Natl Acad Sci U S A. 1993 May 15;90(10):4596-4600. Diamond G, Zasloff M, Eck H, Brasseur M, Maloy WL, Bevins CL.##Diamond G, Jones DE, Bevins CL. Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA.##Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene. DRAMP02903 ILGPILGLVSNALGGLL 17 Bombin H7 No entry found Not found Not found Bombina orientalis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Bacillus megaterium Bm11 (MIC=3.3 µM);##Gram-negative bacterium: Escherichia coli D22 (MIC=3.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02910 LRRIIRKIIHIIKK 14 Ovispirin-2 (OV-2; mammals, animals) No entry found Not found Not found Ovis aries (Sheep) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Pseudomonas aeruginosa (MIC=0.03-16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11557478 Antimicrob Agents Chemother. 2001 Oct;45(10):2838-2844. Saiman L, Tabibi S, Starner TD, San Gabriel P, Winokur PL, Jia HP, McCray PB Jr, Tack BF. Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis. DRAMP02911 IRRIIRKIIHIIKK 14 Ovispirin-3 (OV-3; mammals, animals) No entry found Not found Not found Ovis aries (Sheep) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Pseudomonas aeruginosa (MIC=1-8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11557478 Antimicrob Agents Chemother. 2001 Oct;45(10):2838-2844. Saiman L, Tabibi S, Starner TD, San Gabriel P, Winokur PL, Jia HP, McCray PB Jr, Tack BF. Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis. DRAMP02912 RGLRRLGRKIAHGVKKYGPTVLRIIRIAG 29 SMAP-29 (Cathelin-related peptide SC5; Myeloid antibacterial peptide MAP-29; mammals, animals) P49928, P49929 Belongs to the cathelicidin family Not found Ovis aries (Sheep) Antimicrobial, Antibacterial, Antifungal Protein level Alpha helix Not found 1FRY resolved by NMR. "Function: Broad spectrum bactericidal agent. Biophysicochemical properties: Temperature dependence (Thermostable)." [Ref.8549789][No NaCl]: Escherichia coli DH5a (MIC=0.1 µM), Escherichia coli ML-35p (MIC=0.18 µM), Pseudomonas aeruginosa PAO1 (MIC=0.17 µM), Pseudomonas aeruginosa MR3007 (MIC=0.34 µM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=1.24 µM), Staphylococcus aureus 93918 (MIC=0.31 µM).##[100 mM NaCl]: Escherichia coli DH5a (MIC=0.07 µM), Escherichia coli ML-35p (MIC=0.12 µM), Pseudomonas aeruginosa PAO1 (MIC=0.08 µM), Pseudomonas aeruginosa MR3007 (MIC=0.18 µM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=0.65 µM), Staphylococcus aureus 93918 (MIC=0.43 µM). [Ref.8549789]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Outer membrane protein I (OprI) 8549789##11932493 FEBS Lett. 1995 Dec 27;377(3):519-522.##Protein Eng. 2002 Mar;15(3):225-232. Mahoney MM, Lee AY, Brezinski-Caliguri DJ, Huttner KM.##Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF. Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide.##Impact of single-residue mutations on the structure and Function: of ovispirin/novispirin antimicrobial peptides. DRAMP02913 GLFGRLRDSLQRGGQKILEKAERIWCKIKDIFRG 34 SMAP-34 (cathelicidin; mammals, animals) No entry found Not found Not found Ovis aries (Sheep) Antimicrobial, Antibacterial Not found Not found Not found Function: Has antibacterial activity. [Ref.10768969][No NaCl]: Escherichia coli DH5a (MIC=0.5 μM), Escherichia coli ML-35p (MIC=1.93 μM), Pseudomonas aeruginosa PAO1 (MIC=0.6 μM), Pseudomonas aeruginosa MR3007 (MIC=2 μM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=4 μM), Staphylococcus aureus 93918 (MIC=1.96 μM).100 mM NaCl: Escherichia coli DH5a (MIC=0.23 μM), Escherichia coli ML-35p (MIC=1.03 μM), Pseudomonas aeruginosa PAO1 (MIC=0.77 μM), Pseudomonas aeruginosa MR3007 (MIC=1.9 μM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=13.3 μM), Staphylococcus aureus 93918 (MIC=2.13 μM). [Ref.10768969]30% hemolysis at 1000 μg/ml against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10768969 Infect Immun. 2000 May;68(5):2748-2755. Travis SM, Anderson NN, Forsyth WR, Espiritu C, Conway BD, Greenberg EP, McCray PB Jr, Lehrer RI, Welsh MJ, Tack BF. Bactericidal activity of mammalian cathelicidin-derived peptides. DRAMP02922 KCWNLRGSCREKCIKNEKLYIFCTSGKLCCLKPK 34 Canine beta-defensin (dogs, mammals, animals) No entry found Not found Not found Canis lupus familiaris (Dog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli 25922 (MIC=20 µg/ml), Escherichia coli 700336 (MIC=50 µg/ml);##Gram-positive bacteria: Klebsiella pneumoniae 10031 (MIC=20 µg/ml), Listeria monocytogenes 19115 (MIC=10 µg/ml), Staphylococcus aureus 10832 (MIC=100 µg/ml), N. gonorrhoeae 10150 (MIC=50 µg/ml).##Fungi: Candida albicans 14053 (MIC=50 µg/ml), Candida albicans 11006 (MIC=5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15845463 Infect Immun. 2005 May;73(5):2611-2620. Sang Y, Ortega MT, Blecha F, Prakash O, Melgarejo T. Molecular cloning and characterization of three beta-defensins from canine testes. DRAMP02923 KCWNLRGSCREKCIKNEKLYIFCTSGKLCCLKPKFQPNMLQR 42 cBD-1 (Canine beta-defensin 1; dogs, mammals, animals) No entry found Not found Not found Canis Lupis (Dog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Listeria monocytogenes(MIC=6 mµg/ml), Staphylococcus aureus (MIC=100 mµg/ml);##Gram-negative bacteria: Escherichia coli (MIC=20-25 mµg/ml), Klebsiella pneumoniae (MIC=20 mµg/ml), Neisseria gonorrhoeae (MIC=50 mµg/ml).##Yeast: Candida albicans (MIC=5-50 mµg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15845463 Infect Immun. 2005 May;73(5):2611-2620. Sang Y, Ortega MT, Blecha F, Prakash O, Melgarejo T. Molecular cloning and characterization of three beta-defensins from canine testes. DRAMP18367 GFGSKPLDSFGLNFF 15 Chaxapeptin (a class 2 lasso peptide; class 1 microcin, bacteriocins) No entry found Not found Not found Streptomyces leeuwenhoekii Strain C58 Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Not found Not found Fuction: No activity against the Gram-negative bacteria. It showed dose dependent inhibition of A549 cancer cells. Gram-positive bacteria: S. aureus and B. subtilis (MIC 30-35 ug/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26402731 J Org Chem. 2015 Oct 16;80(20):10252-60. Elsayed SS, Trusch F, Deng H, Raab A, Prokes I, Busarakam K, Asenjo JA, Andrews BA, van West P, Bull AT, Goodfellow M, Yi Y, Ebel R, Jaspars M, Rateb ME Chaxapeptin, a Lasso Peptide from Extremotolerant Streptomyces leeuwenhoekii Strain C58 from the Hyperarid Atacama Desert DRAMP18368 SMSGFSKPHD 10 Bacteriocin TSU4 (bacteria, prokaryotes) No entry found Not found Not found Lactobacillus animalis TSU4 Antimicrobial, Antibacterial Not found Not found Only the N-terminal sequence is available. Active against A. hydrophila, E. coli, P. aeruginosa, S. typhimurium, S. paratyphi, S. flexneri, and S. aureus (inhibition zone 25-28 mm). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26245257 Appl Biochem Biotechnol. 2015 Sep;177(1):90-104 Sahoo TK, Jena PK, Patel AK, Seshadri S. Purification and Molecular Characterization of the Novel Highly Potent Bacteriocin TSU4 Produced by Lactobacillus animalis TSU4 DRAMP02925 RLKELITTGGQKIGEKIRRIGQRIKDFFKNLQPREEKS 38 Cathelicidin (dogs, mammals, animals) No entry found Not found Not found Canis lupus familiaris (Dog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=1.25 µM), Klebsiella pneumoniae (MIC=1.25 µM), Salmonella serotype Typhimurium (MIC=1.25 µM), Pseudomonas aeruginosa (MIC=1.25 µM), Proteus mirabilis (MIC=1.25 µM), Salmonella serotype Enteritidis (MIC=0.5 µM), Neisseria gonorrhoeae (MIC=0.06 µM).##Gram-positive bacteria: Listeria monocytogenes (MIC=0.5 µM), Staphylococcus aureus (MIC=50 µM).##Fungi: Candida albicans (MIC=12.5-50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17462733 Dev Comp Immunol. 2007;31(12):1278-1296. Sang Y, Teresa Ortega M, Rune K, Xiau W, Zhang G, Soulages JL, Lushington GH, Fang J, Williams TD, Blecha F, Melgarejo T. Canine cathelicidin (K9CATH): gene cloning, expression, and biochemical activity of a novel pro-myeloid antimicrobial peptide. DRAMP02931 SPRVSRRYGRPFGGRPFVGGQFGGRPGCVCIRSPCPCANYG 41 Arasin-likeSp (crabs, Arthropods, animals) No entry found Not found Not found Scylla paramamosain (Mud crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus haemolyticus (MIC=6.25-12.5 µM), Aerococcus viridans (MIC=0.19-0.39 µM), Micrococcus luteus (MIC=0.39-0.78 µM), Bacillus subtilis (MIC=6.25-12.5 µM);##Gram-negative bacteria: Escherichia coli 363 (MIC>50 µM), Aeromonas hydrophila (MIC>50 µM), V. harveyi (MIC=0.78-1.56 µM), Vibrio anguillarum (MIC=3.125-6.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21220028 Fish Shellfish Immunol. 2011 Feb;30(2):706-712. Imjongjirak C, Amparyup P, Tassanakajon A. Two novel antimicrobial peptides, arasin-likeSp and GRPSp, from the mud crab Scylla paramamosain, exhibit the activity against some crustacean pathogenic bacteria. DRAMP02932 IPAMEPAARVKRSPGYGGCSPRWACGGYG 29 GRPSp (crabs, Arthropods, animals) No entry found Not found Not found Scylla paramamosain (Mud crab) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus haemolyticus (MIC>50 µM), Aerococcus viridans (MIC=6.25-12.5 µM), Micrococcus luteus (MIC=12.5-25 µM), Bacillus subtilis (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21220028 Fish Shellfish Immunol. 2011 Feb;30(2):706-712. Imjongjirak C, Amparyup P, Tassanakajon A. Two novel antimicrobial peptides, arasin-likeSp and GRPSp, from the mud crab Scylla paramamosain, exhibit the activity against some crustacean pathogenic bacteria. DRAMP02933 RRWCFRVCYRGFCYRKCR 18 Polyphemusin-1 (PM1; crabs, Arthropods, animals) P14215 Belongs to the tachyplesin/polyphemusin family Not found Limulus polyphemus (Atlantic horseshoe crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand (2 strands; 4 residues) The solution structure of polyphemusin I is determined using (1)H-NMR spectroscopy. Polyphemusin I is found to be an amphipathic, beta-hairpin connected by a type I' beta-turn. 1RKK resolved by NMR. "Function: PM1 showes high antimicrobial activity against the Gram-negative, Gram-positive and fungal specimens tested. Tissue specificity: Hemocytes. PTM: Contains two disulfide bonds 4-17; 8-13 and C-terminal amidation." Gram-negative bacteria: Escherichia coli UB1005 (MIC=0.5 µg/ml), E. coli DC2 (MIC=1 µg/ml), Salmonella typhimurium (defensin-sensitive) (MIC=0.25 µg/ml), S. typhimurium (MIC=1 µg/ml), Pseudomonas aeruginosa K799 (MIC=2 µg/ml), P. aeruginosa Z61 (MIC=1 µg/ml);##Gram-positive bacteria: Staphylococcus aureus SAP0017 (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=1 µg/ml), Enterococcus faecalis (MIC=1 µg/ml).##Yeasy: Candida albicans (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys4 and Cys17,Cys8 and Cys13. L No cytotoxicity information found Not found 2514185##15134657 J Biochem. 1989 Oct;106(4):663-668.##Biochim Biophys Acta. 2004 May 6;1698(2):239-250. Miyata T, Tokunaga F, Yonega T, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y.##Powers JP, Rozek A, Hancock RE. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity.##Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I. DRAMP02934 RRWSFRVSYRGFSYRKSR 18 PM1-S (linear derivative of PM1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic No secondary structure (CD) The CD spectra of PM1-S indicates that, in all environments (phosphate buffer, TFE, and liposomes), the peptide displays no observable patterns that could be related to structural features. This indicates that PM1-S is a flexible molecule with no favoured conformation. Function: PM1-S remaines active against Gram-negative bacteria but displayed poor activity to both Gram-positive and fungal microorganisms. Gram-negative bacteria: Escherichia coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=4 µg/ml), Salmonella typhimurium (defensin-sensitive) (MIC=2 µg/ml), S. typhimurium (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), P. aeruginosa Z61 (MIC=16 µg/ml);##Gram-positive bacteria: Staphylococcus aureus SAP0017 (MIC=32 µg/ml), Staphylococcus epidermidis (MIC=16 µg/ml), Enterococcus faecalis (MIC=2 µg/ml).##Yeasy: Candida albicans (MIC=64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15134657 Biochim Biophys Acta. 2004 May 6;1698(2):239-250. Powers JP, Rozek A, Hancock RE. Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I. DRAMP02950 YVDREINLFDHYCIISRSPHISRWELKWQATVTCPGWTPVKGKVRGYSNPLSAEREATRDFVQRIVQRGLVTRDEASEWL 80 PtALF5 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 5; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CIISRSPHISRWELKWQATVTC) and two conserved cysteine residues which can form a disulfide bridge. PtALF5 transcript in hemocytes showes a clear time-dependent response expression pattern with obvious decrease at 6 h and significant increase at 24 h. The recombinant PtALF5 has antimicrobial activity against Gram-negative bacteria Vibrio alginolyticus and Pseudomonas aeruginosa. Gram-negative bacteria: Vibrio alginolyticus (MIC=3.89-7.78 µM), Edwardsiella tarda (MIC=7.78-15.54 µM), Pseudomonas aeruginosa (MIC=15.54-31.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21362485##22516300 Fish Shellfish Immunol. 2011 Jul;31(1):29-42.##Fish Shellfish Immunol. 2012 Jul;33(1):85-91. Liu Y, Cui Z, Song C, Wang S, Li Q.##Liu Y, Cui Z, Li X, Song C, Li Q, Wang S. Multiple isoforms of immune-related genes from hemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.##Molecular cloning, expression pattern and antimicrobial activity of a new isoform of anti-lipopolysaccharide factor from the swimming crab Portunus trituberculatus. DRAMP02951 MARVSLLLIVLSIALVAPSQGFLKDLLFGEAKTALLEDGTTEILDHVCNFRVMPRLRSWELYFRGDVWCPGWTVIKGESL 80 PtALF6 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 6; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CNFPVMPRLRSWELYFRGDVWC) and two conserved cysteine residues which can form a disulfide bridge. Gram-negative bacteria: Vibrio alginolyticus L59 (MIC=1.17-2.33 µM), Pseudomonas aeruginosa P25 (MIC=9.32-18.64 µM);##Gram-positive bacteria: Micrococcus luteus M2 (MIC=9.32-18.64 µM), Staphylococcus aureus S7 (MIC=9.32-18.64 µM).##Fungi: Pichia pastoris GS115 (MIC>74.57 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21362485##23257203 Fish Shellfish Immunol. 2011 Jul;31(1):29-42.##Fish Shellfish Immunol. 2013 Feb;34(2):463-470. Liu Y, Cui Z, Song C, Wang S, Li Q.##Liu Y, Cui Z, Li X, Song C, Shi G. Multiple isoforms of immune-related genes from hemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.##A newly identified anti-lipopolysaccharide factor from the swimming crab Portunus trituberculatus with broad spectrum antimicrobial activity. DRAMP02952 MRKGVVTGLFVALVVMCLYLPQPCEAQYEALTAAILTKLSKMWHSDTLNFLGHTCHVSRTPTVKRFKLYWKGKFWCPGWA 80 PtALF7 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 7; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CHVSRTPTVKRFKLYWKGKFWC) and two conserved cysteine residues which can form a disulfide bridge. Gram-negative bacteria: Vibrio alginolyticus (MIC=0.51-1.02 µM), Edwardsiella tarda (MIC=2.04-4.07 µM), Pseudomonas aeruginosa (MIC=1.02-2.04 µM);##Gram-positive bacteria: Micrococcus luteus (MIC=32.59-65.19 µM), Staphylococcus aureus (MIC=8.15-16.30 µM).##Fungi: Pichia pastoris (MIC>130.37 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21362485##23261507 Fish Shellfish Immunol. 2011 Jul;31(1):29-42.##Fish Shellfish Immunol. 2013 Feb;34(2):652-659. Liu Y, Cui Z, Song C, Wang S, Li Q.##Liu Y, Cui Z, Li X, Song C, Shi G, Wang C. Multiple isoforms of immune-related genes from hemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.##Molecular cloning, genomic structure and antimicrobial activity of PtALF7, a unique isoform of anti-lipopolysaccharide factor from the swimming crab Portunus trituberculatus. DRAMP02953 SRWPSPGRPRPFPGRPKPIFRPRPCNCYAPPCPCDRW 37 Arasin-1 (Pro-rich, Arg-rich; crabs, Arthropods, animals) A6XMY0 Not found Not found Hyas araneus (Great spider crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Corynebacterium glutamicum (MIC=0.8 µM), Listonella anguillarum (MIC=6.3 µM);##Gram-negative bacterium: Escherichia coli (MIC=12.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys25 and Cys34,Cys27 and Cys32. L No cytotoxicity information found Not found 17658600 Dev Comp Immunol. 2008;32(3):275-285. Stensvag K, Haug T, Sperstad S.V, Rekdal O, Indrevoll B, Styrvold O.B. Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. DRAMP02956 SHQDCYEALHKCMASHSKPFSCSMKFHMCLQQQ 33 Dolabellanin B2 P83376 Not found Not found Dolabella auricularia (Sea hare) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. Also possesses antifungal activity. PTM: Contains two disulfide bonds. Up to two of the methionines may be oxidized to methionine sulfoxides." Gram-positive bacteria: Bacillus subtilis RIMD0225014 (MIC=2.5 µg/ml), Staphylococcus aureus IID1677 (MRSA) (MIC=20.0 µg/ml), Listeria monocytogenes VIU206 (MIC=40.0 µg/ml).##Gram-negative bacteria: Haemophilus influenzae IID983 (MIC=5.0 µg/ml), V. vulnificus RIMD2219009 (MIC=5.0 µg/ml), Escherichia coli JM109 (MIC=20.0 µg/ml), E. coli DH5α (MIC=40.0 µg/ml).##Fungi: Candida albicans ATCC36232, Candida tropicalis TIMM0313, S. pombe IFO1628, Saccharomyces cerevisiae A581A. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Contains two disulfide bonds. Up to two of the methionines may be oxidized to methionine sulfoxides. L No cytotoxicity information found Not found 12590964 Dev. Comp. Immunol. 2003;27:305-311. Iijima R, Kisugi J, Yamazaki M. A novel antimicrobial peptide from the sea hare Dolabella auricularia. DRAMP02959 RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP 39 Antibacterial protein PR-39 (pigs, mammals, animals) P80054, Q9TR84 Belongs to the cathelicidin family PR39 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Rich Not found "Tissue specificity: Small intestine and bone marrow. PTM: Proline amide at P39." Gram-negative bacteria: Escherichia coli K12 D21 (MIC=0.3 µM), Escherichia coli Bd2221175 (MIC=0.3 µM), Salmonella typhimurium LT2 (MIC=1µM), Proteus vulgaris Pvll (MIC=300 µM), Pseudomonas aeruginosa OT97 (MIC=200 µM), Acinetobacter calcoaceticus Acl 1 (MIC=3 µM).##Gram-positive bacteria: Bacillus megaterium (MIC=0.3 µM), Bacillus subtilis (MIC=15 µM), Staphylococcus aureus (MIC=200 µM), Streptococcus pyogenes (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1765098##7624374 Eur J Biochem. 1991 Dec 18;202(3):849-854.##Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):7085-7089. Agerberth B, Lee JY, Bergman T, Carlquist M, Boman HG, Mutt V, Jörnvall H.##Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson L, Boman HG. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides.##Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. DRAMP02960 RIIDLLWRVRRPQKPKFVTVWVR 23 Antibacterial peptide PMAP-23 (Myeloid antibacterial peptide 23; pigs, mammals, animals) P49930 Belongs to the cathelicidin family PMAP23 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix Not found "Function: Exerts antimicrobial activity against both Gram-positive and negative bacteria at concentrations of 2-16 micro molar. Its activity appears to be mediated by its ability to damage bacterial membranes. PTM: Contains two disulfide bonds (By similarity)." Gram-negative bacteria: Escherichia coli ML35 (MIC=2 µM), Escherichia coli ATCC 25922 (MIC=4 µM), Salmonella typhimurium ATCC 14028 (MIC=8 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=16 µM).##Gram-positive bacteria: Bacillus megaterium (MIC=2 µM), Staphylococcus aureus ATCC 25923 (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8132502 J Biol Chem. 1994 Mar 18;269(11):7855-7858. Zanetti M, Storici P, Tossi A, Scocchi M, Gennaro R. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. DRAMP02961 GLLSRLRDFLSDRGRRLGEKIERIGQKIKDLSEFFQS 37 Antibacterial peptide PMAP-37 (Myeloid antibacterial peptide 37; pigs, mammals, animals) P49932 Belongs to the cathelicidin family PMAP37 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix Not found "Function: Exerts antimicrobial activity against both Gram-positive and negative bacteria with minimal inhibitory concentrations ranging over 1-4 micro molar. Its activity appears to be mediated by its ability to damage bacterial membranes. PTM: Contains two disulfide bonds (By similarity)." Gram-negative bacteria: Escherichia coli ML35 (MIC=2 µM), Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli D21 (MIC=2 µM), Salmonella typhimurium ATCC 14028 (MIC=4 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=2 µM).##Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=4 µM), Bacillus megaterium local isolate (IC=4 µM), Staphylococcus aureus ATCC 25923 (MIC=32 µM), Staphylococcus aureus Cowan 1 (MIC=64 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7737198 Eur J Biochem. 1995 Mar 15;228(3):941-946. Tossi A, Scocchi M, Zanetti M, Storici P, Gennaro R. PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity. DRAMP02228 SMLSVLKNLGKVGLGFVACKINKQC 25 RANATUERIN 1 (Frogs, amphibians, animals) P82741 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found Function: Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. Has activity against C.albicans. Has no detectable hemolytic activity. [Ref.9784389] Gram-positive bacterium: Staphylococcus aureus (MIC=50 µM);##Gram-negative bacterium: Escherichia coli (MIC=2 µM);##Yeast: Candida albicans (MIC=70 µM). [Ref.9784389] It has no detectable hemolytic activity at aconcentration of 20µg/ml against human red blood cell. Cyclic Free Cyclization (Cys19 and Cys25) Disulfide bond between Cys19 and Cys25. L No cytotoxicity information found Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02963 GRFRRLRKKTRKRLKKIGKV 20 PMAP-36(1-20) No entry found Not found Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Exerts antimicrobial activity against both Gram-positive and negative bacteria. Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=6 µM), Bacillus megaterium Bm11 (MIC=3 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12 µM), E. coli ML35 (MIC=12 µM), S. enterica ser. Typhimurium ATCC 14028 (MIC=48 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=3 µM).##Fungi: Candida albicans c.i. (MIC>64 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16128809 FEBS J. 2005 Sep;272(17):4398-4406. Scocchi M, Zelezetsky I, Benincasa M, Gennaro R, Mazzoli A, Tossi A. Structural aspects and biological properties of the cathelicidin PMAP-36. DRAMP02964 GRFRRLRKKTRKRLKKIGKVLKWIPPIVGSIPLG 34 PMAP-36(1-34) No entry found Not found Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Exerts antimicrobial activity against both Gram-positive and negative bacteria. Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=1 µM), S. aureus 710A (MIC=2 µM), S. aureus SA-62 (MRSA) (MIC=4 µM), Bacillus megaterium Bm11 (MIC=1 µM), S. epidermidis ATCC 12228 (MIC=1 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), E. coli ML35 (MIC=1 µM), E. coli D21 (MIC=1 µM), E. coli D22 (MIC=0.5 µM), S. enterica ser. Typhimurium ATCC 14028 (MIC=1 µM), S. enterica ser. Enteritidis H2 (MIC=1 µM), P. aeruginosa ATCC 27853 (MIC=1 µM), S. marcescens ATCC 8100 (MIC=2 µM).##Fungi: Candida albicans c.i. (MIC=8 µM), Cryptococcus neoformans c.i.(MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16128809 FEBS J. 2005 Sep;272(17):4398-4406. Scocchi M, Zelezetsky I, Benincasa M, Gennaro R, Mazzoli A, Tossi A. Structural aspects and biological properties of the cathelicidin PMAP-36. DRAMP02965 GRFRRLRKKTRKRLKKIGKVLKWIPPIVGSIPLGC 35 PMAP-36(1-35)2 No entry found Not found Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Exerts antimicrobial activity against both Gram-positive and negative bacteria. Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µM), S. aureus 710A (MIC=2 µM), S. aureus SA-62 (MRSA) (MIC=4 µM), Bacillus megaterium Bm11 (MIC=1 µM), S. epidermidis ATCC 12228 (MIC=1 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), E. coli ML35 (MIC=0.5 µM), E. coli D21 (MIC=0.5 µM), E. coli D22 (MIC=0.5 µM), S. enterica ser. Typhimurium ATCC 14028 (MIC=1 µM), S. enterica ser. Enteritidis H2 (MIC=0.5 µM), P. aeruginosa ATCC 27853 (MIC=1 µM), S. marcescens ATCC 8100 (MIC=2 µM).##Fungi: Candida albicans c.i. (MIC=16 µM), Cryptococcus neoformans c.i.(MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16128809 FEBS J. 2005 Sep;272(17):4398-4406. Scocchi M, Zelezetsky I, Benincasa M, Gennaro R, Mazzoli A, Tossi A. Structural aspects and biological properties of the cathelicidin PMAP-36. DRAMP02966 KQATVGDINTERPGILDLKGKAKWDAWNGLKGTSKEDAMKAYINKVEELKKKYGI 55 DBI(32-86) (pigs, mammals, animals) P12026, A7YB23, Q9TSG2 Belongs to the ACBP family DBI Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: DBI(32-86) has antibacterial properties. Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.69 µM);##Gram-negative bacteria: Escherichia coli D22 (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8375398##3289918 Eur J Biochem. 1993 Sep 1;216(2):623-629.##Eur J Biochem. 1988 Jun 1;174(2):239-245. Agerberth B, Boman A, Andersson M, Jörnvall H, Mutt V, Boman HG.##Chen ZW, Agerberth B, Gell K, Andersson M, Mutt V, Ostenson CG, Efendić S, Barros-Söderling J, Persson B, Jörnvall H. Isolation of three antibacterial peptides from pig intestine: gastric inhibitory polypeptide (7-42), diazepam-binding inhibitor (32-86) and a novel factor, peptide 3910.##Isolation and characterization of porcine diazepam-binding inhibitor, a polypeptide not only of cerebral occurrence but also common in intestinal tissues and with effects on regulation of insulin release. DRAMP02970 RGGRLCYCRRRFCVCVGR 18 Protegrin-1 (Protegrin 1; PG-1; pigs, mammals, animals) P32194 Belongs to the cathelicidin family NPG1 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand Not found 1PG1 resolved by NMR. The sequence of IB-367 is RGGLCYCRGRFCVCVGR and the peptide is active against bacteria and fungi. This peptide showed synergistic effect with LL-37 against P. aeruginosa and E. coli (Yan H & Hancock REW 2001 Antimicrob Agents Chemother 45: 1558-60). PG-1 derivatives were subjected to clinical trials. Gram-negative bacteria: Escherichia coli (MIC=64 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=64 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys15,Cys8 and Cys13. L [Ref.31399625] Cytotoxicity: 661W cells(IC50=353.4±70.5μM), HEK293T cells(IC50=2760±54.1μM), NIH-3T3 cells(IC50=719.2±59.5μM), SH-SY5Y cells(IC50=590.4±58.2μM), PMN cells(IC50=948.9±64.1μM), and 3D4/2 cells(IC50=391.1±71.3μM) Cell membrane 8647100 Chem Pharm Bull (Tokyo). 1995 May;43(5):853-858. Tamamura H, Murakami T, Horiuchi S, Sugihara K, Otaka A, Takada W, Ibuka T, Waki M, Yamamoto N, Fujii N. Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity. DRAMP02975 VRRFPWWWPFLRR 13 Tritrpticin (Trp-rich; pigs, mammals, animals) No entry found Belongs to the cathelicidin family Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix (1 helices; 3 residues) Not found 1D6X resolved by NMR. Function: Tritrpticin has strong antimicrobial activity with a wide spectrum. Gram-negative bacteria: Escherichia coli (5 mm), Pseudomonas aeruginosa (3 mm), Klebsiella pneumonia (7 mm), Proteus mirabilis (1 mm);##Gram-positive bacteria: Staphylococcus epidermidis (5 mm), Streptococcus group D (4 mm). [inhibit zones in mm]##Fungi: Aspergillus fumigatus (MIC=250 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8706838##10606506 FEBS Lett. 1996 Jul 15;390(1):95-98.##Biochemistry. 1999 Dec 21;38(51):16749-55. Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K.Schibli DJ, Hwang PM, Vogel HJ.##Schibli DJ, Hwang PM, Vogel HJ. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides.##Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold. DRAMP02980 GLICESCRKIIQKLEDMVGPQPNEDTVTQAASRVCDKMKILRGVCKKIMRTFLRRISKDILTGKKPQAICVDIKICKE 78 Antimicrobial peptide NK-lysin (NKL; pigs, mammals, animals) Q29075 Not found NKL Sus scrofa (Pig) Antimicrobial, Antibacterial, Antifungal, Antitumor Protein level Alpha helix Not found 1NKL resolved by NMR. "Function: May be an effector molecule of cytotoxic activity. High activity against E. coli and B. megaterium, moderate against A. calcoaceticus and S. pyogenes. Has some antifungal activity against Candida albicans. Tissue specificity: Cytotoxic T and NK cells. Induction: By interleukin-2. PTM: Contains three disulfide bonds 4-76; 7-70; 35-45." [with medium E]: Escherichia coli D21 (MIC=0.5 µM), Escherichia coli Bd2221/75 (MIC=10 µM), Acinetobacter calcoaceticus Ac 11 (MIC=7 µM), Bacillus megaterium Bmll (MIC=1.6 µM);##[without medium E]: Escherichia coli D21 (MIC=8 µM), Escherichia coli Bd2221/75 (MIC=39 µM), Bacillus megaterium Bmll (MIC=0.8 µM), Streptococcus pyogenes w.t. (MIC=34 µM), Candida albicans w.t. (MIC=31 µM). [Ref.7737114] It exhibits no hemolytic activity at 170 µM against sheep red blood cells. Cyclic Free Free Disulfide bonds between Cys4 and Cys76; Cys7 and Cys70; Cys35 and Cys45. L [Ref.7737114] NK-lysin at 50μg/ml was able to give 90% lysis of 5'Cr-labelled YAC-1 cells in a medium with 2% fetal calf serum(FCS) and 75% lysis in phosphate-buffered saline(PBS), 15% lysis suspended in medium E. Lipopolysaccharide (LPS)-binding 7737114##9334742 EMBO J. 1995 Apr 18;14(8):1615-1625.##Nat Struct Biol. 1997 Oct;4(10):793-795. Andersson M, Gunne H, Agerberth B, Boman A, Bergman T, Sillard R, Jörnvall H, Mutt V, Olsson B, Wigzell H, et al.##Liepinsh E, Andersson M, Ruysschaert JM, Otting G. NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity.##Saposin fold revealed by the NMR structure of NK-lysin. DRAMP03028 IDWKKLLDAAKQIL 14 Polybia-MP1 No entry found Not found Not found Polybia paulista Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.29075946] Gram-positive bacterium: Bacillus subtilis (MIC=12.5μM), Staphylococcus aureus (MIC=18.8μM);##Gram-negative bacterium:Escherichia coli (MIC=75μM), Shigella dysenteriae (MIC=75μM), Klebsiella pneumoniae (MIC=37.5μM) [Ref.29075946] <1% hemolysis at 12.5μM, 3.2% hemolysis at 25μM against human red blood cells. stapled peptide Free Amidation tethers Lys6 and Arg10 L No cytotoxicity information found Not found 29075946 Arch Pharm Res. 2017 Dec;40(12):1414-1419. Luong HX, Kim DH, Lee BJ, Kim YW Antimicrobial activity and stability of stapled helices of polybia-MP1 DRAMP03721 ILGKIWEGIKSLF 13 IsCT1 Q8MMJ7 Belongs to the scorpion NDBP 5 family Not found Opisthacanthus madagascariensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Residue 6 is important for antibacterial activity, and hemolysis activity Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.28657596] Gram-positive bacterium:Staphylococcus aureus (MIC=50μg/mL);##Gram-negative bacterium: S. typhimurium (MIC=100μg/mL), Escherichia coli (MIC=50μg/mL) [Ref.28657596] 2% hemolysis at 10 μg/ml, 96% hemolysis at 50 μg/ml against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28657596 Antibiotics (Basel). 2017 Jun 28;6(3). pii: E13. de la Salud Bea R, Petraglia AF, Ascuitto MR, Buck QM. Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides DRAMP01377 FMPILSCSRFKRC 13 Odorranain-G1 (OdG1; Frogs, amphibians, animals) A6MBL7, A6MBL8 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Odorranain-G1 adopts 44.1% β-sheet structure in water solution. Function: Odorranain-G1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Has no hemolytic activity against red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=4.68 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=9.37 μg/ml), Bacillus subtilis (MIC=37.5 μg/ml).##Yeast: Candida albicans (MIC=1.10 μg/ml). [Ref:17272268] It has no hemolytic activity against rabbit red blood cells Cyclic Free Cyclization (Cys7 and Cys13) Disulfide bond between Cys7 and Cys13. L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP02995 QERGSIVIQGTKEGKSRPSLDIDYKQRVYDKNGMTGDAYGGLNIRPGQPSRQHAGFEFGKEYKNGFIKGQSEVQRGPGGRLSPYFGINGGFRF 93 Hymenoptaecin (Insects, animals) Q10416 Not found Not found Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli K514 (MIC=0.5-1 µM), E. coli K514 anaerobic, E. coli NCTC9001 (MIC=1-5 µM), Xanthomonas campestris (MIC=0.5-1 µM), Pseudomonas solanacearum (MIC>10 µM), Erwinia carotovora ssp.(MIC=1-5 µM);##Gram-positive bacteria: Micrococcus lysodeikticus (MIC=1-5 µM), Bacillus megaterium (MIC=0.5-1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8463238 J Biol Chem. 1993 Apr 5;268(10):7044-7054. Casteels P, Ampe C, Jacobs F, Tempst P. Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). DRAMP02996 GNNRPIYIPQPRPPHPRL 18 Apidaecin-2 (Apidaecin II; Insects, animals) Q06601, P11525, P11526, P11527 Belongs to the apidaecin family APID14 Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Agrobacterium tumefaciens (MIC=0.2 µg/ml), Erwinia salicis (MIC=0.02 µg/ml), Escherichia coli (MIC=0.2 µg/ml), Pseudomonas syringae (MIC=0.1 µg/ml), Rhizobium meliloti (MIC=0.02 µg/ml), Salmonella Newport (MIC=0.2 µg/ml), Salmonella typhimurium (MIC=0.1 µg/ml);##Gram-positive bacteria: Shigella flexneri (MIC=0.1 µg/ml), Corynebacterium insidiosum (MIC=100 µg/ml), Bacillus megaterium (MIC=100 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2676519 EMBO J. 1989 Aug;8(8):2387-2391. Casteels P, Ampe C, Jacobs F, Vaeck M, Tempst P. Apidaecins: antibacterial peptides from honeybees. DRAMP02441 VXLFPVXLFP 10 Gramicidin S No entry found Not found Not found Bacillus brevis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Beta sheet and beta-turn The peptide have the C2-symmetrical sequence [cyclo-(Val-Orn-Leu-D-Phe-Pro)2]. The two sequences Val-Orn-Leu form an antiparallel Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.29499484] Gram-positive bacterium:Staphylococcus aureus subsp.aureus CIP 4.83 ATCC 6538 (MIC=3.125μg/mL),Bacillus subtilis subsp. subtilis CIP 52.65 (MIC=3.125μg/ml),Enterococcus faecalis CIP 103015 (MIC=3.125μg/ml),Enterococcus faecalis CIP 103214 (MIC=3.125μg/ml),Bacillus cereus CIP 66.24 (MIC=6.25μg/ml),Streptococcus salivarius CIP 102503 (MIC=3.125μg/ml),Enterococcus faecium CIP 103014 (MIC=3.125μg/ml);##Gram-negative bacterium:Escherichia coli CIP 53.126 ATCC 8739 (MIC=12.5μg/ml),Pseudomonas aeruginosa CIP 82.118 ATCC 9027 (MIC>=100μg/ml) [Ref.29499484] It has 74% hemolysis at 50μg/ml, 83% hemolysis at 100μg/ml against human red blood cells. Cyclic No specific N-terminal No specific C-terminal The 'O' in sequence is Ornithine Mixed(D-Phe) No cytotoxicity information found Not found 29499484 Eur J Med Chem. 2018 Apr 10;149:122-128. Wan Y, Stanovych A, Gori D, Zirah S, Kouklovsky C, Alezra V. β,γ-diamino acids as building blocks for new analogues of Gramicidin S: Synthesis and biological activity DRAMP02998 GNNRPVYIPQPRPPHPRI 18 Apidaecin-1A (Apidaecin IA; Insects, animals) Q06602, P11525, P11526 Belongs to the apidaecin family APID73 Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Agrobacterium tumefaciens (MIC=0.2 µg/ml), Erwinia salicis (MIC=0.02 µg/ml), Escherichia coli (MIC=0.1 µg/ml), Pseudomonas syringae (MIC=0.2 µg/ml), Rhizobium meliloti (MIC=0.1 µg/ml), Salmonella Newport (MIC=0.2 µg/ml), Salmonella typhimurium (MIC=0.1 µg/ml), Shigella flexneri (MIC=0.1 µg/ml);##Gram-positive bacteria: Corynebacterium insidiosum (MIC=50 µg/ml), Bacillus megaterium (MIC=150 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2676519 EMBO J. 1989 Aug;8(8):2387-2391. Casteels P, Ampe C, Jacobs F, Vaeck M, Tempst P. Apidaecins: antibacterial peptides from honeybees. DRAMP02999 PFKISIHL 8 Jellein-1 (Jelleine-I; chain of Major royal jelly protein 1; Insects, animals) O18330, Q548D6 Belongs to the major royal jelly protein family MRJP1 Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Jellein-1 has antibacterial and antifungal activity. Tissue specificity: Found in the hypopharyngeal glands of the worker honeybee. Developmental stage: Produced in the cephalic glands of both the nurse bee and the forager bee. This bee milk protein changes to alpha-glucosidase in accordance with the age-dependent role change of the worker bee. Miscellaneous: Exhibits a growth factor-like action on primary-cultured rat hepatocytes by stimulating DNA synthesis and protecting cells from apoptosis induced by serum deprivation. Also activates mitogen-activated protein kinase, as well as protein kinase B, a key regulator of cell survival. Degraded proportionally to the period of storage, and is completely lost during storage at 40 degrees Celsius for 30 days. PTM: Histidine amide at H7." Gram-positive bacteria: Staphylococcus aureus ATCC 6535 (MIC=10 µg/ml), S. saprophyticus (MIC=15 µg/ml), Bacillus subtilis CCT 2471 (MIC=10 µg/ml).##Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=2.5 µg/ml), Enterobacter cloacae ACCT 23355 (MIC=10 µg/ml), Klebsiella pneumoniae ACCT 13883 (MIC=10 µg/ml), Pseudomonas aeruginosa ACCT 27853 (MIC=10 µg/ml).##Yeast: Candida albicans (MIC=2.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15203237##9395329##21516106 Peptides. 2004 Jun;25(6):919-928.##Eur J Biochem. 1997 Nov 1;249(3):797-802.##Nature. 2011 May 26;473(7348):478-483. Fontana R, Mendes MA, de Souza BM, Konno K, César LM, Malaspina O, Palma MS.##Ohashi K, Natori S, Kubo T.##Kamakura M. Jelleines: a family of antimicrobial peptides from the Royal Jelly of honeybees (Apis mellifera).##Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honeybee Apis mellifera L.##Royalactin induces queen differentiation in honeybees. DRAMP03000 TPFKISIHL 9 Jellein-2 (Jelleine-II; chain of Major royal jelly protein 1; Insects, animals) O18330, Q548D6 Belongs to the major royal jelly protein family MRJP1 Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Jellein-2 has antibacterial and antifungal activity. Jellein-2 is probably processed to yield jellein-1 and jellein-4. Tissue specificity: Found in the hypopharyngeal glands of the worker honeybee. Developmental stage: Produced in the cephalic glands of both the nurse bee and the forager bee. This bee milk protein changes to alpha-glucosidase in accordance with the age-dependent role change of the worker bee. Miscellaneous: Exhibits a growth factor-like action on primary-cultured rat hepatocytes by stimulating DNA synthesis and protecting cells from apoptosis induced by serum deprivation. Also activates mitogen-activated protein kinase, as well as protein kinase B, a key regulator of cell survival. Degraded proportionally to the period of storage, and is completely lost during storage at 40 degrees Celsius for 30 days. PTM: Leucine amide at L9." Gram-positive bacteria: Staphylococcus aureus ATCC 6535 (MIC=15 µg/ml), S. saprophyticus (MIC=10 µg/ml), Bacillus subtilis CCT 2471 (MIC=30 µg/ml);##Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=15 µg/ml), Enterobacter cloacae ACCT 23355 (MIC=15 µg/ml), Klebsiella pneumoniae ACCT 13883 (MIC=15 µg/ml), Pseudomonas aeruginosa ACCT 27853 (MIC=15 µg/ml).##Yeast: Candida albicans (MIC=2.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15203237##9395329##21516106 Peptides. 2004 Jun;25(6):919-928.##Eur J Biochem. 1997 Nov 1;249(3):797-802.##Nature. 2011 May 26;473(7348):478-483. Fontana R, Mendes MA, de Souza BM, Konno K, César LM, Malaspina O, Palma MS.##Ohashi K, Natori S, Kubo T.##Kamakura M. Jelleines: a family of antimicrobial peptides from the Royal Jelly of honeybees (Apis mellifera).##Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honeybee Apis mellifera L.##Royalactin induces queen differentiation in honeybees. DRAMP03001 EPFKISIHL 9 Jellein-3 (Jelleine-III; Insects, animals) P84759 Not found MRJP1 Apis mellifera (Honeybee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Jellein-3 has antibacterial and antifungal activity. Tissue specificity: Found in the hypopharyngeal glands of the worker honeybee. PTM: Leucine amide at L9." Gram-positive bacteria: Staphylococcus aureus ATCC 6535 (MIC=30 µg/ml), S. saprophyticus (MIC=30 µg/ml);##Gram-negative bacteria: Escherichia coli CCT1371 (MIC=15 µg/ml), Enterobacter cloacae ATCC 23355, Klebsiella pneumoniae ATCC 13883, Pseudomonas aeruginosa ATCC 27853 (MIC=30 µg/ml).##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15203237 Peptides. 2004 Jun;25(6):919-928. ntana R, Mendes MA, de Souza BM, Konno K, César LM, Malaspina O, Palma MS. Jelleines: a family of antimicrobial peptides from the Royal Jelly of honeybees (Apis mellifera). DRAMP03057 GSKKPVPIIYCNRRTGKCQRM 21 Thanatin(insects, arthropods, invertebrates, animals) P55788 Not found Not found Podisus maculiventris Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand Contain C-terminally a loop of 6 residues, delineated by an intramolecular disulfide bridge. This loop carries a strong positive charge in both molecules and contains a central threonine residue, which separates two subgroups of electropositivity. 8TFV Function: Insect defense peptide with a broad spectrum of activity against Gram-positive and Gram-negative bacteria and fungi. No activity against S.aureus. Stops respiration in bacteria but does not permeabilize their inner membranes. Has no detectable hemolytic activity. [Ref.8577744] Gram-positive bacteria: Aerococcus viridans (MIC=0.6-1.2 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Bacillus megaterium (MIC=2.5-5 µM), Bacillus subtilis (MIC=2.5-5 µM), Pediococcus acidilactici (MIC=20-40 µM);##Gram-negative bacteria: Escherichia coli D22 (MIC=0.3-0.6 µM), Escherichia coli D31 (MIC=0.3-0.6 µM), Escherichia coli 1106 (MIC=0.6-1.2 µM), Salmonella typhimurium (MIC=0.6-1.2 µM), Klebsiella pneumoniae (MIC=0.6-1.2 µM), Enterobacter cloacae (MIC=1.2-2.5 µM), Erwinia carotovora (MIC=10-20 µM), Pseudomonas aeruginosa (MIC=20-40 µM);##Fungi: Neurospora crassa (MIC=0.6-1.2 µM), Botrytis cinerea (MIC=1.2-2.5 µM), Nectria haematococca (MIC=1.2-2.5 µM), Trichoderma viride (MIC=1.2-2.5 µM), Alternaria brassicicola (MIC=2.5-5 µM), Fusarium culmorum (MIC=2.5-5 µM), Ascochyta pisi (MIC=5-10µM), Fusarium oxysporum (MIC=10-20 µM). [Ref.8577744] It exhibits no hemolytic activity at 40 µM against porcine erythrocytes. Cyclic Free Free Disulfide bond between Cys11 and Cys18. L No cytotoxicity information found Not found 8577744##9760181 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225.##Eur J Biochem. 1998 Sep 1;256(2):404-410. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA.##Mandard N, Sodano P, Labbe H, Bonmatin JM, Bulet P, Hetru C, Ptak M, Vovelle F. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.##Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data. DRAMP03003 GFLSILKKVLPKVMAHMK 18 Melectin (MEP; Insects, animals) P86170 Not found Not found Melecta albifrons (Cuckoo bee) (Melecta punctata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria as well as Gram-negative bacteria. Stimulates degranulation from rat peritoneal mast cells with an EC50 of 19.4 µM. Has weak hemolytic activity towards rat erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." [Ref.18942691]Gram-positive bacteria: Bacillus subtilis (MIC=0.8 µM), Staphylococcus aureus (MIC=6.8 µM);##Gram-negative bacteria: Escherichia coli (MIC=2.0 µM), Pseudomonas aeruginosa (MIC=18.5 µM). [Ref.18942691]LC50>100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18942691 Chembiochem. 2008 Nov 24;9(17):2815-2821. Cerovský V, Hovorka O, Cvacka J, Voburka Z, Bednárová L, Borovicková L, Slaninová J, Fucík V. Melectin: a novel antimicrobial peptide from the venom of the cleptoparasitic bee Melecta albifrons. DRAMP03007 GFLSALKKYLPIVLKHV 17 Osmin (Insects, animals) P0CD70 Not found Not found Osmia rufa (Red mason bee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (CD) In absence of TFE, the spectrum shows a random coil type structure. When increasing the concentration of TFE from 0 to 20%, a transition into an α-helix structure is observed. "Function: Synthetic peptide exhibits hemolytic activity to human erythrocytes and inhibits bacterial and fungal growth at micromolar concentrations. A synthetic peptide with a free C-terminus shows weaker hemolytic (5.0 HU/mg), antibacterial and antifungal activities. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." [Ref.19109988]Gram-positive bacterium: Micrococcus luteus (MIC=1.56-0.78 µM);##Gram-negative bacterium: Escherichia coli SBS363 (MIC=3.125-1.56 µM);##fungi: Fusarium oxysporum (MIC=0.78-0.39 µM). [Ref.19109988]5.0 HU/mg hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19109988 Toxicon. 2010 Jan;55(1):20-27. öcklin R, Favreau P, Thai R, Pflugfelder J, Bulet P, Mebs D. Structural identification by mass spectrometry of a novel antimicrobial peptide from the venom of the solitary bee Osmia rufa (hymenoptera: megachilidae). DRAMP03019 INWLKLGKKILGAL 14 Mastoparan PDD-B No entry found Belongs to the mastoparan family Not found Polistes dorsalis dorsolis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. PDD-B has hemolytic activity. [Ref.18375018]Gram-positive bacterium: Bacillus subtilis (MIC=70 µM);##Gram-negative bacterium: Escherichia coli (MIC=15.5 µM). [Ref.18375018]IC50=45 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP03020 INWKKIFEKVKNLV 14 Mastoparan PDD-A No entry found Belongs to the mastoparan family Not found Polistes dorsalis dorsolis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. PDD-A shows little hemolytic activity. [Ref.18375018]Gram-positive bacterium: Bacillus subtilis (MIC=11.8 µM);##Gram-negative bacterium: Escherichia coli (MIC=7.5 µM). [Ref.18375018]IC50>100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP03021 INWKKIASIGKEVLKAL 17 Mastoparan PMM No entry found Belongs to the mastoparan family Not found Polistes major major Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. Shows hemolytic activity. [Ref.18375018]Gram-positive bacterium: Bacillus subtilis (MIC=7.3 µM);##Gram-negative bacterium: Escherichia coli (MIC=25.8 µM). [Ref.18375018]IC50=80 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP03022 INWLKLGKKMMSAL 14 Mastoparan MP No entry found Belongs to the mastoparan family Not found Mischocyttarus phthisicus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antibacterial activity. Has hemolytic activity. [Ref.18375018]Gram-positive bacterium: Bacillus subtilis (MIC=9 µM);##Gram-negative bacterium: Escherichia coli (MIC=65 µM). [Ref.18375018]IC50=100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP01739 LLPIVGNLLKSLL 13 Temporin-B (Frogs, amphibians, animals) P79874 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 6GIL resolved by NMR. "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has hemolytic activity. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." [Ref.9022710] Gram-positive bacteria: Bacillus megaterium BM11 (LC=2.8 µM), Staphylococcus aureus Cowanl (LC=6.0 µM), Streptococcus pyogenes betahemolytic group A (LC=7.0 µM);##Gram-negative bacteria: Escherichia coli D21(LC=21.0 µM), Escherichia coli D21e7 (LC=13.2 µM), Escherichia coli D21f1 (LC=10.0 µM), Escherichia coli D21f2 (LC=3.3 µM), Escherichia coli D22 (LC=11.2 µM),Yersinia pseudotuberculosis (LC=7.0 µM), Pseudomonas aeruginosa ATCC15692 (LC>360 µM);##Yeast: Candida albicans (LC=4.0 µM).(LC: Lethal concentration).##[Ref.28443279] Gram-positive bacterium: S.aureus ATCC 33591 (MIC=12μM), Staphylococcus epidermidis (MIC=6μM);##Gram-negative bacterium: Klebsiella pneumoniae ATCC BAA-1706 (MIC=48μM), Pseudomonas aeruginosa ATCC 27853 (MIC=48μM) [Ref.9022710] LC>120 µM against Human red blood cells. (LC: Lethal concentration)##[Ref.28443279] 1% hemolysis at 96μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710##28443279 Eur J Biochem. 1996 Dec 15;242(3):788-792.##Front Chem. 2017 Apr 11;5:24. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D.##Grassi L, Maisetta G, Maccari G, Esin S, Batoni G. Temporins, antimicrobial peptides from the European red frog Rana temporaria.##Analogs of the Frog-skin Antimicrobial Peptide Temporin 1Tb Exhibit a Wider Spectrum of Activity and a Stronger Antibiofilm Potential as Compared to the Parental Peptide DRAMP03033 INWKGIAAMAKKLL 14 Mastoparan-like peptide 12a (Insects, animals) P0C1M4 Not found Not found Vespa magnifica (Hornet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide. Has little hemolytic activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14). " [Ref.17046111]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=7.5 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.7 µg/ml);##Fungi: Candida albicans ATCC 2002 (MIC=3.7 µg/ml). [Ref.16330062]Little hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16330062##17046111 Toxicon. 2006 Feb;47(2):249-253.##Peptides. 2006 Dec;27(12):3053-3057. Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R.##Xu X, Yang H, Yu H, Li J, Lai R. Two families of antimicrobial peptides from wasp (Vespa magnifica) venom.##The mastoparanogen from wasp. DRAMP03034 INWKGIAAMKKLL 13 Mastoparan-like peptide 12b (Insects, animals) P0C1M5 Not found Not found Vespa magnifica (Hornet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide. Has little hemolytic activity. Shows antimicrobial activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L13)." [Ref.16330062]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.7 µg/ml);##Fungi: Candida albicans ATCC 2002 (MIC=7.5 µg/ml). [Ref.16330062]Little hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16330062 Toxicon. 2006 Feb;47(2):249-53. Epub 2005 Dec 5. Peptides. 2006 Dec;27(12):3053-7. Epub 2006 Oct 13. Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R.Xu X, Yang H, Yu H, Li J, Lai R. Two families of antimicrobial peptides from wasp (Vespa magnifica) venomThe mastoparanogen from wasp. DRAMP03035 INLKAIAALAKKLLG 15 Mastoparan-like peptide 12c (Insects, animals) A0SPI0 Not found Not found Vespa magnifica (Hornet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows mast cell degranulation and antimicrobial activities. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14). " Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.0 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.0 µg/ml).##Fungi: Candida albicans ATCC 2002 (MIC=12.0 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17046111 Peptides. 2006 Dec;27(12):3053-3057. Xu X, Yang H, Yu H, Li J, Lai R. The mastoparanogen from wasp. DRAMP03036 INLKAIAAMAKKLL 14 Mastoparan-like peptide 12d (Insects, animals) P0C5G7 Not found Not found Vespa magnifica (Hornet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows mast cell degranulation and antimicrobial activities. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14). " Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.0 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=1.5 µg/ml).##Fungi: Candida albicans ATCC 2002 (MIC=12.0 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17046111 Peptides. 2006 Dec;27(12):3053-3057. Xu X, Yang H, Yu H, Li J, Lai R. The mastoparanogen from wasp. DRAMP03037 LNLKGIFKKVASLLT 15 Eumenitin (Er-12; Insects, animals) P0C931 Not found Not found Eumenes rubronotatus (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Cationic linear alpha-helical antimicrobial peptide that binds preferentially to charged lipid membranes as compared with zwitterionic ones. It exhibits inhibitory activity against both Gram-positive and Gram-negative bacteria, and moderately stimulates degranulation from the rat peritoneal mast cells. Does not show hemolytic activity. May play a role in preventing infection by microorganisms during prey consumption by their larvae. Tissue specificity: Expressed by the venom gland." [Ref.16762455]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC>60 µM), Staphylococcus aureus ATCC 25923 (MIC=6 µM), Staphylococcus saprophytius (CS) (MIC=6 µM), Staphylococcus epidermius (CS) (MIC>60 µM), Bacillus subtilis CCT 2471 (MIC=60 µM), Bacillus thuringiensis (WT) (MIC>60 µM);##Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=6 µM), Escherichia coli ATCC 25922 (MIC=6 µM), Escherichia cloacae ATCC 23355 (MIC>60 µM), Proteus mirabilis (CS) (MIC>60 µM), Pseudomonas aeruginosa ATCC 15442 (MIC=30 µM). [Ref.16762455]Non-hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 16762455##18206199 Peptides. 2006 Nov;27(11):2624-2631.##Toxicon. 2008 Apr;51(5):736-745. Konno K, Hisada M, Naoki H, Itagaki Y, Fontana R, Rangel M, Oliveira JS, Cabrera MP, Neto JR, Hide I, Nakata Y, Yasuhara T, Nakajima T.##Arcisio-Miranda M, dos Santos Cabrera MP, Konno K, Rangel M, Procopio J. Eumenitin, a novel antimicrobial peptide from the venom of the solitary eumenine wasp Eumenes rubronotatus.##Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity. DRAMP03038 LNLKGLIKKVASLLN 15 Eumenitin-R (Insects, animals) P0CJ36 Not found Not found Eumenes rubrofemoratus (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide by forming pore in membrane. Has antibacterial activities against both Gram-positive and Gram-negative strains. Has more potent activities against the yeast C.albicans. Shows moderate mast cell degranulation and leishmanicidal activities. Has a very low hemolytic activity against mice erythrocytes. Tissue specificity: Expressed by the venom sac." [Ref.21549739]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=60 µM), Staphylococcus epidermidis (clinical sample) (MIC=30 µM), Micrococcus luteus ATCC 10240 (MIC=15 µM), Streptococcus pyogenes (clinical sample) (MIC=15 µM), Bacillus subtilis ATCC 6633 (MIC=7.5 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µM), Proteus mirabilis (clinical sample) (MIC=60 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=30 µM), Stenotrophomonas maltophilia ATCC 13637 (MIC=15 µM);##Fungi: Candida albicans ATCC 90112 (MIC<7.5 µM). [Ref.21549739]EC50=530.3 μM against mice erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 21549739 Toxicon. 2011 Jun;57(7-8):1081-1092. Rangel M, Cabrera MP, Kazuma K, Ando K, Wang X, Kato M, Nihei K, Hirata IY, Cross TJ, Garcia AN, Faquim-Mauro EL, Franzolin MR, Fuchino H, Mori-Yasumoto K, Sekita S, Kadowaki M, Satake M, Konno K. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. DRAMP03039 LNLKGLFKKVASLLT 15 Eumenitin-F (Insects, animals) P0CJ37 Not found Not found Eumenes fraterculus (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide by forming pore in membrane. Has antibacterial activities against both Gram-positive and Gram-negative strains. Has more potent activities against the yeast C.albicans. Shows moderate mast cell degranulation and leishmanicidal activities. Has a very low hemolytic activity against mice erythrocytes. Tissue specificity: Expressed by the venom sac." [Ref.21549739]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>60 µM), Staphylococcus epidermidis (clinical sample) (MIC=30 µM), Micrococcus luteus ATCC 10240 (MIC=30 µM), Streptococcus pyogenes (clinical sample) (MIC=30 µM), Bacillus subtilis ATCC 6633 (MIC=30 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µM), Proteus mirabilis (clinical sample) (MIC>60 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=30 µM), Stenotrophomonas maltophilia ATCC 13637 (MIC=15 µM);##Fungi: Candida albicans ATCC 90112 (MIC=7.5 µM). [Ref.21549739]EC50=353.4 μM against mice erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 21549739 Toxicon. 2011 Jun;57(7-8):1081-1092. Rangel M, Cabrera MP, Kazuma K, Ando K, Wang X, Kato M, Nihei K, Hirata IY, Cross TJ, Garcia AN, Faquim-Mauro EL, Franzolin MR, Fuchino H, Mori-Yasumoto K, Sekita S, Kadowaki M, Satake M, Konno K. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. DRAMP03040 FDVMGIIKKIAGAL 14 Eumenine mastoparan-EF (EMP-EF; Insects, animals) P0CJ39 Not found Not found Eumenes fraterculus (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide by forming pore in membrane. Has antibacterial activities against both Gram-positive and Gram-negative strains. Has more potent activities against the yeast C.albicans. Shows moderate mast cell degranulation and leishmanicidal activities. Has a very low hemolytic activity against mice erythrocytes. Tissue specificity: Expressed by the venom sac. PTM: C-terminal amidation (Leucine amide: L14)." [Ref.21549739]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=30 µM), Staphylococcus epidermidis (clinical sample) (MIC=30 µM), Micrococcus luteus ATCC 10240 (MIC=30 µM), Streptococcus pyogenes (clinical sample) (MIC>30 µM), Bacillus subtilis ATCC 6633 (MIC=30 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µM), Proteus mirabilis (clinical sample) (MIC=60 µM), Pseudomonas aeruginosa ATCC 27853 (MIC>30 µM), Stenotrophomonas maltophilia ATCC 13637 (MIC>30 µM);##Fungi: Candida albicans ATCC 90112 (MIC=7.5 µM). [Ref.21549739]EC50=181.1 μM against mice erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 21549739 Toxicon. 2011 Jun;57(7-8):1081-1092. Rangel M, Cabrera MP, Kazuma K, Ando K, Wang X, Kato M, Nihei K, Hirata IY, Cross TJ, Garcia AN, Faquim-Mauro EL, Franzolin MR, Fuchino H, Mori-Yasumoto K, Sekita S, Kadowaki M, Satake M, Konno K. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. DRAMP03041 FDIMGLIKKVAGAL 14 Eumenine mastoparan-ER (EMP-ER; Insects, animals) P0CJ38 Not found Not found Eumenes rubrofemoratus (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide by forming pore in membrane. Has antibacterial activities against both Gram-positive and Gram-negative strains. Has more potent activities against the yeast C.albicans. Shows moderate mast cell degranulation and leishmanicidal activities. Has a very low hemolytic activity against mice erythrocytes. Tissue specificity: Expressed by the venom sac. PTM: C-terminal amidation (Leucine amide: L14)." [Ref.21549739]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=30 µM), Staphylococcus epidermidis (clinical sample) (MIC=30 µM), Micrococcus luteus ATCC 10240 (MIC>30 µM), Streptococcus pyogenes (clinical sample) (MIC>30 µM), Bacillus subtilis ATCC 6633 (MIC=30 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=30 µM), Proteus mirabilis (clinical sample) (MIC=60 µM), Pseudomonas aeruginosa ATCC 27853 (MIC>30 µM), Stenotrophomonas maltophilia ATCC 13637 (MIC>30 µM);##Fungi: Candida albicans ATCC 90112 (MIC=7.5 µM). [Ref.21549739]EC50=200 μM against mice erythrocytes Linear Free Amidation Free L Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 21549739 Toxicon. 2011 Jun;57(7-8):1081-1092. Rangel M, Cabrera MP, Kazuma K, Ando K, Wang X, Kato M, Nihei K, Hirata IY, Cross TJ, Garcia AN, Faquim-Mauro EL, Franzolin MR, Fuchino H, Mori-Yasumoto K, Sekita S, Kadowaki M, Satake M, Konno K. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. DRAMP03042 INLLKIAKGIIKSL 14 Eumenine mastoparan-AF (EMP-AF; Af-113; Insects, animals) P0C022 Not found Not found Anterhynchium flavomarginatum micado (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Mast cell degranulating peptide. Also permeates anionic liposomes. Has hemolytic activity. Has an amphiphilic alpha-helix conformation. Shows broad-spectrum antimicrobial activity. Blocks the lobster neuromuscular transmission. Induces the depolarization of the muscle membrane. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)." [Ref.15317499]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC=5 µg/ml), S. saprophyticus CS (MIC=5 µg/ml), S. epidermidis CS (MIC=5 µg/ml), Bacillus subtilis CCT 2471 (MIC=40 µg/ml);##Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=20 µg/ml), Escherichia coli ATCC 25922 (MIC=50 µg/ml), Pseudomonas aeruginosa ATCC 15442 (MIC=20 µg/ml). [Ref.10775751]100% hemolytic activity against human erythrocytes at 10^-4 M Linear Free Amidation Free L Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 15317499##11006592##10775751 J Pept Res. 2004 Sep;64(3):95-103.##Rapid Commun Mass Spectrom. 2000;14(19):1828-1834.##Toxicon. 2000 Nov;38(11):1505-1015. dos Santos Cabrera M.P, de Souza B.M, Fontana R, Konno K, Palma M.S, de Azevedo W.F. Jr, Neto J.R.##Hisada M, Konno K, Itagaki Y, Naoki H, Nakajima T.##Konno K, Hisada M, Naoki H, Itagaki Y, Kawai N, Miwa A, Yasuhara T, Morimoto Y, Nakata Y. Conformation and lytic activity of eumenine mastoparan: a new antimicrobial peptide from wasp venom.##Advantages of using nested collision induced dissociation/post-source decay with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: sequencing of novel peptides from wasp venom.##Structure and biological activities of eumenine mastoparan-AF (EMP-AF), a new mast cell degranulating peptide in the venom of the solitary wasp (Anterhynchium flavomarginatum micado). DRAMP03043 INWLKLGKAIIDAL 14 Agelaia-mastoparan (Agelaia-MP; Insects, animals) P69436 Not found Not found Agelaia pallipes pallipes (Neotropical social wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Hemolytic mast cell degranulator, presenting no antimicrobial action and no chemotaxis for polymorphonucleated leukocytes (PMNL). Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)." [Ref.15225564]Gram-negative bacteria: Escherichia coli (MIC=382 µg/ml), Pseudomonas aeruginosa (MIC=257 µg/ml);##Gram-positive bacteria: Bacillus subtilis (MIC=237 µg/ml), Staphylococcus aureus (MIC=191 µg/ml). [Ref.15225564]70% hemolytic activity at 156 ng/ml against rat erythrocytes Linear Free Amidation Free L Not included yet Not found 15225564##15052574 Toxicon. 2004 Jul;44(1):67-74.##Rapid Commun Mass Spectrom. 2004;18(6):636-642. Mendes MA, de Souza BM, Marques MR, Palma MS.##Mendes MA, Monson de Souza B, Delazari dos Santos L, Palma MS. Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes.##Structural characterization of novel chemotactic and mastoparan peptides from the venom of the social wasp Agelaiapallipes pallipes by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. DRAMP03044 ILGTILGLLKGL 12 Protonectin (Agelaia-chemotactic peptide, Agelaia-CP; Insects, animals) P69437 Not found Not found Agelaia pallipes pallipes (Neotropical social wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Mast cell degranulator that induces a potent chemotaxis in polymorphonucleated leukocyte (PMNL) cells. Shows potent antimicrobial action against both Gram-positive and Gram-negative bacteria. Shows no hemolytic activity. [Ref.15225564]Gram-negative bacteria: Escherichia coli (MIC=25 µg/ml), Pseudomonas aeruginosa (MIC=1.7 µg/ml);##Gram-positive bacteria: Bacillus subtilis (MIC=3.1 µg/ml), Staphylococcus aureus (MIC=12.5 µg/ml). [Ref.15052574]Non-hemolytic activity against rat red blood cell Linear Free Amidation Free L Not included yet Not found 15225564##15052574 Toxicon. 2004 Jul;44(1):67-74.##Rapid Commun Mass Spectrom. 2004;18(6):636-642. Mendes MA, de Souza BM, Marques MR, Palma MS.##Mendes MA, Monson de Souza B, Delazari dos Santos L, Palma MS. Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes.##Structural characterization of novel chemotactic and mastoparan peptides from the venom of the social wasp Agelaiapallipes pallipes by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. DRAMP03045 VTCELLMFGGVVGDSACAANCLSMGKAGGSCNGGLCDCRKTTFKELWDKRFG 52 Defensin-NV (Insects, animals) No entry found Not found Not found Nasonia vitripennis (Ectoparasitic wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Bridge Not found Function: Defensin-NV had little hemolytic activity to rabbit red blood cells and has antimicrobial activity against Gram-positive, Gram-negative bacteria, and Fungi. [Ref.20362606]Gram-positive bacteria: Staphylococcus aureus (MIC=0.93 µM), Bacillus cereus (MIC=0.93 µM), B. dysenteriae (MIC=0.46 µM);##Gram-negative bacteria: Escherichia coli (MIC=1.86 µM), Pseudomonas aeruginosa (MIC=9.3 µM).##Yeast: Candida albicans (MIC=1.86 µM). [Ref.20362606]5% hemolytic activity at 200 μg/ml against rabbit red blood cells Cyclic Free Free There are three disulfide bonds(By similar). Not included yet Not included yet Not found 20362606 Toxicon. 2010 Aug 1;56(1):101-106. Ye J, Zhao H, Wang H, Bian J, Zheng R. A defensin antimicrobial peptide from the venoms of Nasonia vitripennis. DRAMP03046 ILGIITSLLKSL 12 Orancis-protonectin (chain of Venom peptide 2-long; Venom peptide 2, OdVP2; Insects, animals) P86147, C7DT08 Belongs to the MCD family (Protonectin subfamily) VP2 Orancistrocerus drewseni (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Has potent hemolytic activity against ovine erythrocytes at micromolar concentrations. Also exhibits strong antimicrobial activity against fungi. Venom peptide 2-long has substantially lower antimicrobial activity against C. albicans and bacteria than Orancis-protonectin but has equivalent activity against Botrytis cinerea. [Ref.19857508]Gram-positive bacteria: Staphylococcus aureus (MIC=25 μg/ml);##Fungi: Candida albicans (MIC<100 µg/ml), Botrytis cinerea (MIC=0.5 µg/ml). [Ref.18695936]84% hemolytic activity at 50 μM against sheep blood cells. Linear Free Amidation Free L Not included yet Not found 19857508##18695936 Toxicon. 2010 Apr 1;55(4):711-718.##Amino Acids. 2009 Jul;37(2):389-394. Baek JH, Lee SH.##Murata K, Shinada T, Ohfune Y, Hisada M, Yasuda A, Naoki H, Nakajima T. Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae).##Novel mastoparan and protonectin analogs isolated from a solitary wasp, Orancistrocerus drewseni drewseni. DRAMP03047 EPILGIITSLLKSL 14 Venom peptide 2-long (OdVP2L; analog of OdVP2; Insects, animals) P86147, C7DT08 Belongs to the MCD family (Protonectin subfamily) VP2 Orancistrocerus drewseni (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has potent hemolytic activity against ovine erythrocytes at micromolar concentrations. Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P86147]Fungi: Botrytis cinerea (MIC=0.5 µg/ml), Candida albicans (MIC=100 µg/ml);##Gram-positive bacterium: S. aureus (MIC=25 µg/ml);##Gram-negative bacterium: Escherichia coli. [Swiss_Prot Entry P86147]has potent hemolytic activity against ovine erythrocytes at micromolar concentrations Linear Free Amidation Free L Not included yet Not found 19857508##18695936 Toxicon. 2010 Apr 1;55(4):711-718.##Amino Acids. 2009 Jul;37(2):389-394. Baek JH, Lee SH.##Murata K, Shinada T, Ohfune Y, Hisada M, Yasuda A, Naoki H, Nakajima T. Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae).##Novel mastoparan and protonectin analogs isolated from a solitary wasp, Orancistrocerus drewseni drewseni. DRAMP03050 INWKKIAEVGGKILSSL 17 Dominulin-A (Insects, animals) P0C1M6 Belongs to the MCD family (Mastoparan subfamily) Not found Polistes dominulus (European paper wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antimicrobial activity. Gram-positive bacterium: Bacillus subtilis ATCC 6633 (MIC=2 µg/ml);##Gram-negative bacterium: Escherichia coli JM109 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16446098 J Am Soc Mass Spectrom. 2006 Mar;17(3):376-383. Turillazzi S, Mastrobuoni G, Dani FR, Moneti G, Pieraccini G, la Marca G, Bartolucci G, Perito B, Lambardi D, Cavallini V, Dapporto L. Dominulin A and B: two new antibacterial peptides identified on the cuticle and in the venom of the social paper wasp Polistes dominulus using MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap. DRAMP03051 INWKKIAEIGKQVLSAL 17 Dominulin-B (Insects, animals) P0C1M7 Belongs to the MCD family (Mastoparan subfamily) Not found Polistes dominulus (European paper wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antimicrobial activity. Gram-positive bacterium: Bacillus subtilis ATCC 6633 (MIC=2 µg/ml);##Gram-negative bacterium: Escherichia coli JM109 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16446098 J Am Soc Mass Spectrom. 2006 Mar;17(3):376-383. Turillazzi S, Mastrobuoni G, Dani FR, Moneti G, Pieraccini G, la Marca G, Bartolucci G, Perito B, Lambardi D, Cavallini V, Dapporto L. Dominulin A and B: two new antibacterial peptides identified on the cuticle and in the venom of the social paper wasp Polistes dominulus using MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap. DRAMP03052 GAARKSIRLHRLYTWKATIYTR 22 PP13 (Insects, animals) No entry found Not found Not found Pteromalus puparum (wasp) Antimicrobial, Antibacterial, Anti-Gram+ Not found Alpha helix (CD) Not found Function: These peptides have net positive charges and are active against both Gram-negative and -positive bacteria, but are not active against fungi tested. Gram-positive bacteria: Staphylococcus aureus CVCC1882 (MIC=23.3 µM), Sarcina lutea CVCC1600 (MIC=8 µM), Bacillus pumilus CVCC709 (MIC=9 µM), Bacillus subtilis CVCC717 (MIC=13.3 µM).##Gram-positive bacterium: Escherichia coli CVCC1570 (MIC=16.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Cell membrane 19950104 J Pept Sci. 2010 Jan;16(1):58-64. Shen X, Ye G, Cheng X, Yu C, Yao H, Hu C. Novel antimicrobial peptides identified from an endoparasitic wasp cDNA library. DRAMP03053 GSCSCSGTISPYGLRTCRATKTKPSHPTTKETHPQTLPT 39 PP102 (Insects, animals) No entry found Not found Not found Pteromalus puparum (wasp) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: These peptides have net positive charges and are active against both Gram-negative and -positive bacteria, but are not active against fungi tested. Gram-positive bacteria: Staphylococcus aureus CVCC1882 (MIC=13.3 µM), Sarcina lutea CVCC1600 (MIC=63.3 µM), Bacillus pumilus CVCC709 (MIC=23.3 µM), Bacillus subtilis CVCC717 (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Cell membrane 19950104 J Pept Sci. 2010 Jan;16(1):58-64. Shen X, Ye G, Cheng X, Yu C, Yao H, Hu C. Novel antimicrobial peptides identified from an endoparasitic wasp cDNA library. DRAMP03054 GKWGWIYITILFADVGGFKSSRHPEERRVQERRFKRITRGPD 42 PP113 (Insects, animals) No entry found Not found Not found Pteromalus puparum (wasp) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: These peptides have net positive charges and are active against both Gram-negative and -positive bacteria, but are not active against fungi tested. Salt-dependency studies revealed that the biocidal activity of these peptides against E. coli decreased with increasing concentration of NaCl. Gram-positive bacteria: Staphylococcus aureus CVCC1882 (MIC=13 µM), Sarcina lutea CVCC1600 (MIC=16.7 µM), Bacillus pumilus CVCC709 (MIC=23.3 µM), Bacillus subtilis CVCC717 (MIC=23.3 µM).##Gram-positive bacterium: Escherichia coli CVCC1570 (MIC=16.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Cell membrane 19950104 J Pept Sci. 2010 Jan;16(1):58-64. Shen X, Ye G, Cheng X, Yu C, Yao H, Hu C. Novel antimicrobial peptides identified from an endoparasitic wasp cDNA library. DRAMP03055 YVPPVQKPHPNGPKFPTFP 19 PP30 (Pro-rich; abaecin-like; Insects, animals) No entry found Not found Not found Pteromalus puparum (wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=23.3±2.1 µM);##Gram-positive bacteria: Bacillus subtilis (MIC=16.7±2.1 µM), Staphylococcus aureus (MIC=133.3±11.6 µM), Sarcina lutea (MIC=13.3±1.2 µM), Bacillus pumilu (MIC=13.3±2.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 20466006 J Invertebr Pathol. 2010 Sep;105(1):24-29. Shen X, Ye G, Cheng X, Yu C, Altosaar I, Hu C. Characterization of an abaecin-like antimicrobial peptide identified from a Pteromaluspuparum cDNA clone. DRAMP03056 SLLSLIRKLIT 11 Decoralin (Insects, animals) P85870 Not found Not found Oreumenes decoratus (Potter wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide. At high concentrations exhibits activity in stimulating degranulation from rat peritoneal mast cells. Inhibits the growth of L.major promastigotes in vitro with an IC50 of 72 µM. Has hemolytic activity towards human and mouse erythrocytes. Tissue specificity: Expressed by the venom gland." [Ref.17981364]Gram-positive bacteria: Staphylococcus aureus CCT 6538 (MIC=40 µM), S. saprophyticus (MIC=40 µM), Bacillus subtilis CCT 2471 (MIC=40 µM), B. thuringiensis (MIC=40 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=80 µM), Escherichia coli CCT 1371 (MIC=160 µM), Klebsiella pneumoniae ATCC 13883 (MIC=80 µM), A. faecalis ATCC 8750 (MIC=40 µM);##Fungi: Candida albicans (MIC=40 µM), L. major promastigotes (IC50=72 µM). [Ref.17981364]EC50=1 mM against mouse erythrocytes Linear Free Amidation Free L Not included yet Cell membrane 17981364 Peptides. 2007 Dec;28(12):2320-2327. Konno K, Rangel M, Oliveira JS, Dos Santos Cabrera MP, Fontana R, Hirata IY, Hide I, Nakata Y, Mori K, Kawano M, Fuchino H, Sekita S, Neto JR. Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus. DRAMP18493 FIHHIIGGLISVGKHIHGLIHGH 23 TP3 L0CMD2 Piscidin TP3 Oreochromis niloticus (Nile tilapia) (Tilapia nilotica) Antibacterial, wound healing, immunomodulatory, Anti-Gram+, Antimicrobial Protein level Alpha helix Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity. Has hemolytic activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=256 μg/ml; MBC=256 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=256 μg/ml; MBC>256 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 2% hemolysis at 3.13 μg/ml, 5% hemolysis at 6.25 μg/ml, 10% hemolysis at 12.50 μg/ml, 55% hemolysis at 25.00 μg/ml, 85% hemolysis at 50.00 μg/ml, 100% hemolysis at 100.00 μg/ml against mouse red blood cell Linear Free Free Free L Not included yet Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP03819 RRWWRF 6 Cyclic hexapeptide CYC-(RRWWRF) No entry found Not found Not found Synthetic construct Antimicrobial, Anti-Gram+, Anti-Gram- Synthetic Non helix or strand structure (Turn) Not found 1QVK,1QVL Function: Antibacterial activity against Escherichia coli and Bacillus subtilis. Has hemolytic activity. [Ref.16075425] Gram-negative bacterium: Escherichia coli(MIC=6.3 μM);##Gram-positive bacterium: Bacillus subtilis(MIC=3.1 μM) [Ref.16075425] It has 24% hemolysis at 100 μM against erythrocytes. Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 16075425##7883644 Chembiochem. 2005 Sep;6(9):1654-1662.##J Appl Bacteriol. 1995 Jan;78(1):39-46. Appelt C, Wessolowski A, S?derh??ll JA, Dathe M, Schmieder P.##Blondelle SE, Takahashi E, Dinh KT, Houghten RA. Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles.##The antimicrobial activity of hexapeptides derived from synthetic combinatorial libraries. DRAMP03820 RRYYRF 6 Cyclic hexapeptide RRYYRF No entry found Not found Not found Synthetic construct Antimicrobial, Anti-Gram+, Anti-Gram- Synthetic Non helix or strand structure (Turn) Not found 1SKI Function: Antibacterial activity against Escherichia coli and Bacillus subtilis. Has hemolytic activity. [Ref.16075425] Gram-negative bacterium: Escherichia coli(MIC>100 μM);##Gram-positive bacterium: Bacillus subtilis(MIC>100 μM) [Ref.16075425] It has 1% hemolysis at 100 μM against erythrocytes. Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 16075425 Chembiochem. 2005 Sep;6(9):1654-1662. Appelt C, Wessolowski A, S?derh??ll JA, Dathe M, Schmieder P. Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles. DRAMP03821 KKWWKF 6 Cyclic hexapeptide KKWWKF No entry found Not found Not found Synthetic construct Antimicrobial, Anti-Gram+, Anti-Gram- Synthetic Non helix or strand structure (Turn) Not found 1SKK Function: Antibacterial activity against Escherichia coli and Bacillus subtilis. Has hemolytic activity. [Ref.16075425] Gram-negative bacterium: Escherichia coli(MIC=25 μM);##Gram-positive bacterium: Bacillus subtilis(MIC=25 μM) [Ref.16075425] It has 10% hemolysis at 100 μM against erythrocytes. Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 16075425 Chembiochem. 2005 Sep;6(9):1654-1662. Appelt C, Wessolowski A, S?derh??ll JA, Dathe M, Schmieder P. Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles. DRAMP03063 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCET 44 Defensin ARD1 (Heliomicin analogs; Insects, animals) P84156 Not found Not found Archaeoprepona demophon (One-spotted leafwing butterfly) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 1OZZ, 1P00, 1P0A resolved by NMR. "Function: Possesses potent anti-fungal activity. PTM: Contains three disulfide bonds 7-32; 18-40; 22-42. " Fungi: Candida albicans IHEM 8060 (MIC=6.25 µg/ml), Cryptococcus neoformans A (MIC=12.5 µg/ml), Aspergillus fumigatus GASP4707 (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic(CSαβ scaffold (an α-helix linked to a β-she Free Free Disulfide bonds between Cys7 and Cys32; Cys18 and Cys40; Cys22 and Cys42. L No cytotoxicity information found Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03069 DLHIPPPDNKINWPQLSGGGGGSPKTGYDININAQQK 37 Diptericin (Insects, animals) Q9TWW2 Belongs to the attacin/sarcotoxin-2 family Not found Sarcophaga peregrina (Flesh fly) Antimicrobial, Antibacterial Protein level Not found Not found By injury to the body wall of the larva. Expression peaks at 10 hours post-injury and is maintained at this level for at least 3 days. Escherichia coli (MIC=6.25 µg/ml), Shigella sonnei (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 1445217 Biochem J. 1992 Oct 15;287 (Pt 2):573-578. Ishikawa M, Kubo T, Natori S. Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly). DRAMP03075 WNPFKELERAGQRVRDAIISAGPAVATVAQATALAK 36 Cecropin-D P01511 Belongs to the cecropin family Not found Antheraea pernyi (Chinese oak silk moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation." Gram-negative bacteria: Escherichia coli D21 (MIC=0.37 µM), E. coli D31 (MIC=0.21 µM), Serratia marsescens (MIC=6.1 µM), S. marsescens Strain 122 (MIC=75 µM), Pseudomonas aeruginosa OT97 (MIC>81 µM), Xenorhabdus nematophilus Xn21 (MIC=16 µM);##Gram-positive bacteria: Bacillus subtilis Bsll (MIC>81 µM), Bacillus megaterium Bmll (MIC=24 µM), Bacillus thuringiensis Btll (MIC>81 µM), Streptococcus fecalis Ds16 (MIC>81 µM), S. fecalis AD-4 (MIC>81 µM), Micrococcus luteus MI11 (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 6754375 Eur J Biochem. 1982 Sep;127(1):219-224. Qu Z, Steiner H, Engström A, Bennich H, Boman HG. Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi. DRAMP03089 GWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR 39 Drosophila cecropin-A1/A2 (Insects, animals) P14954, B3DN02, B3DN08, O16815, O16816, O16817, O16818, O16819, O16820 Belongs to the cecropin family CecA1 AND CecA2 Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Tissue specificity: Strongly expressed in larval, pupal and adult fat body and hemocytes after injection of bacteria. Maximal expression in the adult involves fat body cells of the head, thorax and abdomen. Induction: Induced as part of the humoral response to a bacterial invasion. Transcripts appear within one hour after injection of bacteria into the hemocoel, reach a maximum after 2-6 hours and have almost disappeared after 24 hours. Similar response is seen when flies ingest bacteria present in their food. PTM: C-terminal amidation (By similarity)." Gram-negative bacteria: Escherichia coli D21 (MIC=0.3 µM), Enterobacter cloacae β12 (MIC=0.4 µM), Pseudomonas aeruginosa OT97 (MIC=2.2 µM), Serratia marcescens Db11 (MIC=93 µM);##Gram-positive bacteria: Bacillus megatherium Bm11 (MIC=2.6 µM), Bacillus subtilis Bsll (MIC=16 µM), Micrococcus luteus MI11 (MIC=8.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 2104802##2390977##9725836 EMBO J. 1990 Jan;9(1):217-224.##EMBO J. 1990 Sep;9(9):2969-2976. Kylsten P, Samakovlis C, Hultmark D.##Samakovlis C, Kimbrell DA, Kylsten P, Engström A, Hultmark D. The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection.##The immune response in Drosophila: pattern of cecropin expression and biological activity. DRAMP03090 GWLRKLGKKIERIGQHTRDASIQVLGIAQQAANVAATAR 39 Drosophila cecropin B (CecB; Insects, animals) P14956, O16826, O16827, O16828, O18647, O61274, Q9V425 Belongs to the cecropin family CecB Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Induced as part of the humoral response to a bacterial invasion. Transcripts appear within one hour after injection of bacteria into the hemocoel, reach a maximum after 2-6 hours and have almost disappeared after 24 hours. Similar response is seen when flies ingest bacteria present in their food. [Ref.1] Gram-negative bacteria: Escherichia coli D21 (MIC=1.8 µM), Enterobacter cloacae b12 (MIC=1.0 µM), Pseudomonas aeruginosa OT97 (MIC=4.2 µM);##Gram-positive bacteria: Bacillus megatherium Bm11 (MIC=3.7 µM), Bacillus subtilis Bsll (MIC=3.2 µM), Micrococcus luteus MI11 (MIC=59 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 2390977##2104802 EMBO J. 1990 Sep;9(9):2969-2976.##EMBO J. 1990 Jan;9(1):217-224. Samakovlis C, Kimbrell DA, Kylsten P, Engström A, Hultmark D.##Kylsten P, Samakovlis C, Hultmark D. The immune response in Drosophila: pattern of cecropin expression and biological activity.##The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection. DRAMP03095 VFIDILDKVENAIHNAAQVGIGFAKPFEKLINPK 34 Andropin (Insects, animals) P21663, A9UNE4, O16822, O16823, O16824, Q6LAI1, Q9VA90 Not found Anp Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Andropin is constitutively expressed in the adult male ejaculatory duct in response to mating not bacterial infection. Andropin is less fungicidal than the cecropins (Insect Biochem Mol Biol. 1999;29:965-72). Along with other antimicrobial proteins, this peptide sterilizes the reproduction system of insects and protects sperms from being infected by bacteria (J Insect Physiol. 2001 Jun;47(6):617-622). Similarly, ceratotoxins are expressed in the female reproductive accesary glands and expressed during mating. Gram-negative bacteria: Escherichia coli D21 (MIC=140 µM), Enterobacter cloacae b312 (MIC>300 µM), Pseudomonas aeruginosa OT97 (MIC>300 µM), Serratia marcescens Db 11 (MIC>127 µM), Serratia marcescens Db 1140 (MIC>127 µM);##Gram-positive bacteria: Bacillus megatherium Bml1 (MIC=11 µM), Bacillus subtilis Bs11 (MIC=17 µM), Micrococcus luteus MIll (MIC=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 1899226 EMBO J. 1991; 10:163-169. Samakovlis, C, Kylsten, P, Kimbrell, DA, Engstroem, A, Hultmark, D. The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster. DRAMP03096 RRQGPIFDTRPSPFNPNQPRPGPIY 25 Metchnikowin-2 (Insects, animals) No entry found Not found Not found Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Micrococcus luteus (MIC=0.5-1.0 µM).##Fungi: Neurospora crassa (MIC=0.5-1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 7588819 Eur J Biochem. 1995 Oct 15;233(2):694-700. Levashina EA, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann JA. Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties. DRAMP18495 QCRRLCYKQRCVTYCRGR 18 Gomesin (Gm; Spiders, arachnids, Chelicerata, arthropods, invertebrates, animals) P82358 Belongs to the tachyplesin family Not found Acanthoscurria gomesiana (Tarantula spider) (Phormictopus pheopygus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiparasitic, Antimalarial, Antic Protein level Beta sheet Not found 1KFP resolved by NMR. "Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. It shows hemolytic activity. Tissue specificity: In hemocytes only, but not in all hemocytes observed." [Ref.10942757] Gram-positive bacteria: Aerococcus viridans (MIC=0.8-1.6 μM), Bacillus cereus (MIC=6.25-12.5 μM), Bacillus megaterium (MIC=0.2-0.4 μM), Bacillus thuringiensis (MIC=1.6-3.15 μM), Enterococcus faecalis (MIC=6.2-12.5 μM), Listeria monocytogenes (MIC=0.8-1.6 μM), Micrococcus luteus (MIC=0.4-0.8 μM), Pediococcus acidolacrici (MIC=3.15-6.25 μM), Staphylococcus aureus (MIC=1.6-3.15 μM), Staphylococcus epidermidis (MIC=0.8-1.6 μM), Staphylococcus haemolyticus (MIC=0.8-1.6 μM), Staphylococcus saprophyticus (MIC=0.8-1.6 μM), Streptococcus pyogenes (MIC=1.6-3.15 μM), Nocardia asteroides (MIC=1.6-3.15 μM);##Gram-negative bacteria: Escherichia coli 1106 (MIC=0.8-1.6 μM), Escherichia coli D22 (MIC=0.4-0.8 μM), Escherichia coli D31 (MIC=0.8-1.6 μM), Escherichia coli SBS363 (MIC=0.4-0.8 μM), Erwinia carolovora (MIC=3.15-6.25 μM), Enterobacter cloacae β12 (MIC=3.15-6.25 μM), Klebsiella pneumoniae (MIC=3.15-6.25 μM), Pseudomonas aeruginosa (MIC=1.6-3.15 μM), Salmonella thyphinurium (MIC=0.8-1.6 μM), Xhantomonas campestris pv. orizae (MIC=3.15-6.25 μM);##Fungi: Alternaria brassicola (MIC=0.4-0.8 μM), Aspergillus fumigatus (MIC=1.6-3.15 μM), Beauveria bassiana (MIC=12.5-25 μM), Fusarium culmorum (MIC=0.4-0.8 μM), Fusarium oxysporum (MIC=0.4-0.8 μM), Neurospora crassa (MIC=0.4-0.8 μM), Nectria haematococca (MIC=0.2-0.4 μM), Tricoderma viridae (MIC=0.4-0.8 μM), Tricophvton mentagrophytes (MIC=0.8-1.6 μM);##Yeasts: Candida albicans (MIC=0.15-0.3 μM), Candida glabrata (MIC=12.5-25 μM), Candida tropicalis (MIC=3.15-6.25 μM), Cryptococcus neoformans (MIC=0.8-1.6 μM), Saccharomyces cerevisiae (MIC=1.6-3.15 μM). [Ref.10942757] It exhibits 16% hemolysis at 1 μM and 100 μM against human erythrocytes Cyclic pyroglutamic acid Amidation Disulfide bond between Cys2 and Cys15,Cys6 and Cys11. L No cytotoxicity information found Not found 10942757 J Biol Chem. 2000 Oct 27;275(43):33464-70. Silva PI Jr, Daffre S, Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. DRAMP03098 HRHQGPIFDTRPSPFNPNQPRPGPIY 26 Metchnikowin (Pro-rich; Insects, animals) Q24395, Q24396, Q86BV8, Q9V7B9 Not found Mtk Drosophila melanogaster (Common fruit fly) Antimicrobial, Antibacterial, Antifungal Protein level Rich in Proline Not found Transgenic plants: Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens (J Exp Bot. 2009;60(14):4105-14). Micrococcus luteus (MIC=0.5-1.0 µg/ml), Neurospora crassa (MIC=0.5-1.0 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 7588819 Eur J Biochem. 1995 Oct 15;233(2):694-700. Levashina E.A, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann J.A. Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties. DRAMP03104 ATCDLLSGTGINHSACAAHCLLRGNRGGYCNGKAVCVCRN 40 Sapecin (defensins; Insects, animals) P18313 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Sarcophaga peregrina (Flesh fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Not found 1L4V resolved by NMR. "Function: Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin is cytotoxic to Gram-positive bacteria, and to a lesser extent against Gram-negative bacteria. Tissue specificity: Hemocytes and fat body. Induction: By injury to the larval cell wall. PTM: Contains three disulfide bonds 3-30; 16-36; 20-38." Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=5.0 µg/ml), Staphylococcus smith (MIC=5.0 µg/ml), Micrococcus luteus FDA16 (MIC=1.2 µg/ml), Micrococcus luteus IF03333 (MIC=1.2 µg/ml), Micrococcus luteus PC11001 (MIC=10.0 µg/ml), Bacillus subtilis NRRI B-558 (MIC=39.0 µg/ml), Bacillus subtilis PC1219 (MIC=20.0 µg/ml), Mycobacterium smegmatis ATCC607 (MIC=78.0 µg/ml), Corynebacterium bouis 1810 (MIC=2.5 µg/ml), Corynebacterium michiganense (MIC=2.5 µg/ml).##Gram-negative bacteria: Xantbmonas oryzae (MIC=20.0 µg/ml), Pseudomonas lachrymans (MIC=78.0 µg/ml), Escherichia coli NIHJ (MIC>78.0 µg/ml), Shigella sonnei JS11746 (MIC>78.0 µg/ml), Proteus vulgaris O X19 (MIC>78.0 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys30; Cys16 and Cys36; Cys20 and Cys38. L No cytotoxicity information found Not found 3182836##3182836##2358424 J Biol Chem. 1988 Nov 15;263(32):17117-17121.##J Biol Chem. 1988 Nov 15;263(32):17112-17116.##J Biochem. 1990 Apr;107(4):514-518. Matsuyama K, Natori S.##Matsuyama K, Natori S.##Kuzuhara T, Nakajima Y, Matsuyama K, Natori S. Molecular cloning of cDNA for sapecin and unique expression of the sapecin gene during the development of Sarcophaga peregrina.##Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina.##Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly). DRAMP03113 SQLGDLGSGAGQGGGGGGSIRAAGGAFGKLEAAREEEFFYKKQKEQLERLKNDQIHQAEFHHQQIKEHEEAIQRHKDFLNNLHK 84 SK84 (Gly-rich; Insects, animals) No entry found Not found Not found Drosophila virilis (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal, Antiviral Not found Not found Not found Function: SK84 displays antibacterial activity against the tested Gram-positive bacteria (B. subtilis, Bacillus thuringiensis and Staphylococcus aureus), but had no effect on Gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli) and fungi (Saccharomyces cerevisiae, Candida albicans). Has weak hemolytic activity. [Ref.19799950]Gram-positive bacteria: Bacillus thuringiensis ATCC 1041 (MIC=4 µM), B. subtilis ATCC 9372 (MIC=8 µM), Staphylococcus aureus ATCC 6538 (MIC=8 µM). [Ref.19799950]0.01% hemolytic activity at 100 μM against human red blood cells Linear Free Free Free L Not included yet Not found 19799950 Peptides. 2010 Jan;31(1):44-50. Lu J, Chen ZW. Isolation, characterization and anti-cancer activity of SK84, a novel glycine-rich antimicrobial peptide from Drosophila virilis. DRAMP03116 SLGGVISGAKKVAKVAIPIGKAVLPVVAKLVG 32 Ceratotoxin-C (Insects, animals) Q17313 Not found CTXC1 AND CTCX2 Ceratitis capitata (Mediterranean Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Has hemolytic activity.Temperature dependence: Thermostable. Still active at 100 degrees Celsius. [Ref.9569644]Gram-negative bacteria: Escherichia coli 23739 (MIC=13.6 µM), Escherichia coli LE 392 (MIC=5 µM), Pseudomonas aeruginosa 27853 (MIC>50 µM), P. vulgaris 6380 (MIC>50 µM), S. typhymurium 23853 (MIC>5 µM);##Gram-positive bacteria: E. cloacae 13047 (MIC>5 µM), E. jaecalis 29212 (MIC>50 µM), Staphylococcus aureus 25923 (MIC>50 µM), B. cereus 9634 (MIC>5 µM), Bacillus subtilis 6633 (MIC=5.9 µM). [Swiss_Prot Entry Q17313]has hemolytic activity Linear Free Free Free L Not included yet Not found 9569644 Eur. J. Biochem. 1996; 241:330-337. Rosetto M, Manetti AGO, Giordano PC, Marri L, Amons R, Baldari CT, Marchini D, Dallai R. Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata. DRAMP03117 QSEAGWLKKIGKKIERVGQHTRDATIQGLGVAQQAPNVAATAR 43 Drosophila cecropin-A1 (Insects, animals) O61272 Belongs to the cecropin family CecA1 Drosophila simulans (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation (By similarity)." Gram-negative bacteria: Alcaligenes faecalis (MIC=10-25 µM), Escherichia coli 1106 (MIC=0.25-0.5 µM), Escherichia coli D22 (MIC=0.1-0.25 µM), Escherichia coli D31 (MIC=0.1-0.25 µM), Escherichia coli SBS363 (MIC=0.1-0.25 µM), Enterobacter cloacae β12 (MIC=0.5-1 µM), Erwinia carotovora (MIC=0.5-1 µM), Klebsiella pneumoniae (MIC=1-2.5 µM), Pseudomonas aeruginosa (MIC=1-2.5 µM), Salmonella typhimurium (MIC=0.5-1 µM), Xanthomonas campestris (MIC=0.5-1 µM); ##Gram-positive bacteria: Aerococcus viridans (MIC=5-10 µM), Bacillus megaterium (MIC=1-2.5 µM), Micrococcus luteus (MIC=5-10 µM).##Fungi: Botrytis cinerea (MIC=5-10 µM), Fusarium culmorum (MIC=1-2.5 µM), Fusarium oxysporum (MIC=1-2.5 µM), Neurospora crassa (MIC=2.5-10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9553148##9725836 Immunogenetics. 1998 May;47(6):417-429.##Genetics. 1998 Sep;150(1):157-171.##Insect Mol Biol. 2000 Feb;9(1):75-84. Date A, Satta Y, Takahata N, Chigusa S.I.##Ramos-Onsins S, Aguade M.##Vizioli J, Bulet P, Charlet M, Lowenberger C, Blass C, Müller HM, Dimopoulos G, Hoffmann J, Kafatos FC, Richman A. Evolutionary history and mechanism of the Drosophila cecropin gene family.##Molecular evolution of the Cecropin multigene family in Drosophila: functional genes vs pseudogenes.##Cloning and analysis of a cecropin gene from the malaria vector mosquito, Anopheles gambiae. DRAMP03137 ATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCRN 40 Defensin-A (AaeDefA; Insects, animals) P91793, O77250, P91794, P91795, P91796, Q17EE3, Q6ITZ2, Q963E9 Belongs to the invertebrate defensin family (Type 1 subfamily) DEFA Aedes aegypti (Yellowfever mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found Function: Antibacterial peptide mostly active against Gram-positive bacteria. Has activity against the bacteria Gram-negative E. cloacae beta12. Gram-positive bacteria: Enterobacter cloacae beta12 (MIC=1.2-2.4 µM), Aerococcus viridans (MIC=0.6-1.2 µM), Micrococcus luteus (MIC=0.6-1.2 µM), Bacillus rnegaterium (MIC=0.6-1.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Has three disulfide bonds L No cytotoxicity information found Not found 7633471##7568275 Insect Biochem Mol Biol. 1995 Jul;25(7):867-873.##Proc Biol Sci. 1995 Aug 22;261(1361):217-221. Lowenberger C, Bulet P, Charlet M, Hetru C, Hodgeman B, Christensen BM, Hoffmann JA.##Chalk R, Albuquerque CM, Ham PJ, Townson H. Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti.##Full sequence and characterization of two insect defensins: immune peptides from the mosquito Aedes aegypti. DRAMP03138 GGLKKLGKKLEGAGKRVFNAAEKALPVVAGAKAL 34 Cecropin-A (Insects, animals) P82592, Q17NR3, Q95PI9 Belongs to the cecropin family CECA Aedes aegypti (Yellowfever mosquito) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli D22 (MIC=0.25-0.5 µg/ml), E. coli D31 (MIC=0.25-0.5 µg/ml), E. coli SBS363 (MIC=0.1-0.25 µg/ml), E. coli 1106 (MIC=0.25-0.5 µg/ml), Enterobacter cloacae b12 (MIC=50-100 µg/ml), E. carotovora (MIC=0.25-0.5 µg/ml), Klebsiella pneumoniae (MIC=1-2.5 µg/ml), Pseudomonas aeruginosa (MIC=10-25 µg/ml), Salmonella typhimurium (MIC=1-2.5 µg/ml), X. campestris (MIC=0.5-1 µg/ml);##Gram-positive bacteria: Aerococcus viridans (MIC=2.5-5 µg/ml), Bacillus megaterium (MIC=1-2.5 µg/ml), Micrococcus luteus (MIC=10-25 µg/ml), Streptococcus pyogenes (MIC=10-25 µg/ml).##Fungi: Fusarium culmorum (MIC=1-2.5 µg/ml), Fusarium oxysporum (MIC=2.5-5 µg/ml), Neurospora crassa (MIC=5-10 µg/ml), Candida albicans (MIC=25-50 µg/ml), Cryptococcus neoformans (MIC=25-50 µg/ml), Saccharomyces cerevisiae (MIC=50-100 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Linear L Not included yet Not found 10400619 J Biol Chem. 1999 Jul 16;274(29):20092-20097. Lowenberger C, Charlet M, Vizioli J, Kamal S, Richman A, Christensen BM, Bulet P. Antimicrobial activity spectrum, cDNA cloning, and mRNA expression of a newly isolated member of the cecropin family from the mosquito vector Aedes aegypti. DRAMP03140 GRLKKLGKKIEGAGKRVFKAAEKALPVVAGVKALG 35 Anopheles cecropin-A amidated isoform (Insects, animals) P82290, A7XAX5, A7XAX7, A7XAY1, A7XAY8, A7XAZ7, A7XB12, A7XB23, Q7QEE3 Belongs to the cecropin family CecA Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antibacterial activity against several Gram-positive and Gram-negative bacteria. Also has antifungal activity. Tissue specificity: Relatively abundant in head, thorax and to a lesser extent in abdominal carcass and anterior midgut. Developmental stage: In young pupae, expressed within 2 hours of infection and continued to accumulate over 16 hours. Induction: By bacterial infection. PTM: C-terminal amidation." Gram-negative bacteria: Alcaligenes faecalis (MIC=1-2.5 µM), Escherichia coli 1106 (MIC=0.5-1 µM), E. coli D22 (MIC=0.1-0.25 µM), E. coli D31 (MIC=0.1-0.25 µM), E. coli SBS363 (MIC=0.05-0.1 µM), Enterobacter cloacae β12 (MIC=0.5-1 µM), Erwinia carotovora (MIC=0.5-1 µM), Klebsiella pneumoniae (MIC=1-2.5 µM), Pseudomonas aeruginosa (MIC=1-2.5 µM), Salmonella typhimurium (MIC=0.1-0.25 µM), Xanthomonas campestris (MIC=0.5-1 µM); ##Gram-positive bacteria: Aerococcus viridans (MIC=0.5-1 µM), Bacillus cereus (MIC=50-100 µM), Bacillus megaterium (MIC=0.5-1 µM), Listeria monocytogenes (MIC=50-100 µM), Micrococcus luteus (MIC=0.5-1 µM), Staphylococcus aureus (MIC=50-100 µM), Staphylococcus epidermidis (MIC=10-25 µM), Staphylococcus haemolyticus (MIC=1-2.5 µM), Staphylococcus saprophyticus (MIC=1-2.5 µM), Streptococcus pyogenes (MIC=0.1-0.25 µM).##Fungi: Aspergillus fumigatus (MIC=5-10 µM), Botrytis cinerea (MIC=1-2.5 µM), Fusarium culmorum (MIC=0.5-1 µM), Fusarium oxysporum (MIC=1-2.5 µM), Neurospora crassa (MIC=1-2.5 µM), Candida albicans (MIC=1-2.5 µM), Cryptococcus neoformans (MIC=5-10 µM), Saccharomyces cerevisiae (MIC=25-50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Linear L Not included yet Not found 10672074##12421409 Insect Mol Biol. 2000 Feb;9(1):75-84.##Insect Mol Biol. 2002 Dec;11(6):517-525. Vizioli J, Bulet P, Charlet M, Lowenberger C, Blass C, Müller HM, Dimopoulos G, Hoffmann J, Kafatos FC, Richman A.##Zheng XL, Zheng AL. Cloning and analysis of a cecropin gene from the malaria vector mosquito, Anopheles gambiae.##Genomic organization and regulation of three cecropin genes in Anopheles gambiae. DRAMP03150 MVFAYAPTCARCKSIGARYCGYGYLNRKGVSCDGQTTINSCEDCKRKFGRCSDGFITECFL 61 Gambicin (Insects, animals) No entry found Not found Not found Anopheles albimanus (mosquito) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiparasitic Not found Bridge Not found "Function: In vitro experiments showed that the 6.8-kDa mature peptide can kill both Gram-positive and Gram-negative bacteria, has a morphogenic effect on a filamentous fungus, and is marginally lethal to Plasmodium berghei ookinetes. Induction: Predominantly expressed in the anterior part. PTM: Contains four disulfide bridges." Gram-negative bacterium: E. coli (MIC=6.25-12.5 µM);##Gram-positive bacterium: M. luteus (MIC=25-50 µM).##Fungus: N. crassa. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys9 and Cys20; Cys12 and Cys32; Cys41 and Cys51,Cys44 and Cys59. L No cytotoxicity information found Not found 11606751 Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12630-5. Vizioli J, Bulet P, Hoffmann JA, Kafatos FC, Müller HM, Dimopoulos G. Gambicin: a novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae. DRAMP03153 GIGGKPVQTAFVDNDGIYD 19 27 kDa antibacterial protein P81925 Not found Not found Cyprinus carpio (common carp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity. Forms large ion channels responsible for disrupting the cellular envelope of bacteria leading to cell lysis. Gram-positive bacteria: Staphylococcus aureus (MIC=5 µg/ml), Micrococcus luteus (MIC=0. 5 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=5 µg/ml), Pseudomonas fluorescens (MIC=10 µg/ml), Aeromonas hydrophila (MIC=5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8797847 Eur J Biochem. 1996 Aug 15;240(1):143-149. Lemaître C, Orange N, Saglio P, Saint N, Gagnon J, Molle G. Characterization and ion channel activities of novel antibacterial proteins from the skin mucosa of carp (Cyprinus carpio). DRAMP03162 ATCDLLSAFGVGHAACAAHCIGHGYRGGYCNSKAVCTCRR 40 Phlebotomus duboscqi defensin (PduDef; defensins; Insects, animals) P83404 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Phlebotomus duboscqi Antimicrobial, Antibacterial, Anti-Gram+, Antifungal, Antiparasitic Protein level Bridge Not found "Function: Has antiparasitic and antifungal activity. Tissue specificity: Is synthesized by the fat body and eventually secreted into the hemolymph. Induction: By bacterial and parasitic hemolymph and gut infections. Expression peaks at 24 hours post infection by bacterium P. carotovorum, and at day four post infection by the parasite L. major. PTM: Problely contains three disulfide bonds 3-30; 16-36; 20-36." Gram-positive bacteria: Staphylococcus aureus (MIC=0.78-1.56 µM), Aspergillus fumigatus (MIC=12.5-25 µM).##Fungi: Fusarium culmorum (MIC=1.56-3.12 µM), Fusarium oxysporum (MIC=3.12-6.25 µM), Neurospora crassa (MIC=6.25-12.5 µM), Trichoderma viride (MIC=3.12-6.25 µM), Trichophyton mentagrophytes (MIC=25-50 µM), Candida albicans (MIC=6.25-12.5 µM), Saccharomyces cerevisiae (MIC=25-50 µM).##Parasite: Leishmania major promastigote forms (IC50=68-85 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys30; Cys16 and Cys36; Cys20 and Cys36. L No cytotoxicity information found Not found 15557638 Infect Immun. 2004 Dec;72(12):7140-7146. Boulanger N, Lowenberger C, Volf P, Ursic R, Sigutova L, Sabatier L, Svobodova M, Beverley SM, Späth G, Brun R, Pesson B, Bulet P. Characterization of a defensin from the sand fly Phlebotomus duboscqi induced by challenge with bacteria or the protozoan parasite Leishmania major. DRAMP03166 IRNSLTCRFNFGICLPKRCPGRMRQIGTCF 30 P15 (deer beta-defensin; ruminant, animals) No entry found Not found Not found Cervus elaphus (New Zealand deer) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found "Function: It shows strong activity against Gram-negative bacteria, but lesser activity against Gram-positive bacteria and yeast. Caution: the sequence displayed is N-terminal sequence of P15. " Gram-negative bacterium: Escherichia coli O111 (MIC=0.3 µg/mL);##Gram-positive bacterium: Staphylococcus aureus NCTC 4163 (MIC=1 µg/mL).##Fungi: Candida albicans 3135A (MIC=3 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two disulfide bonds(By similar). Not included yet Not included yet Not found 16011891 Int J Antimicrob Agents. 2005 Aug;26(2):165-169. Treffers C, Chen L, Anderson RC, Yu PL. Isolation and characterisation of antimicrobial peptides from deer neutrophils. DRAMP03169 RARAPHKAWYNCMTDAGISGAIAGAVAGCAATIEIGCVEGAIAGIGPSGIASMIAALWTCRSKY 64 Protease-activated antimicrobial peptide No entry found Not found Not found Propionibacterium jensenii Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Propionibacterium acidipropionici ATCC 4965 (MIC=3.6 nM), P. acidipropionici ATCC 4875 (MIC=7.2 nM), P. acidipropionici (MIC=3.6 nM), P. freudenreichii subsp. freudenreichii ATCC 6207T (MIC=7.2 nM), P. freudenreichii INF-P203 (MIC=116 nM), P. freudenreichii INF-P205 (MIC=58 nM), P. jensenii LMG 2820 (MIC=116 nM), P. jensenii LMG 3032 (MIC=116 nM), P. thoenii INF-P410 (MIC=116 nM), P. thoenii INF-P414 (MIC=0.9 nM), Lactobacillus delbrueckii subsp. lactis ATCC 4797 (MIC=0.5 nM), L. delbrueckii subsp. lactis DSM 20072T (MIC=0.2 nM), L. delbrueckii subsp. bulgaricus DSM 20081T (MIC=7.2 nM), L. helveticus DSM 20075T (MIC=0.9 nM), Lactobacillus plantarum LMG 2003 (MIC=116 nM), L. sakei NCDO 2714 (MIC=0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 12057960 J Bacteriol. 2002 Jul;184(13):3649-3656. Faye T, Brede DA, Langsrud T, Nes IF, Holo H. An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii. DRAMP03173 RWCVYAYVRVRGVLVRYRRCW 21 Arenicin-1 (Ar-1; marine polychaeta, animals) Q5SC60, P84105 Not found Not found Arenicola marina (Lugworm) (Lumbricus marinus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Cytotoxic Protein level Beta strand (2 strands; 16 residues) Arenicin-1 is a two-stranded antiparallel β-sheet (Cys3-Val10 and Val13-Cys20) stabilized by nine intra-backbone hydrogen bonds and a disulfide bond between Cys3 and Cys20. The strands of the β-sheet are connected by a type I´ β-turn. The surface of arenicin is amphiphilic, with distinct hydrophobic and hydrophilic areas (ref.2). 2JSB resolved by NMR. "Function: Has antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteriua as well as yeast C. albicans. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. PTM: Contains one disulfide bond 3-20. Domian: Contains 1 BRICHOS domain." Gram-positive bacterium: Listeria monocytogenes EGD (MIC=0.6 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35p (MIC=4 µg/ml), E. coli WBB01 (MIC=0.3 mM), E. coli ATCC 23716 (MIC=0.6 mM), Salmonella enterica R595 (MIC=0.3 mM), S. enterica R60 (MIC=1.25 mM), Proteus mirabilis R45 (MIC=0.6 mM).##Yeast: Candida albicans 820 (MIC=20 µg/ml).##Human Jurkat T-cells: LD50>40 mM (35.5% lysis at 30 mM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys3 and Cys20. L [Ref.27940358] Cytotoxicity: human embryonic fibroblasts (HEF) and human red blood cells (hRBC)(IC50 for arenicin-1 in the presence or absence of 10% FBS were of 35 and 8 μM,HC50 indicating 50% hemolysis after 24 h incubation, equaled to 16μM). Anionic lipid vesicles 15527787##17935487 FEBS Lett. 2004 Nov 5;577(1-2):209-214.##Biochem J. 2008 Feb 15;410(1):113-122. Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN.##Andrä J, Jakovkin I, Grötzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina.##Structure and mode of action of the antimicrobial peptide arenicin. DRAMP03176 SWLSKTAKKLENSAKKRISEGIAIAIQGGPR 31 Cecropin-P1 (CP1; nematodes, animals) P14661, Q5H7N7 Belongs to the cecropin family ASCEC-1 Ascaris suum (Pig roundworm) (Ascaris lumbricoides) Antimicrobial, Antibacterial, Antifungal Protein level Alpha helix Not found 2N92##7DEH##7VOZ "Function: Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism. Induction: By bacterial infection." P1-NH2 (amidated cecropin P1): [E. coli K-12/ D21 (MIC=0.3 µM), E. coli 853/67/0149/K88 (MIC=0.9 µM), E. coli Bd2221/75/08/K88 (MIC=0.6 µM), E. coli Bd4462/84/0101/K99 (MIC=0.7 µM), E. coli Bd4466/84/064/K99 (MIC=0.3 µM), Salmonella typhimurium LT2 (MIC=0.9 µM), A. calcoaceticus Ac1l (MIC=0.2 µM), Proteus vulgaris Pvll (MIC=5.7 µM), Pseudomonas aeruginosa OT97 (MIC=5.9 µM), Bacillus megaterium Bmll (MIC=1.8 µM), Streptococcus pyogenes (MIC=19 µM)].##P1-OH (non-amidated cecropin P1): [E. coli K-12/ D21 (MIC=0.4 µM), E. coli 853/67/0149/K88 (MIC=0.6 µM), E. coli Bd2221/75/08/K88 (MIC=0.7 µM), E. coli Bd4462/84/0101/K99 (MIC=0.8 µM), E. coli Bd4466/84/064/K99 (MIC=0.6 µM), Salmonella typhimurium LT2 (MIC=1.7 µM), A. calcoaceticus Ac1l (MIC=0.5 µM), Proteus vulgaris Pvll (MIC=12 µM), Pseudomonas aeruginosa OT97 (MIC=13 µM), Bacillus megaterium Bmll (MIC=5.3 µM), Streptococcus pyogenes (MIC=44 µM)]. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 15850460##1396696 Biochem J. 2005 Aug 15;390(Pt 1):207-214.##Eur J Biochem. 1992 Oct 1;209(1):163-169. llai A, Ueno S, Zhang H, Lee JM, Kato Y.##Sipos D, Andersson M, Ehrenberg A. Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum.##The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR. DRAMP03181 HVDKKVADKVLLLKQLRIMRLLTRL 25 Spinigerin (Insects, animals) P82357 Not found Not found Pseudacanthotermes spiniger (Termite) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found 1ZRW, 1ZRV resolved by NMR. Function: Active against Gram-positive bacteria and Gram-negative bacteria and fungi. Gram-positive bacteria: Bacillus megaterium (MIC=0.8-1.5 µM), Micrococcus luteus (MIC=0.8-1.5 µM);##Gram-negative bacteria: Escherichia coli SBS363 (MIC=3-6 µM), E. coli D22 (MIC=3-6 µM), Klebsiella pneumoniae (MIC=50-100 µM), Salmonella typhimurium (MIC=3-6 µM), Pseudomonas aeruginosa (MIC=50-100 µM).##Fungi: Trichoderma viride (MIC=1.5-3 µM), Neurospora crassa (MIC=3-6 µM), Fusarium culmorum (MIC=1.5-3 µM), Nectria haematococca (MIC=0.4-0.8 µM), Candida albicans (MIC=3-6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 11053427##16170803 J Biol Chem. 2001 Feb 9;276(6):4085-4092.##Biopolymers. 2006 Feb 5;81(2):92-103. Lamberty M, Zachary D, Lanot R, Bordereau C, Robert A, Hoffmann JA, Bulet P.##Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F. Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect.##Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation. DRAMP03186 SFGLCRLRRGFCARGRCRFPSIPIGRCSRFVQCCRRVW 38 Spheniscin-2 (Sphe-2; penguin avian beta-defensin 103b; birds ,animals) P83430 Belongs to the beta-defensin family Not found Aptenodytes patagonicus (King penguin) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand (3 strands; 14 residues) The overall fold of Sphe-2 includes a three-stranded antiparallel beta-sheet stabilized by three disulfide bridges with a pairing typical of beta-defensins. In addition, the N-terminal segment shows helical features on most structures.(Ref.2) 1UT3 resolved by NMR. "Function: Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function: with its amphipathic structure. PTM: Contains three disulfide bond: 5-33; 12-27; 17-34. Preserving food in the bird somach for several weeks during egg incubation. The disulfide bond pattern is identical to canonical beta-defensins from mammals. The high potency is related to its high cationicity as well as a hydrophobic patch, which is not observed in mammalian defensins. " [Ref.14525994]Gram-positive bacteria: Micrococcus luteus (MIC=1.5-3.0 µM), Bacillus subtilis (MIC=0.8-1.5 µM), Bacillus cereus ATCC 11778 (MIC=3-6 µM), Bacillus megaterium (MIC=0.4-0.8 µM), Staphylococcus aureus (MIC=1.5-3.0 µM), Staphylococcus saprophyticus (MIC=1.5-3.0 µM), Staphylococcus haemolyticus (MIC=1.5-3.0 µM), Nocardia asteroides (MIC=0.8-1.5 µM), Aerococcus viridans (MIC=0.4-0.8 µM), Listeria monocytogenes (MIC=6-12 µM);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=0.8-1.5 µM), Escherichia coli 1106 (MIC=1.5-3.0 µM), Salmonella typhimurium (MIC=6-12 µM), Klebsiella pneumoniae (MIC=50-100 µM), Pseudomonas aeruginosa ATCC 82118 (MIC=6-12 µM), Vibrio metschnikovii NCTC 8483 (MIC=25-50 µM), Vibrio anguillarum ATCC 19264 (MIC=25-50 µM);##Fungi: Candida glabrata (MIC>100 µM), Candida albicans IHEM 8060 (MIC=50-100 µM), Candida tropicalis (MIC=1.5-3.0 µM), Neurospora crassa (MIC=3-6 µM),Aspergillus fumigatus (MIC=3-6 µM). It has hemolytic activity Cyclic Free Free Disulfide bonds between Cys5 and Cys33; Cys12 and Cys27; Cys17 and Cys34. L No cytotoxicity information found Not found 14525994##15123713 J Biol Chem. 2003 Dec 19;278(51):51053-51058.##J Biol Chem. 2004 Jul 16;279(29):30433-30439. Thouzeau C, Le Maho Y, Froget G, Sabatier L, Le Bohec C, Hoffmann JA, Bulet P.##Landon C, Thouzeau C, Labbé H, Bulet P, Vovelle F. Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus.##Solution structure of spheniscin, a beta-defensin from the penguin stomach. DRAMP03187 QRYFCRVRGGRCAALTCLPRETQIGRCSVKGRKCCR 36 Beta defensin 1(BD-1; mammals, animals) P83943 Belongs to the beta-defensin family DEFB1 Chinchilla lanigera (Long-tailed chinchilla) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antibacterial and antifungal activity. May have a role in maintaining sterility in the middle ear. Gram-negative bacterium: Moraxella catarrhalis (MIC=5 µg/ml);##Gram-positive bacterium: Streptococcus pneumoniae (MIC=5 µg/ml).##Fungi: Candida albicans (MIC=12.5-20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are three disulfide bonds. Not included yet Not included yet Not found 14996845 J Biol Chem. 2004 May 7;279(19):20250-20256. Harris RH, Wilk D, Bevins CL, Munson RS Jr, Bakaletz LO. Identification and characterization of a mucosal antimicrobial peptide expressed by the chinchilla (Chinchilla lanigera) airway. DRAMP03190 RLGNFFRKAKKKIGRGLKKIGQKIKDFLGNLVPRTES 37 PobRL-37 (cathelicidin; primates, mammals, animals) No entry found Not found Not found Cercopithecidae Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Has antibacterial activity. In 20% TSB in SPB medium: Escherichia coli (MIC=0.5 µM), Pseudomonas aeruginosa (MIC=0.5-1 µM), Staphylococcus aureus (MIC=2 µM), Enterococcus faecalis (MIC=2-4 µM).##In 20% SAB in SPB: Candida albicans (MIC=8-16 µM). In 5% TSB in SPB: Escherichia coli (MIC=0.5 µM). In 5% SAB in SPB: Candida albicans (MIC=4-8 µM).##In 20% TSB in PIL: Escherichia coli (MIC=1 µM), Pseudomonas aeruginosa (MIC=1-2 µM); Staphylococcus aureus (MIC=0.5 µM), Enterococcus faecalis (MIC=1-2 µM).##In 20% SAB in PIL: Candida albicans (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP03196 RCVCRRGVCRCVCTRGFC 18 PhTD-1 (PhTD1; primates, mammals, animals) P86722, P86723 Not found Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database In low salt conditions: Escherichia coli ML35p (MIC=1.5 µM), Listeria monocytogenes EGD (MIC=1.6 µM) and methicillin-resistant Staphylococcus aureus ATCC 33591 (MIC=2.5 µM),.##Fungi: Candida albicans 820 (MIC=1.6 µM);##At high physiological salt concentrations: Escherichia coli ML35p (MIC=2.0 µM), Listeria monocytogenes EGD (MIC=1.7 µM), Staphylococcus aureus ATCC 33591 (MIC=3.6 µM), Candida albicans 820 (MIC=6.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys11; Cys4 and Cys9; Cys13 and Cys18. L No cytotoxicity information found Not found 20155756 Rapid Commun Mass Spectrom. 2010 Mar 15;24(5):599-604. Stegemann C, Tsvetkova EV, Aleshina GM, Lehrer RI, Kokryakov VN, Hoffmann R. De novo sequencing of two new cyclic theta-defensins from baboon (Papio hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass spectrometry. DRAMP03197 RCVCTRGFCRCVCTRGFC 18 PhTD-3 (PhTD3; primates, mammals, animals) P86722, P86723 Not found Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database In low salt conditions: Escherichia coli ML35p (MIC=1.7 µM), Listeria monocytogenes EGD (MIC=1.5 µM), Staphylococcus aureus ATCC 33591 (MIC=1.7 µM), Candida albicans 820 (MIC=1.4 µM);##At high physiological salt concentrations: Escherichia coli ML35p (MIC=2.2 µM), Listeria monocytogenes EGD (MIC=1.9 µM), Staphylococcus aureus ATCC 33591 (MIC=4.5 µM), Candida albicans 820 (MIC=7.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys11; Cys4 and Cys9; Cys13 and Cys18. L No cytotoxicity information found Not found 20155756 Rapid Commun Mass Spectrom. 2010 Mar 15;24(5):599-604. Stegemann C, Tsvetkova EV, Aleshina GM, Lehrer RI, Kokryakov VN, Hoffmann R. De novo sequencing of two new cyclic theta-defensins from baboon (Papio hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass spectrometry. DRAMP03198 ACYCRIPACFAGERRYGTCFYLGRVWAFCC 30 Alpha-defensin PhD-4 (primates, mammals, animals) P86724 Belongs to the alpha-defensin family Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial activity in low salt conditions, and the antimicrobial activity decreases significantly at high physiological salt concentrations. PTM: Contains three disulfide bonds (By similarity)." In low salt conditions: Gram-negative bacterium: E. coli ML35p (MIC=2.4 µM),;##Gram-positive bacteria: Listeria monocytogenes EGD (MIC=2.2 µM), methicillin-resistant S. aureus ATCC 33591 (MIC=3.5 µM).##Fungi: Candida albicans 820 (MIC=3.9 µM).##At high physiological salt concentrations: E. coli ML35p (MIC=7.1 µM), L. monocytogenes EGD (MIC=1.8 µM), S. aureus ATCC 33591 (MIC>50 µM), Candida albicans 820 (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys2 and Cys30). Disulfide bonds between Cys2 and Cys30; Cys4 and Cys19; Cys9 and Cys29. L Not included yet Not found 20155756 Rapid Commun Mass Spectrom. 2010 Mar 15;24(5):599-604. Stegemann C, Tsvetkova EV, Aleshina GM, Lehrer RI, Kokryakov VN, Hoffmann R. De novo sequencing of two new cyclic theta-defensins from baboon (Papio hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass spectrometry. DRAMP03215 ZCRRLCYKQRCVTYCRGR 18 Gomesin (Gm; spiders, Arthropods, animals) P82358, Q86RA2 Not found Not found Acanthoscurria gomesiana (Tarantula spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Protein level Beta strand Gm adopts a well-defined β-hairpin-like struc ture, and the disulfide bonds have been reported to be important for the maintenance of this structure. 1KFP resolved by NMR. [Ref.10942757]Function: Gomesin bound to the cell surface of cryptococci neoformans, which resulted in cell death associated with membrane permeabilization (FEMS Microbiol Lett. 2007 Sep;274(2):279-86). Also, this peptide triggers SH-SY5Y cell death through L-type channel calcium influx, MAPK/ERK, PKC and PI3K signaling and generation of reactive oxygen species (Soletti RC et al 2010 Chem Biol Interact 186: 135-43). Although represented by E, the N-terminal residue is a pyroglutamate. In hemocytes only, but not in all hemocytes observed.##[Ref.28741926]Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.10942757]Gram-positive bacteria: Aerococcus viridans (MIC=0.8-1.6 µM), Bacillus cereus (MIC=6.25-12.5 µM), Bacillus megaterium (MIC=0.2-0.4 µM), Bacillus thuringiensis (MIC=1.6-3.15 µM), Enterococcus faecalis (MIC=6.2-12.5 µM), Listeria monocytogenes (MIC=0.8-1.6 µM), Micrococcus luteus (MIC=0.4-0.8 µM), Pediococcus acidolacrici (MIC=3.15-6.25 µM), Staphylococcus aureus (MIC=1.6-3.15 µM), S. epidermidis (MIC=0.8-1.6 µM), S. haemolyticus (MIC=0.8-1.6 µM), S. saprophyticus (MIC=0.8-1.6 µM), Streptococcus pyogenes (MIC=1.6-3.15 µM), Nocardia asteroides (MIC=1.6-3.15 µM);##Gram-negative bacteria: Alcaligenes faecalis (MIC>100 µM), Escherichia coli 1106 (MIC=0.8-1.6 µM), E. coli D22 (MIC=0.4-0.8 µM), E. coli D31 (MIC=0.8-1.6 µM), E. coli SBS363 (MIC=0.4-0.8 µM), Erwinia carolovora carolovora (MIC=3.15-6.25 µM), Enterobacter cloacae beta 12 (MIC=3.15-6.25 µM), Klebsiella pneumoniae (MIC=3.15-6.25 µM), Pseudomonas aeruginosa (MIC=1.6-3.15 µM), Salmonella typhimurium (MIC=0.8-1.6 µM), Xhantomonas campestris pv. orizae (MIC=3.15-6.25 µM).##Fungi: Alternaria brassicola (MIC=0.4-0.8 µM), Aspergillus fumigatus (MIC=1.6-3.15 µM), Beauveria bassiana (MIC=12.5-25 µM), Fusarium culmorum (MIC=0.4-0.8 µM), F. oxysporum (MIC=0.4-0.8 µM), Neurospora crassa (MIC=0.4-0.8 µM), Nectria haematococca (MIC=0.2-0.4 µM), Tricoderma viridae (MIC=0.4-0.8 µM), Tricophvton mentagrophytes (MIC=0.8-1.6 µM), C. albicans (MIC=0.15-0.3 µM), C. glabrata (MIC=12.5-25 µM), C. tropicalis (MIC=3.15-6.25 µM), C. neoformans (MIC=0.8-1.6 µM), Saccharomyces cerevisiae (MIC=1.6-3.15 µM).##[Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=32 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=4 μM), Klebsiella pneumoniae ATCC 700603 (MIC=32 μM), Acinetobacter baumannii ATCC 19606 (MIC=4-8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μM), Helicobacter pylori ATCC 43504 (MIC>80 μM);##Fungi : Candida albicans ATCC 90028 (MIC=8-16 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5-1 μM) [Ref.28741926] It has 0% hemolysis at 6 μM , 3% hemolysis at 10 μM , 10% hemolysis at 5 μM , 41.2-53.2% hemolysis at 64 μM , 50% hemolysis at 100 μM against human red blood cells Cyclic pyroglutamic acid Amidation Disulfide bond between Cys2 and Cys15,Cys6 and Cys11. L [Ref.28741926] CC50 = 67.0 ± 5.0 μM against CRL-1739, CC50 = 3.7 ± 0.2 μM against MM96L, CC50 = 49.9 ±16.6μM against HFF-1, CC50 =54.1±5.0 μM against HeLa, CC50 = 3.8 ± 0.3 μM against K-562. Not found 10942757##28741926 J Biol Chem. 2000 Oct 27;275(43):33464-33470.##ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.  Silva PI Jr, Daffre S, Bulet P.##Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family.##Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP03216 GIRCPKSWKCKAFKQRVLKRLLAMLRQHAF 30 Oxyopinin-4a (Oxt-4a; spiders, Arthropods, animals) F8J4S0, P86350 Not found Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 2L3I resolved by NMR. "Function: Disrupts cell membranes through the formation of pores Probable. Has antibacterial activity. Has hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: Contains one disulfide bond 4-10." [Ref.21933345]Gram-positive bacteria: S. aureus (MIC=10 µM) and Bacillus subtilis (MIC=0.5 µM);##Gram-negative bacteria: P. fluorescens (MIC=1 µM) and E. coli (MIC=0.5 µM). [Ref.21933345] EC50=7 μM against human erythrocytes Cyclic Free Free Disulfide bond between Cys4 and Cys10. L No cytotoxicity information found Cell membrane (Probable) 21933345 FEBS J. 2011 Nov;278(22):4382-4393. Dubovskii PV, Vassilevski AA, Samsonova OV, Egorova NS, Kozlov SA, Feofanov AV, Arseniev AS, Grishin EV. Novel lynx spider toxin shares common molecular architecture with defense peptides from frog skin. DRAMP03217 FRGLAKLLKIGLKSFARVLKKVLPKAAKAGKALAKSMADENAIRQQNQ 48 M-oxotoxin-Ot1a (Oxyopinin-1, Oxki1; spiders, Arthropods, animals) P83247 Not found Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Protein level Alpha helix Not found Function: Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity against Gram-negative bacterium E. coli, Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep erythrocytes. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides. [Ref.11976325]Gram-negative bacterium: Escherichia coli (MIC=1.6 µM);##Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus (MIC=6.2 µM). [Ref.11976325]100% hemolytic activity at 50 µM against sheep red blood cells Linear Free Free Free L Not included yet Cell membrane 11976325##15328050 J Biol Chem. 2002 Jun 28;277(26):23627-23637.##Biochim Biophys Acta. 2004 Aug 30;1664(2):182-188. Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T.##Belokoneva OS, Satake H, Mal'tseva EL, Pal'mina NP, Villegas E, Nakajima T, Corzo G. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins.##Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size. DRAMP03222 GFGALFKFLAKKVAKTVAKQAAKQGAKYVVNKQME 35 M-ctenitoxin-Cs1a (M-CNTX-Cs1a; Cupiennin-1a; spiders, Arthropods, animals) P83619 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Protein level Alpha helix (3 helices; 11 residues) The peptide adopts a helix-hinge-helix structure in a membrane mimicking solvent. The hinge may play a role in allowing the amphipathic N-terminal helix and polar C-terminal helix to orient independently upon membrane binding, in order to achieve maximal antibacterial efficacy.(Ref.2) 2K38 resolved by NMR. Function: Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function: with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. LD50 is 5.9 pmol/mg on Drosophila. [Ref.11792701]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.31-0.63 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=0.31-0.63 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=0.31-0.63 µM), Enterococcus faecalis ATCC 29212 (MIC=2.50-5.00 µM). [Ref.11792701]EC50=24.4 μM against human red blood cells. Linear Free Amidation Free L Not included yet calcium calmodulin 11792701##17319697 J Biol Chem. 2002 Mar 29;277(13):11208-11216.##Biochemistry. 2007 Mar 20;46(11):3576-3585. Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W.##Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae).##Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers. DRAMP03225 GFGSLFKFLAKKVAKTVAKQAAKQGAKYVANKHME 35 M-ctenitoxin-Cs1d (M-CNTX-Cs1d; Cupiennin-1d; spiders, Arthropods, animals) P83622 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial activity. Has insecticidal activity. Probably acts by disturbing membrane Function: with its amphipathic structure. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 6.4 pmol/mg on Drosophila." [Ref.11792701]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.08-0.16 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=0.16-0.31 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=0.63-1.25 µM), Enterococcus faecalis ATCC 29212 (MIC=1.25-2.50 µM). [Ref.11792701]Not determined Linear Free Amidation Free L Not included yet Not found 11792701##10669026 J Biol Chem. 2002 Mar 29;277(13):11208-11216.##Toxicon. 2000 Mar;38(3):373-380. Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W.##Haeberli S, Kuhn-Nentwig L, Schaller J, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae).##Characterisation of antibacterial activity of peptides isolated from the venom of the spider Cupiennius salei (Araneae: Ctenidae). DRAMP03226 SMWSGMWRRKLKKLRNALKKKLKGE 25 M-zodatoxin-Lt1a (M-ZDTX-Lt1a; Latarcin-1, Ltc-1, Ltc1; spiders, Arthropods, animals) Q1ELT9 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 16 residues) The Ltc1 molecule is found to form a straight uninterrupted amphiphilic helix comprising 8-23 residues. The hydrophobic surface of the Ltc1 helix is narrow-shaped and extends with no gradient along the axis. (Ref.2) 2PCO resolved by NMR. Function: Has hemolytic activity against Rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.5 µM), Bacillus subtilis VKM B-501 (MIC=1.0 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=1.0 µM), Escherichia coli MH1 (MIC=0.7µM), Pseudomonas aeruginosa PAO1 (MIC=4.1 µM);##Fungi: Pichia pastoris GS115 (MIC=17 µM), Saccharomyces cerevisiae Y190 (MIC>33 µM). [Ref.16735513]20% hemolytic activity at 80 μM against rabbit erythrocytes Linear Free Free Free L Not included yet Not found 16735513##18293934 J Biol Chem. 2006 Jul 28;281(30):20983-20992.##Biochemistry. 2008 Mar 18;47(11):3525-3533. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV.##Dubovskii PV, Volynsky PE, Polyansky AA, Karpunin DV, Chupin VV, Efremov RG, Arseniev AS. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity.##Three-dimensional structure/hydrophobicity of latarcins specifies their mode of membrane activity. DRAMP03227 GLFGKLIKKFGRKAISYAVKKARGKH 26 M-zodatoxin-Lt2a (M-ZDTX-Lt2a; Latarcin-2a, Ltc-2a, Ltc2a; spiders, Arthropods, animals) Q1ELU1 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (2 helices; 18 residues) The molecule of Ltc2a is found to consist of two helical regions (residues 3-9 and 13-21) connected via a poorly ordered fragment. 2G9P resolved by NMR. Function: Has hemolytic activity against Rabbit erythrocytes and has toxicity to ovarian insect Sf9 cells (EC50=20 µM). Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.7 µM), Bacillus subtilis VKM B-501 (MIC=0.4 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=1.0 µM), Escherichia coli MH1 (MIC=0.7 µM), Pseudomonas aeruginosa PAO1 (MIC=6.7 µM);##Fungi: Pichia pastoris GS115 (MIC=6.7 µM), Saccharomyces cerevisiae Y190 (MIC=54 µM). [Ref.16735513]20% hemolytic activity at 6 μM against rabbit erythrocytes Linear Free Free Free L Not included yet Not found 16735513##16939228 J Biol Chem. 2006 Jul 28;281(30):20983-20992.##Biochemistry. 2006 Sep 5;45(35):10759-10767. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV.##Dubovskii PV, Volynsky PE, Polyansky AA, Chupin VV, Efremov RG, Arseniev AS. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity.##Spatial structure and activity mechanism of a novel spider antimicrobial peptide. DRAMP03229 SWKSMAKKLKEYMEKLKQRA 20 M-zodatoxin-Lt3a (M-ZDTX-Lt3a; Latarcin-3a, Ltc-3a; spiders, Arthropods, animals) Q1ELU3 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has hemolytic activity against Rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland." [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.3 µM), Bacillus subtilis VKM B-501 MIC=1.2 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=2.5 µM), Escherichia coli MH1 (MIC=6.0 µM), Pseudomonas aeruginosa PAO1 (MIC>40 µM);##Fungi: Pichia pastoris GS115 (MIC=20 µM), Saccharomyces cerevisiae Y190 (MIC=20 µM). [Ref.16735513]20% hemolytic activity at >120 μM against rabbit erythrocytes Linear Free Amidation Free L Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-209892. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03230 SWASMAKKLKEYMEKLKQRA 20 M-zodatoxin-Lt3b (M-ZDTX-Lt3b; Latarcin-3b, Ltc-3b; spiders, Arthropods, animals) Q1ELU2 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has hemolytic against Rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland." [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.7 µM), Bacillus subtilis VKM B-501 (MIC=2.9 µM);Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=23 µM), Escherichia coli MH1 (MIC=28 µM), Pseudomonas aeruginosa PAO1 (MIC>45 µM);##Fungi: Pichia pastoris GS115 (MIC=23 µM), Saccharomyces cerevisiae Y190 (MIC=23 µM). [Ref.16735513]20% hemolytic activity at >120 μM against rabbit erythrocytes Linear Free Amidation Free L Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-209892. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03231 GLKDKFKSMGEKLKQYIQTWKAKF 24 M-zodatoxin-Lt4a (M-ZDTX-Lt4a; Latarcin-4a, Ltc-4a; spiders, Arthropods, animals) Q1ELU5 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has hemolytic activity against Rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland." [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.3 µM), Bacillus subtilis VKM B-501 (MIC=1.1 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=4.5 µM), Escherichia coli MH1 (MIC=3.2 µM), Pseudomonas aeruginosa PAO1 (MIC>35 µM);##Fungi: Pichia pastoris GS115 (MIC=36 µM), Saccharomyces cerevisiae Y190 (MIC=18 µM). [Ref.16735513]20% hemolytic activity at >120 μM against rabbit erythrocytes Linear Free Amidation Free L Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-209892. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03232 SLKDKVKSMGEKLKQYIQTWKAKF 24 M-zodatoxin-Lt4b (M-ZDTX-Lt4b; Latarcin-4b, Ltc-4b; spiders, Arthropods, animals) Q1ELU4 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has hemolytic activity against Rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland." [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.3 µM), Bacillus subtilis VKM B-501 (MIC=1.1 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=4.4 µM), Escherichia coli MH1 (MIC=4.4 µM), Pseudomonas aeruginosa PAO1 (MIC>35 µM);##Fungi: Pichia pastoris GS115 (MIC>35 µM), Saccharomyces cerevisiae Y190 (MIC=35 µM). [Ref.16735513]20% hemolytic activity at >120 μM against rabbit erythrocytes Linear Free Amidation Free L Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-209892. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03233 GFFGKMKEYFKKFGASFKRRFANLKKRL 28 M-zodatoxin-Lt5a (M-ZDTX-Lt5a; Latarcin-5, Ltc-5; spiders, Arthropods, animals) Q1ELU9 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Has antimicrobial activity against Gram-positive bacteria and Gram-negative bacteria and and yeasts. Also has hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland. PTM: Leucine amide at L28." [Ref.16735513]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=1.1 µM), Bacillus subtilis VKM B-501 (MIC=0.6 µM);##Gram-negative bacteria: Escherichia coli DH5-alpha (MIC=0.6 µM), Escherichia coli MH1 (MIC=0.6 µM), Pseudomonas aeruginosa PAO1 (MIC=18 µM);##Fungi: Pichia pastoris GS115 (MIC>37 µM), Saccharomyces cerevisiae Y190 (MIC>37 µM). [Ref.16735513]20% hemolytic activity at 40 μM against rabbit erythrocytes Linear Free Amidation Free L Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-20992. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03236 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 M-zodatoxin-Lt8a (M-ZDTX-Lt8a; Cytoinsectotoxin-1a, CIT-1a; spiders, Arthropods, animals) P85253, B3W6H9 Belongs to the cytoinsectotoxin family cit 1-1 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Protein level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S. carnaria, and against the cockroach N. cinerea. CIT 1a Has hemolytic activity against human erythrocytes, and cytolytic activity against insect Sf9 cells in the same concentration range. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 5 µg/g for adult and 20 µg/g for larvae of flesh fly S. carnaria. LD50 is 500 µg/g for cockroach N. cinerea." [Ref.18215128]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.5 µM), Bacillus subtilis VKM B-501 (MIC=0.9 µM), Micrococcus luteus (MIC>30 µM), Staphylococcus aureus (MIC>30 µM);##Gram-negative bacteria: Escherichia coli C600 (MIC=0.5 µM), E. coli DH5alpha (MIC=0.9 µM), E. coli MH1 (MIC=0.5 µM), Pseudomonas aeruginosa PAO1 (MIC=1.9 µM), Pseudomonas fluorescens VKM B-894 (MIC=3.8 µM). [Ref.18215128]EC50=6 μM against human erythrocytes Linear Free Free Free L Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03253 GKLQAFLAKMKEIAAQTL 18 M-lycotoxin-Ls3a (M-LCTX-Ls3a; Lycocitin-1; spiders, Arthropods, animals) P0C2U6 Not found Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Inhibits growth of Gram-positive and Gram-negative bacteria and fungi. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus, Bacillus subtilis ATCC6633 (MIC=1.6-3.2 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=3.2-6.4 µM), Pseudomonas aeruginosa.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 14991689 J Mass Spectrom. 2004 Feb;39(2):193-201. Budnik BA, Olsen JV, Egorov TA, Anisimova VE, Galkina TG, Musolyamov AK, Grishin EV, Zubarev RA. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. DRAMP03254 GRLQAFLAKMKEIAAQTL 18 M-lycotoxin-Ls3b (M-LCTX-Ls3b; Lycocitin-2; spiders, Arthropods, animals) P0C2U7 Not found Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Inhibits growth of Gram-positive and Gram-negative bacteria and fungi. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus 209P, Bacillus subtilis ATCC 6633 (MIC=1.57-3.14 µM);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=3.14-6.29 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=5.02-10.05 µM).##Fungi: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 14991689 J Mass Spectrom. 2004 Feb;39(2):193-201. Budnik BA, Olsen JV, Egorov TA, Anisimova VE, Galkina TG, Musolyamov AK, Grishin EV, Zubarev RA. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. DRAMP03278 IWLTALKFLGKHAAKHLAKQQLSKL 25 M-lycotoxin-Hc1a (M-LCTX-Hc1a; Lycotoxin I; spiders, Arthropods, animals) P61507 Not found Not found Hogna carolinensis (Carolina wolf spider) (Lycosa carolinensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found Function: Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane. Potently inhibits the growth of bacteria, yeast and Leishmania. Is lethal to lepidopteran larvae. May Function: both in the prey capture strategy as well as protection from infectious organisms arising from prey ingestion. Gram-positive bacteria: Bacillus thuringiensis subsp. Israelensis (MIC<5.0 µM);##Gram-negative bacteria: Escherichia coli D31 (MIC=10-20 µM), Escherichia coli DH5 (MIC=80-150 µM).##Fungi: Candida glabrata ATCC 2001 (MIC=100-150 µM), Candida albicans clinical isolate (MIC=100-200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 9442044##18098329 J Biol Chem. 1998 Jan 23;273(4):2059-2066.##J Pept Sci. 2008 Apr;14(4):528-534. Yan L, Adams ME.##Adão R, Seixas R, Gomes P, Pessoa JC, Bastos M. Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis.##Membrane structure and interactions of a short Lycotoxin I analogue. DRAMP03279 KIKWFKTMKSIAKFIAKEQMKKHLGGE 27 M-lycotoxin-Hc2a (M-LCTX-Hc2a; Lycotoxin-2; Lycotoxin II; spiders, Arthropods, animals) P61508 Not found Not found Hogna carolinensis (Carolina wolf spider) (Lycosa carolinensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found Function: Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane. Potently inhibits the growth of bacteria, yeast and Leishmania. May Function: both in the prey capture strategy as well as protection from infectious organisms arising from prey ingestion. Gram-positive bacteria: Bacillus thuringiensis subsp. Israelensis (MIC=10-60 µM);##Gram-negative bacteria: Escherichia coli D31 (MIC<10 µM), Escherichia coli DH5 (MIC<40 µM).##Fungi: Candida glabrata ATCC 2001 (MIC=100-150 µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Cell membrane 9442044##18098329 J Biol Chem. 1998 Jan 23;273(4):2059-2066.##J Pept Sci. 2008 Apr;14(4):528-534. Yan L, Adams ME.##Adão R, Seixas R, Gomes P, Pessoa JC, Bastos M. Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis.##Membrane structure and interactions of a short Lycotoxin I analogue. DRAMP03280 ATYDGKCYKKDNICKYKAQSGKTAICKCYVKVCPRDGAKCEFDSYKGKCYC 51 AcAMP (A. clavatus antimicrobial peptide) No entry found Not found Not found Aspergillus clavatus ES1 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Not found Not found Not found This basic, Cys-rich antifungal peptide is also active against bacteria. AcAMP was sensitive to proteolytic enzymes, stable between pH 5.0 and 10.0, and heat resistant (15 min at 100 degrees C). Gram-positive bacteria: Staphylococcus aureus (MIC=20 µg/ml), Bacillus cereus (MIC=10 µg/ml), Micrococcus luteus (MIC=10 µg/ml), Enterococcus faecalis (MIC=50 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=30 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml).##Fungi: Aspergillus niger, Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys33 and Cys51). Disulfide bonds between Cys7 and Cys26,Cys14 and Cys40,Cys28 and Cys49,Cys33 and Cys51. L Not included yet Not found 20440534 J Ind Microbiol Biotechnol. 2010 Aug;37(8):805-813. Hajji M, Jellouli K, Hmidet N, Balti R, Sellami-Kamoun A, Nasri M. A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization. DRAMP03285 LFCRKGTCHFGGCPAHLVKVGSCFGFRACCKWPWDV 36 Ostricacin-1 (Beta-defensin 2; Birds, animals) P85113 Belongs to the beta-defensin family Not found Struthio camelus (Ostrich) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found PTM: Contains three disulfide bonds 3-29; 8-23; 13-30. Gram-positive bacteria: Staphylococcus aureus 1056-MRSA (MIC=1.25 µg/ml), S. aureus NCTC 4163 (MIC=6.7 µg/ml);##Gram-negative bacteria: Escherichia coli O157:H7 (MIC=0.96 µg/ml), E. coli 0111 (MIC=6.7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys29,Cys8 and Cys23,Cys13 and Cys30. L No cytotoxicity information found Not found 16459058 Biotechnol Lett 2001; 23: 207-210.##Int J Antimicrob Agents. 2006 Mar;27(3):229-235. Yu, PL, Choudhury SD, Ahrens K.##Sugiarto H, Yu PL. Purification and characterization of the antimicrobial peptide, ostricacin.##Identification of three novel ostricacins: an update on the phylogenetic perspective of beta-defensins. DRAMP03286 APGNKAECEREKGYCGFLKCSFPFVVSGKCSRFFFCCKNIW 41 Ostricacin-2 (Beta-defensin 1; Birds, animals) P85114 Belongs to the beta-defensin family Not found Struthio camelus (Ostrich) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found PTM: Contains three disulfide bonds 8-36; 15-30; 20-37. Gram-positive bacterium: Staphylococcus aureus 1056-MRSA (MIC=1.25 µg/ml);##Gram-negative bacterium: Escherichia coli O157:H7 (MIC=0.96 µg/ml);##Yeast: Candida albicans 3153A (MIC=6.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys8 and Cys36,Cys15 and Cys30,Cys20 and Cys37. L No cytotoxicity information found Not found 16459058 Int J Antimicrob Agents. 2006 Mar;27(3):229-235. Sugiarto H, Yu PL. Identification of three novel ostricacins: an update on the phylogenetic perspective of beta-defensins. DRAMP03287 IPRPLDPCIAQNGRCFTGICRYPYFWIGTCRNGKSCCRRR 40 Ostricacin-3 (Beta-defensin 7; Birds, animals) P85115 Belongs to the beta-defensin family Not found Struthio camelus (Ostrich) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found PTM: Contains three disulfide bonds 8-36; 15-30; 20-37. Gram-positive bacterium: Staphylococcus aureus 1056-MRSA (MIC=2.78 µg/ml);##Gram-negative bacterium: Escherichia coli O157:H7 (MIC=2.41 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys8 and Cys36,Cys15 and Cys30,Cys20 and Cys37. L No cytotoxicity information found Not found 16459058 Int J Antimicrob Agents. 2006 Mar;27(3):229-235. Sugiarto H, Yu PL. Identification of three novel ostricacins: an update on the phylogenetic perspective of beta-defensins. DRAMP03288 LPVNEAQCRQVGGYCGLRICNFPSRFLGLCTRNHPCCSRVWV 42 Ostricacin-4 (Beta-defensin 8; Birds, animals) P85116 Belongs to the beta-defensin family Not found Struthio camelus (Ostrich) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found PTM: Contains three disulfide bonds 8-36; 15-30; 20-37. Gram-positive bacterium: Staphylococcus aureus 1056-MRSA (MIC=11.48 µg/ml);##Gram-negative bacterium: Escherichia coli O157:H7 (MIC=12.03 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys8 and Cys36,Cys15 and Cys30,Cys20 and Cys37. L No cytotoxicity information found Not found 16459058 Int J Antimicrob Agents. 2006 Mar;27(3):229-235. Sugiarto H, Yu PL. Identification of three novel ostricacins: an update on the phylogenetic perspective of beta-defensins. DRAMP03311 RGFRKHFNKLVKKVKHTISETAHVAKDTAVIAGSGAAVVAAT 42 Stomoxyn (Insects, animals) Q8T9R8 Not found Not found Stomoxys calcitrans (Stable fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (4 helices; 32 residues) Stomoxyn adoptS a flexible random coil structure in water while both assume a stable helical structure in the presence of TFE. In 50% TFE, the structure of stomoxyn is typical of cecropins, including an amphipathic helix at the N-terminus and a hydrophobic C-terminus with helical features that probably fold in a helical conformation at higher TFE concentration. (Ref.2) 1ZRX resolved by NMR. "Function: Has antimicrobial activity against most Gram-positive and Gram-negative bacteria, filamentous fungi and yeasts tested. Has trypanolytic effect on T.b.rhodesiense and hemolytic activity against bovine red blood cells. May play an important role in protecting the stored blood in the anterior midgut from microorganisms prior to digestion. Adopts an amphipathic alpha-helical structure only in the presence of an organic solvent that mimics a phospholipid membrane. Tissue specificity: Constitutively expressed in the adult anterior midgut; proventriculus, thoracic and reservoir regions." [Ref.12372834]Gram-negative bacteria: Escherichia coli K12 RM148 (MIC=0.19-0.39 µM), E. coli D22 (MIC=0.19-0.39 µM), E. coli D31(MIC=0.19-0.39 µM), E. coli SBS363 (MIC<0.19 µM), E. coli 1106 (MIC=0.19-0.39 µM), Enterobacter cloacae b12 (MIC=3.12-6.25 µM), Erwinia carotovora (MIC=0.78-1.56 µM), Klebsiella pneumoniae (MIC=0.78-1.56 µM), Pseudomonas aeruginosa (MIC=0.39-0.78 µM), Salmonella typhimurium (MIC=0.39-0.78 µM), Xanthomonas campestris ( MIC=0.39-0.78 µM);##Gram-positive bacteria: Aerococcus viridans (MIC=0.78-1.56 µM), Bacillus megaterium (MIC=0.78-1.56 µM), Bacillus subtilis (MIC=6.25-12.5 µM), Enterococcus faecalis (MIC=0.78-1.56 µM), Micrococcus luteus (MIC=0.78-1.56 µM), Streptococcus pyogenes (MIC=1.56-3.12 µM);##Fungi: Aspergillus fumigatus (MIC=50-100 µM), Fusarium culmorum (MIC=0.39-0.78 µM), Fusarium oxysporum (MIC=0.78-1.56 µM), Nectria haematococca (MIC=0.39-0.78 µM), N. crassa (MIC=3.12-6.25 µM), Trichoderma viride (MIC=1.56-3.12 µM), Trichophyton mentagrophytes (MIC=3.12-6.25 µM), Candida albicans (MIC=25-50 µM), C. glabrata (MIC=25-50 µM), C. neoformans (MIC=0.78-1.56 µM). [Ref.12372834]2% hemolytic activity at 10 μM, 9% hemolytic activity at 100 μM against bovine red blood cells Linear Free Amidation Free L Not included yet Not found 12372834##16170803 J. Biol. Chem. 2002; 277: 49921-49926.##Biopolymers. 2006 Feb 5;81(2):92-103. Nathalie Boulanger, Rebecca J. L. Munks, Joanne V. Hamilton, Françoise Vovelle, Reto Brun, Mike J. Lehane, and Philippe Bulet.##Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F. Epithelial innate immunity. A novel antimicrobial peptide with antiparasitic activity in the blood-sucking insect Stomoxys calcitrans.##Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation. DRAMP03312 VDKPDYRPRPRPPNM 15 Metalnikowin-1 (Metalnikowin I; Insects, animals) P80408 Not found Not found Palomena prasina (Green shield bug) (Cimex prasinus) Antimicrobial, Antibacterial, Anti-Gram- Protein level Rich Not found "Function: Antibacterial peptide active against Gram-negative bacteria. Induction: By bacterial infection." Gram-negative bacteria: Escherichia coli D22 (MIC=50-100 µM), Salmonella typhimurium (MIC=50-100 µM), Alcaligenes faecalis (MIC=50-100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found PubMed ID is not available J. Insect Physiol. 1996; 42: 81-89. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin. DRAMP03320 GEILCNLCTGLINTLENLLTTKGADKVKDYISSLCNKASGFIATLCTKVLDFGIDKLIQLIEDKVDANAICAKIHAC 77 Pore-forming peptide ameobapore A (EH-APP; saposin-like protein) P34095, Q24839 Not found Not found Entamoeba histolytica (protozoan parasite) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (5 helices; 53 residues) Amoebapore A belongs to the superfamily of saposin-like proteins that are characterized by a conserved disulfide bond pattern and a fold consisting of five helices.(Ref.3) 1OF9 resolved by NMR. Forms pores in the cytoplasmic membrane of host cells. Implicated in the cytolytic activity of the parasite. Gram-positive bacteria: Micrococcus luteus (MIC=1.9 µM), Bacillus megaterium (MIC=13 µM), Bacillus subtilis (MIC=27 µM), Staphylococcus aureus (MIC>15 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys5 and Cys77). Disulfide bonds between Cys5 and Cys77,Cys8 and Cys71,Cys35 and Cys46. L No cytotoxicity information found Cell membrane 7715451##8146160##14970207 Mol Microbiol. 1994 Dec;14(5):895-904.##Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2602-2606.##J Biol Chem. 2004 Apr 23;279(17):17834-41. Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ.##Leippe M, Andrä J, Müller-Eberhard HJ.##Hecht O, Van Nuland NA, Schleinkofer K, Dingley AJ, Bruhn H, Leippe M, Grötzinger J. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes.##Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.##Solution structure of the pore-forming protein of Entamoeba histolytica. DRAMP03321 VISIIPV 7 Colutellin-A P86168 Not found Not found Colletotrichum dematium (Anthracnose fungus) Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Sclerotinia sclerotiorum (MIC=32.4 µg/ml after 288 hours), Botrytis cinerea (MIC=10.8 µg/ml after 288 hours),Fusarium solani, Aspergillus fumigatus, Geotrichum candidum. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Free L [Ref.18599825] It has less cytotoxicity against human PBMCs. Not found 18599825 Microbiology. 2008 Jul;154(Pt 7):1973-1979. Ren Y, Strobel GA, Graff JC, Jutila M, Park SG, Gosh S, Teplow D, Condron M, Pang E, Hess WM, Moore E. Colutellin A, an immunosuppressive peptide from Colletotrichum dematium. DRAMP03370 QLINSPVTCMSYGGSCQRSCNGGFRLGGHCGHPKIRCCRRK 41 Beta-defensin 6 (BD-6, mBD-6; Defensin, beta 6; Rodents, mammals, animals) Q91VD6 Belongs to the beta-defensin family Defb6 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found "PTM: Contains three disulfide bonds 9-37; 16-30; 20-38. Predominantly expressed in skeletal muscle, also expressed in esophagus, tongue, and trachea. Also expressed in lung when induced by lipopolysaccharide. Expressed constitutively and induced by lipopolysaccharide (LPS)." Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys9 and Cys37,Cys16 and Cys30,Cys20 and Cys38. L No cytotoxicity information found Not found 11408484 J Biol Chem. 2001 Aug 24;276(34):31510-31514. Yamaguchi Y, Fukuhara S, Nagase T, Tomita T, Hitomi S, Kimura S, Kurihara H, Ouchi Y. A novel mouse beta-defensin, mBD-6, predominantly expressed in skeletal muscle. DRAMP03405 GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE 33 mCRAMP-1 (mouse cathelin-related antimicrobial peptide 1; cathelicidin; Rodents, mammals, animals P51437, Q0VB78 Not found Camp Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Alpha helix (CD) The spectra of 10-25 µm synthetic CRAMP-1 in buffer suggest that the peptide is in a random coil configuration and that it will assume a helical structure in the presence of 15–45% (v/v) trifluoroethanol. "Function: Acts as a potent antimicrobial peptide. Tissue specificity: Expressed in testis, spleen, stomach, and intestine. Very low expression found in heart, lung and skeletal muscle. No expression in brain, kidney or liver." Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli ML35 (MIC=2 µM), Escherichia coli D21 (MIC=8 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µM), Serratia marcescens ATCC 8100 (MIC=4 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=32 µM), Staphylococcus aureus Cowan I (MIC=32 µM), Staphylococcus aureus (MRSA) (MIC>64 µM), Staphylococcus aureus (MRSA) (MIC=64 µM), Staphylococcus epidermidis ATCC 12228 (MIC=16 µM), Streptococcus faecalis ATCC 29212 (MIC=16 µM), Bacillus megaterium Bm11 (MIC=4 µM).##Fungi: Candida albicans (MIC>64 µM), Cryptococcus neoformans (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 9148921##8706928 J Biol Chem. 1997 May 16;272(20):13088-13093.##FEBS Lett. 1996 Aug 5;391(1-2):5-8. Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R.##Popsueva AE, Zinovjeva MV, Visser JW, Zijlmans JM, Fibbe WE, Belyavsky AV. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse.##A novel murine cathelin-like protein expressed in bone marrow. DRAMP03406 ISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE 38 mCRAMP-2 (mouse cathelin-related antimicrobial peptide 2; cathelicidin; Rodents, mammals, animals P51437, Q0VB78 Not found Camp Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Alpha helix (CD) The CD spectra of CRAMP-2 (not shown) were similar to CRAMP-1. "Function: Acts as a potent antimicrobial peptide. Tissue specificity: Expressed in testis, spleen, stomach, and intestine. Very low expression found in heart, lung and skeletal muscle. No expression in brain, kidney or liver." Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli ML35 (MIC=2 µM), Escherichia coli D21 (MIC=8 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µM), Serratia marcescens ATCC 8100 (MIC=4 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=32 µM), Staphylococcus aureus Cowan I (MIC=32 µM), Staphylococcus aureus (MRSA) (MIC>64 µM), Staphylococcus aureus (MRSA) (MIC=64 µM), Staphylococcus epidermidis ATCC 12228 (MIC=16 µM), Streptococcus faecalis ATCC 29212 (MIC=32 µM), Bacillus megaterium Bm11 (MIC=4 µM).##Fungi: Candida albicans (MIC>64 µM), Cryptococcus neoformans (MIC=16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 9148921##8706928 J Biol Chem. 1997 May 16;272(20):13088-13093.##FEBS Lett. 1996 Aug 5;391(1-2):5-8. Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R.##Popsueva AE, Zinovjeva MV, Visser JW, Zijlmans JM, Fibbe WE, Belyavsky AV. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse.##A novel murine cathelin-like protein expressed in bone marrow. DRAMP03419 VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR 32 Neutrophil antibiotic peptide NP-1 (RatNP-1; Rodents, mammals, animals) Q62716 Belongs to the alpha-defensin family Not found Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Comment: Active in vitro against S. aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus. Gram-positive bacterium: Staphylococcus aureus 502A [18 h] (MIC<100 cfu/ml);##Gram-negative bacterium: Escherichia coli ML-35 [18 h] (MIC<100 cfu/ml).##Fungi: Candida albicans 820 [18 h] (MIC<100 cfu/ml), Cryptococcus neoformans A-383 [18 h] (MIC=1.7 x 102 cfu/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L No cytotoxicity information found Not found 2543629##7594610 Infect. Immun. 1989;57:2021-2027.##J. Immunol. 1995;155:4476-4484. Eisenhauer P.B, Harwig S.S.S.L, Szklarek D, Ganz T, Selsted M.E, Lehrer R.I.##Yount N.Y, Wang MS.C, Yuan J, Banaiee N, Ouellette A.J, Selsted M.E. Purification and antimicrobial properties of three defensins from rat neutrophils.##Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis. DRAMP03422 ACYCRIGACVSGERLTGACGLNGRIYRLCCR 31 Neutrophil antibiotic peptide NP-4 (RatNP-4; Rodents, mammals, animals) Q62714 Belongs to the alpha-defensin family Np4 Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Protein level Bridge Not found Active in vitro against S. aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus. Gram-positive bacterium: Staphylococcus aureus 502A (MIC=50 µg/ml);##Gram-negative bacteria: Escherichia coli ML-35, Acinetobacter calcoaceticus (MIC=50 µg/ml).Fungi: Cryptococcus neoformans (MIC=10 µg/ml), Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29. L No cytotoxicity information found Not found 2543629##7594610 Infect. Immun. 1989;57:2021-2027.##J. Immunol. 1995;155:4476-4484. Eisenhauer P.B, Harwig S.S.S.L, Szklarek D, Ganz T, Selsted M.E, Lehrer R.I.##Yount N.Y, Wang MS.C, Yuan J, Banaiee N, Ouellette A.J, Selsted M.E. Purification and antimicrobial properties of three defensins from rat neutrophils.##Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis. DRAMP03463 GLVRKGGEKFGEKLRKIGQKIKEFFQKLALEIEQ 34 rCRAMP (rat cathelin-related antimicrobial peptide; Rodents, mammals, animals) No entry found Not found Not found Rattus norvegicus (Norway rat) Antimicrobial, Antibacterial Not found Alpha helix Not found Function: Has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [No NaCl]: Escherichia coli DH5a (MIC=0.54 µM), E. coli ML-35p (MIC=1.55 µM), Pseudomonas aeruginosa PAO1 (MIC=0.69 µM), Pseudomonas aeruginosa MR3007 (MIC=2.01 µM); Staphylococcus aureus ATCC (MRSA) 33591 (MIC=3.19 µM), Staphylococcus aureus 93918 (MIC=2.14 µM).##[100 mM NaCl]: Escherichia coli DH5a (MIC=0.61 µM), Escherichia coli ML-35p (MIC=0.66 µM), Pseudomonas aeruginosa PAO1 (MIC=1.17 µM), Pseudomonas aeruginosa MR3007 (MIC=1.78 µM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC>20.1 µM), Staphylococcus aureus 93918 (MIC=2.16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 10768969 Infect Immun. 2000 May;68(5):2748-2755. Travis SM, Anderson NN, Forsyth WR, Espiritu C, Conway BD, Greenberg EP, McCray PB Jr, Lehrer RI, Welsh MJ, Tack BF. Bactericidal activity of mammalian cathelicidin-derived peptides. DRAMP03464 GLLNGLALRLGKRALKKIIKRLCR 24 Cryptonin (Insects, animals) P85028 Not found Not found Cryptotympana dubia (Korean horse cicada) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found Function: Has very low hemolytic activity on rat erythrocytes. [Ref.18000874]Gram-positive bacteria: Bacillus subtilis KCTC 3086 (MIC=3.12 µg/ml), Staphylococcus aureus KCTC 1928 (MIC=25 µg/ml), Micrococcus luteus KCTC 3063 (MIC=1.56 µg/ml), Staphylococcus aureus (MRSA) (MIC=25 µg/ml), VRE (MIC=25 µg/ml);##Gram-negative bacteria: Escherichia coli K12-594 (MIC=3.12 µg/ml);##Fungi: Candida albicans KCTC 7965 (MIC=50 µg/ml), Candida tropicalis KCTC 1925 (MIC=3.12 µg/ml). [Ref.18000874]<5% hemolytic activity at 25-200 µg/ml against rat erythrocytes Linear Free Free Free L Not included yet Not found 18000874 Arch Insect Biochem Physiol. 2007 Dec;66(4):204-213. Leem JY, Park DS, Suh EY, Hur JH, Oh HW, Park HY. Isolation and functional analysis of a 24-residue linear alpha-helical antimicrobial peptide from Korean blackish cicada, Cryptotympana dubia (Homoptera). DRAMP03465 NEYHGFVDKANNENKRKKQQGRDDFVVKPNNFANRRRKDDYNENYYDDVDAADVV 55 Cicadin (Insects, animals) P83282 Not found Not found Cicada flammata Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Possesses antifungal activity against B.cinerea, M.arachidicola, F.oxysporum, R.solani and C.comatus. Suppresses the activity of HIV-1 reverse transcriptase and stimulates the proliferation of murine splenocytes. Fungi: Botrytis cinerea (MIC=100 nM), Mycosphaerella arachidicola (MIC=70 nM), Fusarium oxysporum (MIC=180 nM), Physalospora piricola (MIC=60 nM), Rhizoctonia solani, Coprinus comatus, HIV-1 reverse transcriptase. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 11814612 Peptides. 2002;23:7-11. Wang H, Ng TB. Isolation of cicadin, a novel and potent antifungal peptide from dried juvenile cicadas. DRAMP03467 PAQPFRFPKHPQGPQTRPPI 20 Antibacterial napin (Plants) P84529 Belongs to the 2S seed storage albumins family Not found Brassica rapa subsp. chinensis (Pak-choi) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: The small, basic, water-soluble napins are one of the two major kinds of storage proteins synthesized in the seed during its maturation. Inhibits cell-free protein synthesis. Has antibacterial activity against Gram-negative bacterium P. fluorescens, and the Gram-positive bacteria B. subtilis, B. cereus, B. megaterium and M. phei. No antibacterial activity against the Gram-positive bacterium S. aureus or the Gram-negative bacteria E. coli, E. aerogenes and P. aeruginosa. Subunit structure: The mature protein consists of a small and a large chain linked by disulfide bonds." Gram-negative bacterium: Pseudomonas fluorescens (MIC=66±3.7 µM);##Gram-positive bacteria: Bacillus subtilis (MIC=236±10.2 µM), Bacillus cereus (MIC=222±9.1 µM), Bacillus megaterium (MIC=215±6.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 15062997 Peptides. 2004 Feb;25(2):171-176. Ngai PH, Ng TB. A napin-like polypeptide from dwarf Chinese white cabbage seeds with translation-inhibitory, trypsin-inhibitory, and antibacterial activities. DRAMP03471 GFGCPGNQLKCNNHCKSISCRAGYCDAATLWLRCTCTDCNGKK 43 Recombinant Crassostrea Gigas Defensin (Cg-Def; molluscs, animals) Q4GWV4 Not found def Crassostrea gigas (Pacific oyster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Not found 2B68 resolved by NMR. Function: Has antibacterial activity (By similarity). Gram-positive bacteria: Micrococcus lysodeikticus (MIC=0.005-0.01 µM), Staphylococcus aureus (MIC=1.25-2.5 µM), Microbacterium maritypicum (MIC=0.5-1 µM), Bacillus megaterium (MIC>20 µM);##Gram-negative bacteria: Escherichia coli 363 (MIC=35-20 µM), Vibrio alginolyticus (MIC>20 µM), Salmonella typhimurium (MIC>20 µM).##Fungi: Fusarium oxysporum (MIC=9-4.5 µM), Botrytis cinerea (MIC>20 µM), Penicillium crustosum (MIC>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys4 and Cys25,Cys11 and Cys34,Cys15 and Cys36,Cys20 and Cys39. Not included yet Not included yet Lipid II 16246846 J Biol Chem. 2006 Jan 6;281(1):313-323. Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, Escoubas JM, Bulet P, Gonzalez M, Lelong C, Favrel P, Bachère E. Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression. DRAMP03472 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR 74 cgUbiquitin No entry found Not found Not found Crassostrea gigas (Pacific oyster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Combine helix and strand structure According to the homology modeling, this peptide is composed of three secondary structural motifs including three α-helices and four β-strands separated by 7 loops regions. 1AAR##1CMX##1D3Z####2AYO Function: cgUbiquitin shows broad potent antimicrobial activity against Gram-positive and -negative bacteria, without hemolytic activity. [Ref.22858580]Gram-positive bacteria: B. subtilis KCTC1021 (MIC=0.4 µM), S. aureus RM4220 (MIC=4.7 µM), S. iniae FP5229 (MIC=0.9 µM);##Gram-negative bacteria: E. coli D31 (MIC=0.2 µM), E. coli ML35p (MIC=1.4 µM), P. aeruginosa KCTC2004 (MIC=0.6 µM), S. flexneri KCTC2517 (MIC=0.7 µM), S. sonnei KCTC2009 (MIC=1.2 µM), A. hydrophila KCTC2358 (MIC=0.7 µM), V. parahemolyticus KCCM41664 (MIC=1.1 µM);##Yeast: C. albicans KCTC7965 (MIC=9.4 µM). [Ref.22858580]Non-hemolytic against human red blood cells up to 100 μg/mL Linear Free Free Free L Not included yet Not found 22858580 Mol Immunol. 2013 Jan;53(1-2):88-98. Seo JK, Lee MJ, Go HJ, Kim GD, Jeong HD, Nam BH, Park NG. Purification and antimicrobial function of ubiquitin isolated from the gill of Pacific oyster, Crassostrea gigas. DRAMP03474 VRPYLVAF 8 Pleurostatin (Fungus) P84866 Not found Not found Pleurotus ostreatus (Oyster mushroom) Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database 20% growth inhibition Fusarium oxysporum (MIC=15.6 µM).##45% growth inhibition Mycosphaerella arachidicola (MIC=15.6 µM).##63% growth inhibition Physalospora piricola (MIC=15.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 15941607 Peptides. 2005 Nov;26(11):2098-103. Epub 2005 Jun 6. Chu K.T, Xia L, Ng T.B. Pleurostrin, an antifungal peptide from the oyster mushroom DRAMP03477 ILGTILGLLKSL 12 Polybia-CP (Polybia chemotactic peptide; Venom protein CP; Insects, animals) P0C1R0, P84879 Not found Not found Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis CCT 2576 (MIC=15 µg/ml), Staphylococcus aureus ATCC 6538 (MIC=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16129513##28981608 Peptides. 2005 Nov;26(11):2157-2164.##Acta Biochim Biophys Sin (Shanghai). 2017 Oct 1;49(10):916-925. Souza BM, Mendes MA, Santos LD, Marques MR, César LM, Almeida RN, Pagnocca FC, Konno K, Palma MS.##Jia F, Wang J, Peng J, Zhao P, Kong Z, Wang K, Yan W, Wang R. Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista.##D-amino acid substitution enhances the stability of antimicrobial peptide polybia-CP. DRAMP03486 GKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH 42 Manduca Sexta Moricin (MS moricin; Insects, animals) Q86MA1 Not found Not found Manduca sexta (Tobacco hornworm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (1 helices; 31 residues) The tertiary structure is composed of an eight-turn alpha-helix spanning almost the entire peptide. Insights of relationships between the structure and function are also presented. (Ref.1) 2JR8 resolved by NMR. "Function: Exhibits potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria with a minimum inhibitory concentration of 1.4 microM. Tissue specificity: expressed in Manduca sexta fat body." Gram-negative bacteria: Klebsiella pneumoniae (MIC=6.25 µg/ml), Salmonella typhimurium (MIC=6.25 µg/ml), S. typhimurium DT104 (MIC=6.25 µg/ml), Escherichia coli O157:H7 (MIC=6.25 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25 923 (MIC=6.25 µg/ml), Methicillin-resistant S. aureus ATCC 43 300 (MIC=6.25 µg/ml), Methicillin-resistant S. aureus ATCC BAA-39 (MIC=12.5 µg/ml), Listeria monocytogenes (MIC=6.25 µg/ml).##NOTE: MIC is defined as the lowest peptide concentration that gives no visible growth after overnight incubation in 100% Muller-Hinton broth. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18265434##12706633 J Pept Sci. 2008 Jul;14(7):855-863.##Insect Biochem Mol Biol. 2003 May;33(5):541-59. Dai H, Rayaprolu S, Gong Y, Huang R, Prakash O, Jiang H.##Zhu Y, Johnson TJ, Myers AA, Kanost MR. Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin.##Identification by subtractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body. DRAMP03493 DKLIGSCVWGAVNYTSDCNGECKRRGYKGGHCGSFANVNCWCET 44 Defensin heliomicin (Insects, animals) P81544 Not found Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 1I2U,1I2V resolved by NMR. Similar to plant defensin RsAFP2 (also in structure), it interacts with glucosylceramide isolated from the membranes of yeast and soybean but not humans (J Biol Chem 2004; 279: 3900-3905). Transgenic plants: expression of this peptide in tobacco improves resistance to pathogens (Montesinos E 2007 FEMS Microbiol Lett 270, 1-11). Fungi: Neurospora crassa (MIC=0.1-0.2 µM), Fusarium culmorum (MIC=0.2-0.4 µM), Fusarium oxysporum (MIC=1.5-3 µM), Nectria haematococca (MIC=0.4-0.8 µM), Aspergillus fumigatus (MIC=6-12 µM), Trichoderma viride (MIC=1.5-3 µM), Candida albicans (MIC=2.5-5 µM), Cryptococcus neoformans (MIC=2.5-5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys7 and Cys32,Cys18 and Cys40, Cys22 and Cys42. Not included yet Not included yet Not found 10092609##11580275 J Biol Chem. 1999 Apr 2;274(14):9320-9326.##Biochemistry. 2001 Oct 9;40(40):11995-2003. Lamberty M, Ades S, Uttenweiler-Joseph S, Brookhart G, Bushey D, Hoffmann JA, Bulet P.##Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity.##Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. DRAMP03507 KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAKAL 35 Cecropin-B (Insects, animals) P01509 Belongs to the cecropin family Not found Antheraea pernyi (Chinese oak silkmoth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.36 µM), Escherichia coli D31 (MIC=0.30 µM), Serratia marsescens (MIC=2.6 µM), Serratia marsescens Strain 122 (MIC=12 µM), Pseudomonas aeruginosa OT97 (MIC=2.9 µM), Xenorhabdus nematophilus Xn21 (MIC=1.6 µM);##Gram-positive bacteria: Bacillus subtilis Bsll (MIC=17 µM), Bacillus megaterium Bmll (MIC=0.64 µM), Bacillus thuringiensis Btll (MIC>88 µM), Streptococcus fecalis Ds16 (MIC>88 µM), Streptococcus fecalis AD-4 (MIC>88 µM), Micrococcus luteus MI11 (MIC=0.29 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 6754375##2962676 Eur J Biochem. 1982 Sep;127(1):219-224.##Biomed Environ Mass Spectrom. 1987 Nov;14(11):669-673. Qu Z, Steiner H, Engström A, Bennich H, Boman HG.##Craig AG, Engström A, Bennich H, Kamensky I. Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi.##Plasma desorption mass spectrometry coupled with conventional peptide sequencing techniques. DRAMP03513 KVNVNAIKKGGKAIGKGFKVISAASTAHDVYEHIKNRRH 39 G. mellonella moricin-like peptide A (Gm-mlpA; Insects, animals; Predicted) A5JSU5 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Micrococcus luteus (MIC=10 µM).##Fungi: Fusarium graminearum mycelia (MIC=70 µM), F;##Graminearum spores (MIC=0.7 µM), Fusarium oxysporum mycelia (MIC=7 µM), F. oxysporum spores (MIC=10 µM), Ascochyta rabiei spores (MIC=7 µM), Leptosphaeria maculans spores (MIC=7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03514 GKIPVKAIKKGGQIIGKALRGINIASTAHDIISQFKPKKKKNH 43 G. mellonella moricin-like peptide B (Gm-mlpB; Insects, animals; Predicted) A5JSU6 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Micrococcus luteus (MIC=100 µM).##Fungi: Fusarium graminearum spores (MIC=10 µM), F;##Graminearum mycelia (MIC=280 µM), Fusarium oxysporum spores (MIC=100 µM), F. oxysporum mycelia (MIC=280 µM), Leptosphaeria maculans spores (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03515 KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVKNRH 38 Moricin-like peptide C1 (Gm-mlpC1; Insects, animals; Predicted) A5JSU7 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Micrococcus luteus (MIC=100 µM).##Fungi: Fusarium graminearum spores (MIC=1 µM), Fusarium oxysporum spores (MIC=10 µM), Ascochyta rabiei spores (MIC=100 µM), Leptosphaeria maculans spores (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03516 KVPIGAIKKGGKIIKKGLGVLGAAGTAHEVYNHVRNRQ 38 Moricin-like peptide C2 (Gm-mlpC2; Insects, animals; Predicted) A5JSU8 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Micrococcus luteus (MIC=100 µM).##Fungi: Fusarium graminearum spores (MIC=1 µM), Fusarium oxysporum spores (MIC=10 µM), Ascochyta rabiei spores (MIC=100 µM), Leptosphaeria maculans spores (MIC=8 µM), Fusarium graminearum mycelia (MIC=8 µM), Fusarium oxysporum mycelia (MIC=8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03517 KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVKNRQ 38 Moricin-like peptide C3 (Gm-mlpC3; Insects, animals; Predicted) A5JSU9 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Micrococcus luteus (MIC=100 µM).##Fungi: Fusarium graminearum spores (MIC=10 µM), Fusarium oxysporum spores (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03518 KVPVGAIKKGGKAIKTGLGVVGAAGTAHEVYSHIRNRH 38 Moricin-like peptide C4/C5 (Gm-mlpC4/C5; Insects, animals; Predicted) A5JSV1 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=100 µM).##Fungi: Fusarium graminearum spores (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03519 KGIGSALKKGGKIIKGGLGALGAIGTGQQVYEHVQNRQ 38 Moricin-like peptide D (Gm-mlpD; Insects, animals; Predicted) A5JSV2 Not found mor Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=10 µM).##Fungi: Fusarium graminearum spores (MIC=10 µM), Fusarium oxysporum spores (MIC=100 µM), Ascochyta rabiei spores(MIC=100 µM), Leptosphaeria maculans spores (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18207081 Insect Biochem Mol Biol. 2008;38:201-212. Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. DRAMP03520 ENFFKEIERAGQRIRDAIISAAPAVETLAQAQKIIKGGD 39 Cecropin-D-like peptide (Insects, animals) P85210 Not found Not found Galleria mellonella (greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus, Listeria monocytogenes, Sarcina Lutea, Escherichia coli D31(MIC=6.9-8.6 µM), Aspergillus niger. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 11995991##17194500 Acta Biochim Pol. 2001;48(4):1191-1195.##Peptides. 2007 Mar;28(3):533-546. Mak P, Chmiel D, Gacek GJ.##Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Antibacterial peptides of the moth Galleria mellonella.##Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03521 DIQIPGIKKPTHRDIIIPNWNPNVRTQPWQRFGGNKS 37 Proline-rich antimicrobial peptide 1 (Insects, animals) P85214 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Micrococcus luteus(MIC=55.0 µM).##Fungi: Pichia pastoris (MIC=16.5 µM), Zygosaccharomyces marxianus (MIC=16.5 µM), Schizosaccharomyces pombe (MIC=11 µM), candida wickerhamii (MIC=16.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 11995991##17194500 Acta Biochim Pol. 2001;48(4):1191-1195.##Peptides. 2007 Mar;28(3):533-546. Mak P, Chmiel D, Gacek GJ.##Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Antibacterial peptides of the moth Galleria mellonella.##Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03523 ETESTPDYLKNIQQQLEEYTKNFNTQVQNAFDSDKIKSEVNNFIESLGKILNTEKKEAPK 60 Anionic antimicrobial peptide 2 (Insects, animals) P85216 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus(MIC=43.3-86.6 µM), Listeria monocytogenes (MIC=86.6 µM), Sarcina Lutea (MIC=86.6 µM).##Fungi: Pichia pastoris (MIC=43.3-86.6 µM), P. stipitis (MIC=43.3-86.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17194500 Peptides. 2007;28:533-546. Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph DRAMP03524 EADEPLWLYKGDNIERAPTTADHPILPSIIDDVKLDPNRRYA 42 Lebocin-like anionic peptide 1 (Insects, animals) P85211 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus(MIC=22.7 µM), Listeria monocytogenes (MIC=90.9 µM).##Fungi: Aspergillus niger (MIC=90.9 µM), Trichoderma harzianum (MIC=90.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17194500 Peptides. 2007;28:533-546. Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03525 VQETQKLAKTVGANLEETNKKLAPQIKSAYDDFVKQAQEVQKKLHEAASKQ 51 Apolipophorin-3 (Apolipophorin-III; Insects, animals) P80703, O76946 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Listeria monocytogenes (MIC=6.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17194500 Peptides. 2007 Mar;28(3):533-46. CytryÅ„ska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03526 EIRLPEPFRFPSPTVPKPIDIDPILPHPWSPRQTYPIIARRS 42 Proline-rich antimicrobial peptide 2 (Insects, animals) P85212 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Micrococcus luteus (MIC=8.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17194500 Peptides. 2007 Mar;28(3):533-546. CytryÅ„ska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03527 DKLIGSCVWGATNYTSDCNAECKRRGYKGGHCGSFWNVNCWCEE 44 Gm defensin-like peptide (Insects, animals) P85215 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Sarcina Lutea (MIC=1.9 µM).##Fungi: Aspergillus niger (MIC=2.9 µM), Candida albicans (MIC=2.9 µM), C. fructus (MIC=2.9 µM), Candida wickerhamii (MIC=2.9 µM), Pichia pastoris (MIC=2.9 µM), P. stiptis (MIC=2.9 µM), Pachysolen tannophilus (MIC=2.9 µM), Trichoderma harzianum (MIC=2.9 µM), Zygosaccharomyces marxianus (MIC=2.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys7 and Cys32,Cys18 and Cys40, Cys22 and Cys42. L No cytotoxicity information found Not found 17194500 Peptides. 2007 Mar;28(3):533-546. CytryÅ„ska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. DRAMP03528 DTLIGSCVWGATNYTSDCNAECKRRGYKGGHCGSFLNVNCWCE 43 Defensin (Galiomicin; Insects, animals) P85213, Q6QR79 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Aspergillus niger (MIC=2.1 µM), Candida albicans (MIC=8.5 µM), C. fructus (MIC=8.5 µM), Fusarium oxysporum (MIC=16.9 µM), Pichia pastoris (MIC=16.9 µM), Pachysolen tannophilus (MIC=8.5 µM), Trichoderma harzianum (MIC=4.2 µM), Zygosaccharomyces Marxianus (MIC=8.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys7 and Cys32,Cys18 and Cys40, Cys22 and Cys42. L Not included yet Not found 17194500##14728668 Peptides. 2007 Mar;28(3):533-546.##Insect Mol Biol 2004; 13: 65-72. Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T.##Lee Y.S, Yun E.K, Jang W.S, Kim I, Lee J.H, Park S.Y, Ryu K.S, Seo S.J, Kim C.H, Lee I.H. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph.##Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella. DRAMP03532 AKIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLKPKKRKH 42 Moricin-1 (Insects, animals) P82818 Belongs to the moricin family MOR1 Bombyx mori (Silk moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (1 helices; 30 residues) The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment o 1KV4 resolved by NMR. Function: Has antibacterial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Gram-negative bacteria: Escherichia coli JM109 (MIC=0.31 µM), Acinetobacter sp. NISL B-4653 (MIC=0.27 µM), Pseudomonas fluorescens IAM1179 (MIC=0.53 µM), Pseudomonas aeruginosa IAM15140 (MIC=0.81 µM);##Gram-positive bacteria: Bacillus subtilis IAM1107 (MIC=0.19 µM), Bacillus megaterium IAM1030 (MI=0.09 µM), Bacillus cereus IFO3457 (MIC=0.38 µM), Staphylococcus aureus ATCC6538P (MIC=0.21 µM), Staphylococcus aureus ATCC6538P (MIC=0.22 µM), Staphylococcus aureus IFO3083 (MIC=0.46 µM), Staphylococcus xylosus IAM1312 (MIC=0.27 µM), Staphylococcus epidermidis IFO12993 (MIC=0.18 µM), Streptococcus pyogenes ATCC21547 (MIC=0.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 8530391##11997013 J Biol Chem. 1995 Dec 15;270(50):29923-29927.##FEBS Lett. 2002 May 8;518(1-3):33-38. Hara S, Yamakawa M.##Hemmi H, Ishibashi J, Hara S, Yamakawa M. Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori.##Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori. DRAMP03539 EWEPVQNGGSSYYMVPRIWA 20 Antifungal protein (Psc-AFP) No entry found Not found Not found Cullen corylifolium Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Fungi: Alternaria brassicae (MIC=10 µM), Aspergillus niger (MIC=10 µM), Fusarium oxysporum (MIC=10 µM), Rhizoctonia cerealis (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 16530884 Peptides. 27:1726-1731(2006) Yang X, Li J, Wang X, Fang W, Bidochka M.J, She R, Xiao Y, Pei Y. Psc-AFP, an antifungal protein with trypsin inhibitor activity from Psoralea corylifolia seeds DRAMP03540 CLAGRLDKQCTCRRSQPSRRSGHEVGRPSPHCGPSRQCGCHMD 43 Human drosomycin-like defensin (DLD; Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Not found Bridge Not found Function: This is the first indication of an endogenous human peptide with specific antifungal activity, which is probably central in the defense against infections with molds. Filamentous fungi: Aspergillus fumigatus (MIC=6.25 µM), A. nidulans (MIC=6.25 µM), A. ustus (MIC=12.5 µM), Fusarium solani (MIC=25 µM), F. oxysporum (MIC=6.25 µM), R. oryzae (MIC=6.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Has three disulfide bonds L No cytotoxicity information found Not found 18212107 Antimicrob Agents Chemother 2008; 52: 1407-1412. Simon A et al Netea MG. Drosomycin-like defensin, a human homologue of Drosophila melanogaster drosomycin with antifungal activity. DRAMP03562 FLAKAVAKAAAKALAKAL 18 P1 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Not found Not found Not found Function: Presentes antifungal activity against Candida albicans. Yeast: Candida albicans (MIC=82 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 22884922 Peptides. 2012 Oct;37(2):301-308. Amaral AC, Silva ON, Mundim NC, de Carvalho MJ, Migliolo L, Leite JR, Prates MV, Bocca AL, Franco OL, Felipe MS. Predicting antimicrobial peptides from eukaryotic genomes: In silico strategies to develop antibiotics. DRAMP03563 KAGLAFPVGRVHRLLRK 17 P2 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Not found Not found Not found Function: Presentes antifungal activity against Candida albicans. Yeast: Candida albicans (MIC=133 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 22884922 Peptides. 2012 Oct;37(2):301-308. Amaral AC, Silva ON, Mundim NC, de Carvalho MJ, Migliolo L, Leite JR, Prates MV, Bocca AL, Franco OL, Felipe MS. Predicting antimicrobial peptides from eukaryotic genomes: In silico strategies to develop antibiotics. DRAMP03567 KRIVQRIKDFLRNLVPRTES 20 KR-20 (Derived from LL-37) No entry found Not found Not found Homo sapiens (Human sweat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus mprF (MIC=16 µM), Staphylococcus aureus ATCC 25923 (MIC>64 µM), Staphylococcus aureus (GAS) (MIC=4 µM);##Gram-negative bacterium: Escherichia coli O29 (MIC>64 µM).##Yeast: Candida albicans ATCC 14053 (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Lipopolysaccharide (LPS)-binding 14978112 J Immunol 2004; 172: 3070-3077. Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. DRAMP03568 RKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 31 RK-31 (Derived from LL-37) No entry found Not found Not found Homo sapiens (Human sweat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found 2K6O##5NMN##5NNK##5NNM##5NNT##7PDC##7SAY Function: Has hemolytic activity against human erythrocytes . [Ref.14978112]Gram-positive bacteria: Staphylococcus aureus mprF (MIC=8 µM), Staphylococcus aureus ATCC 25923 (MIC=16 µM), Group A Staphylococcus aureus (GAS) (MIC=8 µM);##Gram-negative bacterium: Escherichia coli O29 (MIC=8 µM);##Yeast: Candida albicans ATCC 14053 (MIC=4 µM). [Ref.14978112]6% hemolytic activity at 44 μM against human erythrocytes Linear Free Free Free L Not included yet Lipopolysaccharide (LPS)-binding 14978112 J Immunol 2004; 172: 3070-3077. Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. DRAMP03569 KSKEKIGKEFKRIVQRIKDFLRNLVPRTES 30 KS-30 (Derived from LL-37) No entry found Not found Not found Homo sapiens (Human sweat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found 2K6O##5NMN##5NNK##5NNM##5NNT##7PDC##7SAY##2FCG##2LMF Function:Has hemolytic activity against human erythrocytes. [Ref.14978112]Gram-positive bacteria: Staphylococcus aureus mprF (MIC=8 µM), Staphylococcus aureus ATCC 25923 (MIC=16 µM), Group A Staphylococcus aureus (GAS) (MIC=4 µM);##Gram-negative bacterium: Escherichia coli O29 (MIC=8 µM);##Yeast: Candida albicans ATCC 14053 (MIC=2 µM) [Ref.14978112]23% hemolytic activity at 88 μM against human erythrocytes Linear Free Free Free L Not included yet Lipopolysaccharide (LPS)-binding 14978112 J Immunol 2004; 172: 3070-3077. Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. DRAMP03570 LLGDFFRKSKEKIGKEFKRIVQR 23 LL-23 (Derived from LL-37) P49913, Q71SN9 Not found Not found Homo sapiens (Human sweat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix (1 helices; 19 residues) The Ser9 site splits the hydrophobic surface of the amphipathic helix into two domains, which explains its poor antimicrobial activity (active against only susceptible bacterial strains). 2LMF resolved by NMR. Its structure, dynamics, and antimicrobial and immune modulating activities have been characterized (Biochemistry 2012). Gram-negative bacterium: Escherichia coli DC2 (MIC=9 µM);##Gram-positive bacteria: Staphylococcus aureus mprF (presence of carbonate) (MIC=3 µM), S. aureu mprF (absence of carbonate) (MIC=24 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17012259##22185690 FASEB J 2006; 20, 2068-2080.##Biochemistry. 2012 Jan 17;51(2):653-664. Yamasaki K et al. Gallo RL.##Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin.##Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. DRAMP01877 GLMSVLKGVLKTAGKHIFKNVGGSLLDQAKCKITGQC 37 Brevinin-2PRd (Frogs, amphibians, animals) No entry found Not found Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC=3μM), Pseudemonas aeruginosa(MIC=3μM), Enterobacter cloacae(MIC=6μM), Klebsiella pneumoniae(MIC=6μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=25μM);## Yeast: Candida albicans(MIC=100μM) [Ref.15003829] HC50=100 μM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 15003829 Regul Pept. 2004 May 15;118(3):135-141. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP01878 GLLSVLKGVLKTAGKHIFKNVGGSLLDQAKCKISGQC 37 Brevinin-2PRe (Frogs, amphibians, animals) No entry found Not found Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC=3μM), Pseudemonas aeruginosa(MIC=3μM), Enterobacter cloacae(MIC=3μM), Klebsiella pneumoniae(MIC=6μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=25μM);## Yeast: Candida albicans(MIC>100μM) [Ref.15003829] HC50=80 μM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 15003829 Regul Pept. 2004 May 15;118(3):135-141. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP03573 IGKEFKRIVQRIKDFLRNLVPRTES 25 LL-37(13-37)(C-terminal fragment of LL-37; Human, mammals, animals) P49913, Q71SN9 Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram-, Anticancer Protein level Alpha helix (1 helices; 14 residues) Residues 17-29 of LL-37(13-37) are helical. 2FCG resolved by NMR. The slightly lower activity of LL-37(13-37) may result from the interference of the disordered regions with membrane binding of the peptide. Gram-negative bacterium: Escherichia coli K12 (MIC=80 µM).##Drug-resistant KBv cancer cells (LC50=39 µM), Drug-sensitive KB cancer cells (LC50=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bonds L Not included yet Not found 16637646 J Am Chem Soc. 2006 May 3;128(17):5776-5785. Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. DRAMP03574 FKRIVQRIKDFLRNLV 16 LL-37(17-32)(C-terminal fragment of LL-37; Human, mammals, animals) P49913, Q71SN9 Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram-, Anticancer Protein level Not found To achieve selective membrane targeting, D-amino acids were incorporated into LL-37(17-32). The D-peptide showed similar antibacterial activity to the L-diastereomer, it lost toxicity to human cells. Antibacterial and anticancer assays found that LL-37(17-32) was more active than LL-37(13-37). Gram-negative bacteria: Escherichia coli K12(MIC=20 µM).##Drug-resistant KBv cancer cells (LC50=30 µM), Drug-sensitive KB cancer cells (LC50=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bonds L Not included yet Not found 16637646 J Am Chem Soc. 2006 May 3;128(17):5776-5785. Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. DRAMP03598 GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP 41 Human beta-defensin 2 (hBD-2; Defensin, beta 2; Beta-defensin 4A; Human, mammals, animals) O15263, Q52LC0 Belongs to the beta-defensin family DEFB4A AND DEFB4B Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Combine helix and strand structure The structure (one N-terminal helix and 3 beta strands) was found to be monomer in solution (PDB ID: 1E4Q) but a dimer in the crystal (PDB ID: 1FD3). 1FD4, 1FD3 resolved by X-ray.##1FQQ resolved by NMR. "Function: Has anti-HIV and antibacterial activity. Tissue specificity: Expressed in the skin and respiratory tract. Induction: By inflammation. PTM: Contains three disulfide bonds 8-37, 15-30, 20-38. Transgenic plants: expression of this peptide in Arabidopsis thaliana reduced fungal infection." Gram-negative bacteria: Escherichia coli D31(MIC=62 µg/ml), Escherichia coli ATCC (MIC=62 µg/ml), Pseudomonas aeruginosa ATCC (MIC=62 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC (MIC=62 µg/ml), Enterococcus faecalis ATCC (MIC=15 µg/ml). [Ref.15625724] It is slightly hemolytic (<12%) against human erythrocytes at the highest concentration of 500 μg/ml. Cyclic Free Free Disulfide bonds between Cys8 and Cys37,Cys15 and Cys30,Cys20 and Cys38. L No cytotoxicity information found Not found 9202117##10906336##17340092 Nature. 1997 Jun 26;387(6636):861.##J Biol Chem. 2000 Oct 20;275(42):32911-32918.##Plant Cell Rep. 2007 Aug;26(8):1391-1398. Harder J, Bartels J, Christophers E, Schröder JM.##Hoover DM, Rajashankar KR, Blumenthal R, Puri A, Oppenheim JJ, Chertov O, Lubkowski J.##Aerts AM, Thevissen K, Bresseleers SM, Sels J, Wouters P, Cammue BP, François IE. A peptide antibiotic from human skin.##The structure of human beta-defensin-2 shows evidence of higher order oligomerization.##Arabidopsis thaliana plants expressing human beta-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins. DRAMP03599 GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK 45 Human beta-defensin 3 (BD-3, hBD-3; Hbd3; Beta-defensin 103; Human, mammals, animals) P81534, Q8NFG6, Q9NPF6 Belongs to the beta-defensin family DEFB103A AND DEFB103 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Contains three disulfide bonds and a short helical segment preceding a three-stranded antiparallel beta-sheet. 1KJ6 resolved by NMR. "Function: Exhibits antimicrobial activity against Gram-positive bacteria and the Gram-negative bacteria and the yeast C.albicans. Kills multiresistant S. aureus and vancomycin-resistant E. faecium. Has hemolytic activity. Tissue specificity: Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine. Induction: By bacterial infection and by IFNG/IFN-gamma. PTM: Contains three disulfide bonds 11-40; 18-33; 23-41." [Ref.11085990]Gram-negative bacteria: Escherichia coli DSM1103 (MIC=9.4 µg/ml), Klebsiella pneumoniae DSM681 (MIC=25 µg/ml), Pseudomonas aeruginosa DSM1128 (MIC=18.75 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=4.7 µg/ml), Streptococcus pneumoniae DSM11865 (MIC=4.7 µg/ml). [Ref.11085990] It has 9% hemolysis at 250 µg/ml, 15% hemolysis at 500 µg/ml against human erythrocytes. Cyclic Free Free Disulfide bonds between Cys11 and Cys40,Cys18 and Cys33,Cys23 and Cys41. L No cytotoxicity information found Not found 15625724##11085990 Biopolymers. 2005;80(1):34-49.##J Biol Chem. 2001 Feb 23;276(8):5707-5713. Schulz A, Klüver E, Schulz-Maronde S, Adermann K.##Harder J, Bartels J, Christophers E, Schroder JM. Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.##Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. DRAMP03600 EFELDRICGYGTARCRKKCRSQEYRIGRCPNTYACCLRKWDESLLNRTKP 50 Human beta-defensin 4 (hBD-4, BD-4; Beta-defensin 104; Human, mammals, animals) Q8WTQ1, Q496I2, Q496I3, Q496I4 Belongs to the beta-defensin family DEFB104A Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Bridge Not found 5KI9 "Function: Has antimicrobial activity. Synergistic effects with lysozyme and DEFB103. Tissue specificity: High expression in the testis. Gastric antrum exhibited relatively high levels. A lower expression is observed in uterus and neutrophils thyroid gland, lung, and kidney. No detectable expression in other tissues tested. Induction: Antimicrobial activity is decreased when the sodium chloride concentration is increased. PTM: Contains three disulfide bonds (By similarity)." Gram-positive bacterium: Staphylococcus carnosus TM300 (MIC=4.5 µg/ml);##Gram-negative bacteria: Escherichia coli BL21 (MIC>100 µg/ml), Pseudomonas aeruginosa (MIC=4.1 µg/ml).##Yeast: Saccharomyces cerevisiae ATCC9763 (MIC>100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys8 and Cys36,Cys15 and Cys29,Cys19 and Cys37. L No cytotoxicity information found Not found 11481241 FASEB J. 2001 Aug;15(10):1819-1821. García JR, Krause A, Schulz S, Rodríguez-Jiménez FJ, Klüver E, Adermann K, Forssmann U, Frimpong-Boateng A, Bals R, Forssmann WG. Human beta-defensin 4: a novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity. DRAMP03603 ARLKKCFNKVTGYCRKKCKVGERYEIGCLSGKLCCAN 37 Human beta-defensin 28 (hBD-28; hBD28; Human, mammals, animals) No entry found Belongs to the beta-defensin family Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Bridge Not found Function: Has antibacterial activity gaginst Gram-positive and the Gram-negative bacteria. Gram-negative bacteria: Escherichia coli DSM1103 (MIC=37.5 µg/ml), Klebsiella pneumoniae DSM681 (MIC=50 µg/ml), Pseudomonas aeruginosa DSM1128 (MIC=37.5 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=25 µg/ml), Streptococcus pneumoniae DSM11865 (MIC=37.5 µg/ml). [Ref.15625724] It is slightly hemolytic (<12%) against human erythrocytes at the highest concentration of 500 μg/ml. Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys14 and Cys28,Cys18 and Cys35 L No cytotoxicity information found Not found 15625724 Biopolymers. 2005;80(1):34-49. Schulz A, Klüver E, Schulz-Maronde S, Adermann K. Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins. DRAMP03638 LCLDQKPEMEPFRKDAQQALEPSRQRRWLHRRCLSGRGFCRAICSIFEEPVRGNIDCYFGYNCCRRMFSHYRTS 74 VpBD (V.philippinarum beta defensin; big defensin) No entry found Not found Not found Venerupis philippinarum (The manila clam) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: The rVpBD displays broad-spectrum inhibitory activity towards all tested bacteria with the highest activity against Staphyloccocus aureus and Pseudomonas putida. Gram-positive bacteria: Staphyloccocus aureus (MIC=1.64-3.28 µM), Micrococcus luteus (MIC>26.26 µM), Bacillus sp. (MIC=13.13-26.26 µM);##Gram-negative bacteria: Vibrio anguillarum (MIC=13.13-26.26 µM), Entherobacter cloacae (MIC>26.26 µM), Vibrio ichthyoenteri (MIC=3.28-6.56 µM), Pseudomonas putida (MIC=1.64-3.28 µM), Proteus mirabilis (MIC>26.26 µM), Enterobacter sp. (MIC=13.13-26.26 µM) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys33 and Cys63,Cys40 and Cys57,Cys44 and Cys64. L No cytotoxicity information found Not found 20975988 PLoS One. 2010 Oct 20;5(10):e13480. Zhao J, Li C, Chen A, Li L, Su X, Li T. Molecular characterization of a novel big defensin from clam Venerupis philippinarum. DRAMP03642 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCKRIR 39 Chicken heterophil peptides 1 (Antimicrobial peptide CHP1; Birds, animals) P80389 Belongs to the beta-defensin family Not found Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Bactericidal activity; inhibits S. aureus and E. coli. PTM: Contains three disulfide bonds 6-28; 13-34; 18-35." Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=2.7 µg/ml);##Gram-positive bacterium: Staphylococcus aureus (MIC=0.7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys28,Cys13 and Cys34,Cys18 and Cys35. L No cytotoxicity information found Not found 7964174 J Leukoc Biol. 1994 Nov;56(5):661-665. Evans EW, Beach GG, Wunderlich J, Harmon BG. Isolation of antimicrobial peptides from avian heterophils. DRAMP01376 GFMDTAKNAAKNVAVTLLDNLKCKITKAC 29 Odorranain-F1 (OdF1; Frogs, amphibians, animals) A6MBL3 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Odorranain-F1 adopts 55% Function: Odorranain-F1 exhibites antimicrobial activities against the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Also has hemolytic activity against rabbiit red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=4.20 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=2.10 μg/ml), Bacillus subtilis (MIC=8.40 μg/ml).##Yeast: Candida albicans (MIC=1.05 μg/ml). [Ref.17272268] RCH=15.4 ± 3.5% against rabbit red blood cells at 50 μg/ml. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01378 GIFGKILGVGKKVLCGLSGVC 21 Odorranain-H1 (OdH1; Frogs, amphibians, animals) A6MBN4 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Odorranain-H1 adopts 50.3 β-sheet structure in water solution. Function: Odorranain-H1 exhibites antimicrobial activities against Gram-positive and Gram-negative bacteria and fungi. Also has hemolytic activity against rabbit red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=23.60 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=5.90 μg/ml), Bacillus subtilis (MIC=5.90 μg/ml).##Yeast: Candida albicans (MIC=11.80 μg/ml). [Ref.17272268] RCH=21.6 ± 7.3% against rabbit red blood cells. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01386 VIPFVASVAAEMMQHVYCAASKKC 24 Odorranain-P1a (OdP1a; Brevinin-1HS1; Brevinin-1-OA2; Frogs, amphibians, animals) A6MBQ8, A6MBQ6 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Odorranain-P1a exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Also has hemolytic activity against rabbit red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=3.50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.50 μg/ml), Bacillus subtilis (MIC=1.75 μg/ml).##Yeast: Candida albicans (MIC=1.75 μg/ml). [Ref.17272268] RCH=11.2 ± 2.9% against rabbit red blood cells. RCH, red cell hemolysis. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP03646 RVKRFWPLVPVAINTVAAGINLYKAIRRK 29 Cathelicidin-3 (CATH-3; Fowlicidin-3; Birds, animals) Q2IAL6 Not found CATHL3 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (1 helices; 9 residues) NMR spectroscopy reveales that fowlicidin-3 comprises 27 amino-acid residues and adopts a predominantly alpha-helical structure extending from residue 9 to 25 with a slight kink induced by a glycine at position 17.. 2HFR resolved by NMR. "Function: May have antimicrobial activity and play a role in the innate immune response. Tissue specificity: Detected in bone marrow, liver and lung." Gram-negative bacteria: Escherichia coli 25922 (MIC=2 µM), Salmonella typhimurium 14028 (MIC=2 µM), S. typhimurium DT104 700408 (MIC=2 µM), Salmonella enteritidis 13076 (MIC=2 µM), Klebsiella pneumoniae 13883 (MIC=1 µM);##Gram-positive bacteria: Listeria monocytogenes 19115 (MIC=2 µM), Staphylococcus aureus 25923 (MIC=1 µM), S. aureus (MRSA) 43300 (MIC=1 µM), S. aureus (MRSA) BAA-39 (MIC=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Lipopolysaccharide (LPS)-binding 17827276##16326712##17229147 Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15063-15068.##J Biol Chem. 2006 Feb 3;281(5):2858-2867.##FEBS J. 2007 Jan;274(2):418-428. Goitsuka R, Chen CL, Benyon L, Asano Y, Kitamura D, Cooper MD.##Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE, Zhang G.##Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G. Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway.##Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity.##Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. DRAMP03647 PIRNWWIRIWEWLNGIRKRLRQRSPFYVRGHLNVTSTPQP 40 Cathelicidin-B1 (CATH-B1; cathelicidin; Birds, animals) Q5F378, A7M6V2 Not found CATHB1 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=2.5 µM), Pseudomonas aeruginosa (MIC=0.63 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=1.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 17827276##15642098 Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15063-15068.##Genome Biol. 2005;6(1):R6. Goitsuka R, Chen CL, Benyon L, Asano Y, Kitamura D, Cooper MD.##Caldwell RB, Kierzek AM, Arakawa H, Bezzubov Y, Zaim J, Fiedler P, Kutter S, Blagodatski A, Kostovska D, Koter M, Plachy J, Carninci P, Hayashizaki Y, Buerstedde JM. Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway.##Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis. DRAMP03659 LPRDTSRCVGYHGYCIRSKVCPKPFAAFGTCSWRQKTCCVDTTSDFHTCQDKGGHCVSPKIRCLEEQLGLCPLKRWTCCKEI 82 Gallinacin-11 (Gal-11; Beta-defensin 11; Birds, animals) Q6IV20, A0A1W6, Q09MT4, Q9PS49 Belongs to the beta-defensin family GAL11 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Protein level Bridge Not found 6QEU##6QET##6QES Tissue specificity: Detected in outer membrane of the vitelline layer of the egg (at protein level). Expressed in the liver, gall bladder, kidney, testis, ovary and male and female reproductive tracts. Expressed in the ovarian stroma, but not in the ovarian follicles. No expression is detected in bone marrow. PTM: Contains three disulfide bonds 8-38; 15-31; 21-39. Gram-negative bacterium: Escherichia coli (MIC=50 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys8 and Cys38,Cys15 and Cys31, Cys21 and Cys39. L Not included yet Not found 17244739##1520265 Reproduction. 2007 Jan;133(1):127-133.##Biochem J. 1992 Aug 15;286 (Pt 1):17-22. Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Kido S, Morimoto A, Kim F, Doi Y. Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##Isolation of a novel protein from the outer layer of the vitelline membrane. DRAMP03676 APRKNVRWCAISLPEWSKCYQWQRRMRKLGAPSITCIRRTS 41 GLFcin (Lactoferrin fragment) Q29477, Q29479 Belongs to the transferrin family LTF Capra hircus (Goat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: GLFcin is thermal-stable and with high antibacterial activity. Gram-negative bacteria: Escherichia coli (MIC=4.07 µg/ml), Propioni bacterium acnes (MIC=12.32 µg/ml), Pseudemonas aeruginosa (MIC=4.07 µg/ml);##Gram-positive bacteria: Bacillus cereus (MIC=12.32 µg/ml), Staphylococcus aureus (MIC=4.07 µg/ml), Listeria monocytogene (MIC=4.07 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 19780544 J Agric Food Chem. 2009 Oct 28;57(20):9509-9515. Chen GH, Chen WM, Huang GT, Chen YW, Jiang ST. Expression of recombinant antibacterial lactoferricin-related peptides from Pichia pastoris expression system. DRAMP03677 SKCYQWQRRMRKLGAPSITCIRRTS 25 GLFcin II (Lactoferrin fragment) Q29477, Q29479 Belongs to the transferrin family LTF Capra hircus (Goat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: GLFcin is thermal-stable and with high antibacterial activity. Gram-negative bacteria: Escherichia coli (MIC=6.80 µg/ml), Propioni bacterium acnes (MIC=10.50 µg/ml), Pseudemonas aeruginosa (MIC=14.50 µg/ml);##Gram-positive bacteria: Bacillus cereus (MIC=16.00 µg/ml), Staphylococcus aureus (MIC=6.80 µg/ml), Listeria monocytogene (MIC=9.92 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 19780544 J Agric Food Chem. 2009 Oct 28;57(20):9509-9515. Chen GH, Chen WM, Huang GT, Chen YW, Jiang ST. Expression of recombinant antibacterial lactoferricin-related peptides from Pichia pastoris expression system. DRAMP03679 RFRPPIRRPPIRPPFNPPFRPPVRPPFRPPFRPPFRPPIGPFP 43 Cathelicidin-2 (Bactenecin-5, Bac5; ChBac5; ruminant, animals) P82018, Q4JFB9 Not found CATHL2 Capra hircus (Goat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=1 µg/ml), Salmonella typhimurium (MIC=1 µg/ml), Pseudomonas aeruginosa (MIC=1 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC<2 µg/ml), Listeria monocytogenes (MIC<2 µg/ml) and Bacillus subtilis (MIC<2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Lipopolysaccharide (LPS)-binding 10417180 nfect Immun. 1999 Aug;67(8):4106-4111. Shamova O, Brogden KA, Zhao C, Nguyen T, Kokryakov VN, Lehrer RI. Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. DRAMP03682 FLPIIAKLLGGLL 13 Vespid chemotactic peptide 5e (VCP 5e; Insects, animals) P0C1M1 Belongs to the MCD family (Crabrolin subfamily) Not found Vespa magnifica Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide (By similarity). Has little hemolytic activity. Shows antimicrobial activity against the Gram-negative bacteria and the Gram-positive bacteria. Also has antifungal activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (By similarity)." [Ref.16330062]Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=30 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=5 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=25 µg/ml). [Ref.16330062]Little hemolytic activity up to 50 μg/ml against rabbit red blood cells Linear Free Amidation Free L Not included yet Not found 16330062 Toxicon. 2006 Feb;47(2):249-53. Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R. Two families of antimicrobial peptides from wasp (Vespa magnifica) venom. DRAMP03683 FLIIRRPIVLGLL 13 Vespid chemotactic peptide 5g (VCP 5g; Insects, animals) P0C1M3 Belongs to the MCD family (Crabrolin subfamily) Not found Vespa magnifica Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide (By similarity). Has little hemolytic activity. Shows antimicrobial activity against the Gram-negative bacteria and the Gram-positive bacteria. Also has antifungal activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (By similarity)." [Ref.16330062]Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=30 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=10 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=12.5 µg/ml). [Ref.16330062]Little hemolytic activity up to 50 μg/ml against rabbit red blood cells Linear Free Amidation Free L Not included yet Not found 16330062 Toxicon. 2006 Feb;47(2):249-53. Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R. Two families of antimicrobial peptides from wasp (Vespa magnifica) venom. DRAMP03684 FLPIPRPILLGLL 13 Vespid chemotactic peptide 5f (VCP 5f; Insects, animals) P0C1M2 Belongs to the MCD family (Crabrolin subfamily) Not found Vespa magnifica Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide (By similarity). Has little hemolytic activity. Shows antimicrobial activity against the Gram-negative bacteria and the Gram-positive bacteria. Also has antifungal activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (By similarity)." [Ref.16330062]Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=30 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=5 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=25 µg/ml). [Ref.16330062]Little hemolytic activity up to 50 μg/ml against rabbit red blood cells Linear Free Amidation Free L Not included yet Not found 16330062 Toxicon. 2006 Feb;47(2):249-53. Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R. Two families of antimicrobial peptides from wasp (Vespa magnifica) venom. DRAMP18366 GFGSKPIDSFGLSWL 15 Sungsanpin (a class 2 lasso peptide; bacteriocins) No entry found Not found Not found a Marine Streptomyces species Anti-cancer Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Form a lactam bond at position 1 and 8(Gly1, Asp8) L Not included yet Not found 23662937 J Nat Prod. 2013 May 24;76(5):873-9 Um S, Kim YJ, Kwon H, Wen H, Kim SH, Kwon HC, Park S, Shin J, Oh DC. Sungsanpin, a lasso peptide from a deep-sea streptomycete DRAMP03687 FLSLIPSLVGGSISAFK 17 TsAP-1 (T. serrulatus antimicrobial peptide 1; scorpions, arachnids, invertebrates, animals) S6CWV8 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family. Not found Tityus serrulatus (Brazilian yellow scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Anticancer activity against HI57 and H838. [Ref.23770440] Gram-positive bacteria : Staphylococcus aureus(MIC=120 μM, MBC>160 μM);##Gram-negative bacteria : Escherichia coli(MIC=160 μM, MBC>160 μM);##Fungi : Candida albicans(MIC=160 μM, MBC>160 μM) [Ref.23770440] 0% hemolysis at 40 μM , 2% hemolysis at 80 μM , 5% hemolysis at 120 μM , 7% hemolysis at 160 μM against horse red blood cells Linear Free Amidation Free L Not included yet Not found 23770440 Biochimie. 2013 Jun 14. doi: 10.1016/j.biochi.2013.06.003. Guo X, Ma C, Du Q, Wei R, Wang L, Zhou M, Chen T, Shaw C. Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities. DRAMP03688 FLGMIPGLIGGLISAFK 17 TsAP-2 (T. serrulatus antimicrobial peptide 2; scorpions, arachnids, invertebrates, animals) No entry found Not found Not found Tityus serrulatus (Brazilian yellow scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal, Anti-cancer Not found Not found Not found Function: TsAP-2 was of high potency against the Gram-positive bacterium, Staphylococcus aureus and the yeast Candida albicans. Gram-positive bacterium: Staphylococcus aureus (MIC=5 µM).##Yeast: Candida albicans (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 23770440 Biochimie. 2013 Jun 14. pii: S0300-9084(13)00164-8. Guo X, Ma C, Du Q, Wei R, Wang L, Zhou M, Chen T, Shaw C. Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities. DRAMP03691 FSFKRLKGFAKKLWNSKLARKIRTKGLKYVKNFAKDMLSEGEEAPPAAEPPVEAPQ 56 Im-1 (Arthropods, animals) P0CF38 Belongs to the scorpion BPP family Not found Isometrus maculatus (Lesser brown scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Causes cytolysis by the formation of pores in the membrane. Causes rapid and reversible paralysis in crickets. Has antibacterial activity. Tissue specificity: Expressed by the venom gland. Toxic dose: PD50 is 38 mg/kg into the insect A. domestica." Gram-negative bacterium: Escherichia coli NBRC 3972 (MIC=0.4-0.8 µM);##Gram-positive bacteria: Staphylococcus aureus NBRC 13276 (MIC=13-25 µM), Bacillus subtilis NBRC 3009 (MIC=0.8-1.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linera Free Free Free L Not included yet Cell membrane 20139620 Biosci Biotechnol Biochem. 2010;74(2):364-369. Miyashita M, Sakai A, Matsushita N, Hanai Y, Nakagawa Y, Miyagawa H. A novel amphipathic linear peptide with both insect toxicity and antimicrobial activity from the venom of the scorpion Isometrus maculatus. DRAMP03693 KDGYIIEHRGCKYSCFFGTNSWCNTECTLKKGSSGYCAWPACWCYGLPDNVKIFDSNNLKC 61 Bactridin-1 (Bact1; Bactridine 1; Arthropods, animals) P0CF39 Belongs to the long (4 C-C) scorpion toxin superfamily Sodiu Not found Tityus discrepans (Venezuelan scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows antibacterial activity. Modifies membrane sodium permeability on Y.enterocolitica. Is toxic to cockroaches and crabs, but is not to mice. Does not induce haemolysis in human erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity) and C- terminal amidation." Gram-positive bacteria: Bacillus subtillis ICTA-07 (MIC=22 µM), Microccocus luteus ATCC 4698 (MIC=43 µM), Enterococcus faecalis WHO14 (MIC=34 µM);##Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=77 µM), Yersinia enterocolitica ATCC 9610 (MIC=49 µM), Acinetobacter calcoaceticus ATCC 2305-5 (MIC=43 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation(Cyclization with a disulfide bond(Cys11 and Cys61)) Disulfide bond between Cys11 and Cys61,Cys15 and Cys37, Cys23 and Cys42, Cys27 and Cys44. L Not included yet Not found 19540868##22355312 Toxicon. 2009 Nov;54(6):802-817.##PLoS One. 2012;7(2):e30478. Díaz P, D'Suze G, Salazar V, Sevcik C, Shannon JD, Sherman NE, Fox JW.##Guerrero-Vargas JA, Mourão CB, Quintero-Hernández V, Possani LD, Schwartz EF. Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes.##Identification and phylogenetic analysis of Tityus pachyurus and Tityus obscurus novel putative Na+-channel scorpion toxins. DRAMP03694 KDGYLVGNDGCKYSCFTRPGTYCANECSRVKGKDGYCYAWMACYCYSMPNWVKTWNRATNRCGR 64 Bactridin-2 (Bact2, Bactridine 2; P-Mice-Antm-beta* NaTx14.8; Arthropods, animals) P0CF37 Belongs to the long (4 C-C) scorpion toxin superfamily Sodiu Not found Tityus discrepans (Venezuelan scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows antibacterial activity against both Gram-positive bacteria (B.subtilis, M.luteus, E.faecalis) and Gram-negative bacteria (P.aeruginosa, Y.enterocolitica, A.calcoaceticus). Modifies membrane sodium permeability on Y.enterocolitica. Is toxic to mice, but is not to crabs. Induces concentration dependent haemolysis in human erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity) and C-terminal amidation." Gram-positive bacteria: Bacillus subtillis ICTA-07 (MIC=30 µM), Microccocus luteus ATCC 4698 (MIC=27 µM), Enterococcus faecalis WHO14 (MIC=65 µM);##Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=54 µM), Yersinia enterocolitica ATCC 9610 (MIC=46 µM), Acinetobacter calcoaceticus ATCC 2305-5 (MIC=27 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys11 and Cys62,Cys15 and Cys37, Cys23 and Cys43, Cys27 and Cys45. L Not included yet Not found 19540868##22355312 Toxicon. 2009 Nov;54(6):802-817.##PLoS One. 2012;7(2):e30478. Díaz P, D'Suze G, Salazar V, Sevcik C, Shannon JD, Sherman NE, Fox JW.##Guerrero-Vargas JA, Mourão CB, Quintero-Hernández V, Possani LD, Schwartz EF. Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes.##Identification and phylogenetic analysis of Tityus pachyurus and Tityus obscurus novel putative Na+-channel scorpion toxins. DRAMP03700 FLWGLIPGAISAVTSLIKK 19 Antimicrobial peptide ctriporin (Riporin; Arthropods, animals) G1FE62 Not found Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+ Transcript level Not found Not found "Function: Antimicrobial peptide that acts by breaking the cell wall. Has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Is efficient in curing staphylococcal skin infection in mice, when externally applied. Tissue specificity: Expressed by the venom gland. Miscellaneous: Has no activity against Gram-negative bacteria (E.coli and P.aeruginosa)." Gram-positive bacteria: Staphylococcus aureus (MIC=5 µg/ml), Micrococcus luteus (MIC=5 µg/ml), Bacillus thuringiensis (MIC=10 µg/ml), B. subtilis (MIC=10 µg/ml).##Fungi: Candida albicans (MIC=20 µg/ml).##Antibiotic-resistant pathogens: methicillin-resistant Staphylococcus aureus (MIC=5-10 µg/ml), penicillin-resistant S. epidermidis (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 21876042 Antimicrob Agents Chemother. 2011 Nov;55(11):5220-9. Fan Z, Cao L, He Y, Hu J, Di Z, Wu Y, Li W, Cao Z. Ctriporin, a new anti-methicillin-resistant Staphylococcus aureus peptide from the venom of the scorpion Chaerilus tricostatus. DRAMP03702 LFGLIPSLIGGLVSAFK 17 Mucroporin (Antimicrobial peptide 36.21; Arthropods, animals) B9UIY3 Belongs to the short cationic antimicrobial peptide family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Function: Cationic host defense peptide that have antibacterial activity by breaking membranes. Is more effective on Gram-positive than on Gram-negative bacteria. Its synthetic analog mucroporin-M1 is more effective. Tissue specificity: Expressed by the venom gland. Miscellaneous: Minimum inhibitory concentrations (MIC) for Mucroporin-1 analog are the following: MIC=12.5 µg/ml against E.coli AB94012, MIC=100 µg/ml against P.aeruginosa AB93066, MIC=25 µg/ml against B.thuringiensis AB92037, MIC=25 µg/ml against B.subtilis AB91021, MIC=5 µg/ml against S.aureus AB94004, and MIC=5 µg/ml against the methicillin-resistant coagulase-negative Staphylococcus. Furthermore, this analog is as effective against antibiotic-resistant pathogens as it is against antibiotic-sensitive pathogens." Gram-negative bacteria: Escherichia coli AB94012 (MIC>100 µg/ml), Pseudomonas aeruginosa AB93066 (MIC>100 µg/ml);##Gram-positive bacteria: Bacillus thuringiensis AB92037 (MIC=25 µg/ml), Bacillus subtilis AB91021 (MIC=50 µg/ml), Staphylococcus aureus AB94004 (MIC=25 µg/ml), Methicillin-resistant coagulase-negative S. aureus (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 20663230##18779362 BMC Genomics. 2010 Jul 28;11:452.##Antimicrob Agents Chemother. 2008 Nov;52(11):3967-3972. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L.##Dai C, Ma Y, Zhao Z, Zhao R, Wang Q, Wu Y, Cao Z, Li W. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components.##Mucroporin, the first cationic host defense peptide from the venom of Lychas mucronatus. DRAMP03706 FLFSLIPHAIGGLISAFK 18 Antimicrobial peptide 1 (AamAP1; Arthropods, animals) G8YYA5 Not found ap1 Androctonus amoreuxi (African fattail scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial and antifungal activity. Causes hemolysis on horse erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: C-termianal amidation." Gram-positive bacterium: Staphylococcus aureus (MIC=20 µM);##Gram-negative bacterium: Escherichia coli (MIC=150 µM).##Yeast: Candida albicans (MIC=64 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 22484288 Peptides. 2012 Jun;35(2):291-299. Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C. Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog. DRAMP03707 FPFSLIPHAIGGLISAIK 18 Antimicrobial peptide 2 (AamAP2; Arthropods, animals) G8YYA6 Not found ap2 Androctonus amoreuxi (African fattail scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antibacterial and antifungal activity. Causes hemolysis on horse erythrocytes. Tissue specificity: Expressed by the venom gland. PTM: C-termianal amidation." Gram-positive bacterium: Staphylococcus aureus (MIC=48 µM);##Gram-negative bacterium: Escherichia coli (MIC=120 µM).##Yeast: Candida albicans (MIC=64 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 22484288 Peptides. 2012 Jun;35(2):291-299. Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C. Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog. DRAMP01392 GLLSGTSVRGSI 12 Odorranain-V1 (OdV1; Frogs, amphibians, animals) A6MBS7 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Odorranain-V1 exhibites moderate antimicrobial activities against all of the tested microbes. Also has hemolytic activity against rabbit red cells [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=36.00 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=18.00 μg/ml), Bacillus subtilis (MIC=18.00 μg/ml).##Yeast: Candida albicans (MIC=9.00 μg/ml). [Ref.17272268] RCH=23.9 ± 4.7% against rabbit red blood cells. RCH, red cell hemolysis. Linear Free Free Free L Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01393 GLFGKSSVWGRKYYVDLAGCAKA 23 Odorranain-W1 (OdW1; Frogs, amphibians, animals) A6MBS8 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Odorranain-W1 has hemolytic activity against rabbit red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=12.60 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.30 μg/ml), Bacillus subtilis (MIC=6.30 μg/ml).##Yeast: Candida albicans (MIC=3.15 μg/ml). [Ref.17272268] RCH=17.6 ± 2.2% against rabbit red blood cells. RCH, red cell hemolysis. Linear Free Free Free L Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP03715 FLSTLWNAAKSIF 13 Amphiphatic peptide CT2 (VmCT2; Non-disulfide-bridged peptide 5.14, NDBP-5.14; Arthropods, animal I0DEB4 Belongs to the scorpion NDBP 5 family Not found Vaejovis mexicanus smithi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Amphipatic peptide that shows antibacterial activities against both Gram-positive and Gram-negative bacteria. Has hemolytic at its MIC range, but shows a strong cytotoxic activity at higher concentrations, reaching 84% lysis at 50 µM. Tissue specificity: Expressed by the venom gland." [Ref.22342498]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=10 uM), Bacillus subtilis ATCC 6633 (MIC=20 µM), Streptococcus agalactiae (clinical isolate) (MIC=20 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=20 µM), Salmonella typhi ATCC 6399 (MIC=10 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=10 µM). [Ref.22342498]25% hemolytic activity at 25 μM, 84% hemolytic activity at 50 μM against human erythrocytes Linear Free Amidation Free L Not included yet Cell membrane 22342498 Peptides. 2012 Apr;34(2):290-295. Ramírez-Carreto S, Quintero-Hernández V, Jiménez-Vargas JM, Corzo G, Possani LD, Becerril B, Ortiz E. Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae. DRAMP01730 FLPLIGRVLSGIL 13 Temporin-A (Frogs, amphibians, animals) P56917 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found 2MAA resolved by NMR. "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has hemolytic activity. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." [Ref.9022710] Gram-positive bacteria: Bacillus megaterium BM11 (LC=1.2 µM), Staphylococcus aureus Cowan 1 (LC=2.3 µM), Streptococcus pyogenes betahemolytic group A (LC=2.0 µM);##Gram-negative bacteria: Escherichia coli D21 (LC=11.9 µM), Escherichia coli D21e7 (LC=1.4 µM), Escherichia coli D21f1 (LC=0.9 µM), Escherichia coli D21f2 (LC=4.8 µM), Escherichia coli D22 (LC=3.4 µM), Yersinia pseudotuberculosis (LC=2.0 µM), Pseudomonas aeruginosa ATCC 15692 (LC>360 µM);##Yeast: Candida albicans ATCC 10261 (LC=3.4 µM).(LC: Lethal concentration) [Ref.9022710] LC>120 µM against Human red blood cells. (LC: Lethal concentration) Linear Free Amidation Free L Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP03723 GKVWDWIKSAAKKIWSSEPVSQLKGQVLNAAKNYVAEKIGATPT 44 Pandinin-1 (Pin1; Arthropods, animals) P83239 Belongs to the Scorpion family Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found MOA: Disrupts cell membranes through formation of pores. Gram-negative bacteria: Pseudomonas aeruginosa (MIC>20.8 µM), Escherichia coli (MIC=20.8 µM);##Gram-positive bacteria: Enterococcus faecalis (MIC=1.3 µM), Bacillus subtilis (MIC=5.2 µM), Staphylococcus epidermidis (MIC=5.2 µM), Staphylococcus aureus (MIC=2.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Cell membrane 11563967##16199510 Biochem J. 2001 Oct 1;359(Pt 1):35-45.##Biophys J. 2005 Dec;89(6):4067-4080. Corzo G, Escoubas P, Villegas E, Barnham KJ, He W, Norton RS, Nakajima T.##Nomura K, Ferrat G, Nakajima T, Darbon H, Iwashita T, Corzo G. Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.##Induction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived pore-forming peptide. DRAMP03724 FWGALAKGALKLIPSLFSSFSKKD 24 Pandinin-2 (Pin2; Arthropods, animals) P83240 Belongs to the scorpion NDBP 4 family Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Hemolytic Protein level Alpha helix Not found "Function: Disrupts cell membranes through formation of pores. Has strong antimicrobial activity against Gram-positive bacteria and less active against Gram-negative bacteria. Possesses antifungal activity against C. albicans and hemolytic activity against sheep and pig erythrocytes. Tissue specificity: Expressed by the venom gland." [Ref.11563967]Gram-negative bacteria: Pseudomonas aeruginosa (MIC=38.2 µM), Escherichia coli (MIC=19.1 µM);#Gram-positive bacteria: Enterococcus faecalis (MIC=2.4 µM), Bacillus subtilis (MIC=4.8 µM), Staphylococcus epidermidis (MIC=4.8 µM), Staphylococcus aureus (MIC=2.4 µM);##Yeast: Candida albicans (MIC=19.1 µM). [Ref.11563967]Strong hemolytic activity (11.1-44.5 microM) against sheep erythrocytes Linear Free Free Free L Not included yet Cell membrane 11563967##15328050##15298871 Biochem J. 2001 Oct 1;359(Pt 1):35-45.##Biochim Biophys Acta. 2004 Aug 30;1664(2):182-188.##Biophys J. 2004 Oct;87(4):2497-507. Corzo G, Escoubas P, Villegas E, Barnham KJ, He W, Norton RS, Nakajima T.##Belokoneva OS, Satake H, Mal'tseva EL, Pal'mina NP, Villegas E, Nakajima T, Corzo G.##Nomura K, Corzo G, Nakajima T, Iwashita T. Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.##Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size.##Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers. DRAMP03729 KWFNEKSIQNKIDEKIGKNFLGGMAKAVVHKLAKNEFMCVANVDMTKSCDTHCQKASGEKGYCHGTKCKCGVPLSY 76 Opiscorpine-1 (Arthropods, animals) Q5WR03, Q5WQZ8 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: The short amino-terminal segment of opiscorpine 1 (residues 1–35), named Jan-f3, has antimicrobial activity against fungi and the Gram-negative bacteria. Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." Fungi: Fusarium culmorum IMI180420 (IC50=8.8 µM), Fusarium oxysporum MUCL39789 (IC50=10.04 µM).##Gram-negative bacterium: Escherichia coli JM109 (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15241551 Cell Mol Life Sci. 2004 Jul;61(14):1751-1763. Zhu S, Tytgat J. The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition. DRAMP03734 FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYAKGLLEGGSEEVPGQ 45 Parabutoporin (PP; Non-disulfide-bridged peptide 3.2, NDBP-3.2; Arthropods, animals) P83312 Belongs to the scorpion BPP family Not found Parabuthus schlechteri (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: At high concentrations, acts as pore former in cellular membranes and causes the leakage of the cells. At submicromolar concentrations, degranulates granulocytes and has hemolytic activity against human red blood cells. Also strongly inhibits the production of superoxide anions. Has a strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. Induces reversible G-protein dependent Ca2+ release from intracellular stores and increase Ca2+ influx in HL-60 cells. Induces the activation of the Rac pathway in granulocytes. Synergistically enhances the excitatory effects of short and long chain ion-channel-specific neurotoxins by interaction with the neuronal membranes. Tissue specificity: Expressed by the venom gland. NOTE: residue 11, 44, 55 are uncertainty." [Ref.12354111]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.1 µM), Escherichia coli DH5a (MIC=3.1 µM), Pseudomonas aeruginosa ATCC 257853 (MIC=6.3 µM), Klebsiella pneumoniae ATCC 13833 (MIC=1.6 µM), Salmonella choleraesuis ATCC 13311 (MIC=3.1 µM), Haemophilus influenzae ATCC 19418 (MIC=3.1 µM);##Gram-positive bacteria: Bacillus subtilis ATCC 6051 (MIC=6.3 µM), Listeria monocytogenes NCTC 11994 (MIC=6.3 µM), Micrococcus luteus ATCC 9341 (MIC=25 µM);##Fungi: Neurospora crassa (MIC=2.5 µM), Botrytis cinerea (MIC=3.5 µM), Fusarium culmorum (MIC=0.3 µM), Saccharomyces cerevisiae (MIC=2 µM). [Ref.12354111]50% hemolysis is induced by about 38 µM against human red blood cells Linear Free Free Free L Not included yet Cell membrane 12354111##12457879##14575699##15245865 Eur J Biochem. 2002 Oct;269(19):4799-4810.##Toxicon. 2002 Dec;40(12):1679-1683.##iochem Biophys Res Commun. 2003 Nov 7;311(1):90-97.##Peptides. 2004 Jul;25(7):1079-1084. Moerman L, Bosteels S, Noppe W, Willems J, Clynen E, Schoofs L, Thevissen K, Tytgat J, Van Eldere J, Van Der Walt J, Verdonck F.Willems J, Noppe W, Moerman L, van der Walt J, Verdonck F.##Moerman L, Verdonck F, Willems J, Tytgat J, Bosteels S.##Willems J, Moerman L, Bosteels S, Bruyneel E, Ryniers F, Verdonck F. Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa.##Cationic peptides from scorpion venom can stimulate and inhibit polymorphonuclear granulocytes.##Antimicrobial peptides from scorpion venom induce Ca(2+) signaling in HL-60 cells.##Parabutoporin--an antibiotic peptide from scorpion venom--can both induce activation and inhibition of granulocyte cell functions. DRAMP03735 GKVWDWIKSTAKKLWNSEPVKELKNTALNAAKNLVAEKIGATPS 44 Opistoporin-1 (OP1; Non-disulfide-bridged peptide 3.5; Opistoporin-3, OP3; Arthropods, animals) P83313, Q5VJS8, Q5VJT0 Belongs to the antimicrobial peptide scorpion family Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: At high concentrations, acts as pore former in cellular membranes and causes the leakage of the cells. At submicromolar concentrations, degranulates granulocytes and has hemolytic activity against human red blood cells. Also strongly inhibits the production of superoxide anions. Has a strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. Tissue specificity: Expressed by the venom gland." [Ref.12354111]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.5 µM), Escherichia coli DH5a (MIC=6.3 µM), Serratia marcescens ATCC 133880 (MIC=50 µM), Pseudomonas aeruginosa ATCC 257853 (MIC=12.5 µM), Klebsiella pneumoniae ATCC 13833 (MIC=6.3 µM), Salmonella choleraesuis ATCC 13311 (MIC=25 µM), Haemophilus influenzae ATCC 19418 (MIC=1.6 µM);##Gram-positive bacteria: Bacillus subtilis ATCC 6051 (MIC=12.5 µM), Bacillus subtilis IP 5832 (MIC=12.5 µM), Listeria monocytogenes NCTC 11994 (MIC=12.5 µM), Micrococcus luteus ATCC 9341 (MIC>50 µM), Enterococcus faecalis ATCC 19433 (MIC=12.5 µM), Staphylococcus aureus ATCC 292136.3 (MIC>50 µM), Streptococcus pneumoniae ATCC 33400 (MIC=12.5 µM), Nocardia asteroides ATCC 3308 (MIC>50 µM);##Fungi: Neurospora crassa (IC50=0.8 µM), Botrytis cinerea (IC50=3.1 µM), Fusarium culmorum (IC50=0.8 µM), Saccharomyces cerevisiae (IC50=2 µM). [Ref.12354111]10% hemolytic activity at 10 µM, 30% hemolytic activity at 100 µM against human red blood cells Linear Free Free Free L Not included yet Cell membrane 12354111##12457879##14575699 Eur J Biochem. 2002 Oct;269(19):4799-4810.##Toxicon. 2002 Dec;40(12):1679-1683.##iochem Biophys Res Commun. 2003 Nov 7;311(1):90-97. Moerman L, Bosteels S, Noppe W, Willems J, Clynen E, Schoofs L, Thevissen K, Tytgat J, Van Eldere J, Van Der Walt J, Verdonck F.Willems J, Noppe W, Moerman L, van der Walt J, Verdonck F.##Moerman L, Verdonck F, Willems J, Tytgat J, Bosteels S. Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa.##Cationic peptides from scorpion venom can stimulate and inhibit polymorphonuclear granulocytes.##Antimicrobial peptides from scorpion venom induce Ca(2+) signaling in HL-60 cells. DRAMP03738 GWINEEKIQKKIDERMGNTVLGGMAKAIVHKMAKNEFQCMANMDMLGNCEKHCQTSGEKGYCHGTKCKCGTPLSY 75 Scorpine (defensins; Arthropods, animals) P56972 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 7M1D##7M1E Function: Has antibacterial activity and a potent inhibitory effect on the ookinete (ED(50) 0.7 uM) and gamete (ED(50) 10 uM) stages of Plasmodium berghei development. Gram-positive bacterium: Bacillus subtilis (MIC=1.0 µM);##Gram-negative bacterium: Klebsiella pneumoniae (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys39 and Cys62,Cys49 and Cys67, Cys53 and Cys69. L Not included yet Not found 10767415 FEBS Lett. 2000 Apr 14;471(2-3):165-168. Conde R, Zamudio FZ, Rodríguez MH, Possani LD. Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom. DRAMP02828 GLFRRLRDSIRRGQQKILEKARRIGERIKDIFRG 34 BMAP-34 (BMAP 34, bovine cathelicidin, cattle, ruminant, mammals, animals) P56425 Belongs to the cathelicidin family. CATHL7 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Tissue specificity: Expressed in bone marrow myeloid cells, spleen and testis." [Ref.9795251] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=3 μM), Staphylococcus aureus Cowan 1 (MIC=3 μM), Staphylococcus aureus (MRSA, clinical isolate) (MIC=6 μM), Staphylococcus epidermidis ATCC 12228 (MIC=1.5 μM), Bacillus megaterium Bm 11 (MIC=3 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1.5 μM), Escherichia coli ML-35 (MIC=1.5 μM), Escherichia coli D21 (MIC=1.5 μM), Escherichia coli D22 (MIC=1.5 μM), Salmonella typhimurium ATCC 14028 (MIC=3 μM), Salmonella enteritidis (clinical isolate) (MIC=3 μM), Serratia marcescens ATCC 8100 (MIC=1.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC≥48 μM);##Fungus: Candida albicans (clinical isolate) (MIC>96 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 9409740##9795251 FEBS Lett. 1997 Nov 17;417(3):311-5.##Biochim Biophys Acta. 1998 Oct 23;1425(2):361-368. Scocchi M, Wang S, Zanetti M.##Gennaro R, Scocchi M, Merluzzi L, Zanetti M. Structural organization of the bovine cathelicidin gene family and identification of a novel member.##Biological characterization of a novel mammalian antimicrobial peptide. DRAMP02926 KWCFRVCYRGICYRRCR 17 Tachyplesin I (Tac; TP1; Horseshoe Crab, arachnids, Chelicerata, arthropods, invertebrates, animals) P14213 Belongs to the tachyplesin/polyphemusin family. Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Anti-HIV, Anti-cancer Protein level Beta strand This stability is due to the rigid structure imposed by the two disulfide linkages. Its amphipathic nature is closely associated with biological activity. A 1MA2, 1MA5, 6PIN, 1WO0, 1WO1, 2MDB, 2RTV resolved by NMR. "Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria, also anti-HIV activity may be due to the inhibition of virual adsorption to cells. PTM: Contains two disulfide bonds 3-16; 7-12 and Arginine amide at R17." No MICs found in DRAMP database [Ref.29870123] 9.6% hemolytic activity at 8 μg/mL and 72.8% hemolytic activity at 512 μg/mL against human red blood cells. Cyclic Free Amidation (Arg17) Disulfide bond between Cys3 and Cys16,Cys7 and Cys12. L [Ref.28429216]It possessed a cytotoxic effect on HL-60 cells (acutehuman promyelocytic leukemia cells) , K562 cells(myelogenous leukemia cells) , TSU cells (prostatecancer cells) . Cell membrane 12369825##2229025##31455019 Biochemistry 2002; 41: 12359.##J Biochem. 1990 Aug;108(2):261-266.##Int J Mol Sci. 2019 Aug 26;20(17):4184. Laederach A, Andreotti AH, Fulton, DB.##Muta T, Fujimoto T, Nakajima H, Iwanaga S.##Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S. Solution and Micelle-Bound Structures of Tachyplesin I and its Active Aromatic Linear Derivatives.##Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor.##Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties. DRAMP03746 FIGAIARLLSKIF 13 Peptide BmKn2 (Biologically active peptide 4; NDBP-5.1; Arthropods, animals) Q6JQN2 Not found Kn2 Mesobuthus martensii (Buthus martensii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus (MIC=0.6 µg/ml), Micrococcus luteus(MIC=8 µg/ml), Bacillus subtilis (MIC=5 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=1.5 µg/ml), Pseudomonas aeruginosa (MIC=21.3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 15062994 Peptides. 2004 Feb;25(2):143-150. Zeng XC, Wang SX, Zhu Y, Zhu SY, Li WX. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch. DRAMP03748 FRFGSFLKKVWKSKLAKKLRSKGKQLLKDYANKVLNGPEEEAAAPAE 47 Bradykinin-potentiating peptide BmK3 (Bpp BmK3; NDBP-3.3; Arthropods, animals) Q9Y0X4 Belongs to the scorpion BPP family Not found Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Alpha helix (predict) The secondary structure prediction for BmKbpp reveals that BmKbpp is composed of an α-helical structure from amino residues 3-35, followed by a coil-coiled region of three residues (NGP), and ended with an α-helical region of 9 residues (ref.2). "Function: Amphipathic peptide that shows bradykinin potentiating activity and antimicrobial activities against bacteria and fungi. Has higher antibacterial activities against Gram-negative than against Gram-positive bacteria. Also inhibits NADPH oxidase-dependent superoxide production (IC50 is 0.4 µM on granulocytes stimulated with PMA, IC50 is 0.51 µM on HL-60 cells undifferentiated and IC50 is 0.53 µM on HL-60 cells treated with DMSO). The C-terminal peptide shows a higher bradykinin potentiating activity than the complete peptide. Tissue specificity: Expressed by the venom gland. Miscellaneous: Shows hemolytic activity. Shows a alpha-helical structure. The genomic DNA coding for this protein is not a continuous sequence in the genome. The transcript of this protein may be generated by trans-splicing, by which exons from two independently transcribed pre-mRNAs are joined to form a single mature transcript." [Ref.22115565]Gram-negative bacteria: Escherichia coli DH 5-α (MIC=2.3 µM), Haemophilus influenzae ATCC 31517 (MIC=3.2 µM), Klebsiella pneumoniae ATCC 13882 (MIC=2.8 µM), Salmonella enterica ATCC 8090 (MIC=2.3 µM), Pseudomonas aeruginosa ATCC 9229 (MIC=4.7 µM), Serratia marcescens ATCC 13880 (MIC=68.2 µM);##Gram-positive bacteria: Bacillus subtilis ATCC 6051 (MIC=24.4 µM), Listeria monocytogenes ATCC 35152 (MIC=5.7 µM), Micrococcus luteus ATCC 9341 (MIC=20.3 µM), Enterococcus faecalis ATCC 14508 (MIC=57.1 µM), Nocardia asteroides ATCC 3308 (MIC>70 µM), Staphylococcus aureus ATCC 14458 (MIC>70 µM);##Fungi: Neurospora crassa FGSC 2489 (IC50=2 µM), Botrytis cinerea ATCC 28387 (IC50=3.1 µM), Fusarium culmorum ATCC 32973 (IC50=0.2 µM). [Ref.22115565]3.5% hemolytic activity at 6 μM, 11.2% hemolytic activity at 10 μM, 22.5% hemolytic activity at 30 μM, 33.9% hemolytic activity at 50 μM against human red blood cells Linear Free Free Free L Not included yet Not found 10868911##22115565 IUBMB Life. 2000 Mar;49(3):207-210.##Peptides. 2012 Jan;33(1):44-51. Zeng XC, Li WX, Peng F, Zhu ZH.##Zeng XC, Wang S, Nie Y, Zhang L, Luo X. Cloning and characterization of a novel cDNA sequence encoding the precursor of a novel venom peptide (BmKbpp) related to a bradykinin-potentiating peptide from Chinese scorpion Buthus martensii Karsch.##Characterization of BmKbpp, a multifunctional peptide from the Chinese scorpion Mesobuthus martensii Karsch: gaining insight into a new mechanism for the functional diversification of scorpion venom peptides. DRAMP03750 IFGAIAGLLKNIF 13 Venom antimicrobial peptide-6 (Meucin-13; NDBP-5; Arthropods, animals) E4VP07, E4VP35 Belongs to the scorpion NDBP 5 family Not found Mesobuthus eupeus (Lesser Asian scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Amphipathic peptide that exhibits extensive cytolytic activities against both prokaryotic and eukaryotic cells. Is more potent against Gram-positive bacteria (lethal concentration (LC=0.25-2.9 µM) than against Gram-negative bacteria (LC=6.2->50 µM), and fungi (LC=14.1->50 µM). Shows hemolytic activity against rabbit erythrocytes and cytolysis against rat dorsal root ganglions. In vivo, intravenous injection into mice tail provokes uncomfortable symptoms with a death rate of 12.5%. Tissue specificity: Expressed by the venom gland." [Ref.19088182]Gram-positive bacteria: Bacillus sp. DM-1 (MIC=2 µM), Micrococcus luteus (MIC=2.9 µM), Bacillus megaterium (MIC=0.25 µM);##Gram-negative bacteria: Agrobacterium tumefaciens (MIC=11.8 µM), Escherichia coli (MIC=7.90 µM), Shewanella oneidensis (MIC=6.20 µM), Stenotrophomonus sp. YC-1 (MIC=6.20 µM);##Fungi: Beauveria spp. (MIC=14.1 µM), Neurospora crassa (MIC=18.3 µM), Candida albicans (MIC=42.8 µM), Saccharomyces cerevisiae (MIC=18.3 µM). [Ref.19088182]37.7% hemolytic activity at 6.25 M, 59.2% hemolytic activity at 12.5 M against rabbit red blood cells Linear Free Amidation Free L Not included yet Cell membrane 19088182 FASEB J. 2009 Apr;23(4):1230-1245. Gao B, Sherman P, Luo L, Bowie J, Zhu S. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides. DRAMP03751 FFGHLFKLATKIIPSLFQ 18 Venom antimicrobial peptide-9 (Meucin-18; NDBP-5; Arthropods, animals) E4VP50 Belongs to the ponericin-W family Not found Mesobuthus eupeus (Lesser Asian scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Amphipathic peptide that exhibits extensive cytolytic activities against both prokaryotic and eukaryotic cells. Is more potent against Gram-positive bacteria (lethal concentration (LC=1.5-10.9 µM) than against Gram-negative bacteria (LC=6.2-50 µM), and fungi (LC=25.1-8.3 µM). Is lethal to the fungus Beauveria sp (LC=1.9 µM), a highly lethal pathogenic fungus to insects and resistant to many AMPs. Shows hemolytic activity against rabbit erythrocytes and cytolysis against rat dorsal root ganglions. In vivo, intravenous injection into mice tail provokes uncomfortable symptoms with a death rate of 12.5%. Tissue specificity: Expressed by the venom gland." [Ref.19088182]Gram-positive bacteria: Bacillus sp. DM-1 (MIC=0.60 µM), Micrococcus luteus (MIC=0.60 µM), Bacillus megaterium (MIC=0.25 µM);##Gram-negative bacteria: Agrobacterium tumefaciens (MIC=6.00 µM), Escherichia coli (MIC=2.40 µM), Shewanella oneidensis (MIC=1.50 µM), Stenotrophomonus sp. YC-1(MIC=2.60 µM), Salmonella typhimurium (MIC=10.9 µM);##Fungi: Beauveria spp.(MIC=1.9 µM), Neurospora crassa (MIC=5.2 µM), Candida albicans (MIC=25.1 µM), Saccharomyces cerevisiae (MIC=25.1 µM), Aspergillus fumigatus (MIC=8.3 µM), Geotrichum candidum (MIC=3.5 µM). [Ref.19088182]74% hemolytic activity at 6.25 M, 100% hemolytic activity at 12.5 M against rabbit red blood cells Linear Free Free Free L Not included yet Cell membrane 19088182 FASEB J. 2009 Apr;23(4):1230-1245. Gao B, Sherman P, Luo L, Bowie J, Zhu S. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides. DRAMP03752 FLFSLIPSAISGLISAFK 18 Peptide BmKb1 (Non-disulfide-bridged peptide 4.2, NDBP-4.2; Arthropods, animals) Q718F4, Q2M5D6 Q95P85 Not found Kb1 Mesobuthus martensii (Manchurian scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Micrococcus luteus(MIC=81.5 µg/ml), Bacillus subtilis (MIC=48.8 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=18.1 µg/ml), Pseudomonas aeruginosa (MIC=90.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane (Forms a helical membrane channel in the prey) 15062994##16040157 Peptides. 2004 Feb;25(2):143-150.##Peptides. 2005 Dec;26(12):2427-2433. Zeng XC, Wang SX, Zhu Y, Zhu SY, Li WX.##Luo F, Zeng XC, Hahin R, Cao ZJ, Liu H, Li WX. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch.##Genomic organization of four novel nondisulfide-bridged peptides from scorpion Mesobuthus martensii Karsch: gaining insight into evolutionary mechanism. DRAMP03753 GFWGSLWEGVKSVV 14 Amphipathic peptide CT1 (StCT1; Non-disulfide-bridged peptide 5, NDBP-5; Arthropods, animals) P0DJO3 Not found Not found Scorpiops tibetanus (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide that is rapidly bactericidal against Gram-positive bacteria (MIC=12.5 µg/ml against S.aureus, and MIC=100 µg/ml against M. luteus). Is also active against clinical antibiotics-resistant bacterial strains. PTM: C-terminal amidation and Cleavage on pair of basic residues. Miscellaneous: Is highly capable of inhibiting antibiotic-resistant pathogen growth, including methicillin-resistant S.aureus. In vivo, shows high antimicrobial activity on a S.aureus-infected mouse model." Gram-positive bacteria: Staphylococcus aureus AB94004 (MIC=12.5 µg/ml), Bacillus thuringensis AB92037 (MIC>100 µg/ml), Bacillus subtilis AB91021 (MIC>100 µg/ml), Micrococcus luteus AB93113 (MIC=100 µg/ml), MRSA P1374 (MIC=200 µg/ml), MRSA P1386 (MIC=250 µg/ml);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=100 µg/ml), Pseudomonas aeruginosa AB93066 (MIC=100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 19854232 Peptides. 2010 Jan;31(1):22-26. Yuan W, Cao L, Ma Y, Mao P, Wang W, Zhao R, Wu Y, Cao Z, Li W. Cloning and functional characterization of a new antimicrobial peptide gene StCT1 from the venom of the scorpion Scorpiops tibetanus. DRAMP03754 GFWGKLWEGVKSAI 14 Amphipathic peptide CT2 (StCT2; Non-disulfide-bridged peptide 5, NDBP-5; Arthropods, animals) P0DJO4 Not found Not found Scorpiops tibetanus (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "PTM: C-terminal amidation and Cleavage on pair of basic residues. Miscellaneous: Is highly capable of inhibiting antibiotic-resistant pathogen growth, including methicillin-resistant S.aureus. In vivo, shows high antimicrobial activity on a S.aureus-infected mouse model." Gram-positive bacteria: Staphylococcus aureus AB94004 (MIC=6.25 µg/ml), Bacillus thuringensis AB92037 (MIC=50 µg/ml), Bacillus subtilis AB91021 (MIC=25 µg/ml), Micrococcus luteus AB93113 (MIC=25 µg/ml), PRSA P1383 (MIC=12.5 µg/ml), PRSE P1389 (MIC=12.5 µg/ml), MRCNS P1369 (MIC=6.25 µg/ml), MRSA P1374 (MIC=6.25 µg/ml), MRSA P1386 (MIC=12.5 µg/ml), MRSA P1381 (MIC=25 µg/ml), MSSE P1111 (MIC=6.25 µg/ml);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=50 µg/ml), Pseudomonas aeruginosa AB93066 (MIC>100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Cell membrane 22542475 Peptides. 2012 Aug;36(2):213-220. Cao L, Li Z, Zhang R, Wu Y, Li W, Cao Z. StCT2, a new antibacterial peptide characterized from the venom of the scorpion Scorpiops tibetanus. DRAMP03774 GFWGKLWEGVKNAI 14 UyCT1 (Arthropods, animals) No entry found Not found Not found Urodacus yaschenkoi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows minimum inhibitory concentration against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23182832]Gram-positive bacterium: Staphylococcus aureus ATCC 25953 (MIC=15 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=10 µM). [Ref.23182832]20% hemolytic activity at 12.5 μM, 45% hemolytic activity at 25 μM, 80% hemolytic activity at 50 μM, 90% hemolytic activity at 100 μM against human erythrocytes Linear Free Amidation Free L Not included yet Not found 23182832 Toxicon. 2013 Mar 1;63:44-54. Luna-Ramírez K, Quintero-Hernández V, Vargas-Jaimes L, Batista CV, Winkel KD, Possani LD. Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: Molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity. DRAMP03775 FWGKLWEGVKNAI 13 UyCT2 (Arthropods, animals) No entry found Not found Not found Urodacus yaschenkoi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Shows minimum inhibitory concentration against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23182832]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=25 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=40 µM). [Ref.23182832]3% hemolytic activity at 12.5 μM, 6% hemolytic activity at 25 μM, 5% hemolytic activity at 50 μM, 35% hemolytic activity at 100 μM against human erythrocytes Linear Free Amidation Free L Not included yet Not found 23182832 Toxicon. 2013 Mar 1;63:44-54. Luna-Ramírez K, Quintero-Hernández V, Vargas-Jaimes L, Batista CV, Winkel KD, Possani LD. Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: Molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity. DRAMP03776 ILSAIWSGIKSLF 13 UyCT3 (Arthropods, animals) No entry found Not found Not found Urodacus yaschenkoi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows minimum inhibitory concentration against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23182832]Gram-positive bacterium: Staphylococcus aureus ATCC 25953 (MIC=10 µM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=6 µM). [Ref.23182832]30% hemolytic activity at 12.5 μM, 90% hemolytic activity at 25 μM, 92% hemolytic activity at 50 μM, 90% hemolytic activity at 100 μM against human erythrocytes Linear Free Amidation Free L Not included yet Not found 23182832 Toxicon. 2013 Mar 1;63:44-54. Luna-Ramírez K, Quintero-Hernández V, Vargas-Jaimes L, Batista CV, Winkel KD, Possani LD. Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: Molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity. DRAMP03777 IWSAIWSGIKGLL 13 UyCT5 (Arthropods, animals) No entry found Not found Not found Urodacus yaschenkoi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Shows minimum inhibitory concentration against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23182832]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µM), Pseudomonas aeruginosa ATCC 9027 (MIC=2 µM).##Gram-positive bacterium: Staphylococcus aureus ATCC 25953 (MIC=1 µM). [Ref.23182832]27% hemolytic activity at 12.5 μM, 65% hemolytic activity at 25 μM, 95% hemolytic activity at 50 μM, 90% hemolytic activity at 100 μM against human erythrocytes Linear Free Amidation Free L Not included yet Not found 23182832 Toxicon. 2013 Mar 1;63:44-54. Luna-Ramírez K, Quintero-Hernández V, Vargas-Jaimes L, Batista CV, Winkel KD, Possani LD. Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: Molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity. DRAMP03797 GLRKRLRKFRNKIKEKLKKIGQKIQGFVPKLAPRTDY 37 CAP7 (C-terminal fragment of CAP18; lagomorphs, mammals, animals) P25230 Belongs to the cathelicidin family CAP18 Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial Protein level Alpha helix (1 helices; 30 residues) Not found 1LYP resolved by NMR. "Function: CAP18 binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Has antibiotic activity. Tissue specificity: Neutrophils. PTM: Contains two disulfide bonds (By similarity)." [No NaCl]: Escherichia coli DH5a (MIC=0.19 µM), Escherichia coli ML-35p (MIC=0.05 µM), Pseudomonas aeruginosa PAO1 (MIC=0.2 µM), Pseudomonas aeruginosa MR3007 (MIC=0.05 µM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=1.24 µM), Staphylococcus aureus 93918 (MIC=0.41 µM).##[100 mM NaCl]: Escherichia coli DH5a (MIC=0.21 µM), Escherichia coli ML-35p (MIC=0.09 µM), Pseudomonas aeruginosa PAO1 (MIC=0.62 µM), Pseudomonas aeruginosa MR3007 (MIC=0.36 µM), Staphylococcus aureus ATCC (MRSA) 33591 (MIC=1.36 µM), Staphylococcus aureus 93918 (MIC=0.63 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Lipopolysaccharides (LPS)-binding 8132348##10768969##7649303 Antimicrob Agents Chemother. 1993 Dec;37(12):2534-2539.##Infect Immun. 2000 May;68(5):2748-2755.##FEBS Lett. 1995 Aug 14;370(1-2):46-52. Larrick JW, Hirata M, Shimomoura Y, Yoshida M, Zheng H, Zhong J, Wright SC.##Travis SM, Anderson NN, Forsyth WR, Espiritu C, Conway BD, Greenberg EP, McCray PB Jr, Lehrer RI, Welsh MJ, Tack BF.##Chen C, Brock R, Luh F, Chou PJ, Larrick JW, Huang RF, Huang TH. Antimicrobial activity of rabbit CAP18-derived peptides.##Bactericidal activity of mammalian cathelicidin-derived peptides.##The solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytes. DRAMP03814 GILDTLKQFAKGVGKWLVKGAAQGVLSTVSCKLAKTC 37 D16W (GGN4 analogue peptide with single substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Single substitution of aspartic acid 16 by tryptophan (D16W) in the native GGN4. Has hemolytic activity as well as the antimicrobial activity. [Ref.12199716]Gram-positive bacteria: Micrococcus luteus (MIC=25 µg/ml), Bacillus subtilis (MIC=2.5 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=10 µg/ml), Shigella dysentariae (MIC=10 µg/ml), Pseudomonas putida (MIC=100 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml), Eshchericia coli (MIC=10 µg/ml), Salmonella typhimurium (MIC=50 µg/ml). [Ref.12199716] 1.97% hemolytic activity at 10 µg/mL, 52.9% hemolytic activity at 100 µg/mL against human red blood cells. Cyclic Free Cyclization(Cys31 and Cys37). Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 12199716 Eur J Biochem. 2002 Sep;269(17):4367-4374. Won HS, Park SH, Kim HE, Hyun B, Kim M, Lee BJ, Lee BJ. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. DRAMP03815 GILDTLKQFAKGVGKWLVKGAAQ 23 D16W-N23 (single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: Single substitution of aspartic acid 16 by tryptophan (D16W) in the Delta24-37 GGN4, which is a peptide analogue with 14 residues truncated from the C-terminus of GGN4. Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Bacillus subtilis (MIC=25 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=25 µg/ml), Shigella dysentariae (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=125 µg/ml), Eshchericia coli (MIC=25 µg/ml), Salmonella typhimurium (MIC=125 µg/ml). [Ref.12199716] 0.02% hemolytic activity at 10 µg/mL, 0.38% hemolytic activity at 100 µg/mL against human red blood cells. Linear Free Free Free L Not included yet Not found 12199716 Eur J Biochem. 2002 Sep;269(17):4367-4374. Won HS, Park SH, Kim HE, Hyun B, Kim M, Lee BJ, Lee BJ. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. DRAMP03816 GILDTLKQFAKGVGKFLVKGAAQ 23 D16F-N23 (single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: Single substitution of aspartic acid 16 by phenylalanine (D16F) in the Delta24-37 GGN4, which is a peptide analogue with 14 residues truncated from the C-terminus of GGN4. Gram-positive bacterium: Bacillus subtilis (MIC=25 µg/ml);##Gram-negative bacteria: Klebsiella pneumoniae (MIC=100 µg/ml), Shigella dysentariae (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=200 µg/ml), Eshchericia coli (MIC=25 µg/ml). [Ref.12199716] 0.06% hemolytic activity at 10 µg/mL, 0.32% hemolytic activity at 100 µg/mL against human red blood cells. Linear Free Free Free L Not included yet Not found 12199716 Eur J Biochem. 2002 Sep;269(17):4367-4374. Won HS, Park SH, Kim HE, Hyun B, Kim M, Lee BJ, Lee BJ. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. DRAMP03823 ALWKTLLKKVLKA 13 Dermaseptin derivative K4-S4-(1-13) P80280 Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix (1 helices; 5 residues) The Ramachandran plot of P showes that residues 2 and 4-13 are all in α-helix regions of the plot; the residues in all of the structures are in the core α-helix region for residues 2, 3, and 6-11, and both residue 5 and 12 had over 60% in the core and the rest in allowed α-helix regions. 2DD6 resolved by NMR. Function: Has antibacterial activity. Also has hemolytic activity against red blood cells (RBCs). [Ref.15917541]Gram-negative bacterium: Escherichia coli U16318 (MIC=9-3 µM);##Gram-positive bacterium: Staphylococcus aureus B38302 (MIC=4.5-1.5 µM). [Ref.15917541]LC50=50 μM against human red blood cells Linear Free Amidation Free L Not included yet Cell membrane 16407175##15917541 J Biol Chem. 2006 Apr 7;281(14):9432-9438.##Antimicrob Agents Chemother. 2005 Jun;49(6):2412-2420. Shalev DE, Rotem S, Fish A, Mor A.##Radzishevsky IS, Rotem S, Zaknoon F, Gaidukov L, Dagan A, Mor A. Consequences of N-acylation on structure and membrane binding properties of dermaseptin derivative K4-S4-(1-13).##Effects of acyl versus aminoacyl conjugation on the properties of antimicrobial peptides. DRAMP03824 FKCRRWQWR 9 CNBr-cleaved lactoferricin Subfragment 1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: The antibacterial activity of this subfragment 1 is not as potent as that of intact lactoferricin, having an MIC of 10 to 50 µM for most of the bacteria tested. Gram-negative bacteria: Escherichia coli L361 (MIC=10 µM), Pseudomonas fluorescens (MIC=50 µM), Salmonella Salford (MIC>50 µM), Escherichia coli O:9 (MIC=15 µM);##Gram-positive bacteria: Bacillus cereus (MIC=20 µM), Listeria monocytogenes (MIC=10 µM), Staphylococcus aureus (MIC>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Linked with a homoserine lactone Free L Not included yet Not found 8980754 Antimicrob Agents Chemother. 1997 Jan;41(1):54-59. Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. DRAMP03825 KKLGAPSITCVRRAFA 16 CNBr-cleaved lactoferricin Subfragment 2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Subfragment 2 had weak antibacterial activity against L. monocytogenes and both E. coli isolates, being effective in the range of 40 to 60 µM. Gram-negative bacteria: Escherichia coli L361 (MIC=50 µM), Pseudomonas fluorescens (MIC>100 µM), Salmonella Salford (MIC>100 µM), Escherichia coli O:9 (MIC=60 µM);##Gram-positive bacteria: Bacillus cereus (MIC>100 µM), Listeria monocytogenes (MIC=40 µM), Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 8980754 Antimicrob Agents Chemother. 1997 Jan;41(1):54-59. Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. DRAMP03826 KNLRRIIRKIIHIIKKYG 18 Ovispirin-1 (OV-1; N-terminal 18 amino acids of SMAP-29) No entry found Not found Not found Synthetic construct Antibacterial, Cytotoxic, Anti-Gram+, Anti-Gram-, Antimicrobial Synthetic Alpha helix (1 helices; 13 residues) Ovispirin-1 is a uniform α-helix over residues 4-16. 1HU5 resolved by NMR. Function: Possess potently antimicrobial activity. It is also highly cytotoxic to human epithelial cells (ME-180 cervical cells: 100% at 200 µg/ml, 93.6% at 50 µg/ml, 55.3% at 25 µg/ml) and A-549 pulmonary cells: 99.7% at 200 µg/ml, 99.4% at 50 µg/ml, 90.9% at 25 µg/ml) and hemolytic for human Human red blood cells. [Ref.11932493]Gram-negative bacteria: Pseudomonas aeruginosa 9 strains (MIC=0.7-5.6 µg/ml), Stenotrophomonas maltophilia 5 strains (MIC=0.5-2.2 µg/ml);##Gram-positive bacteria: Listeria monocytogenes EGD [n=3] (MIC=1.5±0.3 µg/ml), Staphylococcus aureus 930918 [n=3] (MIC=1.0±0.13 µg/ml). [Ref.11932493]55% hemolytic at 40 µg/mL, 70.2% hemolytic activity at 80 µg/mL against human red blood cells Linear Free Free Free L Not included yet Not found 11932493 Protein Eng. 2002 Mar;15(3):225-232. Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF. Impact of single-residue mutations on the structure and Function: of ovispirin/novispirin antimicrobial peptides. DRAMP03827 KNLRRIIRKGIHIIKKYG 18 Novispirin G-10 (mutation of Ovispirin-1) No entry found Not found Not found Synthetic construct Antibacterial, Cytotoxic, Anti-Gram+, Anti-Gram-, Antimicrobial Synthetic Alpha helix (2 helices; 11 residues) Novispirin G-10 shows an α-helix-hinge-310 helix structural motif with residues 4-11 forming the α-helix, residues 12 and 13 forming the hinge and residues 14-16 forming the 310 helix. 1HU6 resolved by NMR. Function: Possess potently antimicrobial activity. Also has hemolytic activity against Human red blood cells, and has cytotoxicity activity against ME-180 cervical cells (33.2% at 200 µg/ml, 5.0% at 50 µg/ml, 7.1% at 25 µg/ml) and A-549 pulmonary cells (33.2% at 200 µg/ml, 14.6% at 50 µg/ml, 10.0% at 25 µg/ml). [Ref.11932493]Gram-negative bacteria: Pseudomonas aeruginosa 9 strains (MIC=0.11-12.7 µg/ml), Stenotrophomonas maltophilia 5 strains (MIC=0.29-3.6 µg/ml);##Gram-positive bacteria: Listeria monocytogenes EGD [n=3] (MIC=1.4±0.4 µg/ml), Staphylococcus aureus 930918 [n=3] (MIC=4.6±1.7 µg/ml). [Ref.11932493]1.8% hemolytic at 40 µg/mL, 2.5% hemolytic activity at 80 µg/mL against human red blood cells Linear Free Free Free L Not included yet Not found 11932493 Protein Eng. 2002 Mar;15(3):225-232. Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF. Impact of single-residue mutations on the structure and Function: of ovispirin/novispirin antimicrobial peptides. DRAMP03828 KNLRRITRKIIHIIKKYG 18 Novispirin T-7 (mutation of Ovispirin-1) No entry found Not found Not found Synthetic construct Antibacterial, Cytotoxic, Anti-Gram+, Anti-Gram-, Antimicrobial Synthetic Alpha helix (1 helices; 11 residues) Novispirin T-7 is a well-defined α-helix over residues 7-17 with residues 3-6 forming a type IV turn. 1HU7 resolved by NMR. Function: Possess potently antimicrobial activity. Also has hemolytic activity against Human red blood cells, and has cytotoxicity activity against ME-180 cervical cells (81.5% at 200 µg/ml, 28.4% at 50 µg/ml, 15.6% at 25 µg/ml) and A-549 pulmonary cells (81.5% at 200 µg/ml, 22.9% at 50 µg/ml, 15.4% at 25 µg/ml). [Ref.11932493]Gram-negative bacteria: Pseudomonas aeruginosa 9 strains (MIC=0.26-27.8 µg/ml), Stenotrophomonas maltophilia 5 strains (MIC=0.32-1.75 µg/ml);##Gram-positive bacteria: Listeria monocytogenes EGD (MIC=2.4±1.5 [n=3] µg/ml), Staphylococcus aureus 930918 (MIC=3.3±1.5 [n=3] µg/ml). [Ref.11932493]3% hemolytic at 40 µg/mL, 10% hemolytic activity at 80 µg/mL against human red blood cells Linear Free Free Free L Not included yet Not found 11932493 Protein Eng. 2002 Mar;15(3):225-232. Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF. Impact of single-residue mutations on the structure and Function: of ovispirin/novispirin antimicrobial peptides. DRAMP03829 GLKKLLGKLLKKLGKLLLK 19 GLK-19 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anticancer Synthetic Not found Not found Function: GLK-19 showed a higher activity against Escherichia coli than human LL-37. Gram-negative bacterium: Escherichia coli K12 (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 18957441 Nucleic Acids Res. 2009 Jan;37(Database issue):D933-937. Wang G, Li X, Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. DRAMP03830 GLWNSIKIAGKKLFVNVLDKIRCKVAGGCKTSPDVEYHK 39 Palustrin-2ISb + 3aa No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=6.3 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 µM), S. aureus (MRSA) (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys23 and Cys29. L Not included yet Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-3 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03831 GLWNSIKIAGKKLFVNVLDKIRCKVAGGC 29 Palustrin-2ISb-des-C7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=6.3 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=1.6 µM), S. aureus (MRSA) (MIC=12.5 µM).##Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys23 and Cys29). Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-4 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03832 GLWDSIKIAGKKLFVNVLDKIRCKVAGGC 29 Palustrin-2ISb-des-C7-4D No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), S. aureus (MRSA) (MIC=12.5 µM);##yeast Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys23 and Cys29). Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-5 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03833 GLWNSIKIAGKNLFVNVLDKIRCKVAGGC 29 Palustrin-2ISb-des-C7-12N No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 µM), S. aureus (MRSA) (MIC=12.5 µM);##yeast Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys23 and Cys29). Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-6 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03834 GLWNSIKIAGKKLFVNVLDKIRSKVAGGS 29 Palustrin-2ISb-des-C7-23,29S No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=3.1 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 µM), S. aureus (MRSA) (MIC=25 µM);##yeast Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Free L Not included yet Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-7 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03835 GKKLFVNVLDKIRCKVAGGC 20 Palustrin-2ISb-des-C7-des-N9 No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Yeast: Candida albicans (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys14 and Cys20). Disulfide bond between Cys14 and Cys20. L No cytotoxicity information found Not found 21911019 Peptides. 2011 Oct;32(10):2052-2057. Iwakoshi-Ukena E, Okada G, Okimoto A, Fujii T, Sumida M, Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-8 family isolated from the skin of the endangered frog Odorrana ishikawae. DRAMP03852 GLARIVVIRVAR 12 G1 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=125 µg/ml), Escherichia coli (MIC=16 µg/ml), Salmonella typhimurium (MIC=63 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=63 µg/ml), Staphylococcus epidermidis (MIC=16 µg/ml), Enterococcus faecalis (MIC=31 µg/ml).##Yeast: Candida albicans (MIC=125 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03853 RGARIVVIRVAR 12 G2 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=31 µg/ml), Escherichia coli (MIC=8 µg/ml), Salmonella typhimurium (MIC=31 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=31 µg/ml), Staphylococcus epidermidis (MIC=16 µg/ml), Enterococcus faecalis (MIC=31 µg/ml).##Yeast: Candida albicans (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03854 RRARIVVIRVAR 12 R2 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=8 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=16 µg/ml).##Yeast: Candida albicans (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03855 RLRRIVVIRVAR 12 R3 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=8 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=8 µg/ml).##Yeast: Candida albicans (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03856 RLWRIVVIRVAR 12 W3 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=8 µg/ml), Escherichia coli (MIC=2 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=0.5 µg/ml), Enterococcus faecalis (MIC=2 µg/ml).##Yeast: Candida albicans (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03857 RLARRVVIRVAR 12 R5 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=63 µg/ml), Escherichia coli (MIC=16 µg/ml), Salmonella typhimurium (MIC=31 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=63 µg/ml), Staphylococcus epidermidis (MIC=16 µg/ml), Enterococcus faecalis (MIC=125 µg/ml).##Yeast: Candida albicans (MIC=125 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03858 RLARIVKIRVAR 12 K7 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=31 µg/ml), Escherichia coli (MIC=16 µg/ml), Salmonella typhimurium (MIC=63 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=125 µg/ml), Staphylococcus epidermidis (MIC=31 µg/ml), Enterococcus faecalis (MIC=125 µg/ml).##Yeast: Candida albicans (MIC=31 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03859 RLARIVVIRWAR 12 W10 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=16 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=4 µg/ml).##Yeast: Candida albicans (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03860 RLARIVVIRVRR 12 R11 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=16 µg/ml), Escherichia coli (MIC=8 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=8 µg/ml).##Yeast: Candida albicans (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03861 RLARIVVIRVAG 12 G12 (Bac2A variant through single amino acid substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=63 µg/ml), Escherichia coli (MIC=16 µg/ml), Salmonella typhimurium (MIC=63 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=63 µg/ml), Staphylococcus epidermidis (MIC=31 µg/ml), Enterococcus faecalis (MIC=31 µg/ml).##Yeast: Candida albicans (MIC=63 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03862 RLRRIVVIRVRR 12 Sub2 (Bac2A variant through two amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=8 µg/ml), Escherichia coli (MIC=2 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=4 µg/ml).##Yeast: Candida albicans (MIC=31 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03863 RRWRIVVIRVRR 12 Sub3 (Bac2A variant through three amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Half Life: With a half-life of approximately 1h in 25% aqueous mouse serum,Sub3 was relatively stable for a medium-sized peptide. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=2 µg/ml), Escherichia coli (MIC=2.5 µg/ml), Salmonella typhimurium (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=0.2 µg/ml), Enterococcus faecalis (MIC=4 µg/ml).##Yeast: Candida albicans (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03864 RRWKIVVIRWRR 12 Sub5 (Bac2A variant through five amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=2 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=0.5 µg/ml), Enterococcus faecalis (MIC=2 µg/ml).##Yeast: Candida albicans (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03865 RWWKIWVIRWWR 12 Sub6 (Bac2A variant through six amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: Optimized 12-mer peptides shows broad spectrum antibacterial activity against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=31 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=16 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Staphylococcus epidermidis (MIC=1 µg/ml), Enterococcus faecalis (MIC=8 µg/ml).##Yeast: Candida albicans (MIC=31 µg/ml).. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03866 KIWVIRWR 8 Bac8a (Bac2A variant) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: 8-mer substituted peptide that showes broad spectrum activity against bacteria and the yeast C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=16 µg/ml), Escherichia coli (MIC=8 µg/ml), Salmonella typhimurium (MIC=31 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Staphylococcus epidermidis (MIC=4 µg/ml), Enterococcus faecalis (MIC=16 µg/ml).##Yeast: Candida albicans (MIC=16 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03867 RIWVIRWR 8 Bac8b (Bac2A variant) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: 8-mer substituted peptide that showes broad spectrum activity against bacteria and the yeast C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=16 µg/ml), Escherichia coli (MIC=4 µg/ml), Salmonella typhimurium (MIC=16 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=4 µg/ml), Staphylococcus epidermidis (MIC=4 µg/ml), Enterococcus faecalis (MIC=8 µg/ml).##Yeast: Candida albicans (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03868 RIWVIWRR 8 Bac8c (Bac2A variant) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: 8-mer substituted peptide that showes broad spectrum activity against bacteria and the yeast C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=8 µg/ml), Escherichia coli (MIC=2 µg/ml), Salmonella typhimurium (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=2 µg/ml), Enterococcus faecalis (MIC=2 µg/ml).##Yeast: Candida albicans (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03869 RRWVIWRR 8 Bac8d (Bac2A variant) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found "Function: 8-mer substituted peptide that showes broad spectrum activity against bacteria and the yeast C. albicans. Chemical modification: C-terminal amidation." Gram-negative bacteria: Pseudomonas aeruginosa (MIC=250 µg/ml), Escherichia coli (MIC=16 µg/ml), Salmonella typhimurium (MIC=31 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Staphylococcus epidermidis (MIC=8 µg/ml), Enterococcus faecalis (MIC=32 µg/ml).##Yeast: Candida albicans (MIC=63 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041366 Nat Biotechnol. 2005 Aug;23(8):1008-1012. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity. DRAMP03870 RLARIVVIRVAR 12 Bac2A (a linear variant of bovine dodecapeptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=50 µg/ml), Escherichia coli (MIC=17 µg/ml), Salmonella (MIC=34 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=17 µg/ml), Staphylococcus epidermidis (MIC=4 µg/ml), Enterococcus faecalis (MIC=17 µg/ml).##Yeast: Candida albicans (MIC=9 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041366##17052614 Nat Biotechnol. 2005 Aug;23(8):1008-1012.Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. High-throughput generation of small antibacterial peptides with improved activity.Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP03871 YQWQRRMRKL 10 cLf 20-29 (fragment of caprine lalctoferricin, residues 20-29) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=308 µM), Escherichia coli (wild strain) (MIC>300 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=308 µM), Enterococcus faecalis ATCC 29212 (MIC>300 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03875 RRWQWRMKKL 10 bLf 20-29 (fragment of bovine lactoferricin, residues 20-29) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.25 µM), Escherichia coli (wild strain) (MIC=5.63 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=11.25 µM), Enterococcus faecalis ATCC 29212 (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03876 RRWWWRWRRW 10 LFB-RW (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µM), Escherichia coli (wild strain) (MIC=5.63 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=7.5 µM), Enterococcus faecalis ATCC 29212 (MIC=11.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03877 KKWWWKWKKW 10 LFB-KW (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=11.25 µM), Escherichia coli (wild strain) (MIC=7.50 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=11.25 µM), Enterococcus faecalis ATCC 29212 (MIC=22.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03878 RRWWRRWRRW 10 LFB-Rwa (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µM), Escherichia coli (wild strain) (MIC=5.63 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=7.5 µM), Enterococcus faecalis ATCC 29212 (MIC=22.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03879 RRFFFRFRRF 10 LFB-RF (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=22.5 µM), Escherichia coli (wild strain) (MIC=15 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=15 µM), Enterococcus faecalis ATCC 29212 (MIC=22.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03880 RRIIIRWRRI 10 LFB-RI (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=5.63 µM), Escherichia coli (wild strain) (MIC=3.75 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=11.25 µM), Enterococcus faecalis ATCC 29212 (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03881 RRWWWR 6 LFB-6RW (derivative of bovine lactoferrin with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=22.5 µM), Escherichia coli (wild strain) (MIC=22.5 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=11.25 µM), Enterococcus faecalis ATCC 29212 (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03882 SKCYQWQRRMRKLGA 15 LFC (fragment of mature caprine lactoferrin, residues 17 to 31) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=252 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>500 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03883 TKCFQWQWNMRKVRG 15 LFH W8 (tryptophan-modified human lactoferricin derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=74 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>500 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03884 SKCYQWQWRMRKLGA 15 LFC W8 (tryptophan-modified caprine lactoferricin derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=174 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>500 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03885 SKCRQWQWKIRRTNP 15 LFP W8 (tryptophan-modified porcine lactoferricin derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=219 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>500 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03886 FKCRRWQWRMKKLGA 15 LFB (fragment of bovine lalctoferricin, residues 17 to 31) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=24 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=48 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives. DRAMP03887 AKCRRWQWRMKKLGA 15 LFB A1 (derivative of LFB, residue substitution with alanine at position 1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=35 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03888 FACRRWQWRMKKLGA 15 LFB A2 (derivative of LFB, residue substitution with alanine at position 2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=40 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03889 FKARRWQWRMKKLGA 15 LFB A3 (derivative of LFB, residue substitution with alanine at position 3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=51 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03890 FKCARWQWRMKKLGA 15 LFB A4 (derivative of LFB, residue substitution with alanine at position 4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=35 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03891 FKCRAWQWRMKKLGA 15 LFB A5 (derivative of LFB, residue substitution with alanine at position 5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=61 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03892 FKCRRWAWRMKKLGA 15 LFB A7 (derivative of LFB, residue substitution with alanine at position 7) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=15 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=75 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03893 FKCRRWQWAMKKLGA 15 LFB A9 (derivative of LFB, residue substitution with alanine at position 9) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=28 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03894 FKCRRWQWRAKKLGA 15 LFB A10 (derivative of LFB, residue substitution with alanine at position 10) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=70 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03895 FKCRRWQWRMAKLGA 15 LFB A11 (derivative of LFB, residue substitution with alanine at position 11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=35 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03896 FKCRRWQWRMKALGA 15 LFB A12 (derivative of LFB, residue substitution with alanine at position 12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03897 FKCRRWQWRMKKAGA 15 LFB A13 (derivative of LFB, residue substitution with alanine at position 13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03898 FKCRRWQWRMKKLAA 15 LFB A14 (derivative of LFB, residue substitution with alanine at position 14) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=12 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=77 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11095180 J Pept Res. 2000 Nov;56(5):265-274. Strøm MB, Rekdal O, Svendsen JS. Antibacterial activity of 15-residue lactoferricin derivatives DRAMP03899 AKCLRWQWEMRKVGG 15 LFM A1 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=391 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03900 AKCLRWQWAMRKVGG 15 LFM A1,9 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=134 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03901 RKCLRWQWEMRKVGG 15 LFM R1 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=37 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=374 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03902 EKCLRWQWRMRKVGG 15 LFM R9 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03903 AKCLRWQWRMRKVGG 15 LFM A1 R9 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=31 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=257 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03904 RKCLRWQWAMRKVGG 15 LFM A9 R1 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=31 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=257 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03905 RKCLRWQWRMRKVGG 15 LFM R1,9 W8 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=37 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03906 AKCLRWQWEMRKYGG 15 LFM A1 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=151 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03907 AKCLRWQWAMRKYGG 15 LFM A1,9 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=88 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03908 RKCLRWQWEMRKYGG 15 LFM R1 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=19 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=73 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03909 EKCLRWQWRMRKYGG 15 LFM R9 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=63 µM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03910 AKCLRWQWRMRKYGG 15 LFM A1 R9 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03911 RKCLRWQWAMRKYGG 15 LFM A9 R1 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=12 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03912 RKCLRWQWRMRKYGG 15 LFM R1,9 W8 Y13 (LFM W8 derivative with residues substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium S. aureus and the Gram-negative bacteria E. coli. Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11168896 J Pept Res. 2001 Feb;57(2):127-139. Strøm MB, Rekdal O, Stensen W, Svendsen JS. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. DRAMP03920 KWKLFKKIEKVGQGIGAVLKVLTTGL 26 Cecropin A (1-8)-melittin (1-13)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.7 µM), Staphylococcus aureus Cowan 1 (MIC=2 µM), Streptococcus pyogenes (MIC=1 µM);##Gram-negative bacteria: Escherichia coli D21 (MIC=0.5 µM), Pseudomonas aeruginosa OT97 (MIC=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03921 KWKLFKKIGIGAVLKVLTTGLPALIS 26 Cecropin A (1-8)-melittin (1-18)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found 1BH1##2MLT##2MW6##3QRX##6DST##6O4M##8AHS##8AHT Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.3 µM), Pseudomonas aeruginosa OT97 (MIC=0.7 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.4 µM), Bacillus megaterium Bm11 (MIC=0.4 µM), Staphylococcus aureus Cowan 1 (MIC=1 µM), Streptococcus pyogenes (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03922 KWKLFKKIGIGAVLKVLTTG 20 Cecropin A (1-8)-melittin (1-12)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.4 µM), Pseudomonas aeruginosa OT97 (MIC=0.9 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.3 µM), Bacillus megaterium Bm11 (MIC=0.2 µM), Staphylococcus aureus Cowan 1 (MIC=2 µM), Streptococcus pyogenes (MIC=0.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03923 KWKLFKKIGIGAVLKVLT 18 Cecropin A (1-8)-melittin (1-10)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.5 µM), Pseudomonas aeruginosa OT97 (MIC=3 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.3 µM), Bacillus megaterium Bm11 (MIC=0.5 µM), Staphylococcus aureus Cowan 1 (MIC=7 µM), Streptococcus pyogenes (MIC=0.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03924 KWKLFKKGIGAVLKV 15 Cecropin A (1-7)-melittin (1-8)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=4 µM), Pseudomonas aeruginosa OT97 (MIC=15 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=1.4 µM), Bacillus megaterium Bm11 (MIC=0.8 µM), Staphylococcus aureus Cowan 1 (MIC=29 µM), Streptococcus pyogenes (MIC=0.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03925 KWKLFKKGAVLKVLT 15 Cecropin A (1-7)-melittin (3-10)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=3 µM), Pseudomonas aeruginosa OT97 (MIC=15 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=3 µM), Bacillus megaterium Bm11 (MIC=0.9 µM), Staphylococcus aureus Cowan 1 (MIC>200 µM), Streptococcus pyogenes (MIC=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03927 KWKLFKKIGAVLKVL 15 Cecropin A (1-7)-melittin (2-9)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix (1 helices; 10 residues) Adopts an amphipathic helix almost parallel to the surface of the micelle. 2JMY resolved by NMR. CAMEL is also a hybrid peptide obtained by combining residues 1-7 of cecropin (CA) and residues 2-9 of melittin (M). Gram-negative bacteria: Escherichia coli D21 (MIC=1 µM), Pseudomonas aeruginosa OT97 (MIC=4 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.5 µM), Bacillus megaterium Bm11 (MIC=0.7 µM), Staphylococcus aureus Cowan 1 (MIC=2 µM), Streptococcus pyogenes (MIC=0.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777##17397158 FEBS Lett. 1992 Jan 20;296(2):190-194.##J Am Chem Soc. 2007 Apr 25;129(16):5228-5234. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG.##Respondek M, Madl T, Göbl C, Golser R, Zangger K. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity.##Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves. DRAMP03928 KWKLFKKAVLKVLTT 15 Cecropin A (1-7)-melittin (4-11)hybrid peptide (CAM) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.6 µM), Pseudomonas aeruginosa OT97 (MIC=4 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.6 µM), Bacillus megaterium Bm11 (MIC=0.5 µM), Staphylococcus aureus Cowan 1 (MIC=8 µM), Streptococcus pyogenes (MIC=0.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777##20111863 FEBS Lett. 1992 Jan 20;296(2):190-194.##Curr Microbiol. 2010 Sep;61(3):169-175. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG.##Cao Y, Yu RQ, Liu Y, Zhou HX, Song LL, Cao Y, Qiao DR. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity.##Design, recombinant expression, and antibacterial activity of the cecropins-melittin hybrid antimicrobial peptides. DRAMP03929 KWKLFKKVLKVLTTG 15 Cecropin A (1-7)-melittin (5-12)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=0.5 µM), Pseudomonas aeruginosa OT97 (MIC=2 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=0.3 µM), Bacillus megaterium Bm11 (MIC=0.5 µM), Staphylococcus aureus Cowan 1 (MIC=8 µM), Streptococcus pyogenes (MIC=0.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03930 KWKLFKKLKVLTTGL 15 Cecropin A (1-7)-melittin (6-13)hybrid peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli D21 (MIC=2 µM), Pseudomonas aeruginosa OT97 (MIC=8 µM);##Gram-positive bacteria: Bacillus subtilis Bs11 (MIC=1 µM), Bacillus megaterium Bm11 (MIC=0.5 µM), Staphylococcus aureus Cowan 1 (MIC=51 µM), Streptococcus pyogenes (MIC=0.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1733777 FEBS Lett. 1992 Jan 20;296(2):190-194. Andreu D, Ubach J, Boman A, WÃ¥hlin B, Wade D, Merrifield RB, Boman HG. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. DRAMP03931 DPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKPN 39 hPAB-beta (a hBD-2 variant; beta-defensins) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found 1FD3##1FD4##1FQQ##6CS9##1E4Q Comment: No comments found on DRAMP database Type strains: Staphylococcus aureus ATCC25923 (MIC=62.5 µg/ml), Staphylococcus aureus ATCC29215 (MIC=62.5 µg/ml), Escherichia coli ATCC29213 (MIC=125 µg/ml), Enterococcus feces ATCC29212 (MIC=250 µg/ml).##Clinical strains: Salmonella typhoid (MIC=62.5 µg/ml), Salmonella typhoid A (MIC=62.5 µg/ml), Shigella dysentery (MIC=62.5 µg/ml), Escherichia coli (MIC=62.5 µg/ml), Staphylococcus aureus (MIC=31.25 µg/ml), Staphylococcus epidermis (MIC=62.5 µg/ml), Enterobacter cloacae (MIC=62.5 µg/ml), Bacillus proteus curious (MIC=62.5 µg/ml), Acinetobacter lwoffii (MIC=62.5 µg/ml), Pseudomonas aeruginosa Pa6 (MIC=125 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15808901 Peptides. 2005 May;26(5):721-729. Rao X, Hu J, Li S, Jin X, Zhang C, Cong Y, Hu X, Tan Y, Huang J, Chen Z, Zhu J, Hu F. Design and expression of peptide antibiotic hPAB-beta as tandem multimers in Escherichia coli. DRAMP03933 IIYCNRRTGKCQRM 14 I14M (truncated isoform of thanatin, residue 8-21) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=1.2-2.5 µM), Micrococcus luteus (MIC=5-10 µM), Bacillus megaterium (MIC=10-20 µM);##Gram-negative bacteria: Escherichia coli D22 (MIC=20-40 µM), Escherichia coli D31 (MIC=20-40 µM), Klebsiella pneumoniae (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=20-40 µM), Botrytis cinerea (MIC=10-20 µM), Alternaria brassicicola (MIC=5-10 µM), Fusarium culmorum (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03934 YCNRRTGKCQRM 12 Y12M (truncated isoform of thanatin, residue 10-21) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=20-40 µM), Micrococcus luteus (MIC=20-40 µM), Bacillus megaterium (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03935 VPIIYCNRRTGKCQRM 16 V16M (truncated isoform of thanatin, residue 6-21) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=1.2-2.5 µM), Micrococcus luteus (MIC=2.5-5 µM), Bacillus megaterium (MIC=5-10 µM), Bacillus subtilis (MIC=20-40 µM), Pediococcus acidilactici (MIC=20-40 µM);##Gram-negative bacteria: Escherichia coli D22 (MIC=0.6-1.2 µM), Escherichia coli D31 (MIC=0.6-1.2 µM), Klebsiella pneumoniae (MIC=2.5-5 µM), Enterobacter cloacae (MIC=5-10 µM), E. carotovora (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=10-20 µM), Botrytis cinerea (MIC=10-20 µM), Nectria haematococca (MIC=5-10 µM), Trichoderma viride (MIC=20-40 µM), Alternaria brassicicola (MIC=5-10 µM), Fusarium culmorum (MIC=10-20 µM), A. pisi (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03936 KPVPIIYCNRRTGKCQRM 18 K18M (truncated isoform of thanatin, residue 4-21) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=0.6-1.2 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Bacillus megaterium (MIC=2.5-5 µM), Bacillus subtilis (MIC=20-40 µM), Pediococcus acidilactici (MIC=20-40 µM);##Gram-negative bacteria: Escherichia coli D22 (MIC=0.3-0.6 µM), Escherichia coli D31 (MIC=0.3-0.6 µM), Escherichia coli 1106 (MIC=0.6-1.2 µM), Salmonella typhimuriumn (MIC=1.2-2.5 µM), Klebsiella pneumoniae (MIC=1.2-2.5 µM), Enterobacter cloacae (MIC1.2-2.5 µM), E. carotovora (MIC=20-40 µM), Pseudomonas aeruginosa (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=2.5-5 µM), Botrytis cinerea (MIC=1.2-2.5 µM), Nectria haematococca (MIC=5-10 µM), Trichoderma viride (MIC=2.5-5 µM), Alternaria brassicicola (MIC=2.5-5 µM), Fusarium culmorum (MIC=5-10 µM), A. pisi (MIC=10-20 µM), Fusarium oxysporumn (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03937 GSKKPVPIIYCNRRTGKC 18 G18C (truncated isoform of thanatin, residue 1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=2.5-5 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Bacillus megaterium (MIC=5-10 µM), Bacillus subtilis (MIC=5-10 µM), Pediococcus acidilactici (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=10-20 µM), Botrytis cinerea (MIC=5-10 µM), Nectria haematococca (MIC=5-10 µM), Trichoderma viride (MIC=20-40 µM), Alternaria brassicicola (MIC=5-10 µM), Fusarium culmorum (MIC=10-20 µM), A. pisi (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03938 GSKKPVPIIYCNRRTGKCQ 19 G19Q (truncated isoform of thanatin, residue 1-19) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=2.5-5 µM), Micrococcus luteus (MIC=5-10 µM), Bacillus megaterium (MIC=5-10 µM), Pediococcus acidilactici (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=10-20 µM), Botrytis cinerea (MIC=5-10 µM), Nectria haematococca (MIC=5-10 µM), Trichoderma viride (MIC=10-20 µM), Alternaria brassicicola (MIC=5-10 µM), Fusarium culmorum (MIC=10-20 µM), A. pisi (MIC=20-40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03939 GSKKPVPIIYCNRRTGKCQR 20 G20R (truncated isoform of thanatin, residue 1-20) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-positive bacteria: Aerococcus viridans (MIC=2.5-5 µM), Micrococcus luteus (MIC=2.5-5 µM), Bacillus megaterium (MIC=2.5-5 µM), Bacillus subtilis (MIC20-40 µM), Pediococcus acidilactici (MIC=20-40 µM).##Fungi: Neurospora crassa (MIC=5-10 µM), Botrytis cinerea (MIC=5-10 µM), Nectria haematococca (MIC=2.5-5 µM), Trichoderma viride (MIC=10-20 µM), Alternaria brassicicola (MIC=5-10 µM), Fusarium culmorum (MIC=10-20 µM), A. pisi (MIC=10-20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8577744 Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. DRAMP03945 LIKIVPAMICAVTKKC 16 Del 1-4 (Ranalexin analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacterium: Staphylococcus aureus (MIC=256 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=256 µg/ml), Pseudomonas aeruginosa (MIC=256 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8144672 J Biol Chem. 1994 Apr 8;269(14):10849-10855. Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. DRAMP03947 GGLIKIVPAMICAVTKKC 18 Del 1-2 (Ranalexin analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacterium: Staphylococcus aureus (MIC=256 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC>256 µg/ml), Pseudomonas aeruginosa (MIC>256 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8144672 J Biol Chem. 1994 Apr 8;269(14):10849-10855. Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. DRAMP03948 LGGLIKIVPAMICAVTKKC 19 Del 1 (Ranalexin analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacterium: Staphylococcus aureus (MIC=256 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=256 µg/ml), Pseudomonas aeruginosa (MIC>256 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8144672 J Biol Chem. 1994 Apr 8;269(14):10849-10855. Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. DRAMP03949 FLGGLIKIVPAMICAVTKK 19 Del 20 (Ranalexin analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacterium: Staphylococcus aureus (MIC=128 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=256 µg/ml), Pseudomonas aeruginosa (MIC=128 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8144672 J Biol Chem. 1994 Apr 8;269(14):10849-10855. Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. DRAMP03954 MTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERILSVLRHQNL 51 Rat CGA7–57 No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Fungi: Neurospora crassa (MIC=10 µg/ml), Alternaria brassicicola (MIC=20 µg/ml), Nectria haematococca (MIC=10 µg/ml), Fusarium culmorum (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03955 STALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKK 81 Human recombinant Ser-Thr-Ala-CGA1-78 peptide (hrVS-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found 6R2X Comment: No comments found on DRAMP database Gram-positive bacteria: Micrococcus luteus (MIC=30 µM), Bacillus megaterium (MIC=30 µM).##Fungi: Neurospora crassa (MIC=10 µM), Alternaria brassicicola (MIC=1 µM), Nectria haematococca (MIC=3 µM), Fusarium culmorum (MIC=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03957 RILSILRHQNLLKE 14 CGA47-60 (hrVS-1-derived peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Fungi: Neurospora crassa (MIC=7 µM), Aspergillus fumigatus (MIC=50 µM), Alternaria brassicicola (MIC=10 µM), Nectria haematococca (MIC=7 µM), Fusarium culmorum (MIC=20 µM), F. oxyporum (MIC=50 µM), Trichophyton mentagrophytes (MIC=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03958 TLRGDERILSILRHQNLLKE 20 CGA41-60 (hrVS-1-derived peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Fungi: Neurospora crassa (MIC=100 µM), Nectria haematococca (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03959 TLRGDERILSILRHQNLLKELQDLALQGAK 30 CGA41-70 (hrVS-1-derived peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found 6R2X Comment: No comments found on DRAMP database Fungi: Neurospora crassa (MIC=7 µM), Alternaria brassicicola (MIC=7 µM), Nectria haematococca (MIC=7 µM), Fusarium culmorum (MIC=10 µM), F. oxyporum (MIC=30 µM), Trichophyton mentagrophytes (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03960 RILSILRHQNLLKELQDLALQGAK 24 CGA47-70 (hrVS-1-derived peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Fungi: Neurospora crassa (MIC=5 µM), Aspergillus fumigatus (MIC=30 µM), Alternaria brassicicola (MIC=10 µM), Nectria haematococca (MIC=7 µM), Fusarium culmorum (MIC=10 µM), F. oxyporum (MIC=30 µM), Trichophyton mentagrophytes (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10753865 J Biol Chem. 2000 Apr 14;275(15):10745-10753. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. DRAMP03967 KWKLFKKIPKFLHLAKKF 18 P18 (Cecropin A(1-8)-Magainin 2(1−12) hybrid peptide analogue) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Alpha helix Not found MOA: P18 kills cancer cells by disrupting membranes (Tang C et al 2010 Org Biomol Che 8:984-7). Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=1.56 µM), Bacillus megaterium KCTC 1096 (MIC=0.78 µM).##Tumor cells: MDA-MB-361 (IC50=8.0 µM), Jurkat (IC50=4.0 µM), K-562 (IC50=3.5 µM), Normal cells NIH 3T3 (IC50=75.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12005420##12370027 J Pept Res. 2001 Dec;58(6):504-514.##Protein Pept Lett. 2002 Oct;9(5):395-402. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI.##Lee SH, Lee DG, Yang ST, Kim Y, Kim JI, Hahm KS, Shin SY. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs.##Antibiotic activity of reversed peptides of alpha-helical antimicrobial peptide, P18. DRAMP03968 KWKLFKKILKFLHLAKKF 18 [L9]-P18 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=3.125 µM), Proteus vulgaris (MIC=6.25 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=3.0 µM), Jurkat (IC50=9.0 µM), K-562 (IC50=3.0 µM), Normal cells NIH 3T3 (IC50=70.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03969 KWKLFKKISKFLHLAKKF 18 [S9]-P18 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=25.0 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=6.25 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM).##Tumor cells: MDA-MB-361 (IC50=4.0 µM), Jurkat (IC50=7.0 µM), K-562 (IC50=3.0 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03970 WKLFKKIPKFLHLAKKF 17 N-1 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=9.5 µM), Jurkat (IC50=12.0 µM), K-562 (IC50=6.0 µM), Normal cells NIH 3T3 (IC50=75.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03971 FKLFKKIPKFLHLAKKF 17 N-2 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=0.78 µM).##Tumor cells: MDA-MB-361 (IC50=11.0 µM), Jurkat (IC50=11.0 µM), K-562 (IC50=7.0 µM), Normal cells NIH 3T3 (IC50=70.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03972 KWFKKIPKFLHLAKKF 16 N-3 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=17.0 µM), Jurkat (IC50=17.0 µM), K-562 (IC50=11.0 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03973 WFKKIPKFLHLAKKF 15 N-4 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=32.0 µM), Jurkat (IC50=23.0 µM), K-562 (IC50=24.0 µM), Normal cells NIH 3T3 (IC50=100.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03974 WKKIPKFLHLAKKF 14 N-5 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=3.125 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03975 KWFKKIPKFLHLLKKF 16 N-3L (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=3.125 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=3.125 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=1.56 µM), Bacillus megaterium KCTC 1096 (MIC=0.78 µM).##Tumor cells: MDA-MB-361 (IC50=5.0 µM), Jurkat (IC50=4.0 µM), K-562 (IC50=4.2 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03976 WFKKIPKFLHLLKKF 15 N-4L (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=3.125 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=12.5 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=0.78 µM).##Tumor cells: MDA-MB-361 (IC50=5.0 µM), Jurkat (IC50=6.0 µM), K-562 (IC50=3.0 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03977 WKKIPKFLHLLKKF 14 N-5L (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=3.125 µM), Proteus vulgaris (MIC=12.5 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=17.0 µM), Jurkat (IC50=14.0 µM), K-562 (IC50=10.0 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03978 KWKLFKKIPFLHLAKKF 17 C-1 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=26.0 µM), Jurkat (IC50=32.0 µM), K-562 (IC50=31.0 µM), Normal cells NIH 3T3 (IC50=100.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03979 KWKLFKKIPKFLHLAKK 17 C-2 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=38.0 µM), Jurkat (IC50=26.0 µM), K-562 (IC50=23.0 µM), Normal cells NIH 3T3 (IC50=100.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03980 KWKLFKKIPLHLAKKF 16 C-3 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25-12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78-1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM).##Tumor cells: MDA-MB-361 (IC50=79.0 µM), Jurkat (IC50=74.0 µM), K-562 (IC50=62.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03981 KWKLFKKIPKFLHLAK 16 C-4 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=3.125-6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=3.125 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM).##Tumor cells: MDA-MB-361 (IC50=54.0 µM), Jurkat (IC50=31.0 µM), K-562 (IC50=25.0 µM), Normal cells NIH 3T3 (IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03982 KWKLFKKIPHLAKKF 15 C-5 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=12.5 µM), Proteus vulgaris (MIC=1.56 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=1.56 µM).##Tumor cells: MDA-MB-361 (IC50=100.0 µM), Jurkat (IC50=81.0 µM), K-562 (IC50=67.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03983 KWKLFKKIPKFLHLA 15 C-6 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25-12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM).##Tumor cells: MDA-MB-361 (IC50=47.0 µM), Jurkat (IC50=21.0 µM), K-562 (IC50=27.0 µM), Normal cells NIH 3T3 (IC50=100.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03984 KWKLFKKIPLAKKF 14 C-7 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25-12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=12.5 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03985 KWKLFKKIPKFLHL 14 C-8 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Also has antitumor activity. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM).##Tumor cells: MDA-MB-361 (IC50=83.0 µM), Jurkat (IC50=54.0 µM), K-562 (IC50=30.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03986 KWKLFKKIPLKKF 13 C-9 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=12.5 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=12.5 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=12.5 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03987 KWKLFKKIPKFLH 13 C-10 (analog of P18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=6.25-12.5 µM), Proteus vulgaris (MIC=3.125 µM).##Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=1.56 µM), Staphylococcus aureus KCTC 1621 (MIC=6.25 µM), Bacillus megaterium KCTC 1096 (MIC=3.125 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005420 J Pept Res. 2001 Dec;58(6):504-514. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. DRAMP03988 LLKWLKK 7 L3K3W4 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-positive bacteria. Gram-positive bacterium: Micrococcus luteus ATCC 10240 (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03989 LLKWLLK 7 L4K2W4 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=25 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03990 LLKWLKKL 8 L4K3W4 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=50 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=25 µg/ml);##Gram-negative bacterium: Pseudomonas aeruginosa ATCC 27853 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03991 KLLKWLLK 8 L4K3W5 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=50 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03992 KLLKWLLKL 9 L5K3W5 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=12.5 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=3.1 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=12.5 µg/ml), Micrococcus luteus ATCC 10240 (MIC=25 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.5 µg/ml), Shigella dysentariae ATCC 9752 (MIC=12.5 µg/ml), Salmonella typhomurium ATCC 14028 (MIC=25 µg/ml), Klebsiella pneumoniae ATCC 10031 (MIC=6.3 µg/ml), Pseudomonas aeruginosa ATCC 27 853 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03993 KKLLKWLKKLL 11 L5K5W6 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=6.3 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=6.3 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=6.3 µg/ml), Micrococcus luteus ATCC 10240 (MIC=6.3 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.5 µg/ml), Shigella dysentariae ATCC 9752 (MIC=6.3 µg/ml), Salmonella typhomurium ATCC 14028 (MIC=25 µg/ml), Klebsiella pneumoniae ATCC 10031 (MIC=6.3 µg/ml), Pseudomonas aeruginosa ATCC 27 853 (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03994 KKLLKWLLKLL 11 L6K4W6 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=1.6 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=1.6 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=1.6 µg/ml), Micrococcus luteus ATCC 10240 (MIC=1.6 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.3 µg/ml), Shigella dysentariae ATCC 9752 (MIC=3.1 µg/ml), Salmonella typhomurium ATCC 14028 (MIC=25 µg/ml), Klebsiella pneumoniae ATCC 10031 (MIC=3.1 µg/ml), Pseudomonas aeruginosa ATCC 27 853 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03995 LKLLKWLLKLL 11 L7K3W6 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=1.6 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=3.1 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=3.1 µg/ml), Micrococcus luteus ATCC 10240 (MIC=3.1 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=50 µg/ml), Shigella dysentariae ATCC 9752 (MIC=12.5 µg/ml), Klebsiella pneumoniae ATCC 10031 (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03996 LKKLLKWLLKLLK 13 L7K5W7 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=3.1 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=12.5 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=12.5 µg/ml), Micrococcus luteus ATCC 10240 (MIC=3.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03997 LLKLLKWLLKLLK 13 L8K4W7 (LlKmWn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=6.3 µg/ml), Staphylococcus aureus ATCC 6538p (MIC=25 µg/ml), Staphylococcus epidermis ATCC 12228 (MIC=50 µg/ml), Micrococcus luteus ATCC 10240 (MIC=6.3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19544481 J Pept Sci. 2009 Sep;15(9):583-588. Kang SJ, Won HS, Choi WS, Lee BJ. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. DRAMP03999 ILGKIAEGIKSLF 13 [A6]-IsCT (Mutant: W6A; IsCT analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: [A6]-IsCT did not cause any hemolysis at peptide concentrations as high as 100 µM, indicating that Trp6 is important for both the hemolytic activity and antibacterial activity of IsCT. Chemical modification: C-terminal amidation." [Ref.15369808]Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=64 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=32 µM), Salmonella typhimurium KCTC 1926 (MIC>64 µM);##Gram-positive bacteria: Staphylococcus epidermidis KCTC 1917 (MIC>64 µM), Staphylococcus aureus KCTC 1621 (MIC>64 µM). [Ref.15369808]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15369808 Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-719. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. DRAMP04000 ILGKILEGIKSLF 13 [L6]-IsCT (Mutant: W6L; IsCT analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Drastic reduction in antibacterial activity against both Gram-positive and Gram-negative bacteria, and big loss of hemolysis activity. Chemical modification: C-terminal amidation." Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=16 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=16 µM), Salmonella typhimurium KCTC 1926 (MIC=16 µM);##Gram-positive bacteria: Staphylococcus epidermidis KCTC 1917 (MIC=32 µM), Staphylococcus aureus KCTC 1621 (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15369808 Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-719. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. DRAMP04001 ILGKIWKGIKSLF 13 [K7]-IsCT (Mutant: E7K; IsCT analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: [K7]-IsCT displays a similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and complete loss of hemolysis activity. Chemical modification: C-terminal amidation." Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=2 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=2 µM), Salmonella typhimurium KCTC 1926 (MIC=1 µM);##Gram-positive bacteria: Staphylococcus epidermidis KCTC 1917 (MIC=1 µM), Staphylococcus aureus KCTC 1621 (MIC=1 µM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15369808 Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-719. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. DRAMP04002 ILGKILKGIKKLF 13 [L6, K11]-IsCT (IsCT analog through amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: [L6, K11]-IsCT displays a similar or 2-fold higher antibacterial activity relative to that of native IsCT. Chemical modification: C-terminal amidation." Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=2 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=2 µM), Salmonella typhimurium KCTC 1926 (MIC=1 µM);##Gram-positive bacteria: Staphylococcus epidermidis KCTC 1917 (MIC=1 µM), Staphylococcus aureus KCTC 1621 (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15369808 Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-719. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. DRAMP04003 ILGKIWKIKKLF 12 [K7, P8, K11]-IsCT (IsCT analog through amino acids substitution) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: [K7, P8, K11]-IsCT exhibited more potent antibacterial activity than native IsCT but no hemolytic activity, even at concentrations as high as 100 µM. [K7, P8, K11]-IsCT displays a similar or 2-fold higher antibacterial activity relative to that of native IsCT. Chemical modification: C-terminal amidation." [Ref.15369808]Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=2 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=2 µM), Salmonella typhimurium KCTC 1926 (MIC=1 µM);##Gram-positive bacteria: Staphylococcus epidermidis KCTC 1917 (MIC=1 µM), Staphylococcus aureus KCTC 1621 (MIC=2 µM);##Antibiotic-resistant bacteria: Methicillin-resistant Staphylococcus aureus (MRSA) CCARM 3001 (MIC=1 µM), multidrug-resistant Pseudomonas aeruginosa (MDRPA) (CCARM 3543) (MIC=1 µM) and multidrug-resistant Pseudomonas aeruginosa (MDRPA) CCARM 2095 (MIC=1 µM). [Ref.15369808]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15369808 Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-719. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. DRAMP04004 VSLFPVXLFP 10 Gramicidin analogue ([Scr2]-GS) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus ATCC 6538 P(MIC=25 µg/ml), Streptococcus pyogenes N.Y.5 (MIC=25 µg/ml), Myotis flavus ATCC 10240 (MIC=3.1 µg/ml), Bacillus subtilis ATCC 6633 (MIC=6.3 µg/ml);##Gram-negative bacteria: Corynebacterium diphtheriae P.W.8 (MIC=3.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8791160 Int J Pept Protein Res. 1996 May;47(5):369-375. Tamaki M, Akabori S, Muramatsu I. Properties of synthetic analogs of gramicidin S containing L-serine or L-glutamic acid residue in place of L-ornithine residue. DRAMP04005 VSLFPVSLFP 10 Gramicidin analogue ([Ser2,2']-GS) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Streptococcus pyogenes N.Y.5 (MIC=25 µg/ml), Myotis flavus ATCC 10240 (MIC=12.5 µg/ml);##Gram-negative bacteria: Corynebacterium diphtheriae P.W.8 (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8791160 Int J Pept Protein Res. 1996 May;47(5):369-375. Tamaki M, Akabori S, Muramatsu I. Properties of synthetic analogs of gramicidin S containing L-serine or L-glutamic acid residue in place of L-ornithine residue. DRAMP04011 GVVTDLLKTAGKLLGNLFGSLSG 23 Plasticin PD36 KF (analog of PD36) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. The hemolytic activity of the peptides was determined using fresh rat erythrocytes. [Ref.17128968]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=6.5 µM), Bacillus megaterium ATCC 9885 (MIC=50.25 µM);##Gram-negative bacteria: Escherichia coli ATCC 11775 (MIC=6.5 µM), Salmonella typhimurium CIP 6062 (MIC=25.25 µM), Enterobacter cloacae ATCC 11775 (MIC=12.5 µM). [Ref.17128968]25% hemolytic at 50 μM, 50% hemolytic activity at 100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17128968 Biochemistry 2006; 45: 14285-14297. Amri CE et al Bruston F. The plasticins: membrane adsortpion, lipid disorders, and biological activity. DRAMP04012 GVVTDLLKTAGKLLGNLVGSLSG 23 Plasticin PD36 K (analog of PD36) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. The hemolytic activity of the peptides was determined using fresh rat erythrocytes. [Ref.17128968]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=50.5 µM), Bacillus megaterium ATCC 9885 (MIC=12.5 µM);##Gram-negative bacteria: Escherichia coli ATCC 11775 (MIC=12.5 µM). [Ref.17128968]35% hemolytic at 50 μM, 71% hemolytic activity at 100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17128968 Biochemistry 2006; 45: 14285-14297. Amri CE et al Bruston F. The plasticins: membrane adsortpion, lipid disorders, and biological activity. DRAMP04013 GLVTGLLKTAGKLLGDLFGSLTG 23 Plasticin ANC KF (analog of natural peptide ANC) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. The hemolytic activity of the peptides was determined using fresh rat erythrocytes. [Ref.17128968]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=12.5 µM), Bacillus megaterium ATCC 9885 (MIC=12.5 µM);##Gram-negative bacteria: Escherichia coli ATCC 11775 (MIC=25 µM). [Ref.17128968]22% hemolytic at 50 μM, 48% hemolytic activity at 100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17128968 Biochemistry 2006; 45: 14285-14297. Amri CE et al Bruston F. The plasticins: membrane adsortpion, lipid disorders, and biological activity. DRAMP04014 LLGDFFRKAKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 LL-37A9 (LL-37 variants) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against the Gram-negative bacterium E. coli. Gram-negative bacteria: Escherichia coli DC2 (MIC=6 µM), Escherichia coli K12 (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22185690 Biochemistry. 2012 Jan 17;51(2):653-664. Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE. Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. DRAMP04015 LLGDFFRKVKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 LL-37V9 (LL-37 variants) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against the Gram-negative bacterium E. coli. Gram-negative bacteria: Escherichia coli DC2 (MIC=12 µM), Escherichia coli K12 (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22185690 Biochemistry. 2012 Jan 17;51(2):653-664. Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE. Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. DRAMP04016 LLGDFFRKAKEKIGKEFKRIVQR 23 LL-23A9 (LL-23 variants) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negagtive bacteria: Escherichia coli DC2 (MIC=9 µM), Escherichia coli K12 (MIC=80 µM);##Gram-positive bacteria: Staphylococcus aureus mprF (presence of carbonate) (MIC=0.35-0.7 µM), S. aureus mprF (absence of carbonate) (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22185690 Biochemistry. 2012 Jan 17;51(2):653-664. Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE. Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. DRAMP04017 LLGDFFRKVKEKIGKEFKRIVQR 23 LL-23V9 (LL-23 variants) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli DC2 (MIC=2 µM), Escherichia coli K12 (MIC=40 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µM), S. aureus mprF (presence of carbonate) (MIC=0.35-0.7 µM), S. aureus mprF (absence of carbonate) (MIC=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22185690 Biochemistry. 2012 Jan 17;51(2):653-664. Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE. Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. DRAMP04019 RAVAVIIRLRRV 12 Bac014 (Scrambled Variants of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=23 µg/ml), Escherichia coli (MIC=11 µg/ml), Salmonella (MIC=11 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=23 µg/ml), Staphylococcus epidermidis (MIC=6 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04020 RRAAVVLIVIRR 12 Bac020 (Scrambled Variants of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=11 µg/ml), Escherichia coli (MIC=6 µg/ml), Salmonella (MIC=23 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=11 µg/ml), Staphylococcus epidermidis (MIC=1.5 µg/ml).##Yeast: Candida albicans (MIC=11 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04021 VRLRIRVAVIRA 12 Bac034 (Scrambled Variants of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=25 µg/ml), Escherichia coli (MIC=3 µg/ml), Salmonella (MIC=12 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermidis (MIC=3 µg/ml).##Yeast: Candida albicans (MIC=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04022 VRFRIRVAVIRA 12 F3 (single amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=1.6 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04023 VRWRIRVAVIRA 12 W3 (single amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=1.6 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04024 VRLWIRVAVIRA 12 W4 (single amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC>50 µg/ml), Escherichia coli (MIC=6 µg/ml), Salmonella (MIC>50 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=50 µg/ml), Staphylococcus epidermidis (MIC=3 µg/ml).##Yeast: Candida albicans (MIC=50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04025 VRLRIRVAVRRA 12 R10 (single amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=12 µg/ml), Escherichia coli (MIC=6 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04026 VRLRIRVAVIRK 12 K12 (single amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=3 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04027 VQLRIRVRVIRK 12 opt1 (multiple amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=3 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04028 VRLRIRVRVIRK 12 opt2 (multiple amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=3 µg/ml), Escherichia coli (MIC=1.6 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6 µg/ml), Staphylococcus epidermidis (MIC=0.8 µg/ml).##Yeast: Candida albicans (MIC=3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04029 KQFRIRVRVIRK 12 opt3 (multiple amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=3 µg/ml), Salmonella (MIC=6 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12 µg/ml), Staphylococcus epidermidis (MIC=1.6 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04030 KRFRIRVRVIRK 12 opt4 (multiple amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=6 µg/ml), Escherichia coli (MIC=1.6 µg/ml), Salmonella (MIC=3 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6 µg/ml), Staphylococcus epidermidis (MIC=0.8 µg/ml).##Yeast: Candida albicans (MIC=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04031 KRWRIRVRVIRK 12 opt5 (multiple amino acid substitution of Bac034, which is a scrambled Variant of Bac2A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (MIC=3 µg/ml), Escherichia coli (MIC=1.6 µg/ml), Salmonella (MIC=3 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=3 µg/ml), Staphylococcus epidermidis (MIC=0.8 µg/ml).##Yeast: Candida albicans (MIC=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17052614 Chem Biol. 2006 Oct;13(10):1101-1107. Hilpert K, Elliott MR, Volkmer-Engert R, Henklein P, Donini O, Zhou Q, Winkler DF, Hancock RE. Sequence requirements and an optimization strategy for short antimicrobial peptides. DRAMP04032 ALRLAIRKR 9 Modified defensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=5 µg/ml), Staphylococcus aureus (MRSA) (MIC>48 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=4 µg/ml), Pseudomonas aeruginosa (MIC=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-623. Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP04033 ALLLAIRKR 9 Modified defensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=4 µg/ml), Staphylococcus aureus (MRSA) (MIC=40 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=6 µg/ml), Pseudomonas aeruginosa (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-623. Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP04034 AWLLAIRKR 9 Modified defensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=3 µg/ml), Staphylococcus aureus (MRSA) (MIC=25 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=5 µg/ml), Pseudomonas aeruginosa (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-623. Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP04035 ALYLAIRKR 9 Modified defensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=3 µg/ml), Staphylococcus aureus (MRSA) (MIC=30 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=4 µg/ml), Pseudomonas aeruginosa (MIC=4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-623. Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP04036 ALWLAIRKR 9 Modified defensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=4 µg/ml), Staphylococcus aureus (MRSA) (MIC=40 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=10 µg/ml), Pseudomonas aeruginosa (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-623. Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. DRAMP04048 RRLCRIVVIRVCRR 14 BacR (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=2 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Salmonella typhimurium 14028s (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=64 µg/ml), Staphylococcus epidermidis C621 (MIC=8 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=32 µg/ml), Listeria monocytogenes (MIC<0.125 µg/ml), Corynebacterium xerosis (MIC=1 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=8 µg/ml), S. mitis (MIC=0.5 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys4 and Cys12. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04049 RRRCPIVVIRVCRR 14 BacP3R (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=2 µg/ml), Pseudomonas aeruginosa K799 (MIC=8 µg/ml), Salmonella typhimurium 14028s (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>64 µg/ml), Staphylococcus epidermidis C621 (MIC=16 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=32 µg/ml), Listeria monocytogenes (MIC+0.5 µg/ml), Corynebacterium xerosis (MIC=4 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=8 µg/ml), S. mitis (MIC=1 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys4 and Cys12. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04050 RRRLCPIVIRVCRR 14 BacP3R-V (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=2 µg/ml), Pseudomonas aeruginosa K799 (MIC=8 µg/ml), Salmonella typhimurium 14028s (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>64 µg/ml), Staphylococcus epidermidis C621 (MIC=16 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>64 µg/ml), Listeria monocytogenes (MIC=1 µg/ml), Corynebacterium xerosis (MIC=4 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=4 µg/ml), S. mitis (MIC=1 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys5 and Cys12. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04051 RICRIVVIRCIR 12 Bac2I-NH2 (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=4 µg/ml), Pseudomonas aeruginosa K799 (MIC=16 µg/ml), Salmonella typhimurium 14028s (MIC=8 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=32 µg/ml), Staphylococcus epidermidis C621 (MIC=8 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys3 and Cys10. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04052 RLCPRVRIRVCR 12 BacP2R-NH2 (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=4 µg/ml), Pseudomonas aeruginosa K799 (MIC=16 µg/ml), Salmonella typhimurium 14028s (MIC=32 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>32 µg/ml), Staphylococcus epidermidis C621 (MIC=16 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys3 and Cys11. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04053 RLCRIVPVIRVCR 13 BacP1 (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=32 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Salmonella typhimurium 14028s (MIC>64 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=64 µg/ml), Staphylococcus epidermidis C621 (MIC=64 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>64 µg/ml), Listeria monocytogenes (MIC=2 µg/ml), Corynebacterium xerosis (MIC=8 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=64 µg/ml), S. mitis (MIC=4 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys3 and Cys12. L No cytotoxicity information found Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04054 RLCRIVWVIRVCR 13 BacW (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=4 µg/ml), Salmonella typhimurium 14028s (MIC=4 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4 µg/ml), Staphylococcus epidermidis C621 (MIC=2 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=8 µg/ml), Listeria monocytogenes (MIC=0.5 µg/ml), Corynebacterium xerosis (MIC=1 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=2 µg/ml), S. mitis (MIC=1 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04055 RRLCRIVWVIRVCRR 15 BacW2R (cyclic derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=2 µg/ml), Pseudomonas aeruginosa K799 (MIC=2 µg/ml), Salmonella typhimurium 14028s (MIC=2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µg/ml), Staphylococcus epidermidis C621 (MIC=1 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=2 µg/ml), Listeria monocytogenes (MIC=0.25 µg/ml), Corynebacterium xerosis (MIC=0.25 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=1 µg/ml), S. mitis (MIC=0.25 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04056 RLSRIVVIRVSR 12 Lin Bac2S-NH2 (linear derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=2 µg/ml), Pseudomonas aeruginosa K799 (MIC=16 µg/ml), Salmonella typhimurium 14028s (MIC=32 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4 µg/ml), Staphylococcus epidermidis C621 (MIC=1 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=4 µg/ml), Listeria monocytogenes (MIC=0.25 µg/ml), Corynebacterium xerosis (MIC=0.25 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=2 µg/ml), S. mitis (MIC=0.125 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=16 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP04057 RLSRIVVIRVCR 12 Lin BacS-NH2 (linear derivative of bactenecin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli K-12 (MIC=4 µg/ml), Pseudomonas aeruginosa K799 (MIC=16 µg/ml), Salmonella typhimurium 14028s (MIC>64 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=16 µg/ml), Staphylococcus epidermidis C621 (MIC=2 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=16 µg/ml), Listeria monocytogenes (MIC=0.5 µg/ml), Corynebacterium xerosis (MIC=0.5 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=8 µg/ml), S. mitis (MIC=0.5 µg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10223951 Antimicrob Agents Chemother. 1999 May;43(5):1274-1276. Wu M, Hancock RE. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. DRAMP18364 WTTIVKVSKAVCKTGTCICTTSCSNCK 27 Thuricin 4A-4 (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Bacillus thuringiensis serovar thuringiensis T01001 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against B. cereus, B. firmus, B. thuringiensis, B. subtilis, B. pumilus, E. faecalis, M. Paenibacillus, S. aureus, and S. sciuri. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25548056 Appl Environ Microbiol. 2015 Mar;81(5):1765-74. The Bacillus cereus group is an excellent reservoir of novel lanthipeptides. DRAMP18365 INTWNTTATSTSIIISETFGNKGKVCTYTVECVNNCRG 38 Thusin (ThsA1, ThsA2; a two-chain lantibiotic, type 2, class 1 bacteriocins) No entry found Belongs to the lantibiotic family (class I bacteriocins) Not found Bacillus thuringiensis strain BGSC 4BT1, serovar rongseni Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against S. pneumoniae ATCC 49619, B. cereus ATCC 14579, B. thuringiensis BMB171, B. pumilus SCG I , B. subtilis Bsn5, L. monocytogenes LM201 (MIC 6.25 uM), L. monocytogenes LM605, S. aureus ATCC 43300, S. sciuri Bom1, B. amyloliquefaciens X1 (MIC 12.5 uM), S. aureus CMCC 26003, MRSA (MIC 25 uM), and E. faecalis ATCC 29212 (MIC 50 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27486447 Front Microbiol. 2016 Jul 19;7:1115. Xin B, Zheng J, Liu H, Li J, Ruan L, Peng D, Sajid M, Sun M Thusin, a Novel Two-Component Lantibiotic with Potent Antimicrobial Activity against Several Gram-Positive Pathogens. DRAMP18363 CVWGGDCTDFLGCGTAWICV 20 Sviceucin (bacteriocin) No entry found Not found Not found Streptomyces sviceus Antimicrobial, Antibacterial, Anti-Gram+ Beta Not found Comment: No comments found on DRAMP database Gram-positive bacteria: B. megaterium, L. bulgaricus 340, S. aureus subsp. aureus ATCC 6538, L. sakei subsp. sakei DSM 20017. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 26343290 ACS Chem Biol. 2015 Nov 20;10(11):2641-9. Li Y, Ducasse R, Zirah S, Blond A, Goulard C, Lescop E, Giraud C, Hartke A, Guittet E, Pernodet JL, Rebuffat S. Characterization of Sviceucin from Streptomyces Provides Insight into Enzyme Exchangeability and Disulfide Bond Formation in Lasso Peptides DRAMP18361 APKGVQGPNG 10 YD1 (bacteriocin) No entry found Not found Not found Bacillus amyloliquefaciens Antimicrobial, Antibacterial Not found Not found YD1 binds to the plasmid DNA of E. coli. Active against Gram- S. typhimurium KCTC 1925 (MIC 32 ug/ml), E. coli KCTC 1923 (MIC 8 ug/ml), P. aeruginosa KCTC 1637 (MIC 16 ug/ml), Gram+ M. smegmatis ATCC 9341 (MIC 8 ug/ml), S. aureus KCTC 1928, MRSA B15 (MIC 32 ug/ml), E. faecalis ATCC 29212, B. subtilis ATCC 6633, M. luteus ATCC 9341, VRE 2, and VRE5 (MIC 64 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28050849 AMB Express. 2017 Dec;7(1):8 Rahman MS, Choi YH, Choi YS, Yoo JC. Glycin-rich antimicrobial peptide YD1 from B. amyloliquefaciens, induced morphological alteration in and showed affinity for plasmid DNA of E. coli. DRAMP18362 CEWYNISCQLGNKGQWCTLTKECQRSCK 28 Formicin (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Bacillus paralicheniformis APC 1576 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: L. s delbrueckii subsp. bulgaricus, L. amylophilus, L. lactis, M. luteus, S. smutans, including clinical strains S. aureus, C. difficile, and L. monocytogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27450592 Microbiology. 2016 Sep;162(9):1662-1671. Collins FW, O'Connor PM, O'Sullivan O, Rea MC, Hill C, Ross RP. Formicin - a novel broad-spectrum two-component lantibiotic produced by Bacillus paralicheniformis APC 1576 DRAMP18360 VLSIVACSSGCGSGKTAASCVATCGNKCFTNVGSLC 36 Paenicidin B (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Paenibacillus terrae; old: Bacillus circulans NRRL B-30644 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against B. subtilis JH642 (MIC 50 uM), L. lactis subsp. cremoris HP (12.5 uM), L. monocytogenes ATCC 15313 (100 uM), and S. aureus ATCC 25923 (MIC 100 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24382692 Chembiochem. 2014 Jan 24;15(2):243-9. Lohans CT1, van Belkum MJ, Cochrane SA, Huang Z, Sit CS, McMullen LM, Vederas JC. Biochemical, structural, and genetic characterization of tridecaptin A?, an antagonist of Campylobacter jejuni. DRAMP18359 KCSWWNASCHLGNNGKICTVSHECAAGCNL 30 Sh-lantibiotic-alpha (bacteriocin) No entry found Belongs to the lantibiotic family. Not found human skin bacterium, Staphylococcus hominis A9 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found "Function: Active against S. aureus, but not commensal bacteria. PTM: Three thioether bonds are proposed: S8-C18, T19-C24, S21-C28 and one S-S bond between C2-C9." Gram-positive bacteria: S. aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28228596 Sci Transl Med. 2017 Feb 22;9(378) Nakatsuji T, Chen TH, Narala S, Chun KA, Two AM, Yun T, Shafiq F, Kotol PF, Bouslimani A, Melnik AV, Latif H, Kim JN, Lockhart A, Artis K, David G, Taylor P, Streib J, Dorrestein PC, Grier A, Gill SR, Zengler K, Hata TR, Leung DY, Gallo RL. Antimicrobials from human skin commensal bacteria protect against Staphylococcus aureus and are deficient in atopic dermatitis DRAMP18358 ATPTITTSSATCGGIIVAASAAQCPTLACSSRCGKRKK 38 Sh-lantibiotic-beta (bacteriocin) No entry found Belongs to the lantibiotic family. Not found human skin bacterium, Staphylococcus hominis A9 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found "Function: Active against S. aureus, but not commensal bacteria. PTM: Four thioether bonds are proposed: S9-C12, S20-C24, T26-C29 and S30-C33. In addition, there are five dehydrated S/T at the N-terminus of the peptide." Gram-positive bacteria: S. aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28228596 Sci Transl Med. 2017 Feb 22;9(378). Nakatsuji T, Chen TH, Narala S, Chun KA, Two AM, Yun T, Shafiq F, Kotol PF, Bouslimani A, Melnik AV, Latif H, Kim JN, Lockhart A, Artis K, David G, Taylor P, Streib J, Dorrestein PC, Grier A, Gill SR, Zengler K, Hata TR, Leung DY, Gallo RL Antimicrobials from human skin commensal bacteria protect against Staphylococcus aureus and are deficient in atopic dermatitis DRAMP04064 CVKCKCKCGSGVKVKVKVC 19 Cyclic cationic V1 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity against human erythrocytes, and also Cytotoxic activity against THP-1 cells (EC50=0.045 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=5 nM), Pseudomonas aeruginosa ATTC 27853 (MIC>619 nM), Klebsiella pneumoniae ATTC 13883 (MIC=145 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=5 nM), Shigella sonnei ATTC 25931 (MIC=5 nM). [Ref.15328096]EC50=880000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04065 CVKVSVKVGSGVKVSVKVC 19 Cyclic cationic V2 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=5.6 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=5 nM), Pseudomonas aeruginosa ATTC 27853 (MIC>643 nM), Klebsiella pneumoniae ATTC 13883 (MIC=643 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=5 nM), Shigella sonnei ATTC 25931 (MIC=5 nM). [Ref.15328096]EC50=589000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04066 CVKVRVKVGSGVKVRVKVC 19 Cyclic cationic V3 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=0.042 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=300 nM), Pseudomonas aeruginosa ATTC 27853 (MIC=5 nM), Klebsiella pneumoniae ATTC 13883 (MIC=10 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=300 nM), Shigella sonnei ATTC 25931 (MIC=5 nM). [Ref.15328096]EC50=590000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04067 CVKVQVKVGSGVKVQVKVC 19 Cyclic cationic V4 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=0.047 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=10 nM), Pseudomonas aeruginosa ATTC 27853 (MIC=5 nM), Klebsiella pneumoniae ATTC 13883 (MIC<5 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=5 nM), Shigella sonnei ATTC 25931 (MIC=10 nM). [Ref.15328096]EC50=3226000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04068 CAKAKAKAGSGAKAKAKAC 19 Cyclic cationic V5 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=0.14 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=173 nM), Pseudomonas aeruginosa ATTC 27853 (MIC=5 nM), Klebsiella pneumoniae ATTC 13883 (MIC>692 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=5 nM), Shigella sonnei ATTC 25931 (MIC=692 nM). [Ref.15328096]EC50=1055000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04069 CFKFKFKFGSGFKFKFKFC 19 Cyclic cationic V6 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=0.045 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=518 nM), Pseudomonas aeruginosa ATTC 27853 (MIC=4 nM), Klebsiella pneumoniae ATTC 13883 (MIC=4 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=528 nM), Shigella sonnei ATTC 25931 (MIC=4 nM). [Ref.15328096]EC50=35000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04070 CWKWKWKWGSGWKWKWKWC 19 Cyclic cationic V7 peptide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy. Has hemolytic activity for human erythrocytes, and also Cytotoxic activity for THP-1 cells (EC50=0.085 mM). [Ref.15328096]Gram-negative bacteria: Escherichia coli ATTC 25922 (MIC=114 nM), Pseudomonas aeruginosa ATTC 27853 (MIC=4 nM), Klebsiella pneumoniae ATTC 13883 (MIC=458 nM), Salmonella enterica serovar Typhimurium ATTC 14028 (MIC=4 nM), Shigella sonnei ATTC 25931 (MIC=7 nM). [Ref.15328096]EC50=45000 nM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-3357. Frecer V, Ho B, Ding JL. De Novo Design of Potent Antimicrobial Peptides. DRAMP04075 AKKVFKRLEKLFSKIQNDK 19 Antimicrobial peptide HP (2-20) P56029 Not found rplA Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 11 residues) Not found 1P0G resolved by NMR. Function: Peptides originating from the N-terminal end of L1 have antibacterial activity against bacteria such as E. coli and Bacillus megaterium and modest antifungal activities. Has no effect on H. pylori itself. Peptides are not hemolytic against mammalian cells. These peptides may be released in the stomach during altruistic lysis to kill other fast growing bacteria. [Ref.16255716]Gram-positive bacteria: Bacillus subtilis (MIC=3.13 µg/ml), Staphylococcus epidermidis (MIC=6.25 µg/ml), Staphylococcus aureus (MIC=12.5 µg/ml), Listeria monocytogenes (MIC=6.25 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=3.13 µg/ml), Salmonella typhimurium (MIC=1.56 µg/ml), Proteus vulgaris (MIC=6.25 µg/ml), Pseudomonas aeruginosa (MIC=6.25 µg/ml), Escherichia coli O157 (MIC=12.5 µg/ml);##Fungi: Trichosporon beigelii (MIC=3.13 µg/ml), Candida albicans (MIC>25 µg/ml), Saccharomyces cerevisiae (MIC>25 µg/ml), Aspergillus flavus (MIC=50 µg/ml), Aspergillus fumigatus (MIC>50 µg/ml), Botrytis cinerea (MIC=12.5 µg/ml), Fusarium moniliforme (MIC=25 µg/ml). [Swiss_Prot Entry P56029]Non-hemolytic against mammalian cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phospholipids 16255716##PubMed ID is not available##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##Submitted (SEP-2004) to the PDB data bank.##To be published Lee KH, Lee DG, Park YK, Harm KS, Kim YM.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Structure of antimicrobial peptide, HP (2-20) and its analogues derived from Helicobacter pylori, as determined by 1H NMR spectroscopy.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04076 AKKVFKRLEKLFSKIQNWK 19 Anal 1 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 14 residues) Not found 1P0J resolved by NMR. Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=1.56 µg/ml), Staphylococcus epidermidis (MIC=3.13 µg/ml), Staphylococcus aureus (MIC=3.13 µg/ml), Listeria monocytogenes (MIC=0.78 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=0.78 µg/ml), Salmonella typhimurium (MIC=0.39 µg/ml), Proteus vulgaris (MIC=3.13 µg/ml), Pseudomonas aeruginosa (MIC=3.13 µg/ml), Escherichia coli O157 (MIC=6.25 µg/ml).##Fungi: Trichosporon beigelii (MIC=1.56 µg/ml), Candida albicans (MIC=25 µg/ml), Saccharomyces cerevisiae (MIC=25 µg/ml), Aspergillus flavus (MIC=50 µg/ml), Aspergillus fumigatus (MIC>50 µg/ml), Botrytis cinerea (MIC=6.25 µg/ml), Fusarium moniliforme (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04077 AKKVFKRLEKLFSKIWNDK 19 Anal 2 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 14 residues) Not found 1P0L resolved by NMR. Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=1.56 µg/ml), Staphylococcus epidermidis (MIC=3.13 µg/ml), Staphylococcus aureus (MIC=6.25 µg/ml), Listeria monocytogenes (MIC=1.56 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=3.13 µg/ml), Salmonella typhimurium (MIC=0.78 µg/ml), Proteus vulgaris (MIC=3.13 µg/ml), Pseudomonas aeruginosa (MIC=6.25 µg/ml), Escherichia coli O157 (MIC=6.25 µg/ml).##Fungi: Trichosporon beigelii (MIC=1.56 µg/ml), Candida albicans (MIC=25 µg/ml), Saccharomyces cerevisiae (MIC=25 µg/ml), Aspergillus flavus (MIC=50 µg/ml), Aspergillus fumigatus (MIC>50 µg/ml), Botrytis cinerea (MIC=6.25 µg/ml), Fusarium moniliforme (MIC=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04078 AKKVFKRLEKLFSKIWNWK 19 Anal 3 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 14 residues) Not found 1P0O resolved by NMR. Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=1.56 µg/ml), Staphylococcus epidermidis (MIC=3.13 µg/ml), Staphylococcus aureus (MIC=1.56 µg/ml), Listeria monocytogenes (MIC=0.39 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=1.56 µg/ml), Salmonella typhimurium (MIC=0.39 µg/ml), Proteus vulgaris (MIC=3.13 µg/ml), Pseudomonas aeruginosa (MIC=3.13 µg/ml), Escherichia coli O157 (MIC=3.13 µg/ml).##Fungi: Trichosporon beigelii (MIC=1.56 µg/ml), Candida albicans (MIC=12.5 µg/ml), Saccharomyces cerevisiae (MIC=25 µg/ml), Aspergillus flavus (MIC=25 µg/ml), Aspergillus fumigatus (MIC=25 µg/ml), Botrytis cinerea (MIC=3.13 µg/ml), Fusarium moniliforme (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04079 AKKVFKRLEKSFSKIQNDK 19 Anal 4 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 13 residues) Not found 1P5K resolved by NMR. Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=6.25 µg/ml), Staphylococcus epidermidis (MIC>12.5 µg/ml), Staphylococcus aureus (MIC>12.5 µg/ml), Listeria monocytogenes (MIC>12.5 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=12.5 µg/ml), Salmonella typhimurium (MIC=12.5 µg/ml), Proteus vulgaris (MIC>12.5 µg/ml), Pseudomonas aeruginosa (MIC=12.5 µg/ml), Escherichia coli O157 (MIC>12.5 µg/ml).##Fungi: Trichosporon beigelii (MIC=12.5 µg/ml), Candida albicans (MIC>25 µg/ml), Saccharomyces cerevisiae (MIC>25 µg/ml), Aspergillus flavus (MIC>50 µg/ml), Aspergillus fumigatus (MIC>50 µg/ml), Botrytis cinerea (MIC>50 µg/ml), Fusarium moniliforme (MIC>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04080 AKKVSKRLEKLFSKIQNDK 19 Anal 5 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix (1 helices; 12 residues) Not found 1P5L resolved by NMR. Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=3.13 µg/ml), Staphylococcus epidermidis (MIC=12.5 µg/ml), Staphylococcus aureus (MIC>12.5 µg/ml), Listeria monocytogenes (MIC>12.5 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=6.25 µg/ml), Salmonella typhimurium (MIC=12.5 µg/ml), Proteus vulgaris (MIC>12.5 µg/ml), Pseudomonas aeruginosa (MIC=12.5 µg/ml), Escherichia coli O157 (MIC=6.25 µg/ml).##Fungi: Trichosporon beigelii (MIC=12.5 µg/ml), Candida albicans (MIC>25 µg/ml), Saccharomyces cerevisiae (MIC>25 µg/ml), Aspergillus flavus (MIC>50 µg/ml), Aspergillus fumigatus (MIC>50 µg/ml), Botrytis cinerea (MIC>50 µg/ml), Fusarium moniliforme (MIC>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04081 AKKVFKRLEKLFSKIFNFK 19 Anal 6 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=1.56 µg/ml), Staphylococcus epidermidis (MIC=6.25 µg/ml), Staphylococcus aureus (MIC=3.13 µg/ml), Listeria monocytogenes (MIC=0.78 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=3.13 µg/ml), Salmonella typhimurium (MIC=0.39 µg/ml), Proteus vulgaris (MIC=3.125 µg/ml), Pseudomonas aeruginosa (MIC=6.25 µg/ml), Escherichia coli O157 (MIC=6.25 µg/ml).##Fungi: Trichosporon beigelii (MIC=3.13 µg/ml), Candida albicans (MIC>25 µg/ml), Saccharomyces cerevisiae (MIC=25 µg/ml), Aspergillus flavus (MIC=50 µg/ml), Aspergillus fumigatus (MIC=50-25 µg/ml), Botrytis cinerea (MIC=12.5 µg/ml), Fusarium moniliforme (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04082 AKKVFKRLEKLFSKIYNYK 19 Anal 7 (antimicrobial peptide HP (2-20)analogue) P56029 Not found Not found Synthetic construct (amino acid substitution) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Bacillus subtilis (MIC=1.56 µg/ml), Staphylococcus epidermidis (MIC=3.13 µg/ml), Staphylococcus aureus (MIC=3.13 µg/ml), Listeria monocytogenes (MIC=0.78 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC=3.13 µg/ml), Salmonella typhimurium (MIC=0.39 µg/ml), Proteus vulgaris (MIC=6.25-3.13 µg/ml), Pseudomonas aeruginosa (MIC=3.13 µg/ml), Escherichia coli O157 (MIC=3.13 µg/ml).##Fungi: Trichosporon beigelii (MIC=1.56 µg/ml), Candida albicans (MIC=12.5 µg/ml), Saccharomyces cerevisiae (MIC=25 µg/ml), Aspergillus flavus (MIC=50 µg/ml), Aspergillus fumigatus (MIC=50-25 µg/ml), Botrytis cinerea (MIC=6.25 µg/ml), Fusarium moniliforme (MIC=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16255716##PubMed ID is not available Biochem J. 2006 Feb 15;394(Pt 1):105-114.##To be published Lee KH, Lee DG, Park Y, Kang DI, Shin SY, Hahm KS, Kim Y.##Lee KH, Lee DG, Park YK, Harm KS, Kim YM. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.##Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy. DRAMP04083 GIGKFLKKAKKFGKAFVKILKK 22 D-amino-acid pexiganan (MSI-214) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found MSI-214 is a peptide identical in sequence to pexiganan but comprising all D-amino acids. Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=16 µg/ml), Enterococcus faecium ATCC 51559 (vancomycin resistant) (MIC=4 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=16 µg/ml), Streptococcus bovis ATCC 49133 (MIC=4 µg/ml), Micrococcus luteus ATCC 4698 (MIC=2-4 µg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8-16 µg/ml), Proteus mirabilis ATCC 29245 (MIC>256 µg/ml), Serratia marcescens ATCC 8100 (MIC>256 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16-32 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10103181 Antimicrob Agents Chemother. 1999 Apr;43(4):782-788. Ge Y, MacDonald DL, Holroyd KJ, Thornsberry C, Wexler H, Zasloff M. In vitro antibacterial properties of pexiganan, an analog of magainin. DRAMP04095 GFGSLFKFLAKKVAKTVAKQAAKQGAKYVANKHMQ 35 Cupiennin-1D (spiders, Arthropods, animals) P83622 Belongs to the cupiennin family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function: with its amphipathic structure. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 6.4 pmol/mg on Drosophila." [Ref.11792701]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.31-0.63 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=0.31-0.63 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=0.31-0.63 µM), Enterococcus faecalis ATCC 29212 (MIC=1.25-2.50 µM). [Swiss_Prot Entry P83622]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11792701##10669026 J Biol Chem. 2002 Mar 29;277(13):11208-11216.##Toxicon. 2000 Mar;38(3):373-380. Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W.##Haeberli S, Kuhn-Nentwig L, Schaller J, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae).##Characterisation of antibacterial activity of peptides isolated from the venom of the spider Cupiennius salei (Araneae: Ctenidae). DRAMP04096 EQEENVVKIQAFWKGYKQRKEYM 23 2IQ2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=2.1 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=32 µM).##Yeast: Candida albicans (MIC=28 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04097 DNTDSVVKIQSWFRMATARKSYL 23 2IQ3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=1.2 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=26 µM).##Yeast: Candida albicans (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04098 ANVGFVIQLQARLRGFLVRQKFA 23 3IQ1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=1.7 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=1.7 µM).##Yeast: Candida albicans (MIC>94 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04099 TWLPAVIKIQAHWRGYRQRKIYL 23 3IQ2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=1.9 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=1.6 µM).##Yeast: Candida albicans (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04100 ANLDAIIKIQAWARMWAARRQYL 23 3IQ3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=2 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=11 µM).##Yeast: Candida albicans (MIC>89 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04101 KNVNSIVKIQAFFRARKAQDDYR 23 3IQ4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Displays antimicrobial activity against bacteria and yeast C. albicans. Gram-negative bacterium: Escherichia coli (MIC=3.5 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC=4.6 µM).##Yeast: Candida albicans (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23238369 Biochimie. 2013 Apr;95(4):875-880. McLean DT, Lundy FT, Timson DJ. IQ-motif peptides as novel anti-microbial agents. DRAMP04102 KWKSFIKKLTSKFLHLAKKF 20 CP-P No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Also has hemolytic activity against human erythrocytes. [Ref.22518150]Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml). [Ref.22518150]MHC=250 µg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP04103 KWKSFIKKLTSKFLHSAKKF 20 S16 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=3.125 µg/ml).##Clinical isolates: Acinetobacter baumannii b-01 (MIC=3.125 µg/mL), Acinetobacter baumannii b-02 (MIC=6.25 µg/mL), Acinetobacter baumannii b-03 (MIC=6.25 µg/mL), Acinetobacter baumannii b-04 (MIC=3.125 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04104 KFKSFIKKLTSKFLHSAKKF 20 F2 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Also has hemolytic activity against human erythrocytes. [Ref.22518150]Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml). [Ref.22518150]MHC=250 µg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04105 KWNSFIKKLTSKFLHSAKKF 20 N3 (derivative of CP-P) No entry found Derived from the peptide CP-P Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04106 KWKSFKKKLTSKFLHSAKKF 20 K6 (derivative of CP-P) No entry found Derived from the peptide CP-P Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04107 KWKSFINKLTSKFLHSAKKF 20 N7 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04108 KWKSFIKKAKTSFLHSAKKF 20 A9 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04111 KWKSFIKKSTSKFLHSAKKF 20 S9 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=50 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04112 KWKSFIKKLLSKFLHSAKKF 20 L10 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Also has hemolytic activity against human erythrocytes. [Ref.22518150]Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml). [Ref.22518150]MHC<125 µg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04113 KWKSFIKKLASKFLHSAKKF 20 A10 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Also has hemolytic activity against human erythrocytes. [Ref.22518150]Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml). [Ref.22518150]MHC=250 µg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04114 KWKSFIKKLTDKFLHSAKKF 20 D11 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04115 KWKSFIKKLTKKFLHSAKKF 20 K11 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix (CD) Not found Function: Has antibacterial activity. Gram-positive bacteria: Staphylococcus aureus CMCC26003 (MIC=0.5 µg/mL), Bacillus subtilis DB430 (MIC=2 µg/mL), Bacillus pumilus CMCC63202 (MIC=0.5 µg/mL), Soluble wall Micrococcus S1.634 (MIC=1 µg/mL), Micrococcus luteus CMCC28001 (MIC=2 µg/mL).##Gram-negative bacteria: E. coli ATCC8099 (MIC=0.5 µg/mL), Klebsiella pneumoniae CMCC46117 (MIC=2 µg/mL), Salmonella paratyphi BCMCC50094 (MIC=2 µg/mL), Pseudomonas aeruginosa CMCC10104 (MIC=4 µg/mL).##Clinical isolates: Acinetobacter baumannii b-01 (MIC=0.8 µg/mL), Acinetobacter baumannii b-02 (MIC=3.125 µg/mL), Acinetobacter baumannii b-03 (MIC=3.25 µg/mL), Acinetobacter baumannii b-04 (MIC=1.6 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04117 KWKSFIKKLTSKALHSAKKF 20 A13 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=6.25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04119 KWKSFIKKLTSKFLHSKKKF 20 K17 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=12.5 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04120 KWKSFIKKLTSKFLHSADKF 20 D18 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04121 KWKSFIKKLTSKFLHSANKF 20 N18 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=6.25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04122 KWKSFIKKLTSKFLHSAKKN 20 N20 (derivative of CP-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Pseudomonas aeruginosa (MIC=6.25 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150 Int J Microbiol. 2012;2012:764834. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide. DRAMP04123 SGKLCCRRKK 10 D0-NH2(Derived from HBD-28 variant) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=12±0.17 µM), Pseudomonas aeruginosa ATCC 27853 (MIC>100 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>100 µM). [Ref.23860860] 2.2% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04124 SGKLYYRRKK 10 D1-NH2 (Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=12±0.01 µM), Pseudomonas aeruginosa ATCC 27853 (MIC>100 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>100 µM). [Ref.23860860] 2.0% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04125 SGKLWWRRKK 10 D2-NH2 (Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150]Gram-negative bacteria: Escherichia coli (MIC=6±0.012 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=12±0.01 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=12±0.01 µM). [Ref.23860860] 2.5% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04126 SGKRWWRRKK 10 D3-NH2 (Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=6±0.012 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=6±0.078 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=25±0.01 µM). [Ref.23860860] 5.0% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04127 RGKRWWRRKK 10 D4-NH2(Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=3±0.012 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=6±0.04 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6±0.01 µM). [Ref.23860860] 5.0% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04128 RWKRWWRRKK 10 D5-NH2 (Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=3±0.012 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=3±0.012 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6±0.012 µM). [Ref.23860860] 6.5% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04129 RKKRWWRRKK 10 D6-NH2 (Derived from D0) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Chemical modification: C-terminal amidation." [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=3±0.07 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=3±0.012 µM);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6±0.012 µM). [Ref.23860860] 6.5% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22518150##23860860 Int J Microbiol. 2012;2012:764834. ##Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003. Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.##Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS. The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.##Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility DRAMP04136 LRRLWLRANRL 11 LRR-1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli ATCC 25922 (MIC=128 µM), P. aeruginosa ATCC 27853 (MIC>128 µM), S. typhimurium C7731 (MIC>128 µM);##Gram-positive bacteria: S. epidermidis ATCC12228 (MIC>128 µM), E. faecalis ATCC 29212 (MIC>128 µM), S. aureus ATCC 29213 (MIC=128 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23430306 Amino Acids. 2013 Apr;44(4):1215-1224. Ma QQ, Lv YF, Gu Y, Dong N, Li DS, Shan AS. Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat. DRAMP04137 LRRLWLRANRLLRRLWLRANRL 22 LRR-2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli ATCC 25922 (MIC=4 µM), P. aeruginosa ATCC 27853 (MIC=4 µM), S. typhimurium C7731 (MIC=2 µM);##Gram-positive bacteria: S. epidermidis ATCC12228 (MIC=2 µM), E. faecalis ATCC 29212 (MIC=2 µM), S. aureus ATCC 29213 (MIC=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23430306 Amino Acids. 2013 Apr;44(4):1215-1224. Ma QQ, Lv YF, Gu Y, Dong N, Li DS, Shan AS. Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat. DRAMP04138 APRKNVRW 8 L1 (first 8 N-terminal residues of bovine LF) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=62.36 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04139 APRKNVRF 8 L2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=129.66 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04140 APRKNVKW 8 L3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=64.11 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04141 APRKNLKW 8 L4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=31.61 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04142 APRKQLKW 8 L5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=7.79 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04143 APRRQLKW 8 L6 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=15.17 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04144 APKKQLKW 8 L7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=16.02 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04145 AFRKQLKW 8 L8 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=3.71 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04146 LFRKQLKW 8 L9 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli ATCC 25923 (MIC=1.78 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04147 WFRKQLKW 8 L10 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Escherichia coli ATCC 25923 (MIC=0.8 µM), Klebsiella pneumoniae (MIC=3.35 µM), Acinetobacter sp. (MIC=3.35 µM), Psudomonas aruginosa (MIC=6.71 µM).##Fungi: Candida albicans ATCC SC5314 (MIC=10.49 µM), C. tropicalis ATCC 13803 (MIC=20.98 µM), C. parapsilosis ATCC 22019 (MIC=5.24 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 23026014 Biochim Biophys Acta. 2013 Feb;1828(2):677-686. Mishra B, Leishangthem GD, Gill K, Singh AK, Das S, Singh K, Xess I, Dinda A, Kapil A, Patro IK, Dey S. A novel antimicrobial peptide derived from modified N-terminal domain of bovine lactoferrin: Design, synthesis, activity against multidrug-resistant bacteria and Candida. DRAMP04159 RIKRFWPVVIRTVVAGYNLYRAIKK 25 LR2 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04160 RIKRFWPVVIRTVVAGYNLYRAIK 24 LR3 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=7.032 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=2.344 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=0.586 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04161 RIKRFWPVVIRTVVAGYNLYRAI 23 LR4 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=37.5 µg/ml), Staphylococcus aureus ATCC25923 (MIC=37.5 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=9.375 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04162 RIKRFWPVVIRTVVAGYNLYRA 22 LR5 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus ATCC25923 (MIC=75 µg/ml);##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=4.688 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=4.688 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04163 RIKRFWPVVIRTVVAGYNLYR 21 LR6 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04164 RIKRFWPVVIRTVVAGYNLY 20 LR7 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04165 RIKRFWPVVIRTVVAGYNL 19 LR8 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04166 RIKRFWPVVIRTVVAGYN 18 LR9 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04167 RIKRFWPVVIRTVVAGY 17 LR10 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04168 RIKRFWPVVIRTVVAG 16 LR11 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04169 RIKRFWPVVIRTVV 14 LR13 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04170 RIKRFWPVVIRT 12 LR15 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04171 RIKRFWPVVIR 11 LR16 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis (MIC=4.688 µg/ml), Staphylococcus aureus ATCC25923 (MIC=9.375 µg/ml).##Gram-negative bacterium: Escherichia coli ATCC25922 (MIC=3.516 µg/ml).##Yeast: Candida albicans ATCC2002 (MIC=2.344 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04174 KWLKKWL 7 L2K3W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=80 µg/ml), S. aureus (MIC=80 µg/ml), S. epidermis (MIC>80 µg/ml), M. luteus (MIC>80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC>80 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC>80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04175 KWLLKWL 7 L3K2W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=20 µg/ml), S. aureus (MIC=20 µg/ml), S. epidermis (MIC=80 µg/ml), M. luteus (MIC=80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC=40 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC=80 µg/ml), P. aeruginosa (MIC=80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04176 KKWLKKWLK 9 L2K5W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=80 µg/ml), S. aureus (MIC=40 µg/ml), S. epidermis (MIC>80 µg/ml), M. luteus (MIC>80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC=40 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC=80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04177 LKWLKKWLK 9 L3K4W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=40 µg/ml), S. aureus (MIC=10 µg/ml), S. epidermis (MIC=40 µg/ml), M. luteus (MIC=80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC=40 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC=80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04178 LKWLLKWLK 9 L4K3W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=5 µg/ml), S. aureus (MIC=2.5 µg/ml), S. epidermis (MIC=5 µg/ml), M. luteus (MIC=10 µg/ml), S. aureus (MRSA) (MIC=20 µg/ml).##Gram-negative bacteria: E. coli (MIC=5 µg/ml), S. dysentariae (MIC=40 µg/ml), S. typhimorium (MIC=20 µg/ml), K. pneumoniae (MIC=20 µg/ml), P. aeruginosa (MIC=40 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04179 LKWLLKWLL 9 L5K2W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC<1.3 µg/ml), S. aureus (MIC<1.3 µg/ml), S. epidermis (MIC<1.3 µg/ml), M. luteus (MIC=2.5 µg/ml), S. aureus (MRSA) (MIC=2.5 µg/ml).##Gram-negative bacteria: E. coli (MIC=5 µg/ml), S. dysentariae (MIC=2.5 µg/ml), S. typhimorium (MIC=10 µg/ml), K. pneumoniae (MIC=5 µg/ml), P. aeruginosa (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04180 LKKWLKKWLKK 11 L3K6W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=20 µg/ml), S. aureus (MIC=10 µg/ml), S. epidermis (MIC=40 µg/ml), M. luteus (MIC=40 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC=20 µg/ml), S. dysentariae (MIC=80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC=40 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04181 LLKWLKKWLKK 11 L4K5W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC=2.5 µg/ml), S. aureus (MIC=2.5 µg/ml), S. epidermis (MIC=2.5 µg/ml), M. luteus (MIC=2.5 µg/ml), S. aureus (MRSA) (MIC=40 µg/ml).##Gram-negative bacteria: E. coli (MIC=40 µg/ml), S. dysentariae (MIC=80 µg/ml), S. typhimorium (MIC=40 µg/ml), K. pneumoniae (MIC=40 µg/ml), P. aeruginosa (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04182 LLKWLLKWLKK 11 L5K4W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC<1.3 µg/ml), S. aureus (MIC<1.3 µg/ml), S. epidermis (MIC<1.3 µg/ml), M. luteus (MIC<1.3 µg/ml), S. aureus (MRSA) (MIC=5 µg/ml).##Gram-negative bacteria: E. coli (MIC=10 µg/ml), S. dysentariae (MIC=10 µg/ml), S. typhimorium (MIC=20 µg/ml), K. pneumoniae (MIC=20 µg/ml), P. aeruginosa (MIC=10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04183 LLKWLLKWLLK 11 L6K3W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC<1.3 µg/ml), S. aureus (MIC=2.5 µg/ml), S. epidermis (MIC<1.3 µg/ml), M. luteus (MIC=2.5 µg/ml), S. aureus (MRSA) (MIC=5 µg/ml).##Gram-negative bacteria: E. coli (MIC>80 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC>80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04184 GLLSLLSLLGKLL 13 DFTamP1 No entry found Not found Not found Synthetic construct (Ab Initio Design) Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antimicrobial activities. Gram-positive bacterium: S. aureus USA300 (MIC=3.12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22803960 J Am Chem Soc. 2012 Aug 1;134(30):12426-9. Mishra B, Wang G. "Ab Initio Design of Potent Anti-MRSA Peptides Based on Database Filtering Technology." DRAMP04185 GLLPLLSLLGKLL 13 DFTamP1-p No entry found Not found Not found Synthetic construct (Ab Initio Design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antimicrobial activities. Gram-positive bacteria: S. aureus USA300 (MIC=1.56 µM), B. subtilis (MIC=3.12 µM).##Gram-negative bacteria: E. coli K12 (MIC=25 µM), P. aeruginosa (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22803960 J Am Chem Soc. 2012 Aug 1;134(30):12426-9. Mishra B, Wang G. "Ab Initio Design of Potent Anti-MRSA Peptides Based on Database Filtering Technology." DRAMP04186 WLKKLLKKLLK 11 L5K5W1 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=8 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=2 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04187 KWLKKLLKKLL 11 L5K5W2 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=8 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=1 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=2 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04188 LKWLKKLLKKL 11 L5K5W3 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=4 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=8 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=4 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04189 LLKWLKKLLKK 11 L5K5W4 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=16 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=4 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=4 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04190 KLLKWLKKLLK 11 L5K5W5 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=2 µg/mL), MRSA-TK784 (MIC=8 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=2 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP18357 ASVVKTTIKASKKLCKGATLTCGCNITGKK 30 Warnerin (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Staphylococcus warneri KL-1 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against S. epidermis (MIC <1 ug/ml), S. epidermis ATCC 700566 (MIC 8 ug/ml), S. epidermis ATCC 700567 (MIC 8 ug/ml), Staphylococcus sp. ATCC 700575 (MIC 32 ug/ml), S. aureus (VISA) CCUG 45315 (MIC 1.5 ug/ml), K. pneumoniae ATCC 700603 (MIC 96 ug/ml), E. faecium ATCC 51559 (MIC 64 ug/ml), and E. faecium (VRE) ATCC 700221 (MIC 32 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19361283 Biol Chem. 2009 May-Jun;390(5-6):437-44 Petersen J, Boysen A, Fogh L, Tabermann K, Kofoed T, King A, Schrotz-King P, Hansen MC Identification and characterization of a bioactive lantibiotic produced by Staphylococcus warneri. DRAMP04192 LKKLLKWLKKL 11 L5K5W7 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=16 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=4 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04193 LLKKLLKWLKK 11 L5K5W8 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=4 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=4 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=16 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=4 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=4 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=4 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04194 KLLKKLLKWLK 11 L5K5W9 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=8 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=2 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04195 KKLLKKLLKWL 11 L5K5W10 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=1 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=1 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=1 µg/mL), Micrococcus luteus ATCC 10240 (MIC=2 µg/mL), MRSA-TK784 (MIC=4 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=1 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=1 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=2 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04196 LKKLLKKLLKW 11 L5K5W11 (L5K5Wn model peptide) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antibacterial activity against the Gram-positive, Gram-negative bacteria and a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC=2 µg/mL), Staphylococcus aureus ATCC 6538p (MIC=2 µg/mL), Staphylococcus epidermis ATCC 12228 (MIC=2 µg/mL), Micrococcus luteus ATCC 10240 (MIC=4 µg/mL), MRSA-TK784 (MIC=16 µg/mL).##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 µg/mL), Shigella dysenteriae ATCC 9752 (MIC=2 µg/mL), Salmonella typhimurium ATCC 14028 (MIC=4 µg/mL), Klebsiella pneumoniae ATCC 10031 (MIC=4 µg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC=8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23344198 Molecules. 2013 Jan 11;18(1):859-876. Kim SJ, Kim JS, Lee YS, Sim DW, Lee SH, Bahk YY, Lee KH, Kim EH, Park SJ, Lee BJ, Won HS. Structural characterization of de novo designed L5K5W model peptide isomers with potent antimicrobial and varied hemolytic activities. DRAMP04233 FLGVVFKLASKVFPAVFGKV 20 D28 (Rational design peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has strong bacteriostatic activity against several species of bacteria, including Staphylococcus aureus and Bacillus anthracis. Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), Bacillus anthracis (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17051220 Nature. 2006 Oct 19;443(7113):867-869. Loose C, Jensen K, Rigoutsos I, Stephanopoulos G. A linguistic model for the rational design of antimicrobial peptides. DRAMP04234 FLFRVASKVFPALIGKFKKK 20 D51 (Rational design peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has strong bacteriostatic activity against several species of bacteria, including Staphylococcus aureus and Bacillus anthracis. Gram-positive bacteria: Staphylococcus aureus (MIC=16 µg/ml), Bacillus anthracis (MIC=16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17051220 Nature. 2006 Oct 19;443(7113):867-869. Loose C, Jensen K, Rigoutsos I, Stephanopoulos G. A linguistic model for the rational design of antimicrobial peptides. DRAMP04235 LGALFRVASKVFPAVISMVK 20 D22 (Rational design peptide) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has strong bacteriostatic activity against several species of bacteria, including Staphylococcus aureus and Bacillus anthracis. Gram-positive bacteria: Staphylococcus aureus (MIC=64 µg/ml), Bacillus anthracis (MIC=64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17051220 Nature. 2006 Oct 19;443(7113):867-869. Loose C, Jensen K, Rigoutsos I, Stephanopoulos G. A linguistic model for the rational design of antimicrobial peptides. DRAMP04237 GLFDIVKKLVSDF 13 Antibacterial peptide A4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix (1 helices; 8 residues) Not found 1VM4 resolved by NMR. Function: Has antibacterial activity against the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15572363 J Biol Chem. 2005 Feb 18;280(7):5803-5811. Wang G, Li Y, Li X. Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor. DRAMP04240 KLKLLLLL 8 Synthetic 1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=8 µg/ml), S. aureus (MRSA) (MIC>35 µg/ml).##Gram-negative bacterium: Escherichia coli (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8093007 Biochem J. 1994 Sep 1;302 ( Pt 2):535-538. Alvarez-Bravo J, Kurata S, Natori S. Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. DRAMP04241 KLKLLLLLKLK 11 Synthetic 2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), S. aureus (MRSA) (MIC=30 µg/ml).##Gram-negative bacterium: Escherichia coli (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8093007 Biochem J. 1994 Sep 1;302 ( Pt 2):535-538. Alvarez-Bravo J, Kurata S, Natori S. Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. DRAMP04242 RLKLLLLLRLK 11 Synthetic 3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=1 µg/ml), S. aureus (MRSA) (MIC=30 µg/ml).##Gram-negative bacterium: Escherichia coli (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8093007 Biochem J. 1994 Sep 1;302 ( Pt 2):535-538. Alvarez-Bravo J, Kurata S, Natori S. Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. DRAMP04243 RLKLLLLRLK 10 Synthetic 4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), S. aureus (MRSA) (MIC>35 µg/ml).##Gram-negative bacterium: Escherichia coli (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8093007 Biochem J. 1994 Sep 1;302 ( Pt 2):535-538. Alvarez-Bravo J, Kurata S, Natori S. Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. DRAMP04244 RLKLLLRLK 9 Synthetic 5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activity against the Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC=2 µg/ml), S. aureus (MRSA) (MIC>35 µg/ml).##Gram-negative bacterium: Escherichia coli (MIC=20 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8093007 Biochem J. 1994 Sep 1;302 ( Pt 2):535-538. Alvarez-Bravo J, Kurata S, Natori S. Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. DRAMP04264 KWKSFIKKLTSAAKKVVTTAKPLISS 26 CP26 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=1 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=1 μg/ml), Pseudomonas aeruginosa Z61 (MIC=1 μg/ml), Pseudomonas aeruginosa H744 (MIC=1 μg/ml), Pseudomonas aeruginosa H374 (MIC=1 μg/ml), Pseudomonas aeruginosa H547 (MIC=1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04265 KWKSFIKKLTTAVKKVLTTGLPALIS 26 CP29 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=2 μg/ml), Pseudomonas aeruginosa K799 (MIC=6 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H374 (MIC=2 μg/ml), Pseudomonas aeruginosa H547 (MIC=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04279 ILKKWPWWPWRRK 13 CP11CN No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Chemical modification: C-terminal amidation. Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=16 µg/ml), S. aureus SAP0017 MRSA (MIC=16 µg/ml), Staphylococcus haemolyticus Clinical isolate (MIC=2 µg/ml), S. haemolyticus Vancomycin-resistant isolate (MIC=1 µg/ml), Staphylococcus epidermidis Clinical isolate (MIC=8 µg/ml), Enterococcus faecalis ATCC 29212 (MIC>64 µg/ml), Listeria monocytogenes NCTC 7973 (MIC=16 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=8 µg/ml), Corynebacterium xerosis Lab strain (MIC=0.5 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11294848 Antimicrob. Agents Chemother. 1999,43:1542-1548. Friedrich, C, M. G. Scott, N. Karunaratne, H. Yan, and R. E. Hancock. "Salt-resistant alpha-helical cationic antimicrobial peptides.##Antibacterial Action of Structurally Diverse Cationic Peptides on Gram-Positive Bacteria." DRAMP04359 INWKKIFQKVKNLV 14 PDD-A-1 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. PDD-A also shows hemolytic activity. [Ref.18375018]Gram-negative bacterium: Escherichia coli (MIC=8 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=45 µM). [Ref.18375018]IC50 = 100 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04360 INWKKIFEKVKDLV 14 PDD-A-2 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=9 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04361 IDWKKIFEKVKNLV 14 PDD-A-3 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=13 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=8.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04362 IDWKKIFEKVKDLV 14 PDD-A-4 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=47.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=17.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04363 INWSKIFEKVKNLV 14 PDD-A-5 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=17 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04364 INWSSIFEKVKNLV 14 PDD-A-6 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=35 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04365 INWSSIFESVKNLV 14 PDD-A-7 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=87.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04367 INWKKIFEKVSNLV 14 PDD-A-9 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=22.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04368 INWKKIFESVKNLV 14 PDD-A-10 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=10 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04369 INWKSIFEKVKNLV 14 PDD-A-11 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=15 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04370 NIWKKIFEKVKNLV 14 PDD-A-12 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04371 INWLKLGKKILGAI 14 PDD-B-1 (PDD-B analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=67.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04372 INWLRLGRRILGAL 14 PDD-B-2 (PDD-B analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=17.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04373 INFLKLGKKILGAL 14 PDD-B-3 (PDD-B analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=22.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04374 INWKKLGKKILGAL 14 PDD-B-4 (PDD-B analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=43 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=15.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04376 INWLKLGKKIISAL 14 MP-1 (MP analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04377 INWLKLGKKLLSAL 14 MP-2 (MP analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=25 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04378 INWLKLGKKMMSAI 14 MP-5 (MP analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=70 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04379 SNWLKLGKKMMSAL 14 MP-6 (MP analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04380 INWKKIASIGKEVLKAI 17 PMM-1 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=5.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=27.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04381 NWKKIASIGKEVLKAL 16 PMM-2 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=21 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=46 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04382 WKKIASIGKEVLKAL 15 PMM-3 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=62 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=125 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04383 KKIASIGKEVLKAL 14 PMM-4 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=75 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04385 INWKKIASIGKEVLKA 16 PMM-6 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=75 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=70 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04386 INWKKIASIGKEVLK 15 PMM-7 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04387 INWKKIASIGKEVL 14 PMM-8 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04389 IWNKIAKSIGKVLEKAL 17 PMM-10 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=15 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04390 INWKKGKEVLKAL 13 PMM-11 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04391 NIWKKIASIAKEVLKAL 17 PMM-12 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=6.25 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04392 KNWKKIASIGKEVLKAL 17 PMM-13 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=12.5 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=60 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04393 SNWKKIASIGKEVLKAL 17 PMM-14 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC=25 µM);##Gram-positive bacterium: Bacillus subtilis (MIC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04528 TCRYWCKTPENQTYCCEDEREIPSKVGLKPGKCPPVRPVCPPTRGFFEPPKTCSNDGSCYGADKCCFDRCLGEHVCKPIQTRG 83 CrusEs (cDNA encoding crustin-like peptide) No entry found Not found Not found Chinese mitten crab, Eriocheir sinensis Antibacterial, Antifungal, Antiviral, In, Anti-Gram+, Antimicrobial Not found Not found Not found Function: CrusEs is a potent antibacterial protein against Gram-positive bacteria infection. Gram-positive bacteria: M. luteus (MIC=0.23 µM), B. subtilis (MIC=0.11 µM), B. thuringiensis (MIC=0.11 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20144896 Dev Comp Immunol. 2010 Jul;34(7):734-740. Mu C, Zheng P, Zhao J, Wang L, Zhang H, Qiu L, Gai Y, Song L. Molecular characterization and expression of a crustin-like gene from Chinese mitten crab, Eriocheir sinensis. DRAMP04542 IDWKKLLDAAKQIL 6 Polybia-MP-I (insects, vertebrates, animals) No entry found Not found Not found Polybia paulista (Neotropical social wasp) Antimicrobial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli (MIC=5 µM), Pseudomonas aeruginosa (MIC=5 µM).##Gram-positive bacterium: Staphylococcus aureus (MIC=9 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463874 Peptides. 2009 Aug;30(8):1387-1395. de Souza BM, da Silva AV, Resende VM, Arcuri HA, Dos Santos Cabrera MP, Ruggiero Neto J, Palma MS. Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista. DRAMP04543 IDWLKLGKMVIDAL 14 Polybia-MP-II (insects, vertebrates, animals) No entry found Not found Not found Polybia paulista (Neotropical social wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytotoxic Not found Alpha helix It forms amphipathic alpha-helical conformations under membrane-mimetic conditions. "Function: Both peptides (Polybia-MP-II and -III) are polyfunctional, causing pronounced cell lysis of rat mast cells and erythrocytes, in addition to having antimicrobial activity against both Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation." Gram-negative bacteria: Escherichia coli (MIC=5 µM), Pseudomonas aeruginosa (MIC=38 µM).##Gram-positive bacteria: Staphylococcus aureus (MIC=2 µM), Bacillus cereus (MIC=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463874 Peptides. 2009 Aug;30(8):1387-1395. de Souza BM, da Silva AV, Resende VM, Arcuri HA, Dos Santos Cabrera MP, Ruggiero Neto J, Palma MS. Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista. DRAMP04544 IDWLKLGKMVMDVL 14 Polybia-MP-III (insects, vertebrates, animals) No entry found Not found Not found Polybia paulista (Neotropical social wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytotoxic Not found Alpha helix It forms amphipathic alpha-helical conformations under membrane-mimetic conditions. "Function: Both peptides (Polybia-MP-II and -III) are polyfunctional, causing pronounced cell lysis of rat mast cells and erythrocytes, in addition to having antimicrobial activity against both Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation." Gram-negative bacteria: Escherichia coli (MIC=38 µM), Pseudomonas aeruginosa (MIC=310 µM).##Gram-positive bacteria: Staphylococcus aureus (MIC=19 µM), Bacillus cereus (MIC=38 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463874 Peptides. 2009 Aug;30(8):1387-1395. de Souza BM, da Silva AV, Resende VM, Arcuri HA, Dos Santos Cabrera MP, Ruggiero Neto J, Palma MS. Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista. DRAMP04545 SFPFFPPGICKRLKRC 16 Limnonectin-1Fa (Frogs, amphibians, animals) No entry found Not found Not found Limnonectes fujianensis (Fujian large-headed frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Possesses relatively potent growth inhibitory activity against the Gram-negative bacterium E. coli. Ineffective against the Gram-positive bacterium S. aureus and the potentially pathogenic yeast C. albicans at concentrations up to 160 µM. Gram-negative bacterium: Escherichia coli (MIC=35 µM) [Ref.21396976] It exhibits no hemolytic activity at a concentration of up to 160 μM. Cyclic Free Cyclization(Cys10 and Cys16). Disulfide bond between Cys10 and Cys16. L No cytotoxicity information found Not found 21396976 Biochimie. 2011 Jun;93(6):981-987. Wu Y, Wang L, Zhou M, Ma C, Chen X, Bai B, Chen T, Shaw C. Limnonectins: A new class of antimicrobial peptides from the skin secretion of the Fujian large-headed frog (Limnonectes fujianensis). DRAMP04546 SFHVFPPWMCKSLKKC 16 Limnonectin-1Fb (Frogs, amphibians, animals) No entry found Not found Not found Limnonectes fujianensis (Fujian large-headed frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Possesses relatively potent growth inhibitory activity against the Gram-negative bacterium E. coli. Ineffective against the Gram-positive bacterium S. aureus and the potentially pathogenic yeast C. albicans at concentrations up to 160 µM. Gram-negative bacterium: Escherichia coli (MIC=70 µM) [Ref.21396976] It exhibits no hemolytic activity at a concentration of up to 160 μM. Cyclic Free Cyclization(Cys10 and Cys16). Disulfide bond between Cys10 and Cys16. L No cytotoxicity information found Not found 21396976 Biochimie. 2011 Jun;93(6):981-987. Wu Y, Wang L, Zhou M, Ma C, Chen X, Bai B, Chen T, Shaw C. Limnonectins: A new class of antimicrobial peptides from the skin secretion of the Fujian large-headed frog (Limnonectes fujianensis). DRAMP04553 GVIKSVLKGVAKTVALGML 19 H. erythraea B2RP No entry found Not found Not found Hylarana erythraea Antimicrobial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (MIC=12.5 microM);##Gram-poaitive bacteria: Staphylococcus aureus (MIC=12.5 microM), multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 microM).##Yeast: Candida albicans (MIC=50 microM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20015460 Peptides. 2010 Apr;31(4):548-554. Al-Ghaferi N, Kolodziejek J, Nowotny N, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD, Conlon JM. Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae). DRAMP04640 GMASKAGSVLGKLAKVAIGAL 21 PGLa-AN2 No entry found Not found Not found Xenopus andrei Antimicrobial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: E. coli (MIC=25 µM);##Gram-positive bacterium: S. aureus (MIC=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP04665 KPFKKLEKVGRNIRDGIIKAGPAVAVIGQATSIARPTGK 39 Px-cec1 No entry found Not found Not found Plutella xylostella (Diamondback moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix (CD) A circular dichroism (CD) analysis revealed that the recombinant Px-cec1 mainly contained α-helixes. Function: Recombinant Px-cec1 exhibites a broad spectrum of anti-microbial properties against fungi, Gram-positive and Gram-negative bacteria, but it does not exhibit hemolytic activity against human erythrocytes. [Ref.22921836]Gram-positive bacterium: S. aureus (MIC=2 µM);##Gram-negative bacteria: E. coli (MIC=0.1 µM), Pseudomonas fluorescent (MIC=1.1 µM), Salmonella choleraesuis (MIC=2.1 µM);##Fungi: Aureobasidium pullulans (MIC=4.0 µM), Aspergillus flavus (MIC=14.5 µM), Aspergillus fumigatus (MIC=16.0 µM), Aspergillus niger (MIC=14.6 µM), Fusarium oxysporum (MIC=8.0 µM). [Ref.22921836]Non-hemolytic activity against human erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22921836 Protein Expr Purif. 2012 Oct;85(2):230-238. Jin F, Sun Q, Xu X, Li L, Gao G, Xu Y, Yu X, Ren S. cDNA cloning and characterization of the antibacterial peptide cecropin 1 from the diamondback moth, Plutella xylostella L. DRAMP04670 KNIGNSVSCLRNKGVCMPGKCAPKMKQIGTCGMPQVKCCKRK 42 PBD1-42 No entry found Not found Not found Boletus edulis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: The recombinant pBD142 exhibited antimicrobial activity against both Gram-positive Staphylococcus aureus and Gram-negative E. coli including the multi-resistant E. coli. Shows hemolytic activity and high thermal stability. [Ref.23220638]Gram-negative bacterium: Escherichia coli (MIC=100 µg/mL);##Gram-positive bacterium: Staphylococcus aureus (MIC=80 µg/mL). [Ref.23220638]5% hemolytic activity at 10 μg/mL, 10% hemolytic activity at 20 μg/mL, 10% hemolytic activity at 100 μg/mL against porcine fresh blood Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23220638 Protein Expr Purif. 2013 Mar;88(1):47-53. Li CL, Xu TT, Chen RB, Huang XX, Zhao YC, Bao YY, Zhao WD, Zheng ZY. Cloning, expression and characterization of antimicrobial porcine b defensin 1 in Escherichia coli. DRAMP04671 TDHQMAQSACIGVSQDNAYASAIPRDCHGG 30 Myticusin-1 No entry found Not found Not found Mytilus coruscus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Myticusin-1 exhibites stronger anti-microbial properties against Gram-positive bacteria more than Gram-negative bacteria and fungus. Gram-negative bacteria: Escherichia coli (MIC=6.7-12.5 µM), Vibrio Parahaemolyticus (MIC>25.0 µM), Pseudomonas aeruginosa (MIC>25.0 µM), Vibrio.harveyi (MIC=12.5-25.0 µM).##Gram-positive bacteria: Bacillus subtilis (MIC=1.2-2.5 µM), Staphylococcus aureus (MIC=2.5-5.0 µM), Sarcina luteus (MIC=1.2-2.5 µM), Bacillus megaterium (MIC=2.5-5.0 µM).##Fungi: Candida albicans (MIC=6.7-12.5 µM), Monilia albican (MIC=12.5-25.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23247103 Fish Shellfish Immunol. 2013 Feb;34(2):610-616. Liao Z, Wang XC, Liu HH, Fan MH, Sun JJ, Shen W. Molecular characterization of a novel antimicrobial peptide from Mytilus coruscus. DRAMP04676 MFTLKKPLLLLFFLGTISLSLCQEERDADEEEGEMIEEEVKRSLLGTVKDLLIGAGKSAAQSVLKGLSCKLSKDC 75 Brevinin-2HS2A E7EKE0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Odor frog) (Rana hainanensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against some Gram-positive bacteria and fungi but has no activity against a range of Gram- negative bacteria except P.faecalis. Has extremely low hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.22450466]Gram-positive bacteria: S.aureus ATCC 25923 (MIC=19 µM), B.licheniformis X39 (MIC=37.5 µM) and R.rhodochrous X15 (MIC=9.5 µM);##Gram-negative bacterium: P. faecalis X29 (MIC=9.5 µM);##Fungi: C. albicans ATCC 2002 (MIC=19 µM), slime mold 090223 (MIC=37.5 µM). [Ref.22450466]LC50=300 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22450466 Peptides. 2012 Jun;35(2):285-290. Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP04677 MFTMKKPLLLIVLLGIISLSLCEQERAADEEEGEMIEEEVKRSLLGTVKDLLIGAGKSAAQSVLKGLSCKLSKDC 75 Brevinin-2HS2B E7EKE1 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hainanensis (Odor frog) (Rana hainanensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against some Gram-positive bacteria and fungi but has no activity against a range of Gram- negative bacteria except P. faecalis. Has low hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.22450466]Gram-positive bacteria: S.aureus ATCC 25923 (MIC=19 µM), B. licheniformis X39 (MIC=37.5 µM) and R. rhodochrous X15 (MIC=9.5 µM);##Gram-negative bacterium: P. faecalis X29 (MIC=9.5 µM);##Fungi: C. albicans ATCC 2002 (MIC=19 µM), slime mold 090223 (MIC=37.5 µM). [Ref.22450466]LC50=300 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22450466 Peptides. 2012 Jun;35(2):285-290. Wang H, Yu Z, Hu Y, Li F, Liu L, Zheng H, Meng H, Yang S, Yang X, Liu J. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis. DRAMP04679 FLPFLIPALTSLISSL 16 Senegalin L0P323 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Kassina senegalensis (Senegal running frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptide with activity against the Gram-positive bacterium S. aureus NCTC 10788 and the yeast C. albicans NCPF 1467. Ineffective against the Gram-negative bacterium E. coli NCTC 10418. Induces a dose-dependent contraction of rat urinary bladder smooth muscle (EC50=2.9 nM) and a dose-dependent relaxation of rat tail artery smooth muscle (EC50=37.7 nM). Gram-positive bacterium: S. aureus NCTC 10788 (MIC=50 µM). Yeast: C. albicans NCPF 1467 (MIC=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23430307 Amino Acids. 2013 May;44(5):1347-1355. Wang H, Li R, Xi X, Meng T, Zhou M, Wang L, Zhang Y, Chen T, Shaw C. Senegalin: a novel antimicrobial/myotropic hexadecapeptide from the skin secretion of the African running frog, Kassina senegalensis. DRAMP00001 GSGVIPTISHECHMNSFQFVFTCCS 25 Variacin (Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Micrococcus varians (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has a broad host range of inhibition against Gram-positive food spoilage bacteria. Variacin is resistant to heat and pH conditions from 2 to 10. Biophysicochemical properties: Variacin is resistant to heat and pH conditions from 2 to 10." Gram-positive bacteria: Lactobacillus helveticus (+++), L. bulgaricus (+++), Lactobacillus lactis (++), Lactobacillus delbrueckii (+++), Lactobacillus acidophilus (++), Lactobacillus plantarum (+), Lactobacillus sake (LSK) (++), Lactobacillus curvatus (++), Leuconostoc mesenteroides (+), Streptococcus thermophilus (++), Lactococcus lactis (SL2) (++), Enterococcus faecalis (++), Enterococcus faecium (++), Listeria innocua (++), Listeria monocytogenes (++++), Listeria welhia (++).##Note: Inhibitory activity tested with supernatant adjusted to pH 7. No hemolysis information or data found in the reference(s) presented in this entry Linear Not included yet Not included yet Not included yet L Not found Not found 8633879 Appl Environ Microbiol. 1996 May;62(5):1799-1802. Pridmore D, Rekhif N, Pittet AC, Suri B, Mollet B. Variacin, a new lanthionine-containing bacteriocin produced by Micrococcus varians: comparison to lacticin 481 of Lactococcus lactis. DRAMP00002 WKSESVCTPGCVTGLLQTCFLQTITCNCKISK 32 Entianin (Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Bacillus subtilis subsp. spizizenii DSM 15029(T) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Entianin is very active against several Gram-positive pathogens, such as Staphylococcus aureus and Enterococcus faecalis. [Ref.21239550] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC = 4-8 μg/ml),Staphylococcus aureus ATCC 43300 (MRSA)(MIC = 8 μg/ml), Enterococcus faecalis ATCC 29212(MIC = 16μg/ml), Micrococcus luteus ATCC 9341(MIC = 4-8μg/ml), Enterococcus faecalis ATCC 51299 (VRE) (MIC = 8-16 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Succinylation Free There are two dehydroalanines (S5; S31),one dehydrobutyrine (T18),one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Not found 21239550 Appl Environ Microbiol. 2011 Mar;77(5):1698-1707. Fuchs SW, Jaskolla TW, Bochmann S, Kötter P, Wichelhaus T, Karas M, Stein T, Entian KD. Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis DSM 15029T with High Antimicrobial Activity. DRAMP00003 ADRGWIKTLTKDCPNVISSICAGTIITACKNCA 33 Bovicin HJ50 (Bacteriocin; Predicted) Q83ZN8 Belongs to the lantibiotic family (Class I bacteriocin) bovA Streptococcus bovis HJ50 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found 2M8V PTM: There are two thioether rings (T8-C13 and T10-C32) and one unique disulfide bridge between C21-C29. Gram-positive bacteria: Bacillus megaterium AS1.941 (IZ=14 mm), Bacillus subtilis AS1.1087 (IZ=12 mm), Lactobacillus curvatus LTH1174 (IZ=13 mm), Leuconostoc mesenteroides AS1.2 (IZ=10 mm), Leuconostoc dextranicum 181 (IZ=13 mm), Micrococcus flavus NCIB8166 (IZ=21 mm).##NOTE: IZ = zone of inhibition. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14702402##19202107 Microbiology. 2004 Jan;150(Pt 1):103-108.##Microbiology. 2009 Feb;155(Pt 2):584-593. Xiao H, Chen X, Chen M, Tang S, Zhao X, Huan L.##Liu G, Zhong J, Ni J, Chen M, Xiao H, Huan L. Bovicin HJ50, a novel lantibiotic produced by Streptococcus bovis HJ50.##Characteristics of the bovicin HJ50 gene cluster in Streptococcus bovis HJ50. DRAMP00004 MNNTIKDFDLDLKTNKKDTATPYVGSRYLCTPGSCWKLVCFTTTVK 46 Lantibiotic (Bacteriocin) Q48TR2 Belongs to the lantibiotic family (Class I bacteriocin) srtA Streptococcus pyogenes serotype M28 (strain MGAS6180) (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Function: Active on certain Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16088825 J Infect Dis. 2005 Sep 1;192(5):760-770. Green NM, Zhang S, Porcella SF, Nagiec MJ, Barbian KD, Beres SB, LeFebvre RB, Musser JM. Genome sequence of a serotype M28 strain of group a streptococcus: potential new insights into puerperal sepsis and bacterial disease specificity. DRAMP00006 GNGVIKTISHECHMNTWQFIFTCCS 25 Butyrivibriocin OR79 (Bacteriocin) O85355 Belongs to the lantibiotic family (Class I bacteriocin) bvi79 Butyrivibrio fibrisolvens (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Gram-positive bacteria: Fibrisolvens, Butyrivibrio crossotus, Clostridium clostridiforme, Lachnospira multiparus, Ruminococcus flavefaciens. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10224011 Appl Environ Microbiol. 1999 May;65(5):2128-2135. Kalmokoff ML, Lu D, Whitford MF, Teather RM. Evidence for production of a new lantibiotic (butyrivibriocin OR79A) by the ruminal anaerobe Butyrivibrio fibrisolvens OR79: characterization of the structural gene encoding butyrivibriocin OR79A. DRAMP18350 CLGIGSCNDFAGCGYAIVCFW 21 Siamycin II(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces strains AA3891 Antiviral, Anti-HIV, Antimicrobial Beta strand It differs from Siamycin I only by one amino acid. Siamycin I has a valine residue at position 4. In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus (XXJ). The original has been replaced since antimicrobial assays revealed no activity. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7787424 J Biomol NMR. 1995 Apr;5(3):271-86. Constantine KL, Friedrichs MS, Detlefsen D, Nishio M, Tsunakawa M, Furumai T, Ohkuma H, Oki T, Hill S, Bruccoleri RE, et al. High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion. DRAMP18351 EDGLHPRLCSC 11 Trichamide(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Trichodesmium erythraeum Unknown Not found Trichamide consists of 11 amino acids, including two cysteine-derived thiazole groups, and is cyclized by an N-C terminal amide bond. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16751554 Appl Environ Microbiol. 2006 Jun;72(6):4382-7. Sudek S, Haygood MG, Youssef DT, Schmidt EW. Structure of trichamide, a cyclic peptide from the bloom-forming cyanobacterium Trichodesmium erythraeum, predicted from the genome sequence. DRAMP00008 CSTNTFSLSDYWGNNGAWCTLTHECMAWCK 30 Lacticin 3147 A1 (LtnA1; Bacteriocin; Preclinical) O87236 Belongs to the lantibiotic family (Class I bacteriocin) ltnA1 Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 it displays strong activity towards all three strains. PTM: There are two 2,3-dehydrobutyrines (T3; T5), one 2,3-didehydroalanine (S7), two Lanthionines (C1-S2; S9-C19) and two Beta-methyllanthionines (T20-C25; T22-C29)." Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two 2,3-dehydrobutyrines (T3; T5), one 2,3-didehydroalanine (S7), two Lanthionines (C1-S2; S9-C19) and two Beta-methyllanthionines (T20-C25; T22-C29). Mixed(D-Ala) No cytotoxicity information found Lipid II 10971756##15023056##10608807 J Appl Microbiol. 2000 Aug;89(2):249-260.##Biochemistry. 2004 Mar 23;43(11):3049-3056.##J Biol Chem. 1999 Dec 31;274(53):37544-37550. Mart­nez-Cuesta MC, Buist G, Kok J, Hauge HH, Nissen-Meyer J, Pel¡ez C, Requena T.##Martin NI, Sprules T, Carpenter MR, Cotter PD, Hill C, Ross RP, Vederas JC.##Ryan MP, Jack RW, Josten M, Sahl HG, Jung G, Ross RP, Hill C. Biological and molecular characterization of a two-peptide lantibiotic produced by Lactococcus lactis IFPL105.##Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity.##Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. DRAMP00009 TTPATPAISILSAYISTNTCPTTKCTRAC 29 Bacteriocin lacticin 3147 A2 (LtnA2; Bacteriocin; Preclinical) O87237 Belongs to the lantibiotic family (Class I bacteriocin) ltnA2 Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains. PTM: There are one 2-oxobutanoic acid (T1), two 2,3-dehydrobutyrines (T2; T5), two 2,3-dehydroalanines (S9; S12), one Lanthionine (S16-C20) and two Beta-methyllanthionines (T22-C24; T26-C29)." Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Amidation Free There are one 2-oxobutanoic acid (T1), two 2,3-dehydrobutyrines (T2; T5), two 2,3-dehydroalanines (S9; S12), one Lanthionine (S16-C20) and two Beta-methyllanthionines (T22-C24; T26-C29). Mixed(D-Ala) No cytotoxicity information found Lipid II 10971756##15023056##10608807 J Appl Microbiol. 2000 Aug;89(2):249-260.##Biochemistry. 2004 Mar 23;43(11):3049-3056.##J Biol Chem. 1999 Dec 31;274(53):37544-37550. Mart­nez-Cuesta MC, Buist G, Kok J, Hauge HH, Nissen-Meyer J, Pel¡ez C, Requena T.##Martin NI, Sprules T, Carpenter MR, Cotter PD, Hill C, Ross RP, Vederas JC.##Ryan MP, Jack RW, Josten M, Sahl HG, Jung G, Ross RP, Hill C. Biological and molecular characterization of a two-peptide lantibiotic produced by Lactococcus lactis IFPL105.##Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity.##Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. DRAMP00010 KCKWWNISCDLGNNGHVCTLSHECQVSCN 29 Plantaricin W alpha (Plw-alpha; Bacteriocin) Q9AF67, D2KR94 Belongs to the lantibiotic family (Class I bacteriocin) plWalpha Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found "Function: Plantaricin W (Plw) is a new two-peptide bacteriocin, from Lactobacillus plantarum, which inhibits a large number of Gram-positive bacteria. The two individual peptides, Plwalpha (comprising 29 residues) and Plwbeta (comprising 32 residues), had low antimicrobial activity but acted synergistically. The data indicate that the two peptides work in a 1:1 ratio. PTM: Chemical analyses showed that both peptides are lantibiotics, but two unmodified cysteines and one serine residue were present in Plwa, and Plwb contained one cysteine residue." Gram-positive bacteria: Lactobacillus spp, Lactococcus lactis, Listeria innocua, Listeria monocytogenes, Oenococcus oeni, Leuconostoc mesenteroides, Pediococcus acidilactici, Pediococcus pentosaceus, Enterococcus faecalis, Propionibacterium freudenreichii, Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys9,two lanthionines (S8-C18,S21-C28),one β-methyllanthionine(T19-C24). L No cytotoxicity information found Not found 11238971 Microbiology. 2001 Mar;147(Pt 3):643-651. Holo H, Jeknic Z, Daeschel M, Stevanovic S, Nes IF. Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics. DRAMP00011 SGIPCTIGAAVAASIAVCPTTKCSKRCGKRKK 32 Plantaricin W beta (Plw-beta; Bacteriocin) Q9AF68 Belongs to the lantibiotic family (Class I bacteriocin) plWbeta Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found "Function: Plantaricin W (Plw) is a new two-peptide bacteriocin, from Lactobacillus plantarum, which inhibits a large number of Gram-positive bacteria. The two individual peptides, Plwalpha (comprising 29 residues) and Plwbeta (comprising 32 residues), had low antimicrobial activity but acted synergistically. The data indicate that the two peptides work in a 1:1 ratio. PTM: Chemical analyses showed that both peptides are lantibiotics, but two unmodified cysteines and one serine residue were present in Plwa, and Plwb contained one cysteine residue. Plwbeta is synthesized with a 29 aa leader, processed by an ABC transporter and then subjected to further proteolytic attack, resulting in the removal of the six Nterminal residues." Gram-positive bacteria: Lactobacillus spp, Lactococcus lactis, Listeria innocua, Listeria monocytogenes, Oenococcus oeni, Leuconostoc mesenteroides, Pediococcus acidilactici, Pediococcus pentosaceus, Enterococcus faecalis, Propionibacterium freudenreichii, Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Deaminated Free one lanthionine (S14-C18),two β-methyllanthionines(T20-C23,T21-C27). L No cytotoxicity information found Not found 11238971 Microbiology. 2001 Mar;147(Pt 3):643-651. Holo H, Jeknic Z, Daeschel M, Stevanovic S, Nes IF. Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics. DRAMP00012 TITLSTCAILSKPLGNNGYLCTVTKECMPSCN 32 Lantibiotic lichenicidin VK21 A1 (LchA1; Lchalpha; Bacteriocin) P86475, E0YCK1, Q65DC4, Q62NU5 Belongs to the lantibiotic family (Class I bacteriocin) lchA1 Bacillus licheniformis (strain ATCC 14580/VK21/DSM 13) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Alpha helix (1 helices; 3 residues) The Lchalpha peptide displays structural homology with mersacidin-like lantibiotics and involves relatively well-structured N- and C-terminal domains connected by a flexible loop stabilized by a thioether bridge Ala11-S-Ala21. 2KTN resolved by NMR. "Function: The mature peptides, Lchalpha and Lchbeta, interact synergistically to possess antibiotic activity against Gram-positive bacteria within a nanomolar concentration range, though the individual peptides were shown to be active at micromolar concentrations. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Only Lchalpha: Bacillus megaterium VKM41 (IC50=1.8 uM), Bacillus subtilis L1 (IC50=9 uM), Rhodococcus sp. SS2 (IC50=9 uM), Micrococcus luteus B1314 (IC50=1.2 uM), Staphylococcus aureus 209p (IC50=3.1 uM).##Lchalpha+Lchbeta: Bacillus megaterium VKM41 (IC50=0.12 uM), Bacillus subtilis L1 (IC50=0.64 uM), Rhodococcus sp. SS2 (IC50=0.64 uM), Micrococcus luteus B1314 (IC50=0.09 uM), Staphylococcus aureus 209p (IC50=0.64 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 19561184##19707558##20578714 Appl Environ Microbiol. 2009 Sep;75(17):5451-5460.##PLoS One. 2009 Aug 26;4(8):e6788.##Biochemistry. 2010 Aug 3;49(30):6462-6472. Begley M, Cotter PD, Hill C, Ross RP.##Dischinger J, Josten M, Szekat C, Sahl HG, Bierbaum G.##Shenkarev ZO, Finkina EI, Nurmukhamedova EK, Balandin SV, Mineev KS, Nadezhdin KD, Yakimenko ZA, Tagaev AA, Temirov YV, Arseniev AS, Ovchinnikova TV. Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins.##Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13.##Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21. DRAMP00013 TTPATTSSWTCITAGVTVSASLCPTTKCTSRC 32 Lantibiotic lichenicidin VK21 A2 (LchA2; Lchbeta; Bacteriocin) P86476, P86720, E0YCK0 Belongs to the lantibiotic family (Class I bacteriocin) lchA2 Bacillus licheniformis (strain ATCC 14580/VK21/DSM 13) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Alpha helix (1 helices; 14 residues) The Lchbeta peptide represents a prolonged hydrophobic alpha-helix flanked with more flexible N- and C-terminal domains. 2KTO resolved by NMR. "Function: The mature peptides, Lchalpha and Lchbeta, interact synergistically to possess antibiotic activity against Gram-positive bacteria within a nanomolar concentration range, though the individual peptides were shown to be active at micromolar concentrations. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Only Lchbeta: Bacillus megaterium VKM41 (IC50=2 uM), Bacillus subtilis L1 (IC50=30 uM), Rhodococcus sp. SS2 (IC50=16.6 uM), Micrococcus luteus B1314 (IC50=2.6 uM), Staphylococcus aureus 209p (IC50=20 uM).##Lchalpha+Lchbeta: Bacillus megaterium VKM41 (IC50=0.12 uM), Bacillus subtilis L1 (IC50=0.64 uM), Rhodococcus sp. SS2 (IC50=0.64 uM), Micrococcus luteus B1314 (IC50=0.09 uM), Staphylococcus aureus 209p (IC50=0.64 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 19561184##19707558##20578714 Appl Environ Microbiol. 2009 Sep;75(17):5451-5460.##PLoS One. 2009 Aug 26;4(8):e6788.##Biochemistry. 2010 Aug 3;49(30):6462-6472. Begley M, Cotter PD, Hill C, Ross RP.##Dischinger J, Josten M, Szekat C, Sahl HG, Bierbaum G.##Shenkarev ZO, Finkina EI, Nurmukhamedova EK, Balandin SV, Mineev KS, Nadezhdin KD, Yakimenko ZA, Tagaev AA, Temirov YV, Arseniev AS, Ovchinnikova TV. Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins.##Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13.##Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21. DRAMP00014 VTSKSLCTPGCITGVLMCLTQNSCVSCNSCIRC 33 Geobacillin I (nisin analog; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) sunA Geobacillus thermodenitrificans NG80-2 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Extensive NMR characterization demonstrated that geobacillin I contains seven thioether cross-links, two more than the five cross-links found in nisin and the most cross-links found in any lantibiotic to date. "Function: Geobacillin I is active against a wide range of Gram positive bacteria but it not active against Gram-negative bacterium E. coli. PTM: Contains seven thioether cross-links. Biophysicochemical properties: Geobacillin I is more stable than nisin at pH 7 and 8 at 37 and at 60 °C." Gram-positive bacteria: Streptococcus dysgalatiae subsp dysgalactiae ATCC 27957 (IC50=0.69±0.05 µM), Vancomycin-resistant Enterococcusfaecium CNRZ 481 (IC50=0.84±0.05 µM), Methicillin-resistant Staphylococcus aureus C5 (IC50=2.23±0.03 µM), Bacillus anthracis Sterne 7702 (IC50=0.49±0.02 µM), Bacillus subtilis ATCC 6633 (IC50=0.55±0.01 µM), Lactococcus lactis HP ATCC 11602 (IC50=0.12±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization between S29 and C33 Four lanthionines (S3-C7,S23-C27,S26-C30,S29-C33) and three β-methyllanthionines (T8-C11; T13-C18; T20-C24),S5 is dehydroalanines. L No cytotoxicity information found Not found 22431611 Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5241-5246. Garg N, Tang W, Goto Y, Nair SK, van der Donk WA. Lantibiotics from Geobacillus thermodenitrificans. DRAMP00015 STIVCVSLRICNWSLRFCPSFKVRCPM 27 Geobacillin II (nisin analog; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Geobacillus thermodenitrificans NG80-2 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Geobacillin II only demonstrated antimicrobial activity against Bacillus strains. Gram-positive bacteria: Bacillus cereus Z4222, Bacillus subtilis ATCC 6633. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization between S29 and C33 Four lanthionines (S3-C7,S23-C27,S26-C30,S29-C33) and three β-methyllanthionines (T8-C11; T13-C18; T20-C24),S5 is dehydroalanines. L No cytotoxicity information found Not found 22431611 Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5241-5246. Garg N, Tang W, Goto Y, Nair SK, van der Donk WA. Lantibiotics from Geobacillus thermodenitrificans. DRAMP00016 GNGVVLTLTHECNLATWTKKLKCC 24 Salivaricin 9 (Sal9; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) sivA Streptococcus salivarius (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Note: The Sal9 genetic determinants appear generally (but not always) to be megaplasmid-associated, and production seems often to occur in strains that also produce SalA. As is the case for SalA, the production of Sal9 appears to be autoinducible. Gram-positive bacteria: Streptococcus pyogenes and some Enterococci. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21310787 Microbiology. 2011 May;157(Pt 5):1290-1299. Wescombe PA, Upton M, Renault P, Wirawan RE, Power D, Burton JP, Chilcott CN, Tagg JR. Salivaricin 9, a new lantibiotic produced by Streptococcus salivarius. DRAMP00018 GTTVVNSTFSIVLGNKGYICTVTVECMRNCSK 32 SmbA1 (Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Streptococcus mutans GS5 (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Rich Not found The two peptides (SmbA and SmbB) are encoded by two chromosomal DNA genes in the same operon. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15673730 Antimicrob Agents Chemother. 2005 Feb;49(2):541-548. Yonezawa H, Kuramitsu HK. Genetic analysis of a unique bacteriocin, Smb, produced by Streptococcus mutans GS5. DRAMP00019 STPACAIGVVGITVAVTGISTACTSRCINK 30 SmbA2 (Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Streptococcus mutans GS5 (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Not found Not found The two peptides (SmbA and SmbB) are encoded by two chromosomal DNA genes in the same operon. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15673730 Antimicrob Agents Chemother. 2005 Feb;49(2):541-548. Yonezawa H, Kuramitsu HK. Genetic analysis of a unique bacteriocin, Smb, produced by Streptococcus mutans GS5. DRAMP00020 CAWYNISCRLGNKGAYCTLTVECMPSCN 28 HalA1 (one chain of haloduracin; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Bacillus halodurans C-125 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Rich Not found Function: Active on certain Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Surface of a bacterial target 17085596 Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17243-17248. McClerren AL, Cooper LE, Quan C, Thomas PM, Kelleher NL, van der Donk WA. Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic. DRAMP00021 TTWPCATVGVSVALCPTTKCTSQC 24 HalA2 (one chain of haloduracin; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Bacillus halodurans C-125 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Function: Active on certain Gram-positive bacteria. HalA2 causes pore formation and K+ efflux. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17085596 Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17243-17248. McClerren AL, Cooper LE, Quan C, Thomas PM, Kelleher NL, van der Donk WA. Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic. DRAMP00022 CSTNTFSLSDYWGNKGNWCTATHECMSWCK 30 Staphylococcin C55alpha (SacAalpha; chain alpha of Staphylococcin C55; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Staphylococcus aureus C55 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Active on certain Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus and Micrococcus luteus (C55alpha and C55beta work synergistically at a ratio of 1:1). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9835565##10417203 Appl Environ Microbiol. 1998 Dec;64(12):4803-4808.##Infect Immun. 1999 Aug;67(8):4268-4271. Navaratna MA, Sahl HG, Tagg JR.##Navaratna MA, Sahl HG, Tagg JR. Two-component anti-Staphylococcus aureus lantibiotic activity produced by Staphylococcus aureus C55.##Identification of genes encoding two-component lantibiotic production in Staphylococcus aureus C55 and other phage group II Staphylococcus aureus strains and demonstration of an association with the exfoliative toxin B gene. DRAMP00023 GTPLALLGGAATGVIGYISNQTCPTTACTRAC 32 Staphylococcin C55beta (SacAbeta; chain beta of Staphylococcin C55; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Staphylococcus aureus C55 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Active on certain Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus, Micrococcus luteus (C55alpha and C55beta work synergistically at a ratio of 1:1). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9835565##10417203 Appl Environ Microbiol. 1998 Dec;64(12):4803-4808.##Infect Immun. 1999 Aug;67(8):4268-4271. Navaratna MA, Sahl HG, Tagg JR.##Navaratna MA, Sahl HG, Tagg JR. Two-component anti-Staphylococcus aureus lantibiotic activity produced by Staphylococcus aureus C55.##Identification of genes encoding two-component lantibiotic production in Staphylococcus aureus C55 and other phage group II Staphylococcus aureus strains and demonstration of an association with the exfoliative toxin B gene. DRAMP00024 TTPACFTIGLGVGALFSAKFC 21 CylLS (a structural subunit of cytolysin; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Enterococcus faecalis (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found CylLL and CylLS are activated by an extracellular protease, CylA. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8898386 Mol Microbiol. 1996 Sep;21(6):1175-1184. Booth MC, Bogie CP, Sahl HG, Siezen RJ, Hatter KL, Gilmore MS. Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic. DRAMP00025 TTPVCAVAATAAASSAACGWVGGGIFTGVTVVVSLKHC 38 CylLL (a structural subunit of cytolysin; Bacteriocin) No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Enterococcus faecalis (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found CylLL and CylLS are activated by an extracellular protease, CylA. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8898386 Mol Microbiol. 1996 Sep;21(6):1175-1184. Booth MC, Bogie CP, Sahl HG, Siezen RJ, Hatter KL, Gilmore MS. Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic. DRAMP00026 KRGSGWIATITDDCPNSVFVCC 22 Salivaricin A (SalA; Bacteriocin; Preclinical) P36500 Belongs to the type A lantibiotic family (Class I bacteriocin) salA Streptococcus salivarius 20P3 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Contains one lanthionine (S17-C22) and two Beta-methyllanthionines (T9-C14; T11-C21), which is followed by membrane translocation and cleavage of the modified precursor. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8357242 Appl Environ Microbiol. 1993 Jul;59(7):2014-2021. Ross KF, Ronson CW, Tagg JR. Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3. DRAMP00027 GGGVIQTISHECRMNSWQFLFTCCS 25 Salivaricin B (SboB; Bacteriocin; Preclinical) No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Streptococcus salivarius K12 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found PTM: Thioether bonds are predicted between 7-12; 9-23; 16-24. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17194838 Appl Environ Microbiol. 2007 Feb;73(4):1107-1113. Hyink O, Wescombe PA, Upton M, Ragland N, Burton JP, Tagg JR. Salivaricin A2 and the novel lantibiotic salivaricin B are encoded at adjacent loci on a 190-kilobase transmissible megaplasmid in the oral probiotic strain Streptococcus salivarius K12. DRAMP00028 IASKFICTPGCAKTGSFNSYCC 22 Lantibiotic epidermin (Bacteriocin) P08136, Q54093 Belongs to the type A lantibiotic family (Class I bacteriocin) epiA Staphylococcus epidermidis TU 3298 / DSM 3095 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one didehydrobutyrine (T14), two lanthionines (S3-C7; S16-C21) and one Beta-methyllanthionine (T8-C11) and one S-(2-aminovinyl)-D-cysteine (S19-C22)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 2835685##3769923 Nature. 1988 May 19;333(6170):276-268.##Eur J Biochem. 1986 Oct 1;160(1):9-22. Schnell N, Entian KD, Schneider U, Götz F, Zähner H, Kellner R, Jung G.##Allgaier H, Jung G, Werner RG, Schneider U, Zähner H. Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings.##Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic. DRAMP00029 GKNGVFKTISHECHLNTWAFLATCCS 26 Streptococcin A-FF22 (Antibacterial peptide SA-FF22; Bacteriocin) P36501 Belongs to the type A lantibiotic family (Class I bacteriocin) scnA Streptococcus pyogenes FF22 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one 2,3-didehydrobutyrine at T23, two Beta-methyllanthionine (T8-C13; T17-C25), and one Lanthionine (S10-C24)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8328813##8125103 Appl Environ Microbiol. 1993 Jun;59(6):1969-1971.##Eur J Biochem. 1994 Mar 1;220(2):455-462. Hynes WL, Ferretti JJ, Tagg JR.##Jack RW, Carne A, Metzger J, Stefanović S, Sahl HG, Jung G, Tagg J. Cloning of the gene encoding Streptococcin A-FF22, a novel lantibiotic produced by Streptococcus pyogenes, and determination of its nucleotide sequence.##Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22. DRAMP18349 CLGVGSCNDFAGCGYAVVCFW 21 Siamycin I (Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces strain AA6532 Antiviral, Anti-HIV, Antimicrobial Beta strand It differs from Siamycin I only by one amino acid. Siamycin I has a valine residue at position 4. In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus (XXJ). The original has been replaced since antimicrobial assays revealed no activity. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8557614 J Antibiot (Tokyo). 1995 Dec;48(12):1515-7. Detlefsen DJ, Hill SE, Volk KJ, Klohr SE, Tsunakawa M, Furumai T, Lin PF, Nishio M, Kawano K, Oki T, et al. Siamycins I and II, new anti-HIV-1 peptides: II. Sequence analysis and structure determination of siamycin I. DRAMP00031 GSEIQPR 7 Lantibiotic carnocin-UI49 (Bacteriocin) P36960 Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Carnobacterium sp. (strain UI49) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic). Active on Gram-positive bacteria. Biophysicochemical properties: Bacteriocin activity is very stable below pH 8 and is moderately heat stable in the crude extract." Gram-positive bacteria: Lactobacillus acidophilus, Lactobacillus casei, Lactobacillus sakei, L. lactis, Pediococcus acidilactici, all Carnobacterium species (six NCDO strains). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1622206 Appl Environ Microbiol. 1992;58(5):1417-1422. Stoffels G, Nissen-Meyer J, Gudmundsdottir A, Sletten K, Holo H, Nes IF. Purification and characterization of a new bacteriocin isolated from a Carnobacterium sp. DRAMP00033 ASIVKTTIKASKKLCRGFTLTCGCHFTGKK 30 Lantibiotic epilancin 15X (Bacteriocin) P86047 Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Staphylococcus epidermidis 15X154 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Non helix or strand structure The molecule contains ten post-translationally modified amino acids, three lanthionine ring structures and a hydroxy-propionyl N-terminal moiety. 1W9N resolved by NMR. "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria: such as staphylococci, enterococci and streptococci. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one Lactic acid (S1), one 2,3-didehydroalanine (S3) and three 2,3-dehydrobutyrines (T7; T8; T28); also one Lanthionine (S12-C16) and two Beta-methyllanthionines (T20-C23; T22-C25)." Gram-positive bacteria: resistant bacterial strains Staphylococcus aureus (MRSA) and VRE. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15792796 FEBS Lett. 2005 Mar 28;579(9):1917-1922. Ekkelenkamp MB, Hanssen M, Danny Hsu ST, de Jong A, Milatovic D, Verhoef J, van Nuland NA. Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis. DRAMP00034 SASVLKTSIKVSKKYCKGVTLTCGCNITGGK 31 Lantibiotic epilancin K7 (Bacteriocin) Q57312 Belongs to the type A lantibiotic family (Class I bacteriocin) elkA Staphylococcus epidermidis K7 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are two dihydroalanines (Dha): S3 and S8; two dehydrobutyrines (Dhb): T7, T28; one lanthionine: S12-C16; and two Beta-methyllanthionine: T20-C23, T22-C25." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7607233 Eur J Biochem. 1995 Jun 1;230(2):587-600. van de Kamp M, van den Hooven HW, Konings RN, Bierbaum G, Sahl HG, Kuipers OP, Siezen RJ, de Vos WM, Hilbers CW, van de Ven FJ. Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7. DRAMP00035 ASIIKTTIKVSKAVCKTLTCICTGSCSNCK 30 Lantibiotic paenibacillin (Bacteriocin) P86013 Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Paenibacillus polymyxa (Bacillus polymyxa) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacks antibacterial activity against Gram-negative bacteria. Physicochemical properties: water solubility, thermal resistance, and stability against acid/alkali (pH 2.0 to 9.0) treatment." Gram-positive bacteria: Bacillus spp, Clostridium sporogenes, Lactobacillus spp, Lactococcus lactis, Leuconostoc mesenteroides, Listeria spp, Pediococcus cerevisiae, Staphylococcus aureus, Streptococcus agalactiae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17071789##18625234 Appl Environ Microbiol. 2007 Jan;73(1):168-178.##FEBS Lett. 2008 Aug 6;582(18):2787-2792. He Z, Kisla D, Zhang L, Yuan C, Green-Church KB, Yousef AE.##He Z, Yuan C, Zhang L, Yousef AE. Isolation and identification of a Paenibacillus polymyxa strain that coproduces a novel lantibiotic and polymyxin.##N-terminal acetylation in paenibacillin, a novel lantibiotic. DRAMP00036 ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK 34 Nisin A (Bacteriocin; Preclinical) P13068 Belongs to the type A lantibiotic family (Class I bacteriocin) spaN Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Non helix or strand structure Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four Beta-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). Medical use: Urogenital tract infections and spermicidal activity in-vivo; animal model: rabbit (Reproduction. 2004 Jul;128(1):117-126)." Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc, Listeria, clostridium. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Lipid II 3141403##5131162##1575686 J Biol Chem. 1988 Nov 5;263(31):16260-16266.##J Am Chem Soc. 1971 Sep 8;93(18):4634-4635.##Biochem J. 1992 Apr 15;283 (Pt 2):413-420. Buchman GW, Banerjee S, Hansen JN.##Gross E, Morell JL.##Lian LY, Chan WC, Morley SD, Roberts GC, Bycroft BW, Jackson D. Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic.##The structure of nisin.##Solution structures of nisin A and its two major degradation products determined by n.m.r. DRAMP00037 ITSISLCTPGCKTGALMGCNMKTATCNCSIHVSK 34 Nisin Z (Bacteriocin; Preclinical) P29559 Belongs to the type A lantibiotic family (Class I bacteriocin) nisZ Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 4 residues) The structure shows a novel lipid II-binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds. This cage structure provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics. 1WCO resolved by NMR. "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are two dehydroalanines (Dha): S5, S33; one didehydrobutyrine (Dhb): T2; one lanthionine: S3-C7; and four methyllanthionines: T8-C11, T13-C19, T23-C26, and T25-C28." Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc, Listeria, clostridium. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Lipid II 1935953##7626780##15361862 Eur J Biochem. 1991 Nov 1;201(3):581-584.##DNA Seq. 1995;5(4):203-218.##Nat Struct Mol Biol. 2004 Oct;11(10):963-967. Mulders JW, Boerrigter IJ, Rollema HS, Siezen RJ, de Vos WM.##Immonen T, Ye S, Ra R, Qiao M, Paulin L, Saris PE.##Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Identification and characterization of the lantibiotic nisin Z, a natural nisin variant.##The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon.##The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. DRAMP00038 ITSKSLCTPGCKTGILMTCPLKTATCGCHFG 31 Nisin U (Bacteriocin) Q2QBT0 Belongs to the type A lantibiotic family (Class I bacteriocin) nsuA Lactococcus uberis ATCC 27958 Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are two dihydroalanines (Dha)(S5; T18), one didehydrobutyrine (Dhb)(T2), one lanthionine (S3-C7) and four methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). Biotechnological use: Used as a food preservative." Gram-positive bacteria: Streptococcus pyogenes, Streptococcus uberis, Streptococcus agalactiae, Streptococcus dysgalactiae, Staphylococcus simulans, Staphylococcus cohnii, Lactococcus lactis, Lactobacillus acidophilus, Streptococcus mitis. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two dihydroalanines (Dha)(S5; T18), one didehydrobutyrine (Dhb)(T2), one lanthionine (S3-C7) and four methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Lipid II 16461661 Appl Environ Microbiol. 2006 Feb;72(2):1148-1156. Wirawan RE, Klesse NA, Jack RW, Tagg JR. Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis. DRAMP00039 TAGPAIRASVKQCQKTLKATRLFTVSCKGKNGCK 34 Pep5 (Bacteriocin) P19578 Belongs to the type A lantibiotic family (Class I bacteriocin) pepA Staphylococcus epidermidis (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.After proteolysis of the propeptide, the N-terminal 2,3-didehydrobutyrine hydrolyzes to 2-oxobutanoic acid, possibly spontaneously." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 2764678##7556197 Arch Microbiol. 1989;152(1):16-19.##Eur J Biochem. 1995 Sep 1;232(2):478-489. Kaletta C, Entian KD, Kellner R, Jung G, Reis M, Sahl HG.##Meyer C, Bierbaum G, Heidrich C, Reis M, S¼ling J, Iglesias-Wind MI, Kempter C, Molitor E, Sahl HG. Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence.##Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation. DRAMP00040 IASKFLCTPGCAKTGSFNSYCC 22 Gallidermin (Bacteriocin; Preclinical) P21838 Belongs to the type A lantibiotic family (Class I bacteriocin) gdmA Staphylococcus gallinarum TU 3928 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one didehydrobutyrine (Dhb): T14; two lanthionines: S3-C7, S16-C21; one Beta-methyllanthionine: T8-C11; and S-(2-aminovinyl)-D-cysteine (Ser-Cys): S19-C22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 3181159 Eur J Biochem. 1988 Oct 15;177(1):53-59. Kellner R, Jung G, Hörner T, Zähner H, Schnell N, Entian KD, Götz F. Gallidermin: a new lanthionine-containing polypeptide antibiotic. DRAMP00041 FKSWSLCTPGCARTGSFNSYCC 22 Mutacin-1140 (Mutacin III; Bacteriocin) O68586 Belongs to the type A lantibiotic family (Class I bacteriocin) lanA Streptococcus mutans (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one dihydroalanine (Dha): S5; one didehydrobutyrine (Dhb): T14; two lanthionines: S3-C7, S16-C21; one Beta-methyllanthionine: T8-C11; and S-(2-aminovinyl)-D-cysteine (Ser-Cys): S19-C22." Gram-positive bacteria: Streptococcus cricetus E49, Streptococcus rattus BHT-2, Streptococcus mutans NG8, S. mutans OMZ175, S. mutans V100, Streptococcus sobrinus SL1, S. sobrinus ATCC 27352, Streptococcus downeii ATCC 33748, Streptococcus salivarius ATCC 25975, Streptococcus salivariusATCC 27945, Streptococcus mitis ATCC 19950, Streptococcus sanguinis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11082191 Eur J Biochem. 2000 Dec;267(23):6810-6816. Smith L, Nov¡k J, Rocca J, McClung S, Hillman JD, Edison AS. Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics. DRAMP00042 FKSWSFCTPGCAKTGSFNSYCC 22 Bacteriocin mutacin B-Ny266 (Preclinical) P80666 Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Streptococcus mutans Ny266 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Rich Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: There are one dihydroalanines (Dha): S5; one didehydrobutyrine (Dhb): T14; two lanthionines: S3-C7, S16-C21; one Beta-methyllanthionine: T8-C11; and S-(2-aminovinyl)-D-cysteine (Ser-Cys): S19-C22." Gram-positive bacterium: Micrococcus luteus ATCC 272. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 9237644 FEBS Lett. 1997 Jun 30;410(2-3):275-279. Mota-Meira M, Lacroix C, LaPointe G, Lavoie MC. Purification and structure of mutacin B-Ny266: a new lantibiotic produced by Streptococcus mutans. DRAMP00043 KKKSGVIPTVSHDCHMNTFQFMFTCCS 27 Bacteriocin nukacin (Nukacin KQ-1; Nukacin KQU-131) B5MFD0 Belongs to the type A lantibiotic family (Class I bacteriocin) nukA Staphylococcus hominis KQU-131 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity). Biophysicochemical properties: Temperature dependence (Retains 50% of its antimicrobial activity after heating at 100 degrees Celsius for 100 minutes, and retains 25% antimicrobial activity after heating at 121 Celsius for 15 minutes)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18685189 Biosci Biotechnol Biochem. 2008 Aug;72(8):2232-2235. Wilaipun P, Zendo T, Okuda K, Nakayama J, Sonomoto K. Identification of the nukacin KQU-131, a new type-A(II) lantibiotic produced by Staphylococcus hominis KQU-131 isolated from Thai fermented fish product (Pla-ra). DRAMP00044 KKKSGVIPTVSHDCHMNSFQFVFTCCS 27 Bacteriocin nukacin (Nukacin 3299; Simulancin 3299) E0WX65 Belongs to the type A lantibiotic family (Class I bacteriocin) nukA Staphylococcus simulans Antimicrobial, Antibacterial Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity). Biophysicochemical properties: pH dependence (Optimum pHs for antimicrobial activity are 3.0 and 6.0. Activity is reduced by 50% at alkaline pHs 9.0 and 11.0); Temperature dependence (No change in antimicrobial activity between 80 or 100 degrees Celsius after 15 minutes, but reduction in 50% antimicrobial activity at 121 degrees Celsius after 15 minutes). ptm: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20627619 Vet Microbiol. 2010 Nov 20;146(1-2):124-131. Ceotto H, Holo H, da Costa KF, Nascimento Jdos S, Salehian Z, Nes IF, Bastos Mdo C. Nukacin 3299, a lantibiotic produced by Staphylococcus simulans 3299 identical to nukacin ISK-1. DRAMP18346 ITPLATLATPEATPVGFAATSATAAAVNMITHDVTRH 37 Legonaridin(Bacteriocin) No entry found Belongs to the class I bacteriocin legA Streptomyces sp. CT34 Unknown Not found Despite the same chemical features as those observed in cypemycin and grisemycin, legonaridin 1 has a structurally different C-terminus with a free carboxylic acid. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26256511 Org Biomol Chem. 2015 Oct 7;13(37):9585-92. Rateb ME, Zhai Y, Ehrner E, Rath CM, Wang X, Tabudravu J, Ebel R, Bibb M, Kyeremeh K, Dorrestein PC, Hong K, Jaspars M, Deng H. Legonaridin, a new member of linaridin RiPP from a Ghanaian Streptomyces isolate. DRAMP18347 CLGVGSCNDFAGCGYAIVCFW 21 Siamycin(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces sp. No. 73264 Antiviral, Anti-HIV, Antimicrobial Not found It differs from siamycin I only at position 17 (V to I). Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8619594 Antimicrob Agents Chemother. 1995 Oct;39(10):2345-7. Chokekijchai S, Kojima E, Anderson S, Nomizu M, Tanaka M, Machida M, Date T, Toyota K, Ishida S, Watanabe K, et al. NP-06: a novel anti-human immunodeficiency virus polypeptide produced by a Streptomyces species. DRAMP18348 GNWHGTAPDWFFNYYW 16 RES-701-1(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces spp. Unknown Not found Not found RES-701-1 is an endothelin B receptor (ET) selective peptidic antagonist. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Letters in Peptide Science. 1997 Jun;4(3):167-170. Shibata K,Yano K,Tanaka T,Matsuda Y,Yamasaki M. C-terminal modifications of an endothelin antagonist RES-701-1: Production of ETA/ETB dual selective analogs. DRAMP00046 GSRYLCTPGSCWKLVCFTTTVK 22 Lantibiotic streptin (Bacteriocin) P0C0H8, Q9FDV1, P0C0H9, Q48YZ4, Q9FDV1 Belongs to the type A lantibiotic family (Class I bacteriocin) srtA Streptococcus pyogenes & Streptococcus pyogenes serotype M1 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Induction: Induces its own expression in at least strain M25. Miscellaneous: A longer form (streptin 2, with three more amino acids at the N-terminus) is probably due to incomplete processing. Other forms also exist, some of which are due to differing levels of dehydration. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Active on certain Gram-positive bacteria. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11328600##12732544##11296296##16088826 J Biochem. 2001 May;129(5):769-775.##Appl Environ Microbiol. 2003 May;69(5):2737-2747.##Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4658-4663.##J Infect Dis. 2005 Sep 1;192(5):771-782. Karaya K, Shimizu T, Taketo A.##Wescombe PA, Tagg JR.##Ferretti JJ, McShan WM, Ajdic D, Savic DJ, Savic G, Lyon K, Primeaux C, Sezate S, Suvorov AN, Kenton S, Lai HS, Lin SP, Qian Y, Jia HG, Najar FZ, Ren Q, Zhu H, Song L, White J, Yuan X, Clifton SW, Roe BA, McLaughlin R.##Sumby P, Porcella SF, Madrigal AG, Barbian KD, Virtaneva K, Ricklefs SM, Sturdevant DE, Graham MR, Vuopio-Varkila J, Hoe NP, Musser JM. New gene cluster for lantibiotic streptin possibly involved in streptolysin S formation.##Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes.##Complete genome sequence of an M1 strain of Streptococcus pyogenes.##Evolutionary origin and emergence of a highly successful clone of serotype M1 group a Streptococcus involved multiple horizontal gene transfer events. DRAMP00047 VGSRYLCTPGSCWKLVCFTTTVK 23 Streptin 1 (Bacteriocin) No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Bacillus subtilis A1/3 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Rich Not found Two possible structures have been proposed for streptin 1 due to insufficient info. The first lanthionine S3-C7 and the second methyllanthionine T8-C12 are identical in the two proposed structures. A third intra-bond is either S11-C17 or C17-T19 (or C17-T20 or C17-T21). Compared to Streptin 1, Streptin 2 contains 3 additional residues TPY at the N-terminus. Small quantities of peptides at various degrees of dehydration were also detected. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12732544 Appl Environ Microbiol. 2003 May;69(5):2737-2747. Wescombe PA, Tagg JR. Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes. DRAMP00048 WKSESLCTPGCVTGALQTCFLQTLTCNCKISK 32 Lantibiotic subtilin (Bacteriocin) P10946 Belongs to the type A lantibiotic family (Class I bacteriocin) spaS Bacillus subtilis (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.Succinylated subtilin is 10-20 times less active than subtilin. The ratio subtilin/succinylated subtilin is about 1:2 after 24 hours growth.The 2,3-didehydrobutyrine is determined to be the Z-isomer." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Succinylation Free There are two dehydroalanines (S5; S31),one dehydrobutyrine (T18),one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Lipid II 4154277##21239550 "Hoppe Seylers Z Physiol Chem. 1973 Jul;354(7):810-812.##Appl Environ Microbiol . 2011 Mar;77(5):1698-707." Gross E, Kiltz HH, Nebelin E.##Sebastian W Fuchs, Thorsten W Jaskolla, Sophie Bochmann, Peter Kötter, Thomas Wichelhaus, Michael Karas, Torsten Stein, Karl-Dieter Entian Subtilin, VI: the structure of subtilin (author's transl).##Entianin, a novel subtilin-like lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029T with high antimicrobial activity DRAMP00049 KGGSGVIHTISHECNMNSWQFVFTCCS 27 Bacteriocin lacticin-481 (Lactococcin-DR) P36499 Belongs to the type A lantibiotic family (Class I bacteriocin) lctA Lactococcus lactis CNRZ 481 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Gram-positive bacteria: Lactic acid bacteria, Clostridium tyrobutyricum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 16348628##8344922##8764998 Appl Environ Microbiol. 1992 Jan;58(1):279-284.##J Biol Chem. 1993 Aug 5;268(22):16361-16368.##FEBS Lett. 1996 Aug 12;391(3):317-322. Piard JC, Muriana PM, Desmazeaud MJ, Klaenhammer TR.##Piard JC, Kuipers OP, Rollema HS, Desmazeaud MJ, de Vos WM.##van den Hooven HW, Lagerwerf FM, Heerma W, Haverkamp J, Piard JC, Hilbers CW, Siezen RJ, Kuipers OP, Rollema HS. Purification and Partial Characterization of Lacticin 481, a Lanthionine-Containing Bacteriocin Produced by Lactococcus lactis subsp. lactis CNRZ 481.##Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis.##The structure of the lantibiotic lacticin 481 produced by Lactococcus lactis: location of the thioether bridges. DRAMP18345 CLGIGSCNNFAGCGYAVVCFW 21 Tricyclic peptide RP 71955 (Bacteriocin) P37046 Not found Not found Streptomyces sp. (strain SP9440) Antiviral, Anti-HIV, Antimicrobial Beta strand An internal amide bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well as two disulfide bridges, one between C1 and C13 and one between C7 and C19. 1RPB, 1RPC resolved by NMR Caution:The isopeptide linked residue 9 is shown as Asn rather than Asp as mentioned in PubMed:8286361, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible.(From Swiss-prot) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8270499 J Antibiot (Tokyo). 1993 Nov;46(11):1756-7. Helynck G, Dubertret C, Mayaux JF, Leboul J. Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite. DRAMP00051 FSSLSLCSLGCTGVKNPSFNSYCC 24 Mutacin I (Bacteriocin) No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Streptococcus mutans CH43); also Streptococcus mutans UA140 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus, Staphylococcus epidermidis, enterococci, pneumococci, group A streptococci. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10919773##11133423 Appl Environ Microbiol. 2000 Aug;66(8):3221-3229.##Appl Environ Microbiol. 2001 Jan;67(1):15-21. Qi F, Chen P, Caufield PW.##Qi F, Chen P, Caufield PW. Purification and biochemical characterization of mutacin I from the group I strain of Streptococcus mutans, CH43, and genetic analysis of mutacin I biosynthesis genes.##The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV. DRAMP00052 NRWWQGVVPTVSYECRMNSWQHVFTCC 27 Mutacin-2 (Mutacin II mutacin H-29B; Bacteriocin) O54329, P84110 Belongs to the type A lantibiotic family (Class I bacteriocin) mutA Streptococcus mutans (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Rich Not found "Function: Mutacin-2 inhibits other mutans streptococci as well as many gram-positive exogenous pathogens. Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool. Biophysicochemical properties: pH dependence (Stable from pH 4.0 to 10.0); Temperature dependence (Thermostable). PTM: There are one didehydrobutyrine (T25), two lanthionines (S12-C26; S19-C27) and one Beta-methyllanthionine (T10-C15)." Gram-positive bacteria: Micrococcus luteus, Staphylococcus aureus, Peptostreptococcus micros, Pediococcus acidilactici, Clostridium sporogenes, Corynebacterium diphtheriae, Actinomyces viscosus, Gardnerella vaginalis, Propionibacterium acnes, Listeria monocytogenes, Mycobacterium smegmatis.##Gram-negative bacteria: Campylobacter jejuni, Helicobacter pylori, Neisseria gonorrhoeae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10821848##8592997##16626493##8021218 J Biol Chem. 2000 May 26;275(21):15845-15850.##Antimicrob Agents Chemother. 1995 Dec;39(12):2656-2660.##BMC Microbiol. 2006 Apr 20;6:36.##J Bacteriol. 1994 Jul;176(14):4316-4320. Krull RE, Chen P, Novak J, Kirk M, Barnes S, Baker J, Krishna NR, Caufield PW.##Chikindas ML, Nov¡k J, Driessen AJ, Konings WN, Schilling KM, Caufield PW.##Nicolas G, Morency H, LaPointe G, Lavoie MC.##Nov¡k J, Caufield PW, Miller EJ. Biochemical structural analysis of the lantibiotic mutacin II.##Mutacin II, a bactericidal antibiotic from Streptococcus mutans.##Mutacin H-29B is identical to mutacin II (J-T8).##Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans. DRAMP00053 ITSISLCTPGCKTGALMGCNMKTATCNCSVHVSK 34 Nisin F (Bacteriocin; Perclinical) No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Lactococcus lactis F10 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: defense response to Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus, Staphylococcus carnosus, Lactobacillus curvatus N1902, Lactobacillus plantarum, Lactobacillus reuteri. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Lipid II 18039827 Appl Environ Microbiol. 2008 Jan;74(2):547-549. de Kwaadsteniet M, Ten Doeschate K, Dicks LM. Characterization of the structural gene encoding nisin F, a new lantibiotic produced by a Lactococcus lactis subsp. lactis isolate from freshwater catfish (Clarias gariepinus). DRAMP00054 ITSISLCTPGCKTGVLMGCNLKTATCNCSVHVSK 34 Nisin Q (Bacteriocin) No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) nisQ Lactococcus lactis 61-14 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: defense response to Gram-positive bacteria. Gram-positive bacteria: LAB, Bacillus sp, Listeria sp, Micrococcus sp. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28). L No cytotoxicity information found Not found 12913315 Biosci Biotechnol Biochem. 2003 Jul;67(7):1616-1619. Zendo T, Fukao M, Ueda K, Higuchi T, Nakayama J, Sonomoto K. Identification of the lantibiotic nisin Q, a new natural nisin variant produced by Lactococcus lactis 61-14 isolated from a river in Japan. DRAMP00055 ITSVSWCTPGCTSEGGGSGCSHCC 24 Bacteriocin 97518 No entry found Belongs to the type A lantibiotic family (Class I bacteriocin) Not found Planomonospora sp. (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram- Not found Rich Not found Function: It inhibits cell wall synthesis of Gram-positive bacteria, including Staphylococcus aureus (MRSA). Gram-negative bacteria: Escherichia coli, Moraxella catarrhalis.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17469849 Biochemistry. 2007 May 22;46(20):5884-5895. Castiglione F, Cavaletti L, Losi D, Lazzarini A, Carrano L, Feroggio M, Ciciliato I, Corti E, Candiani G, Marinelli F, Selva E. A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp. DRAMP00056 CVQSCSFGPLTWSCDGNTK 19 Bacteriocin ancovenin P38655 Belongs to the type B lantibiotic family (Class I bacteriocin) Not found Streptomyces sp. A647P-2 (Gram-positive bacteria) Antimicrobial Protein level Not found Not found "MOA: Acts as an inhibitor of angiotensin I converting enzyme. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Tetrahedron Lett. 1985;26:665-668. Wakamiya T, Ueki Y, Shiba T, Kido Y, Motoki Y. The structure of ancovenin, a new peptide inhibitor of angiotensin I converting enzyme. DRAMP00057 CKQSCSFGPFTFVCDGNTK 19 Bacteriocin duramycin (Leucopeptin; Bacteriocin) P36504 Belongs to the type B lantibiotic family (Class I bacteriocin) Not found Streptoverticillium griseoverticillatum (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Acts as inhibitor of human phospholipase A2. PTM: Methyllanthionine rings between residues 1 and18 as well as between residues 5 and 11; a lanthionine occurs between Cys14 and residue 4. In addition, addition of Lys19 to dehydralanine at position 6 forms a lysinoalanine bridge. The Asp residue at position 15 is hydroxylated. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet phosphatidylethanolamine 2272918##2125590 J Antibiot (Tokyo). 1990 Nov;43(11):1421-1430.##J Antibiot (Tokyo). 1990 Nov;43(11):1403-1412. Hayashi F, Nagashima K, Terui Y, Kawamura Y, Matsumoto K, Itazaki H.##Fredenhagen A, Fendrich G, Märki F, Märki W, Gruner J, Raschdorf F, Peter HH. The structure of PA48009: the revised structure of duramycin.##Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin. DRAMP00058 CRQSCSFGPLTFVCDGNTK 19 Lantibiotic duramycin B (Bacteriocin) P36502 Belongs to the type B lantibiotic family (Class I bacteriocin) Not found Streptoverticillium strain R2075 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found Methyllanthionine rings between residues 1 and18 as well as between residues 5 and 11; a lanthionine occurs between Cys14 and residue 4. In addition, addition of Lys19 to dehydralanine at position 6 forms a lysinoalanine bridge. The Asp residue at position 15 is hydroxylated. Duramycins and cinnamycin specifically binds to phosphatidylethanolamine, thereby indirectly inhibiting the activity of phospholipase A2. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phosphatidylethanolamine 2125590 J Antibiot (Tokyo). 1990 Nov;43(11):1403-1412. Fredenhagen A, Fendrich G, Märki F, Märki W, Gruner J, Raschdorf F, Peter HH. Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin. DRAMP00059 CANSCSYGPLTWSCDGNTK 19 Lantibiotic duramycin C (Bacteriocin) P36503 Belongs to the type B lantibiotic family (Class I bacteriocin) Not found Streptomyces griseoluteus R2107 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Rich Not found "Function: Acts as inhibitor of phospholipase A2. PTM: Methyllanthionine rings between residues 1 and 18 as well as between residues 5 and 11; a lanthionine occurs between Cys14 and residue 4. In addition, addition of Lys19 to dehydralanine at position 6 forms a lysinoalanine bridge. The Asp residue at position 15 is hydroxylated." Bacillus No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet phosphatidylethanolamine 2125590##8375380 J Antibiot (Tokyo). 1990 Nov;43(11):1403-1412.##Eur J Biochem. 1993 Sep 1;216(2):419-428. Fredenhagen A, Fendrich G, Märki F, Märki W, Gruner J, Raschdorf F, Peter HH. Zimmermann N, Freund S, Fredenhagen A, Jung G. Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A3. Structural revision of duramycin and cinnamycin.Solution structures of the lantibiotics duramycin B and C. DRAMP00060 CRQSCSFGPFTFVCDGNTK 19 Bacteriocin cinnamycin (Lanthiopeptin Ro 09-0198) P29827 Belongs to the type B lantibiotic family (Class I bacteriocin) cinA Streptomyces cinnamoneus cinnamoneus DSM 40005 (Gram-positive bacteria) Antimicrobial, Antbacterial, Antiviral Protein level Beta strand (2 strands; 2 residues) The peptide has a hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanolamine head group would be unable to fit the pocket. 2DDE resolved by NMR. "Function: Can act as inhibitor of the enzyme phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. Its antimicrobial activities are not very pronounced. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor." Bacillus, herpes simplex virus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet phosphatidylethanolamine 2125590##2544544##8882709 J Antibiot (Tokyo). 1990 Nov;43(11):1403-1412.##J Antibiot (Tokyo). 1989 Jun;42(6):837-845.##J Biochem. 1996 Feb;119(2):226-230. Fredenhagen A, Fendrich G, Märki F, Märki W, Gruner J, Raschdorf F, Peter HH.##Naruse N, Tenmyo O, Tomita K, Konishi M, Miyaki T, Kawaguchi H, Fukase K, Wakamiya T, Shiba T.##Hosoda K, Ohya M, Kohno T, Maeda T, Endo S, Wakamatsu K. Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin.##Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin.##Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1. DRAMP00061 ASGWVCTLTIECGTVICAC 19 Actagardine (Gardimycin; Bacteriocin) P56650 Belongs to the type B lantibiotic family (Class I bacteriocin) Not found Actinoplanes liguriae (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Non helix or strand structure Actagardine shows a rigid compact globular shape based on the constraining bridging pattern, which is composed of an N-terminal lanthionine ring from residues 1-6 and three intertwined C-terminal methyllanthionine rings comprising residues 7-12, 9-17 and 14-19. In addition, this C-terminal ring system is stabilised by a short antiparallel beta sheet. A feature of the actagardine structure is the presence of two putative binding pockets. 1AJ1 resolved by NMR. "Function: The molecule has a compact shape. Like mersacidin, this peptide inhibits cell wall biosynthesis by binding to lipid II. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 14-19 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor." Gram-positive bacteria: streptococci, Streptococcus pyogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 2211371##9219543 J Antibiot (Tokyo). 1990 Sep;43(9):1082-1088.##Eur J Biochem. 1997 Jun 15;246(3):809-819. Kettenring JK, Malabarba A, V©key K, Cavalleri B.##Zimmermann N, Jung G. Sequence determination of actagardine, a novel lantibiotic, by homonuclear 2D NMR spectroscopy.##The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR. DRAMP00062 CTFTLPGGGGVCTLTSECIC 20 Mersacidin (Bacteriocin; Preclinical) P43683 Belongs to the type B lantibiotic family (Class I bacteriocin) mrsA Bacillus sp. HIL-Y85/54728 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Non helix or strand structure (Turn) Not found 1QOW resolved by NMR. "Function: Kills a number of Gram-positive bacteria. Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. May interact with the peptidoglycan precursor rather than with the enzyme. PTM: There are one dihydroalanine (Dha): S16; three Beta-methyllanthionines: C1-T2, T4-C12, T13-C18; and S-(2-aminovinyl)-3-methyl-D-cysteine: T15-C20." Gram-positive bacteria: Methicillin-resistant Staphylococcus aureus, Vancomycin-resistant Enterococcus, Clostridium difficile. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet The sugar phosphate head group of the peptidoglycan precursorLipid II 7737474##9119018##10831439##10818347 FEMS Microbiol Lett. 1995 Mar 15;127(1-2):121-126.##Eur J Biochem. 1997 Mar 1;244(2):501-512.##Appl Environ Microbiol. 2000 Jun;66(6):2565-2571.##Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):705-713. Bierbaum G, Brötz H, Koller KP, Sahl HG.##Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler H, Griesinger C.##Altena K, Guder A, Cramer C, Bierbaum G.##Schneider TR, Kärcher J, Pohl E, Lubini P, Sheldrick GM. Cloning, sequencing and production of the lantibiotic mersacidin.##Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.##Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster.##Ab initio structure determination of the lantibiotic mersacidin. DRAMP00064 MSKRDCNLMKACCAGQAVTYAIHSLLNRLGGDSSDPAGCNDIVRKYCK 48 Enterocin 96 (Bacteriocin) Q82YI9 Belongs to the class II bacteriocin Not found Enterococcus faecalis (strain ATCC 700802 / V583) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found Search in protein databases revealed that enterocin 96 was identical to the C-terminal part of a putative uncharacterized protein from Enterococcus faecalis V583 (accession number EF_B0056) identified after complete genome sequencing of this strain. The amino acid sequence of this protein contains an N-terminal extension of 26 amino acids with two C-terminal 1 glycyl residues. The likely presence of such an extension for enterocin 96 was investigated by sequencing its structural gene. Gram-positive bacteria: Enterococcus faecalis, E. faecium WHE, E. hirae, E. pseudoavium, E. sulfureus, E. saccharolyticus, E. columbae, Lactobacillus plantarum, L. acidophilus, Lactobacillus sakeii subsp. sakei, L. paracasei subsp. paracasei, Lactococcus lactis, Lactococcus lactis subsp. cremoris, Leuconostoc mesenteroides, Bacillus subtilis, Bacillus cereus, Listeria innocua, Listeria monocytogenes, Staphylococcus xylosus, Staphylococcus aureus;##Gram-negative bacteria: Salmonella enterica serovar Typhimurium, S. enterica serovar Infantis, Klebsiella pneumoniae, Serratia liquefaciens, Proteus vulgaris, Enterobacter cloacae, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12663927 Science. 2003 Mar 28;299(5615):2071-2074. Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM. Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. DRAMP00065 KKKKKKVACTWGNAATAAASGAVXGILGGPTGALAGAIWGVSQCASNNLHGMH 53 Plantaricin 1.25 beta (thermostable Bacteriocin) Q9ZEU9 Belongs to the class II bacteriocin plnB Lactobacillus plantarum TMW1.25 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Lactobacillus plantarum TMW1.25 produces two bacteriocins plantaricin 1.25a and plantaricin 1.25b. Plantarum, Plantarum sp, Plantarum coryniformis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10684981 Biochim Biophys Acta. 2000 Feb 29;1490(3):355-361. Ehrmann MA, Remiger A, Eijsink VG, Vogel RF. A gene cluster encoding plantaricin 1.25beta and other bacteriocin-like peptides in Lactobacillus plantarum TMW1.25. DRAMP00066 AGFLKVVQLLAKYGSKAVQWAWANKGKILDWLNAGQAIDWVVSKIKQILGIK 52 Lacticin Q (Bacteriocin) A4UVR2 Belongs to the class II bacteriocin lnqQ Lactococcus lactis QU 5 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found 2N8P##7P5R Lacticin Q was very stable against heat treatment and changes in pH; in particular, it was stable at alkaline pH values, while nisin A was inactivated. Moreover, lacticin Q induced ATP efflux from a Listeria sp. strain in a shorter time and at a lower concentration than nisin A, indicating that the former affected indicator cells in a different manner from that of the latter. Gram-positive bacteria: Bacillus cereus JCM 2152, Bacillus circulans JCM 2504, Bacillus coagulans JCM 2257, Bacillus subtilis JCM 1465, Enterococcus faecalis JCM 5803, Enterococcus faecium JCM 5804, Enterococcus mundtii QU 2, Enterococcus hirae ATCC 10541, Lactococcus lactis ATCC 19435, Lactococcus lactis NCDO 497, Lactobacillus acidophilus JCM 1132, Lactobacillus alimentarius JCM 1095, Lactobacillus brevis JCM 1059, Lactobacillus casei JCM 1134, Lactobacillus coryniformis JCM 1164, Lactobacillus sakeii JCM 1157, Leuconostoc mesenteroides JCM 6124, Listeria innocua ATCC 33090, Micrococcus luteus IFO 12708, Pediococcus pentosaceus JCM 5885. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17351096 Appl Environ Microbiol. 2007 May;73(9):2871-2877. Fujita K, Ichimasa S, Zendo T, Koga S, Yoneyama F, Nakayama J, Sonomoto K. Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria. DRAMP00067 KNYGNGVHCTKKGCSVDWGYAATNIANNSVMNGLTG 36 Leucocin C-TA33a (Bacteriocin) No entry found Belongs to the class II bacteriocin Not found Leuconostoc mesenteroides TA33a (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9611809 Microbiology. 1998 May;144 (Pt 5):1343-1348. Papathanasopoulos MA, Dykes GA, Revol-Junelles AM, Delfour A, von Holy A, Hastings JW. Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a. DRAMP00070 ACQCPDAISGWTHTDYQCHGLENKMYRHVYAICMNGTQVYCRTEWGSSC 49 Laterosporulin (Bacteriocin) No entry found Belongs to the class II bacteriocin Not found Brevibacillus sp. Strain GI-9 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found 4OZK The bacteriocin was produced after 12 hours in the lag phase and the use of Diaion HP-20 hydrophobic resin increased yield. Partial sequence was determined and the entire sequence was deduced. This peptide is thermal stable, pH tolerant, and resistant to proteases. Reducing agent DTT had no effect on peptide activity or migration on gel. Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus, Listeria monocytogenesa;##Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22403615 PLoS One. 2012;7(3):e31498. Singh PK, Chittpurna, Ashish, Sharma V, Patil PB, Korpole S. Identification, Purification and Characterization of Laterosporulin, a Novel Bacteriocin Produced by Brevibacillus sp. Strain GI-9. DRAMP00071 KTVNYGNGLYCNQKKCWVNWSETATTIVNNSIMNGLTGGNAGWHSGGRA 49 Ubericin-A (Bacteriocin) A9Q0M7 Belongs to the class IIa bacteriocin ubaA Streptococcus uberis (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Heat-stable antibiotic Gram-positive bacteria: Listeria spp., Enterococcus hirae, Enterococcus faecalis ATCC 19433, Streptococcus bovis 83, Streptococcus uberis 42 and Lactococcus lactis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17933926 Appl Environ Microbiol. 2007 Dec;73(23):7763-7766. Heng NC, Burtenshaw GA, Jack RW, Tagg JR. Ubericin A, a class IIa bacteriocin produced by Streptococcus uberis. DRAMP00072 AYPGNGVHCGKYSCTVDKQTAIGNIGNNAA 30 Bacteriocin curvaticin P84886 Belongs to the class IIa bacteriocin Not found Lactobacillus curvatus L442 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity. PTM: Problely contains one disulfide bond 9-14. Biophysicochemical properties: pH dependence (Stable below pH 6) and Temperature dependence (Stable below 60 degrees Celsius. Activity decreases sharply at temperatures above 60 degrees Celsius)." Gram-positive bacteria: Listeria monocytogenes, Lactobacillus sakeii, Lactobacillus plantarum, Lactobacillus farciminis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16244793 Antonie Van Leeuwenhoek. 2006 Jan;89(1):19-26. Xiraphi N, Georgalaki M, Driessche GV, Devreese B, Beeumen JV, Tsakalidou E, Metaxopoulos J, Drosinos EH. Purification and characterization of curvaticin L442, a bacteriocin produced by Lactobacillus curvatus L442. DRAMP00073 KNYGNGVYCNKHKCSVDWATFSANIANNSVAMAGLTGGNAGNK 43 Weissellin-A (Bacteriocin) B3A0N4 Belongs to the class IIa bacteriocin Not found Weissella paramesenteroides DX (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: The mode of action appears to be non-lytic. Inactivated by proteinase K, but insensitive to trypsin, alpha-chymotrypsin, pepsin and papain. Biophysicochemical properties: pH dependence (Remains active between pH 2 and 10); Temperature dependence (Remains active after incubation at 121 degrees Celsius for 1 hour). PTM: Contains one disulfide bond 9-14. " Gram-positive bacteria: Myotis flavus strain ATCC 400, Micrococcus luteus strain CECT241, C. soprogenes strain NCTC533, Listeria monocytogenes strain ATCC 19111, L.inocua strain ATCC BAA-680D and Staphylococcus carnosus strain LMG13564 (+++); Bacillus cereus strain LMG13569, C. thiaminolyticum strain ATCC 15579, Enterococcus faecalis strain NCTC8176, Lactococcus lactis strain LM0230, Lactobacillus casei strain ATCC 344, Lactococcus lactis strain IL1403, L. jensenii strain ATCC 25258, Lactobacillus plantarum strain CECT220, L. brevis strain ATCC 8287, L. bulgaricus strain LMG13551, Pediococcus acidilactici strain ATCC 25740, P. pentosaceus strain ATCC 33316 and P. pentosaceus strain LMG13560 (+). Leuconostoc mesenteroides strain ATCC 19254, Lactococcus lactis strain ATCC 1454, L. sakei strain CECT906T, Lactococcus lactis subsp. cremoris strain MC1363 and L. curvatus strain ATCC 51436 (++). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21511463 Bioresour Technol. 2011 Jun;102(12):6730-6734. Papagianni M, Papamichael EM. Purification, amino acid sequence and characterization of the class IIa bacteriocin weissellin A, produced by Weissella paramesenteroides DX. DRAMP00075 ATRSYGNGVYCNNSKCWNVGEAKENIAGIVISGKASGL 38 Enterocin M (Bacteriocin) P85876 Belongs to the class IIa bacteriocin Not found Enterococcus faecium AL 41 (Streptococcus faecium) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Bacteriocin that inhibits the growth of closely related Enterococcus species and a wide range of Gram-positive bacterial species. Inhibits the growth of several strains of the Gram-negative bacterium E.coli, but not the growth of Gram-negative Pseudomonas species. Biophysicochemical properties: pH dependence (Stable at pH 5.0); Temperature dependence (Thermostable, retains activity after heating at 60, 80 and 100 degrees Celsius for 1 hour. Long-term storage at 4 degrees Celsius or -20 degrees Celsius does not affect activity). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17551760 J Ind Microbiol Biotechnol. 2007 Aug;34(8):533-537. Marekov¡ M, Laukov¡ A, Skaugen M, Nes I. Isolation and characterization of a new bacteriocin, termed enterocin M, produced by environmental isolate Enterococcus faecium AL41. DRAMP00076 KYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWSK 43 Mundticin ATO6 (Bacteriocin) P80925 Belongs to the class IIa bacteriocin Not found Enterococcus mundtii ATO6 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: This bacteriocin inhibits the growth of a wide range of Gram-positive bacteria at nanomolar concentrations, especially pathogenic L. monocytogenes and C. botulinum but has no effect on the growth of a number of yeasts and Gram-negative bacteria. Biophysicochemical properties: pH dependence (Stable from pH 1 to 10); Temperature dependence (Thermostable; Retains 100% of its maximal activity after heating at 100 degrees Celsius for 15 min, but only 50% of activity after heating 1 hour at this same temperature)." Gram-positive bacteria: Listeria monocytogenes, Lactobacillus salivarius, L. sake, Leuconostoc paramesenteroides, Leuconostoc mesenteroides, Carnobacterium piscicola, Pediococcus dextrinicus, P. pentosaseus, Enterococcus faecalis, E. hirae, Listeria inocua, Clostridium botulinum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9733915 Biochim Biiophys Acta 1998; 1373: 47-58. Bennik MHJ et al Smid EJ. A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: full characterization and interaction with target organisms. DRAMP00077 KYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWKS 43 Mundticin KS (Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Enterococcus mundtii NFRI 7393 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found "Function: Mundticin KS is active against closely related lactic acid bacteria and the food-borne pathogen Listeria monocytogenes. Sequence similarity: Mundticin KS comprises a 43-amino-acid peptide with an amino acid sequence similar to that of mundticin ATO6 produced by E. mundtii ATO6. Mundticin KS and mundticin ATO6 are distinguished by the inversion of the last two amino acids at their respective C termini." Gram-positive bacteria: Enterococcus faecium IFO13712 (+++), Enterococcus faecalis IFO12964 (+++), Enterococcus mundtii JCM 8731 (+++), Lactobacillus plantarum ATCC 8041 (+), Lactobacillus lactis NFRI 7307 (+), Lactobacillus curvatus JCM 1096 (+), Listeria monocytogenes ATCC 15313 and ATCC 49594 (++).##Note: Symbols: +, sensitive to mundticin KS (+, ++, and +++ reflect the degree of sensitivity). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12147478 Appl Environ Microbiol. 2002 Aug;68(8):3830-3840. Kawamoto S, Shima J, Sato R, Eguchi T, Ohmomo S, Shibato J, Horikoshi N, Takeshita K, Sameshima T. Biochemical and genetic characterization of munddticin KS, an antilisterial peptide produced by Enterococcus mundtii NFRI 7397. DRAMP00078 KNYGNGVHCTKKGCSVDWGYAWTNIANNSVMNGLTGGNAGWHN 43 Leucocin C (Leu C; Pediocin-like peptide; Bacteriocin) P81053 Belongs to the class IIa bacteriocin Not found Leuconostoc mesenteroides (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Inhibits a wide spectrum of lactic acid bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12127968##9611809 Biochem Biophys Res Commun. 2002 Jul 26;295(4):826-827.##Microbiology. 1998 May;144 (Pt 5):1343-1348. Fimland G, Sletten K, Nissen-Meyer J.##Papathanasopoulos MA, Dykes GA, Revol-Junelles AM, Delfour A, von Holy A, Hastings JW. The complete amino acid sequence of the pediocin-like antimicrobial peptide leucocin C.##Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a. DRAMP00079 ATYYGNGLYCNKEKCWVDWNQAKGEIGKIIVNGWVNHGPWAPRR 44 Bacteriocin hiracin-JM79 (HirJM79; Bacteriocin) Q0Z8B6 Belongs to the class IIa bacteriocin hirJM79 Enterococcus hirae DCH5 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has antibacterial activity. Lacks antibacterial activity against Gram-negative bacteria. Gram-positive bacteria: Lactobacillus helveticus, Lactobacillus curvatus, Lactobacillus bulgaricus, Lactobacillus sakeii, Pediococcus pentosaceus, Enterococcus faecium, Enterococcus faecalis, Propionibacterium sp, Propionibacterium acidipropionici, Clostridium tyrobutiricum, Listeria monocytogenes, Listeria ivanovii, Listeria seeligeri, Listeria welshimeri, Listeria grayi, Staphylococcus aureus, Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17326750 FEMS Microbiol Lett. 2007 May;270(2):227-236. S¡nchez J, Diep DB, Herranz C, Nes IF, Cintas LM, Hern¡ndez PE. Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hiracin JM79, a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos). DRAMP00080 ARSYGNGVYCNNKKCWVNRGEATQSIIGGMISGWASGLAGM 41 Curvacin A (Bacteriocin) P0A311, P35619, P80097 Belongs to the class IIa bacteriocin curA Lactobacillus curvatus LTH1174 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (2 helices; 17 residues) In DPC micelles, the cationic and hydrophilic N-terminal half of the peptide forms an S-shaped beta-sheet-like domain stabilized by a disulfide bridge and a few hydrogen bonds. This domain is followed by a helix-hinge-helix motif: a hydrophilic 6-mer helix (residues 19-24) and an amphiphilic/hydrophobic 11-mer helix (residues 29-39). 2A2B resolved by NMR. PTM: Contains one disulfide bond 10-15. Gram-positive bacteria: Closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7694558##16331975 Arch Microbiol. 1993;160(4):279-283.##Biochemistry. 2005 Dec 13;44(49):16149-16157. Tichaczek PS, Vogel RF, Hammes WP.##Haugen HS, Fimland G, Nissen-Meyer J, Kristiansen PE. Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174.##Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A. DRAMP00081 KYYGNGVHCTKSGCSVNWGEAFSAGVHRLANGGNGFW 37 Leucocin-A (Leucocin A-UAL 187; Leu A; Bacteriocin) P34034 Belongs to the class IIa bacteriocin lcnA Leuconostoc gelidum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure In both TFE and DPC micelle, The region encompassing residues 17-31 assumes an essentially identical amphiphilic alpha-helix conformation. A three-strand antiparallel beta-sheet domain (residues 2-16), anchored by the disulfide bridge. In TFE, these two regions have a more defined relationship relative to each other, while, in DPC micelles, the C-terminus is folded back onto the alpha-helix. 1CW6 resolved by NMR. "Function: Inhibits a wide spectrum of lactic acid bacteria. PTM: Contains one disulfide bond 9-14." Gram-positive bacteria: Lactic acid bacteria, Listeria monocytogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1840587##8418850##9398233 J Bacteriol. 1991 Dec;173(23):7491-7500.##Biochemistry. 1993 Jan 12;32(1):310-318.##Biochemistry. 1997 Dec 9;36(49):15062-15072. Hastings JW, Sailer M, Johnson K, Roy KL, Vederas JC, Stiles ME.##Sailer M, Helms GL, Henkel T, Niemczura WP, Stiles ME, Vederas JC.####Fregeau Gallagher NL, Sailer M, Niemczura WP, Nakashima TT, Stiles ME, Vederas JC. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum.##15N- and 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis.##Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid DRAMP00082 TKYYGNGVYCNSKKCWVDWGQAAGGIGQTVVXGWLGGAIPGK 42 Bavaricin-MN (Bacteriocin) P80493 Belongs to the class IIa bacteriocin Not found Lactobacillus sakeii (Gram-positive bacteria) Antimicrobial, Anti-Gram+ Protein level Not found Not found PTM: contains one disulfide bond 10-15. Gram-positive bacterium: Listeria monocytogenes Scott A. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8953724 Appl Environ Microbiol. 1996 Dec;62(12):4529-4535. Kaiser AL, Montville TJ. Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles. DRAMP00083 KYYGNGVHXGKHSXTVDWGTAIGNIGNNAAANXATGXNAGG 41 Bavaricin-A (Bacteriocin) P80953 Belongs to the class IIa bacteriocin Not found Lactobacillus sakeii (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Lactobacillus, Listeria monocytogenes, Pediococcus, Enterococcus, Leuconostoc, Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8407671 J Appl Bacteriol. 1993 Aug;75(2):113-122. Larsen AG, Vogensen FK, Josephsen J. Antimicrobial activity of lactic acid bacteria isolated from sour doughs: purification and characterization of bavaricin A, a bacteriocin produced by Lactobacillus bavaricus MI401. DRAMP00084 KYYGNGVTCGKHSXSVDWXKXT 22 Mutacin F-59.1 (Bacteriocin) P86386 Belongs to the class IIa bacteriocin Not found Streptococcus mutans (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2009) to UniProtKB Nicolas GG, Lavoie MC, Lapointe G, Mota-Meira M. Characterization of mutacin F-59.1, a pediocin-like bacteriocin produced by Streptococcus mutans 59.1. DRAMP00085 TSYGNGVHCNKSKCWIDVSELETYKAGTVSNPKDILWSLKE 41 Bacteriocin P86291 Belongs to the class IIa bacteriocin Not found Lactococcus sp Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has bacteriocin active. Gram-positive bacteria: Streptococcus aureus, Bacillus thuringiensis;##Gram-negative bacteria: Salmonella typhi, Klebsiella sp., Escherichia coli KL16 and Escherichia coli Gj137. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2009) to UniProtKB Ingale A.G. Molecular characterisation of bacteriocin from microflora associated with radish and ginger. DRAMP00086 TKYYGNGVYCNSKKCWVDWGTAQGCIDVVIGQLGGGIPGKGKC 43 Divergicin M35 (Pediocin-like peptide; Bacteriocin) P84962 Belongs to the class IIa bacteriocin Not found Carnobacterium divergens M35 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Bacteriocin with antibacterial activity against Gram-positive bacteria. Biophysicochemical properties: Displays a high degree of stability when incubated at temperatures of up to 121 degrees Celsius for 60 minutes. Biotechnological use: Has potential for use as a biopreservative for inhibiting Listeria monocytogenes in seafood products that do not usually undergo an adequate heat treatment." Gram-positive bacteria: Many strains of Listeria monocytogenes, L. seeligeri, L. welshimeri, L. grayi, L. murayi, L. ivanovii, L. innocus, Ceanothus divergens and Carnobacterium piscicola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15541799 Int J Food Microbiol. 2004 Dec 15;97(2):123-136. Tahiri I, Desbiens M, Benech R, Kheadr E, Lacroix C, Thibault S, Ouellet D, Fliss I. Purification, characterization and amino acid sequencing of divergicin M35: a novel class IIa bacteriocin produced by Carnobacterium divergens M35. DRAMP18344 CLGIGSCNNFAGCGYAVVCFW 21 Tricyclic peptide RP 71955 (Bacteriocin) P37046 Belongs to the class I bacteriocin Not found Streptomyces sp. (strain SP9440) Antiviral, Anti-HIV, Antimicrobial Beta strand An internal amide bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well as two disulfide bridges, one between C1 and C13 and one between C7 and C19. In contrast. Class 2 lassos do not have disulfide bonds. 1RPB, 1RPC resolved by NMR Caution:The isopeptide linked residue 9 is shown as Asn rather than Asp as mentioned in PubMed:8286361, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible.(From Swiss-prot) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8270499 J Antibiot (Tokyo). 1993 Nov;46(11):1756-7. Helynck G, Dubertret C, Mayaux JF, Leboul J. Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite. DRAMP00088 KYYGNGVSCNKKGCSVDWGKAIGIIGNNAAANLTTGGKAAWAC 43 Enterocin-HF (Bacteriocin) P86183 Belongs to the class IIa bacteriocin Not found Enterococcus faecium (Streptococcus faecium) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Bacteriocin. PTM: Contains one disulfide bond 9-14." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JAN-2009) to UniProtKB. Almeida T, Brandao A, Campanero C, Igrejas G, Torres C, Herandez P.E, Poeta P, Cintas L.M, Herranz C. Amino acid sequence of Enterocin-HF, a new pediocin-like bacteriocin produced by E. faecium HS and E. faecium TA29 isolated from humans and fish (thin-lipped grey mullet; Liza ramada) in Portugal. DRAMP00091 AISYGNGVYCNKEKCWVNKAENKQAITGIVIGGWASSLAGMGH 43 Carnobacteriocin BM1 (Carnobacteriocin B1; Bacteriocin) P38579 Belongs to the class IIa bacteriocin cbnBM1 Carnobacterium piscicola LV17B (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Has antibacterial activity. PTM: Probablely contains one disulfide bond 10-15." Listeria and Enterococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163526 J Biol Chem 1994; 269: 12204-12211. Quadri LE et al Stiles ME Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B DRAMP00092 ATYYGNGLYCNKQKHYTWVDWNKASREIGKIIVNGWVQH 39 Bacteriocin SRCAM 602 (Preclinical) P86393 Belongs to the class IIa bacteriocin Not found Paenibacillus polymyxa (Bacillus polymyxa) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Bacteriocin with antibacterial activity. Miscellaneous: Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. Biophysicochemical properties: pH dependence (Stable from pH 3.0-9.0, inactivated at pH 10.0); Temperature dependence (Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes)." Gram-positive bacteria: Clostridium jejuni. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15690798 J Food Prot. 2005 Jan;68(1):11-17. Svetoch EA, Stern NJ, Eruslanov BV, Kovalev YN, Volodina LI, Perelygin VV, Mitsevich EV, Mitsevich IP, Pokhilenko VD, Borzenkov VN, Levchuk VP, Svetoch OE, Kudriavtseva TY. Isolation of Bacillus circulans and Paenibacillus polymyxa strains inhibitory to Campylobacter jejuni and characterization of associated bacteriocins. DRAMP00093 FVYGNGVTSILVQAQFLVNGQRRFFYTPDK 30 Bacteriocin SRCAM 37 P86395 Belongs to the class IIa bacteriocin Not found Paenibacillus polymyxa (Bacillus polymyxa) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Bacteriocin with antibacterial activity. Biophysicochemical properties: pH dependence (Stable from pH 3.0-9.0, inactivated at pH 10.0); Temperature dependence (Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes). Miscellaneous: Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. " Gram-positive bacteria: Clostridium jejuni. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15690798##16977842 J Food Prot. 2005 Jan;68(1):11-17.##Poult Sci. 2006 Sep;85(9):1570-1575. Svetoch EA, Stern NJ, Eruslanov BV, Kovalev YN, Volodina LI, Perelygin VV, Mitsevich EV, Mitsevich IP, Pokhilenko VD, Borzenkov VN, Levchuk VP, Svetoch OE, Kudriavtseva TY.##Cole K, Farnell MB, Donoghue AM, Stern NJ, Svetoch EA, Eruslanov BN, Volodina LI, Kovalev YN, Perelygin VV, Mitsevich EV, Mitsevich IP, Levchuk VP, Pokhilenko VD, Borzenkov VN, Svetoch OE, Kudryavtseva TY, Reyes-Herrera I, Blore PJ, Solis de los Santos F, Donoghue DJ. Isolation of Bacillus circulans and Paenibacillus polymyxa strains inhibitory to Campylobacter jejuni and characterization of associated bacteriocins.##Bacteriocins reduce Campylobacter colonization and alter gut morphology in turkey poults. DRAMP00094 VNYGNGVSCSKTKCSVNWGIITHQAFRVTSGVASG 35 Bacteriocin SRCAM 1580 P86394 Belongs to the class IIa bacteriocin Not found Bacillus circulans (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Bacteriocin with antibacterial activity. Biophysicochemical properties: pH dependence (Stable from pH 3.0-9.0, inactivated at pH 10.0); Temperature dependence (Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes). Miscellaneous: Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. " Gram-positive bacteria: Clostridium jejuni. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15690798##16977842 J Food Prot. 2005 Jan;68(1):11-17.##Poult Sci. 2006 Sep;85(9):1570-1575. Svetoch EA, Stern NJ, Eruslanov BV, Kovalev YN, Volodina LI, Perelygin VV, Mitsevich EV, Mitsevich IP, Pokhilenko VD, Borzenkov VN, Levchuk VP, Svetoch OE, Kudriavtseva TY.##Cole K, Farnell MB, Donoghue AM, Stern NJ, Svetoch EA, Eruslanov BN, Volodina LI, Kovalev YN, Perelygin VV, Mitsevich EV, Mitsevich IP, Levchuk VP, Pokhilenko VD, Borzenkov VN, Svetoch OE, Kudryavtseva TY, Reyes-Herrera I, Blore PJ, Solis de los Santos F, Donoghue DJ. Isolation of Bacillus circulans and Paenibacillus polymyxa strains inhibitory to Campylobacter jejuni and characterization of associated bacteriocins.##Bacteriocins reduce Campylobacter colonization and alter gut morphology in turkey poults. DRAMP00095 KYYGNGVHCTKSGCSVNWGEAASAGIHRLANGGNGFW 37 Mesentericin Y105 (MesY105; Bacteriocin) P38577 Belongs to the class IIa bacteriocin mesY Leuconostoc mesenteroides (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has bacteriocin activity. PTM: Probablely contains one disulfide bond 9-14." Lactobacillus, Leuconostoc, Pediococcus, Listeria monocytogenes, Listeria innocua, Listeria ivanovii. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1487737##7551032 J Gen Microbiol. 1992 Dec;138(12):2725-2731.##Microbiology. 1995 Jul;141 (Pt 7):1637-1645. H©chard Y, D©rijard B, Letellier F, Cenatiempo Y.##Fremaux C, H©chard Y, Cenatiempo Y. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides.##Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105. DRAMP00096 KYYGNGVTCGKHSCSVDWGKATTCIINNGAMAWATGGHQGNHKC 44 Pediocin PA-1 (Pediocin ACH; Bacteriocin) P29430, P34912 Belongs to the class IIa bacteriocin pedA Pediococcus acidilactici PAC-1.0 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found "Function: Has bacteriocin activity. PTM: Probablely contains one disulfide bond 9-14." Gram-positive bacteria: Listeria monocytogenes ATCC 19115, L. seeligeri ATCC 35967, Pediococcus pentosaceus JCM2026, P. pentosaceus JCM5890, Pediococcus acidilactici IAM1233, Lactobacillus plantarum JCM1149, Lactobacillus sakei IAM1900. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1514784##1575516 Appl Environ Microbiol. 1992 Aug;58(8):2360-2367.##Arch Biochem Biophys. 1992 May 15;295(1):5-12. Marugg JD, Gonzalez CF, Kunka BS, Ledeboer AM, Pucci MJ, Toonen MY, Walker SA, Zoetmulder LC, Vandenbergh PA.##Henderson JT, Chopko AL, van Wassenaar PD. Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, and bacteriocin from Pediococcus acidilactici PAC1.0.##Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. DRAMP00097 TSYGNGVHCNKSKCWIDVSELETYKAGTVSNPKDILW 37 Lactococcin MMFII (Pediocin-like peptide; Bacteriocin) P83002 Belongs to the class IIa bacteriocin Not found Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Bacteriocin active against Listeria monocytogenes and Lactococcus cremoris. Lactococcus cremoris, Listeria ivanovii. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11728715##11708769 FEMS Microbiol Lett. 2001 Nov 27;205(1):49-55.##Biochem Biophys Res Commun. 2001 Nov 23;289(1):13-18. Ferchichi M, Fr¨re J, Mabrouk K, Manai M.##Ferchichi M, Fathallah M, Mansuelle P, Rochat H, Sabatier JM, Manai M, Mabrouk K. Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product.##Chemical synthesis, molecular modeling, and antimicrobial activity of a novel bacteriocin, MMFII. DRAMP18343 GLPWGCPSDIPGWNTPWAC 19 BI-32169(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces sp. (DSM 14996) Antidiabetic Not found BI-32169 consists exclusively of protein amino acids and is cyclized from the side chain of Asp9 to the N-terminus of Gly1. One disulfide bond between Cys6 and Cys19 forms a bicyclic structure. BI-32169 and its methyl ester derivative (2) showed potent inhibitory activity against the human glucagon receptor (IC50 440 and 320 nM, respectively) in a functional cell-based assay. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15387654 J Nat Prod. 2004 Sep;67(9):1528-31. Potterat O, Wagner K, Gemmecker G, Mack J, Puder C, Vettermann R, Streicher R. BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp. DRAMP00099 KYYGNGLSCNKSGCSVDWSKAISIIGNNAVANLTTGGAAGWKS 43 Sakacin 5X (Sak5X; Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found lactic acid bacteria (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Bridge Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Lactobacillus lactis 105, L. collinoides 110, L. brevis 111, L. brevis 112, Pediococcus damnosus 113, P. damnosus 114, Enterococcus faecalis 109. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11442722 J Appl Microbiol. 2001 Jul;91(1):131-138. Vaughan A, Eijsink VG, O'Sullivan TF, O'Hanlon K, van Sinderen D. An analysis of bacteriocins produced by lactic acid bacteria isolated from malted barley DRAMP00100 KYYGNGVSCNSHGCSVNWGQAWTCGVNHLANGGHGVC 37 Sakacin G (SakG; Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin skgA2 Lactobacillus sakei 2512 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found MOA: The mode of activity against Listeria innocua 2030C and L. ivanovii subsp. ivanovii ATCC 19119 was bactericidal, resulting in cell lysis and enzyme- and DNA-leakage. Gram-positive bacteria: Streptococcus caprinus, S. macedonicus, Listeria innocua, L. sakei, L. ivanovii subsp. ivanovii and Listeria monocytogenes, Lactococcus lactis subsp. Lactis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12450870##20152920 Appl Environ Microbiol 2002; 68: 6416-6420.##Anaerobe. 2011 Feb;17(1):23-31. Simon L, Fremaux C, Cenatiempo Y, Berjeaud JM.##Todorov SD, Rachman C, Fourrier A, Dicks LM, van Reenen CA, Pr©vost H, Dousset X. Sakacin G, a new type of antilisterial bacteriocin.##Characterization of a bacteriocin produced by Lactobacillus sakeii R1333 isolated from smoked salmon. DRAMP00101 KYYGNGVHCGKHSCTVDWGTAIGNIGNNAAANWATGGNAGWNK 43 Sakacin P (Sakacin 674; Pediocin-like peptide; Bacteriocin) P35618, Q57121 Belongs to the class IIa bacteriocin sakP Lactobacillus sakei Lb674 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Structures in TFE and DPC were determined (Uteng M et al 2003 Biochemistry 42: 11417-26). The N-terminal region formed a 3-stranded beta sheet-like structure, while a well defined helical region was found between residues 18-33. The beta-like structure and the helical region are not packed together. 1OG7, 1OHM, 1OHN resolved by NMR. "Function: Has bactericidal activity. PTM: Contains one disulfide bond 9-14." Gram-positive bacteria: Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8138128##14516192 FEMS Microbiol Lett. 1994 Jan 15;115(2-3):143-149.##Biochemistry. 2003 Oct 7;42(39):11417-11426. Holck AL, Axelsson L, H¼hne K, Kröckel L.##Uteng M, Hauge HH, Markwick PR, Fimland G, Mantzilas D, Nissen-Meyer J, Muhle-Goll C. Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sakei Lb674.##Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge. DRAMP00102 KYYGNGVSCNKNGCTVDWSKAIGIIGNNAAANLTTGGAAGWNKG 44 Piscicolin-126 (Pisc126; Bacteriocin) P80569, Q934J2 Belongs to the class IIa bacteriocin pisA Carnobacterium piscicola JG126 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Inhibits the growth of several Gram-positive bacteria, especially the food-borne pathogen Listeria monocytogenes, but has no effect on the growth of a number of yeasts and Gram-negative bacteria. PTM: Contains one disulfide bond 9-14 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702282 Appl Environ Microbiol. 1996 Aug;62(8):2897-2903. Jack RW, Wan J, Gordon J, Harmark K, Davidson BE, Hillier AJ, Wettenhall RE, Hickey MW, Coventry MJ. Characterization of the chemical and antimicrobial properties of piscicolin 126, a bacteriocin produced by Carnobacterium piscicola JG126. DRAMP00103 KTYYGTNGVHCTKNSLWGKVRLKNMKYDQNTTYMGRLQDILLGWATGAFGKTFH 54 Bacteriocin OR-7 (Preclinical) No entry found Belongs to the class IIa bacteriocin Not found Lactobacillus salivarius NRRL B-30514 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found "Function: OR-7 had activity to a gram-negative bacterium. Biophysicochemical properties: Temperature dependence (Remains active after exposure to 90 degrees C for 15 min), pH dependence (Stable from pH 3.0 to 9.1)." Campylobacter jejuni NCTC 11168. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16940109 Antimicrob. Agents Chemother. 2006 50 (9):3111-3116. Stern NJ, Svetoch EA, Eruslanov BV, Perelygin VV, Mitsevich EV, Mitsevich IP, Pokhilenko VD, Levchuk VP, Svetoch OE, Seal BS. Isolation of a Lactobacillus salivarius Strain and Purification of Its Bacteriocin, Which Is Inhibitory to Campylobacter jejuni in the Chicken Gastrointestinal System DRAMP00108 KNYGNGVHCTKKGCSVDWGYAWANIANNSVMNGLTGGNAGWHN 43 Leucocin C (Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Lactococcus lactis MMFI (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12127968 Biochem Biophys Res Commun 2002; 295: 826-827. Fimland G, Sletten K, Nissen-Meyer J. The complete amino acid sequence of the pediocin-like antimicrobial peptide leucocin C. DRAMP00109 KYYGNGLSCSKKGCTVNWGQAFSCGVNRVATAGHGK 36 Plantaricin C19 (Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Lactobacillus plantarum C19 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found MOA: Plantaricin C19 exerts a bacteriostatic action on sensitive cells of Listeria grayi IP 6818 in BHI broth. Gram-positive bacterium: Listeria grayi. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11545225 Int J Food Microbiol. 2001 Aug 15;68(1-2):93-104. Atrih A, Rekhif N, Moir AJ, Lebrihi A, Lefebvre G. Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19. DRAMP00110 KYYGNGVTCGKHSCSVNWGQAFSCSVSHLANFGHGKC 37 Plantaricin 423 (Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin plaA Lactobacillus plantarum 423 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Bridge Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Listeria spp., Staphylococcus spp., Pediococcus spp., Lactobacillus spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12423916##17056693 Int J Food Microbiol. 2003 Feb 25;81(1):29-40.##Appl Environ Microbiol. 2006 Dec;72(12):7644-7651. Van Reenen CA, Chikindas ML, Van Zyl WH, Dicks LM.##Van Reenen CA, Van Zyl WH, Dicks LM. Characterization and heterologous expression of a class IIa bacteriocin, plantaricin 423 from Lactobacillus plantarum 423, in Saccharomyces cerevisiae.##Expression of the immunity protein of plantaricin 423, produced by Lactobacillus plantarum 423, and analysis of the plasmid encoding the bacteriocin.isiae. DRAMP00111 KYYGNGVHCGKKTCYVDWGQATASIGKIIVNGWTQHGPWAHR 42 Penocin A (PenA; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Pediococcus pentosaceus (strain ATCC 25745/183-1w) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Piscicola, Clostridia butyricum, Enterococcus faecium, Enterococcus faecalis, Lactobacillus curvatus, Lactobacillus casei, Lactobacillus sakeii, L. raffinolactis, Leuconostoc mesenteroides, Listeria innocua, Listeria monocytogenes, Pediococcus acidilactici, P. pentosaceus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17030793##16735728 Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15611-15616.##Microbiology. 2006 Jun;152(Pt 6):1649-1659. Makarova K. et al Mills D.##Diep DB, Godager L, Brede D, Nes IF. Comparative genomics of the lactic acid bacteria.##Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745. DRAMP18342 GLPWGCPSDIPGWNTPWAC 19 BI-32169(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Streptomyces sp. (DSM 14996) Unknown Not found Its structure has been established by amino acid analysis, mass spectrometry, and 2D NMR analysis. BI-32169 consists exclusively of protein amino acids and is cyclized from the side chain of Asp9 to the N-terminus of Gly1. One disulfide bond between Cys6 and Cys19 forms a bicyclic structure. BI-32169 showed potent inhibitory activity against the human glucagon receptor (IC50 440 nM) in a functional cell-based assay. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2004391##15387654 Cas Lek Cesk. 1991 Jan 18;130(3):76-8.##J Nat Prod. 2004 Sep;67(9):1528-31. Marel M, Mel "[Pleural exudates in patients with lung cancer. Comparative study]. ##BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp." DRAMP00113 TTHSGKYYGNGVYCTKNKCTVDWAKATTCIAGMSIGGFLGGAIPGKC 47 Enterocin A (EntA; Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Enterococcus faecium (Streptococcus faecium) (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8633865 Appl Environ Microbiol 1996; 62: 1676-1682. erich T et al Nes IF. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. DRAMP00114 KSYGNGVHCNKKKCWVDWGSAISTIGNNSAANWATGGAAGWKS 43 Listeriocin 743A (Pediocin-like peptide; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Listeria innocua 743 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11526003 Appl Environ Microbiol 2001; 67: 4041-4047. Kalmokoff ML, Banerjee SK, Cyr T, Hefford MA, Gleeson T. Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743. DRAMP00116 FTPSVSFSQNGGVVEAAAQRGYIYKKYPKGAKVPNKVKMLVNIRGKQTMRTCYLMSWTASSRTAKYYYYI 70 Bacteriocin 32 (Bac 32; Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Enterococcus faecium (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Enterococcus faecium, E. hirae, E. durans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16569830 Antimicrob Agents Chemother. 2006 Apr;50(4):1202-1212. Inoue T, Tomita H, Ike Y. Bac 32, a novel bacteriocin widely disseminated among clinical isolates of Enterococcus faecium. DRAMP18341 WNDTGKDADGSEY 13 Daptomycin(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Streptomyces roseosporus NRRL11379 Unknown Not found the sequence is a close mimic of the natural counterpart. The natural form is cyclic due to the ester bond between the hydroxyl of T4 and the carboxyl of kynurenine-13 (represented by Y here). The N-terminus is lipidated with n-decanoyl fatty acid chain. Other nonstandard amino acids include ornithine-6 (represented with K), (2S,3R)-3-methyl-glutamic acid-12 (represented with E), and three D-amino acids at positions N2, A8, and S11. In 2003, FDA approved daptomycin as a new peptide antibiotic. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3024560 Antimicrob Agents Chemother. 1986 Oct;30(4):532-5. Eliopoulos GM, Willey S, Reiszner E, Spitzer PG, Caputo G, Moellering RC Jr. In vitro and in vivo activity of LY 146032, a new cyclic lipopeptide antibiotic. DRAMP18340 WNDTGKDADGSEY 13 Daptomycin(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Streptomyces roseosporus NRRL11379 Antimicrobial, Antibacterial, Anti-Gram+ Not found the sequence is a close mimic of the natural counterpart. The natural form is cyclic due to the ester bond between the hydroxyl of T4 and the carboxyl of kynurenine-13 (represented by Y here). The N-terminus is lipidated with n-decanoyl fatty acid chain. Other nonstandard amino acids include ornithine-6 (represented with K), (2S,3R)-3-methyl-glutamic acid-12 (represented with E), and three D-amino acids at positions N2, A8, and S11. In 2003, FDA approved daptomycin as a new peptide antibiotic. Active against various Gram-positive bacteria such as S. aureus. This is another anionic peptide that is distinct from many of the cationic AMPs. Its activity requires the presence of Ca2+ (calcium) that causes the aggregation of the peptide. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3024560 Antimicrob Agents Chemother. 1986 Oct;30(4):532-5. Eliopoulos GM, Willey S, Reiszner E, Spitzer PG, Caputo G, Moellering RC Jr. In vitro and in vivo activity of LY 146032, a new cyclic lipopeptide antibiotic. DRAMP00119 KSYGNGVQCNKKKCWVDWGSAISTIGNNSAANWATGGAAGWKS 43 Listeriocin 743A No entry found Not found Not found Listeria innocua Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Listeria monocytogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11526003 Appl Environ Microbiol. 2001 Sep;67(9):4041-4047. Kalmokoff ML, Banerjee SK, Cyr T, Hefford MA, Gleeson T. Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743. DRAMP00121 ATYYGNGVYCNKQKCWVDWSRARSEIIDRGVKAYVNGFTKVLGGIGGR 48 Enterocin SE-K4 Q8GR39 Not found orf6 Enterococcus faecalis (Streptococcus faecalis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Doi K, Eguchi T, Iwatake A, Shima J, Ohmomo S, Ogata S. High production of enterocin SE-K4 from Enterococcus faecalis strain K-4. DRAMP00122 TYYGNGVSCNKKGCSVDWGKAISIIGNNSAANLATGGAAGWKS 43 Avicin A D2DXK5 Not found avcA Enterococcus avium (Streptococcus avium) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19933345 Appl Environ Microbiol. 2010 Jan;76(2):483-492. Birri DJ, Brede DA, Forberg T, Holo H, Nes IF. Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants. DRAMP00123 TKYYGNGVYCNSKKCWVDWGQASGCIGQTVVGGWLGGAIPGKC 43 Divercin V41 (Bacteriocin) No entry found Not found Not found Carnobacterium divergens V41 Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9802025 Microbiology. 1998 Oct;144 ( Pt 10):2837-2844. Métivier A, Pilet MF, Dousset X, Sorokine O, Anglade P, Zagorec M, Piard JC, Marion D, Cenatiempo Y, Fremaux C. Divercin V41, a new bacteriocin with two disulfide bonds produced by Carnobacterium divergens V41: primary structure and genetic organization. DRAMP00124 KYYGNGVTCGKHSCSVDWGKATTCIINNGAMAWATGGHQGTHKC 44 Coagulin (Bacteriocin) No entry found Not found Not found Bacillus coagulans I-4 Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11097892 Appl Environ Microbiol. 2000 Dec;66(12):5213-5220. Le Marrec C, Hyronimus B, Bressollier P, Verneuil B, Urdaci MC. Biochemical and genetic characterization of coagulin, a new antilisterial bacteriocin in the pediocin family of bacteriocins, produced by Bacillus coagulans I(4). DRAMP00125 KYYGNGVTCGLHDCRVDRGKATCGIINNGGMWGDIG 36 Bifidocin B (Bacteriocin) No entry found Not found Not found Bifidobacterium bifidum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23384878 Biotechnol Adv. 2013 Jul;31(4):482-488. Martinez FA, Balciunas EM, Converti A, Cotter PD, de Souza Oliveira RP. Bacteriocin production by Bifidobacterium spp. A review. DRAMP00130 SIWGDIGQGVGKAAYWVGKAMGNMSDVNQASRINRKKKH 39 Lactococcin Q alpha (Qalpha; Bacteriocin) Q1JV79 Belongs to the class IIb bacteriocin laqA Lactococcus lactis QU 4 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Lactococcus lactis subsp. lactis ATCC 19435 (MIC>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16672481 Appl Environ Microbiol. 2006 May;72(5):3383-3389. Zendo T, Koga S, Shigeri Y, Nakayama J, Sonomoto K. Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4. DRAMP00131 KKWGWLAWVEPAGEFLKGFGKGAIKEGNKDKWKNI 35 Lactococcin Q beta (Qbeta; Bacteriocin) Q1JV78 Belongs to the class IIb bacteriocin laqB Lactococcus lactis QU 4 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Lactococcus lactis subsp. lactis ATCC 19435 (MIC>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16672481 Appl Environ Microbiol. 2006 May;72(5):3383-3389. Zendo T, Koga S, Shigeri Y, Nakayama J, Sonomoto K. Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4. DRAMP00132 GTWDDIGQGIGRVAYWVGKALGNLSDVNQASRINRKKKH 39 Lactococcin G subunit alpha (Galpha; Bacteriocin) P36961 Belongs to the class IIb bacteriocin Not found Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Alpha helix In DPC, LcnG-alpha has an N-terminal alpha-helix (residues 3-21) that contains a GxxxG helix-helix interaction motif (residues 7-11) and a less well defined C-terminal alpha-helix (residues 24-34), and in between (residues 18-22) there is a second somewhat flexible GxxxG-motif. Its structure in TFE was similar. 2JPJ, 2JPL resolved by NMR. "MOA: The N-terminal halves of both the alpha and beta peptides may form amphiphilic alpha-helices, suggesting that the peptides are pore-forming toxins that create cell membrane channels through a ""barrel-stave"" mechanism. Bacteriocin activity requires interaction of alpha and beta peptides in a molar ratio of 7:1 or 8:1 respectively." Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1512201##18187052 J Bacteriol. 1992 Sep;174(17):5686-5692.##Biochim Biophys Acta. 2008 Mar;1784(3):543-554. Nissen-Meyer J, Holo H, H¥varstein LS, Sletten K, Nes IF.##Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides.##Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G. DRAMP00133 KKWGWLAWVDPAYEFIKGFGKGAIKEGNKDKWKNI 35 Lactococcin G subunit beta (Gbeta ; Bacteriocin) P36962 Belongs to the class IIb bacteriocin Not found Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Alpha helix In DPC, LcnG-beta has an N-terminal alpha-helix (residues 6-19). The region from residues 20 to 35, which also contains a flexible GxxxG-motif (residues 18-22), appeared to be fairly unstructured in DPC. 2JPK, 2JPM resolved by NMR. "MOA: The N-terminal halves of both the alpha and beta peptides may form amphiphilic alpha-helices, suggesting that the peptides are pore-forming toxins that create cell membrane channels through a ""barrel-stave"" mechanism. Bacteriocin activity requires interaction of alpha and beta peptides in a molar ratio of 7:1 or 8:1 respectively." Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1512201##18187052 J Bacteriol. 1992 Sep;174(17):5686-5692.##Biochim Biophys Acta. 2008 Mar;1784(3):543-554. Nissen-Meyer J, Holo H, H¥varstein LS, Sletten K, Nes IF.##Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides.##Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G. DRAMP00134 SVPTSVYTLGIKILWSAYKHRKTIEKSFNKGFYH 34 Plantaricin NC8 beta peptide (PLNC8 beta; Bacteriocin) Q84HW1 Belongs to the class IIb bacteriocin plnc8B Lactobacillus plantarum NC8 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12514019##14973042##18819721 Appl Environ Microbiol. 2003 Jan;69(1):383-339.##J Bacteriol. 2004 Mar;186(5):1556-1564.##Int J Food Microbiol. 2008 Dec 10;128(2):390-394. Maldonado A, Ruiz-Barba JL, Jim©nez-D­az R.##Maldonado A, Jim©nez-D­az R, Ruiz-Barba JL.##Navarro L, Rojo-Bezares B, S¡enz Y, D­ez L, Zarazaga M, Ruiz-Larrea F, Torres C. Purification and genetic characterization of plantaricin NC8, a novel coculture-inducible two-peptide bacteriocin from Lactobacillus plantarum NC8.##Induction of plantaricin production in Lactobacillus plantarum NC8 after coculture with specific Gram-positive bacteria: is mediated by an autoinduction mechanism.##Comparative study of the pln locus of the quorum-sensing regulated bacteriocin-producing Lactobacillus plantarum J51 strain. DRAMP00135 LTTKLWSSWGYYLGKKARWNLKHPYVQF 28 Plantaricin NC8 alpha peptide (PLNC8 alpha; Bacteriocin) Q84HW0 Belongs to the class IIb bacteriocin plnc8A Lactobacillus plantarum NC8 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12514019 Appl Environ Microbiol. 2003 Jan;69(1):383-389. Maldonado A, Ruiz-Barba JL, Jim©nez-D­az R. Purification and genetic characterization of plantaricin NC8, a novel coculture-inducible two-peptide bacteriocin from Lactobacillus plantarum NC8. DRAMP00137 KKKKQSWYAAAGDAIVSFGEGFLNAW 26 Plantaricin S beta (Bacteriocin) O32830 Belongs to the class IIb bacteriocin plsB Lactobacillus plantarum LPCO10 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found 6GO0 Although beta alone appeared to retain a trace of inhibitory activity, the complementary action of both the alpha and beta peptides was required for full bacteriocin activity. Enterococcus, Lactobacillus, Lactococcus, Leuconostoc. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8534111##9572965 Appl Environ Microbiol. 1995 Dec;61(12):4459-4463.##Appl. Environ. Microbiol. 1998;64 (5):1871-1877. Jim©nez-D­az R, Ruiz-Barba JL, Cathcart DP, Holo H, Nes IF, Sletten KH, Warner PJ.##Stephens SK, Floriano B, Cathcart DP, Bayley SA, Witt VF, Jim©nez-D­az R, Warner PJ, Ruiz-Barba JL. Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides.##Molecular analysis of the locus responsible for production of plantaricin S, a two-peptide bacteriocin produced by Lactobacillus plantarum LPCO10. DRAMP00138 NPKVAHCASQIGRSTAWGAVSGA 23 Acidocin J1132 alpha peptide (Bacteriocin) Q9R4A0 Belongs to the class IIb bacteriocin Not found Lactobacillus acidophilus JCM 1132 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Comment: Acidocin J1132 is a pore-forming bacteriocin that creates cell membrane channels through the ""barrel-stave"" mechanism. Both alpha and beta had inhibitory activity, and an increase in activity by the complementary action of the two components was observed." Lactobacillus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8975617 Appl Environ Microbiol. 1996 Mar;62(3):892-897. Tahara T, Oshimura M, Umezawa C, Kanatani K. Isolation, partial characterization, and mode of action of Acidocin J1132, a two-component bacteriocin produced by Lactobacillus acidophilus JCM 1132. DRAMP00139 GNPKVAHCASQIGRSTAWGAVSGA 24 Acidocin J1132 beta peptide (Bacteriocin) Q9R499 Belongs to the class IIb bacteriocin Not found Lactobacillus acidophilus JCM 1132 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Comment: Acidocin J1132 is a pore-forming bacteriocin that creates cell membrane channels through the ""barrel-stave"" mechanism. Both alpha and beta had inhibitory activity, and an increase in activity by the complementary action of the two components was observed." Lactobacillus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8975617 Appl Environ Microbiol. 1996 Mar;62(3):892-897. Tahara T, Oshimura M, Umezawa C, Kanatani K. Isolation, partial characterization, and mode of action of Acidocin J1132, a two-component bacteriocin produced by Lactobacillus acidophilus JCM 1132. DRAMP00140 RNNWQTNVGGAVGSAMIGATVGGTICGPACAVAGAHYLPILWTAVTAATGGFGKIRK 57 Lactacin-F subunit LafA (Bacteriocin) P24022 Belongs to the class IIb bacteriocin lafA Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Heat stable bacteriocin. peptides for activity: lafA and lafX. Associated with a 180 kDa bacteriocin complex. Enterococcus faecalis and other Lactobacilli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1903624##14983040 Appl Environ Microbiol. 1991 Jan;57(1):114-121.##Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2512-2517. Fremaux C, Ahn C, Klaenhammer TR.##Pridmore RD, Berger B, Desiere F, Vilanova D, Barretto C, Pittet AC, Zwahlen MC, Rouvet M, Altermann E, Barrangou R, Mollet B, Mercenier A, Klaenhammer T, Arigoni F, Schell MA. Purification and partial characterization of lactacin F, a bacteriocin produced by Lactobacillus acidophilus 11088.##The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533. DRAMP00141 NRWGDTVLSAASGAGTGIKACKSFGPWGMAICGVGGAAIGGYFGYTHN 48 Lactacin-F subunit LafX (Bacteriocin) Q48509 Belongs to the class IIb bacteriocin lafX Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) (Gram-positive bacteria) Antimicrobial, Antibacterial Homology Not found Not found Heat stable bacteriocin. peptides for activity: lafA and lafX. Associated with a 180 kDa bacteriocin complex. Enterococcus faecalis and other Lactobacilli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8285694##14983040 Appl Environ Microbiol. 1993 Nov;59(11):3906-3915.##Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2512-2517. Fremaux C, Ahn C, Klaenhammer TR.##Pridmore RD, Berger B, Desiere F, Vilanova D, Barretto C, Pittet AC, Zwahlen MC, Rouvet M, Altermann E, Barrangou R, Mollet B, Mercenier A, Klaenhammer T, Arigoni F, Schell MA. Molecular analysis of the lactacin F operon.##The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533. DRAMP00142 RNNWAANIGGVGGATVAGWALGNAVCGPACGFVGAHYVPIAWAGVTAATGGFGKIRK 57 Gassericin T (gassericin K7 B; Bacteriocin) Q9XDR7 Belongs to the class IIb bacteriocin gatA Lactobacillus gasseri LA158 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11129595 Biosci Biotechnol Biochem. 2000 Oct;64(10):2201-2208.##DNA Sequence and HPLC Purification of Gassericin T, a Class IIb Bacteriocin Produced by Lactobacillus gasseri LA158, from Cheese Whey-based Medium. Kawai Y, Saitoh B, Takahashi O, Kitazawa H, Saito T, Nakajima H, Itoh T.##Yasuta N, Chujo T, Nakamura K, Arakawa K, Kawai Y, Ito Y, Ishikawa J, Itoh M, Sakai A, Nishimura J, Makino Y, Shigenobu S, Kitazawa H, Saito T. Primary amino acid and DNA sequences of gassericin T, a lactacin F-family bacteriocin produced by Lactobacillus gasseri SBT2055.##Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. DRAMP00143 KSSAYSLQMGATAIKQVKKLFKKWGW 26 Plantaricin-A (PlnA; Bacteriocin) P80214, F9UU02 Belongs to the class IIb bacteriocin plnA Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Alpha helix Active plantaricin A is composed of an alpha chain and a beta chain. The sequence of alpha chain and beta chain, however, are essential identical with the only difference being one additional Ala at the N-terminus of chain b. The 3D structure of chain a in DPC micelles has been determined by NMR spectroscopy (J Biol Chem. 2005 Jun 17;280(24):22945-50). 1YTR resolved by NMR. "Function: This heat stable bacteriocin inhibits the growth of closely related Lactobacillus species. It may act as a pore-forming protein, creating a channel in the cell membrane through a ""barrel stave"" mechanism. Antibacterial activity requires both chain a (PlnA) and chain b (PlnB). The sequence of chain a and chain b, however, are essential identical with the only difference being one additional Ala at the N-terminus of chain b. Subunit structure: Active plantaricin A is composed of an alpha chain and a beta chain. Miscellaneous: The beta chain sequence is shown." Closely related Lactobacillus No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8245827 J Gen Microbiol. 1993 Sep;139(9):1973-1978. Nissen-Meyer J, Larsen AG, Sletten K, Daeschel M, Nes IF. Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides. DRAMP00144 NRWTNAYSAALGCAVPGVKYGKKLGGVWGAVIGGVGGAAVCGLAGYVRKG 50 Amylovorin-L (Lactobin-A; Amylovorin-L471; Bacteriocin) P80696 Belongs to the class IIb bacteriocin amyL Lactobacillus amylovorus (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: This heat stable bacteriocin inhibits the growth of closely related Lactobacillus species. It may act as a pore-forming protein, creating a channel in the cell membrane. Subunit structure: Active lactobin is composed of two different peptides, one which is lactobin A. Regions: Contains a transmembrane helix region." Lactobacillus helveticus ATCC 15009. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10517609##14672834##8979334 Microbiology. 1999 Sep;145 (Pt 9):2559-2568.##Int J Food Microbiol. 2004 Jan 1;90(1):93-106.##Appl Environ Microbiol. 1997 Jan;63(1):13-20. Callewaert R, Holo H, Devreese B, Van Beeumen J, Nes I, De Vuyst L.##De Vuyst L, Avonts L, Neysens P, Hoste B, Vancanneyt M, Swings J, Callewaert R.##Contreras BG, De Vuyst L, Devreese B, Busanyova K, Raymaeckers J, Bosman F, Sablon E, Vandamme EJ. Characterization and production of amylovorin L471, a bacteriocin purified from Lactobacillus amylovorus DCE 471 by a novel three-step method.##The lactobin A and amylovorin L471 encoding genes are identical, and their distribution seems to be restricted to the species Lactobacillus amylovorus that is of interest for cereal fermentations.##Isolation, purification, and amino acid sequence of lactobin A, one of the two bacteriocins produced by Lactobacillus amylovorus LMG P-13139. DRAMP00145 GMSGYIQGIPDFLKGYLHGISAANKHKKGRL 31 Lactocin-705 (Bacteriocin) P80959 Belongs to the class IIb bacteriocin Not found Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Potentially useful to control food-borne pathogens in ground meat. several lactic acid bacteria, Listeria, Streptococci, etc. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8796440 Int J Food Microbiol. 1996 Apr;29(2-3):397-402. Vignolo G, Fadda S, de Kairuz MN, de Ruiz Holgado AA, Oliver G. Control of Listeria monocytogenes in ground beef by 'Lactocin 705', a bacteriocin produced by Lactobacillus casei CRL 705). DRAMP00146 KRGPNCVGNFLGGLFAGAAAGVPLGPAGIVGGANLGMVGGALTCL 45 Abp118 alpha (Salivaricin CRL1328 alpha peptide) Q8KWI0 Belongs to the class IIb bacteriocin abp118alpha Lactobacillus salivarius (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Function: Abp118alpha alone exhibits the antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11932444##19591924 Microbiology. 2002 Apr;148(Pt 4):973-984.##Res Microbiol. 2009 Jul-Aug;160(6):401-408. Flynn S, van Sinderen D, Thornton GM, Holo H, Nes IF, Collins JK.##Vera Pingitore E, Hebert E.M, Nader-Macias M.E, Sesma F. Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118.##Characterization of salivaricin CRL 1328, a two-peptide bacteriocin produced by Lactobacillus salivarius CRL 1328 isolated from the human vagina. DRAMP00147 KNGYGGSGNRWVHCGAGIVGGALIGAIGGPWSAVAGGISGGFTSCR 46 Abp118 beta (Salivaricin CRL1328 beta peptide) Q8KWH9 Belongs to the class IIb bacteriocin abp118beta Lactobacillus salivarius (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Function: Abp118beta can enhanced the antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11932444##19591924 Microbiology. 2002 Apr;148(Pt 4):973-984.##Res Microbiol. 2009 Jul-Aug;160(6):401-408. Flynn S, van Sinderen D, Thornton GM, Holo H, Nes IF, Collins JK.##Vera Pingitore E, Hebert E.M, Nader-Macias M.E, Sesma F. Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118.##Characterization of salivaricin CRL 1328, a two-peptide bacteriocin produced by Lactobacillus salivarius CRL 1328 isolated from the human vagina. DRAMP00148 LSCDEGMLAVGGLGAVGGPWGAAVGVLVGAALYCF 35 Thermophilin 9 (BlpDst; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Streptococcus thermophilus LMD-9 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18156339 Appl Environ Microbiol. 2008 Feb;74(4):1102-1110. Fontaine L, Hols P. The inhibitory spectrum of thermophilin 9 from Streptococcus thermophilus LMD-9 depends on the production of multiple peptides and the activity of BlpG(St), a thiol-disulfide oxidase. DRAMP18339 GFIGWGNNIFGHYSGDF 17 Anantin(Bacteriocin) Q7M0J9 Not found Not found Streptomyces coerulescens Unknown Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available The Journal of antibiotics. 1991 Feb;44(2):164-71.##The Journal of antibiotics. 1991 Feb;44(2):172-80. Weber W,Fischli W,Hochuli E,Kupfer E,Weibel E K.##Wyss D F,Lahm H W,Manneberg M,Labhardt A M. Anantin--a peptide antagonist of the atrial natriuretic factor (ANF). I. Producing organism, fermentation, isolation and biological activity.##Anantin--a peptide antagonist of the atrial natriuretic factor (ANF). II. Determination of the primary sequence by NMR on the basis of proton assignments. DRAMP00150 KNGYGGSGNRWVHCGAGIVGGALIGAIGGPWSAVAGGISGGFASCH 46 Sln2 (chain b of Salivaricin P; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus salivarius DPC6005 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17416691 Appl Environ Microbiol. 2007 Jun;73(11):3719-3723. Barrett E, Hayes M, O'Connor P, Gardiner G, Fitzgerald GF, Stanton C, Ross RP, Hill C. Salivaricin P, one of a family of two-component antilisterial bacteriocins produced by intestinal isolates of Lactobacillus salivarius. DRAMP00151 ESVFSKIGNAVGPAAYWILKGLGNMSDVNQADRINRKKH 39 Enterocin 1071A (Ent1071A; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Enterococcus faecalis BFE 1071 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976133 Appl Environ Microbiol. 2002 May;68(5):2550-2554. Franz CM, Grube A, Herrmann A, Abriouel H, Stärke J, Lombardi A, Tauscher B, Holzapfel WH. Biochemical and genetic characterization of the two-peptide bacteriocin enterocin 1071 produced by Enterococcus faecalis FAIR-E 309. DRAMP00152 GPGKWLPWLQPAYDFVTGLAKGIGKEGNKNKWKNV 35 Enterocin 1071B (Ent1071B; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Enterococcus faecalis BFE 1071 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976133 Appl Environ Microbiol. 2002 May;68(5):2550-2554. Franz CM, Grube A, Herrmann A, Abriouel H, Stärke J, Lombardi A, Tauscher B, Holzapfel WH. Biochemical and genetic characterization of the two-peptide bacteriocin enterocin 1071 produced by Enterococcus faecalis FAIR-E 309. DRAMP00153 KVSGGEAVAAIGICATASAAIGGLAGATLVTPYCVGTWGLIRSH 44 NlmA (chain a of Mutacin IV; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Streptococcus mutans UA140 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Streptococci sanguinis NY101, S. sanguinis ATCC 10556, Streptococcus parasanguinis ATCC 15911, S. oralis TCC 10557, S. mitis ATCC 903, S. mitis ATCC 33399, S. gordonii ATCC 10558, S. crista ATCC 49999, S. sobrinus OMZ176. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11133423 Appl Environ Microbiol. 2001 Jan;67(1):15-21. Qi F, Chen P, Caufield PW. The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV. DRAMP00154 DKQAADTFLSAVGGAASGFTYCASNGVWHPYILAGCAGVGAVGSVVFPH 49 NlmB (chain b of Mutacin IV; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Streptococcus mutans UA140 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Streptococci sanguinis NY101, S. sanguinis ATCC 10556, Streptococcus parasanguinis ATCC 15911, S. oralis TCC 10557, S. mitis ATCC 903, S. mitis ATCC 33399, S. gordonii ATCC 10558, S. crista ATCC 49999, S. sobrinus OMZ176. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11133423 Appl Environ Microbiol. 2001 Jan;67(1):15-21. Qi F, Chen P, Caufield PW. The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV. DRAMP00155 YSSKDCLKDIGKGIGAGTVAGAAGGGLAAGLGAIPGAFVGAHFGVIGGSAACIGGLLGN 59 BrcA (chain a of Brochocin C; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Brochothrix campestris ATCC 43754 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Chain A has an identical sequence to NKR-5-3A from E. faecium NKR-5-3 (Ishbashi N et al 2012 Biosci Biotechnol Biochem 76: 947-953). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9835559 Appl Environ Microbiol. 1998 Dec;64(12):4757-4766. McCormick JK, Poon A, Sailer M, Gao Y, Roy KL, McMullen LM, Vederas JC, Stiles ME, Van Belkum MJ. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. DRAMP00156 KINWGNVGGSCVGGAVIGGALGGLGGAGGGCITGAIGSIWDQW 43 BrcB (NKR-5-3A; chain b of Brochocin C; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Brochothrix campestris ATCC 43754 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9835559 Appl Environ Microbiol. 1998 Dec;64(12):4757-4766. McCormick JK, Poon A, Sailer M, Gao Y, Roy KL, McMullen LM, Vederas JC, Stiles ME, Van Belkum MJ. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. DRAMP00157 RNKLAYNMGHYAGKATIFGLAAWALLA 27 Plantaricin S alpha (Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus plantarum LPCO10 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found 6GNZ Although beta alone appeared to retain a trace of inhibitory activity, the complementary action of both the alpha and beta peptides was required for full bacteriocin activity. Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8534111##9572965 Appl Environ Microbiol. 1995 Dec;61(12):4459-4463.##Appl. Environ. Microbiol. 1998;64 (5):1871-1877. Jim©nez-D­az R, Ruiz-Barba JL, Cathcart DP, Holo H, Nes IF, Sletten KH, Warner PJ.##Stephens SK, Floriano B, Cathcart DP, Bayley SA, Witt VF, Jim©nez-D­az R, Warner PJ, Ruiz-Barba JL. Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides.##Molecular analysis of the locus responsible for production of plantaricin S, a two-peptide bacteriocin produced by Lactobacillus plantarum LPCO10. DRAMP00158 GMSGYIQGIPDFLKGYLHGISAANKHKKGRLGY 33 Lactocin 705alpha (lac705alpha; chain a of Lactocin 705; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus casei CRL 705 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Several lactic acid bacteria, Listeria, Streptococci, etc. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10754241 FEMS Microbiol Lett. 2000 Apr 15;185(2):157-161. Cuozzo SA, Sesma F, Palacios JM, de Ru­z Holgado AP, Raya RR. Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705. DRAMP00159 GFWGGLGYIAGRVGAAYGHAQASANNHHSPING 33 Lactocin 705beta (lac705beta; chain b of Lactocin 705; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus casei CRL 705 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Several lactic acid bacteria, Listeria, Streptococci, etc. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10754241 FEMS Microbiol Lett. 2000 Apr 15;185(2):157-161. Cuozzo SA, Sesma F, Palacios JM, de Ru­z Holgado AP, Raya RR. Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705. DRAMP00160 YSGKDXLKDMGGYALAGAGSGALXGAPAGXVGALPGAFVGAHVGAIAG 48 ThmA (chain a of Thermophilin 13; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Streptococcus thermophilus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Streptococcus thermophilus SFi3, Clostridium botulinum, Listeria monocytogenes, Bacillus cereus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9162062 J Biol Chem. 1997 May 30;272(22):14277-14284. Marciset O, Jeronimus-Stratingh MC, Mollet B, Poolman B. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. DRAMP00161 QINWGSVVGHCIGGAIIGGAFSGGAAAGVGCLVGSGKAIINGL 43 ThmB (chain b of Thermophilin 13; Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Streptococcus thermophilus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found ThmB, by itself, is not bactericidal. An equal amount of ThmB can increase the activity of ThmA by 40 fold, however, an excess of ThmB inhibits the activity of ThmA. Disulfide bonds are not required for activity. Gram-positive bacteria: Streptococcus thermophilus SFi3, Clostridium botulinum, Listeria monocytogenes, Bacillus cereus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9162062 J Biol Chem. 1997 May 30;272(22):14277-14284. Marciset O, Jeronimus-Stratingh MC, Mollet B, Poolman B. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. DRAMP00162 GNAACVIGCIGSCVISEGIGSLVGTAFTLG 30 Thuricin CDalpha (Trn-alpha; one peptide of Thuricin CD; Bacteriocin) F5AT07 Belongs to the class IIb bacteriocin Not found Bacillus thuringiensis DPC 6431 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Alpha helix (3 helices; 16 residues) Trn-α has L-stereochemistry at Ser21 (alpha-R), L-stereochemistry at Thr25 (alpha-R), and D-stereochemistry at Thr28 (alpha-S) (an LLD isomer). 2L9X resolved by NMR. "Function: Thuricin CD is produced by Bacillus thuringiensis DPC 6431, a bacterial strain isolated from a human fecal sample, and it consists of two distinct peptides, Trn-alpha and Trn-beta, that act synergistically to kill a wide range of clinical C. difficile isolates. Thuricin CD showes no activity against any Gram-negative organisms tested, including Escherichia coli, Pseudomonas sp., Salmonella sp., and Bacteroides fragilis. Biophysicochemical properties: Cell-free supernatants of thuricin were active throughout the pH range of 2-9 and heat stable up to 85 °C. There was, however, a reduction in activity at 90 °C and a complete loss of activity at 100 °C after 15 min." Gram-positive bacteria: Clinical Clostridium difficile isolates (MIC in the range of nM) and Listeria monocytogenes, Lactobacillus fermentum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20435915##21526839 Proc Natl Acad Sci U S A. 2010 May 18;107(20):9352-9357.##J Am Chem Soc. 2011 May 25;133(20):7680-7683. Rea MC, Sit CS, Clayton E, O'Connor PM, Whittal RM, Zheng J, Vederas JC, Ross RP, Hill C.##Sit CS, McKay RT, Hill C, Ross RP, Vederas JC. Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile.##The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links. DRAMP00163 GWVACVGACGTVCLASGGVGTEFAAASYFL 30 Thuricin CDdbeta (Trn-beta; one peptide of Thuricin CD; Bacteriocin) F5AT06 Belongs to the class IIb bacteriocin Not found Bacillus thuringiensis DPC 6431 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Alpha helix (3 helices; 22 residues) Trn-β was also found to be the LLD isomer, with L-stereochemistry at Thr21 (alpha-R), L-stereochemistry at Ala25 (alpha-R), and D-stereochemistry at Tyr28 (alpha-S). 2LA0 resolved by NMR. "Function: Thuricin CD is produced by Bacillus thuringiensis DPC 6431, a bacterial strain isolated from a human fecal sample, and it consists of two distinct peptides, Trn-alpha and Trn-beta, that act synergistically to kill a wide range of clinical C. difficile isolates. Thuricin CD showes no activity against any Gram-negative organisms tested, including Escherichia coli, Pseudomonas sp., Salmonella sp., and Bacteroides fragilis. Biophysicochemical properties: Cell-free supernatants of thuricin were active throughout the pH range of 2-9 and heat stable up to 85 °C. There was, however, a reduction in activity at 90 °C and a complete loss of activity at 100 °C after 15 min." Gram-positive bacteria: Clinical Clostridium difficile isolates (MIC in the range of nM) and Listeria monocytogenes, Lactobacillus fermentum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20435915##21526839 Proc Natl Acad Sci U S A. 2010 May 18;107(20):9352-9357.##J Am Chem Soc. 2011 May 25;133(20):7680-7683. Rea MC, Sit CS, Clayton E, O'Connor PM, Whittal RM, Zheng J, Vederas JC, Ross RP, Hill C.##Sit CS, McKay RT, Hill C, Ross RP, Vederas JC. Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile.##The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links. DRAMP00164 LAGYTGIASGTAKKVVDAIDKGAAAFVIISIISTVISAGALGAVSASADFIILTVKNYISRNLKAQAVIW 70 Bacteriocin uberolysin (Bacteriocin) A5H1G9 Belongs to the class IIc bacteriocin ublA Streptococcus uberis strain 42 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database Most streptococci (except S.rattus and S. mutans), Listeria spp., enterococci and staphylococci. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 17464077 Microbiology. 2007 May;153(Pt 5):1619-1630. Wirawan RE, Swanson KM, Kleffmann T, Jack RW, Tagg JR. Uberolysin: a novel cyclic bacteriocin produced by Streptococcus uberis. DRAMP00165 IYWIADQFGIHLATGTARKLLDAMASGASLGTAFAAILGVTLPAWALAAAGALGATAA 58 Gassericin A (GaaA; Bacteriocin) O24790 Belongs to the class IIc bacteriocin gaaA Lactobacillus gasseri LA39 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Alpha helix Not found It causes K+ ion efflux from indicator cells and liposome.Circularized by forming a peptide bond between the N- and C-ends. Initially, it was thought to differ from Reutericin 6 only by the number of D-amino acids (Kawai et al., 2004). A re-study corrected this and concluded that gassericin A and reutericin 6 are identical bacteriocins (Arakawa et al. 2010 Lett Appl. Microbiol 50:406-411). However, reutericin 6 was isolated from Lactobacillus reuteri LA6. Gram-positive bacterium: L. reuteri LA6. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 9648219##19666732 Biosci Biotechnol Biochem. 1998 May;62(5):887-892.##Appl Environ Microbiol. 2009 Oct;75(19):6340-6351. Kawai Y, Saito T, Suzuki M, Itoh T.##Ito Y, Kawai Y, Arakawa K, Honme Y, Sasaki T, Saito T. Sequence analysis by cloning of the structural gene of gassericin A, a hydrophobic bacteriocin produced by Lactobacillus gasseri LA39.##Conjugative plasmid from Lactobacillus gasseri LA39 that carries genes for production of and immunity to the circular bacteriocin gassericin A. DRAMP00166 IYFIADKMGIQLAPAWYQDIVNWVSAGGTLTTGFAIIVGVTVPAWIAEAAAAFGIASA 58 Butyrivibriocin AR10 (Bacteriocin) Q9ZGP5 Belongs to the class IIc bacteriocin bviA Butyrivibrium fibrisolvens AR10 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Clostridium clostridiforme ATCC25537, C. perfringens, Eubacterium ruminentium ATCC17233, Lachnospira multiperus ATCC19207, L. vitulinus ATCC27783, Lactobacillus ruminis ATCC27780, Ruminococcus albus SY3, Streptococcus bovis ATCC33317, Listeria ivanovii 80, L. gray 83. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 9023920##15162201 Appl Environ Microbiol. 1997 Feb;63(2):394-402.##Can J Microbiol. 2003 Dec;49(12):763-773. Kalmokoff ML, Teather RM.##Kalmokoff ML, Cyr TD, Hefford MA, Whitford MF, Teather RM. Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: evidence in support of the widespread occurrence of bacteriocin-like activity among ruminal isolates of B. fibrisolvens.##Butyrivibriocin AR10, a new cyclic bacteriocin produced by the ruminal anaerobe Butyrivibrio fibrisolvens AR10: characterization of the gene and peptide. DRAMP00167 NKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG 35 Subtilosin A (Antilisterial bacteriocin subtilosin; D-amino acid; Bacteriocin; Preclinical) O07623 Belongs to the class IIc bacteriocin sboA Bacillus subtilis (strain 168) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 6 residues) The NMR study results demonstrate that in addition to having a cyclized peptide backbone (amide between N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the alpha-positions of Phe22, Thr28, and Phe31, respectively. 1PXQ resolved by NMR. PTM: This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys- 15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence. [Ref.17213266] MICs between 1 and 12.5 mg/L: E. faecalis OGX-1, L. monocytogenes ATCC 19115, P. gingivalis ATCC 33277, K. rhizophila ATCC 9341, Enterobacter aerogenes ATCC 13408, Streptococcus pyogenes ATCC 19615 and Shigella sonnei ATCC 25931. ##MICs between 25 and 100 mg/L: Escherichia coli ATCC 8739, Pseudomonas aeruginosa ATCC 9027, S. gordonii Challis ATCC 49818 and Staphylococcus aureus ATCC 6538. ##MICs over 100mg/L: B. subtilis ATCC 6633,Fusobacterium nucleatum ATCC 25586,P. gingivalis W83 ,K. pneumoniae ATCC 4352 ,K. pneumoniae UMN1, Bacillus cereus ATCC 10876, Staphylococcus epidermidis ATCC 12228,Proteus mirabilis ATCC 25933 ,Salmonella enterica Typhi ATCC 12048. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Thioether bridges between Cys4 and Phe31,Cys7 and Thr28,Cys13 and Phe22. Mixed(D-Thr28,D-Phe31) No cytotoxicity information found Not found 3936839##15035610 J Biochem. 1985 Sep;98(3):585-603.##Biochemistry. 2004 Mar 30;43(12):3385-3395. Babasaki K, Takao T, Shimonishi Y, Kurahashi K.##Kawulka KE, Sprules T, Diaper CM, Whittal RM, McKay RT, Mercier P, Zuber P, Vederas JC. Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis.##Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to alpha-carbon cross-links: formation and reduction of alpha-thio-alpha-amino acid derivatives. DRAMP00168 AAPKITQKQKNCVNGQLGGMLAGALGGPGGVVLGGIGGAIAGGCFN 46 Divergicin A (Bacteriocin) Q3SAX6 Belongs to the class IIc bacteriocin Not found Carnobacterium divergens (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7768812##16385127 J Bacteriol. 1995 Jun;177(11):3143-3149.##Microbiology. 2006 Jan;152(Pt 1):171-178. Worobo RW, Van Belkum MJ, Sailer M, Roy KL, Vederas JC, Stiles ME.##van Belkum MJ, Stiles ME. A signal peptide secretion-dependent bacteriocin from Carnobacterium divergens.##Characterization of the theta-type plasmid pCD3.4 from Carnobacterium divergens, and modulation of its host range by RepA mutation. DRAMP00169 MAKEFGIPAAVAGTVINVVEAGGWVTTIVSILTAVGSGGLSLLAAAGRESIKAYLKKEIKKKGKRAVIAW 70 Enterocin AS-48 (AS-48; Bacteriocin) Q47765 Belongs to the class IIc bacteriocin as-48 Enterococcus faecalis S-48 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (6 helices; 54 residues) The NMR structure of AS-48 at pH 3 showed that AS-48 is a monomer consisting of a bundle of five helices arranged with the topology of the saposin fold. 1E68 resolved by NMR.##1O82,1O83,1O84 resolved by X-ray. Function: The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The antimicrobial effect of AS-48 is due to its ability to form pores in the membranes of sensitive bacteria, leading to the efflux of small molecules and the depletion of the membrane electrical potential and ultimately leading to cell death. Gram-positive bacteria: Bacillus subtilus, Bacillus cereus, Bacillus circulans, Bacillus megaterium, Corynebacterium glutamicum, Corynebacterium bovis, Mycobacterium phlei, Nocardia corrallina, Micrococcus luteus, Micrococcus lysodeikticus, Staphylococcus aureus, Streptococcus faecalis, Streptococcus faecium;##Gram-negative bacteria: Enterobacter cloacae, Escherichia coli, Klebsiella pneumoniae, Proteus inconstans, Salmonella typhimurium, Shigella sonnei, Pseudomonas fluorescens, Pseudomonas aeruginosa, Pseudomonas reptilivora. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Hydrogen bonds between Ala-2 and Ile-7, Val-18 and Gly-23, Thr-33 and Gly-36, the backbone carbonyl oxygen of Phe-5 and the side-chain hydroxylic proton of Ser-50 L No cytotoxicity information found Cell membrane 2501837##14623193##11005847 Res Microbiol. 1989 Jan;140(1):57-68.##J Mol Biol. 2003 Nov 28;334(3):541-549.##Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6. G¡lvez A, Maqueda M, Mart­nez-Bueno M, Valdivia E.##S¡nchez-Barrena MJ, Mart­nez-Ripoll M, G¡lvez A, Valdivia E, Maqueda M, Cruz V, Albert A.##Gonz¡lez C, Langdon GM, Bruix M, G¡lvez A, Valdivia E, Maqueda M, Rico M. Bactericidal and bacteriolytic action of peptide antibiotic AS-48 against gram-positive and Gram-negative bacteria and other organisms.##Structure of bacteriocin AS-48: from soluble state to membrane bound state.##Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin. DRAMP00170 LVAYGIAQGTAEKVVSLINAGLTVGSIISILGGVTVGLSGVFTAVKAAIAKQGIKKAIQL 60 Carnocyclin A (CclA; Bacteriocin) B2MVM5 Belongs to the class IIc bacteriocin cclA Carnobacterium maltaromaticum UAL307 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (4 helices; 38 residues) The NMR study results reveal that CclA preferentially binds halide anions and has a structure that is surprisingly similar to that of AS-48 despite low sequence identity, different oligomeric state, and disparate function. CclA folds into a compact globular bundle, comprised of four helices surrounding a hydrophobic core. 2KJF resolved by NMR. "Function: Carnocyclin A (CclA) is a potent antimicrobial peptide from Carnobacterium maltaromaticum UAL307 that displays a broad spectrum of activity against numerous Gram-positive organisms. Biophysicochemical properties: pH dependence (Stable from pH 2 to 12); Temperature dependence (Displays a high degree of stability when incubated at temperatures between -80 and 75 degrees Celsius for 60 minutes. Autoclaving the peptide at 121 degrees Celsius for 15 minutes had no effect but incubation at 100 degrees Celsius for 60 minutes caused a 32-fold reduction in activity)." Gram-positive bacteria: Carnobacterium maltaromaticum UAL26, C. maltaromaticum LV17A, C. divergens LV13, Brochothrix campestris ATCC 43754, B. thermosphacta ATCC 11509, Enterococcus faecalis ATCC 7080, E. faecium ATCC 19434, E. faecium BFE900, Lactococcus lactis subsp. lactis ATCC 11454, Lactococcus lactis subsp. cremoris ATCC 11602, Lactococcus lactis subsp. lactis DPC3147, Lactobacillus sakeii 706, L. sakei UAL1218, Leuconostoc mesenteroides Y105, Pediococcus acidilactici PAC1.0, Listeria monocytogenes ATCC 15313, Listeria monocytogenes H7762, Listeria monocytogenes ATCC 43256, Listeria monocytogenes HPB 642, Listeria monocytogenes UAFM 1, Listeria monocytogenes UAFM 15, Staphylococcus aureus ATCC 25923, Staphylococcus aureus ATCC 6538, Staphylococcus aureus ATCC 29213. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Lipid II 18552180##19692336 Appl Environ Microbiol. 2008 Aug;74(15):4756-4763.##J Biol Chem. 2009 Oct 16;284(42):28674-81. Martin-Visscher LA, van Belkum MJ, Garneau-Tsodikova S, Whittal RM, Zheng J, McMullen LM, Vederas JC.##Martin-Visscher LA, Gong X, Duszyk M, Vederas JC. Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307.##The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif. DRAMP00172 LVATGMAAGVAKTIVNAVSAGMDIATALSLFSGAFTAAGGIMALIKKYAQKKLWKQLIAA 60 Garvicin ML (Bacteriocin) D2KC49 Belongs to the class IIc bacteriocin garML Lactococcus garvieae DCC43 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found The peptide is expressed as a 63mer precursor. The leader sequence was removed and covalent link of the N and C-termini leading to the mature peptide. This bacteriocin inhibits other Gram-positive bacteria. The cyclic structure of the peptide confers stability to heat (80-100oC), pH (2-10) and proteases (trypsin, pepsin, papain and proteinase K). Gram-positive bacteria: Lactobacillus reuteri 20016 (378), L. helveticus 15009 (492), L. curvatus 2739 (177), L. casei 334 (1-174), L. acidophilus 4356 (236), L. sakei 2714 (1-445), Lactococcus lactis BB24 (928), L. lactis NZ9000 (163), L. lactis DPC5598 (1-541)，L. garvieae 5274 (617), L. garvieae 5806 (2-807), L. garvieae 5807 (2-705), L. raffinolactis 988 (228), Pediococcus acidilactici 347 (1-398), P. pentosaceus FBB61 (1-131), Enterococcus faecium P13 (1-291), E. faecium L50 (719), E. faecialis DBH18 (25), E. faecalis P4 (123), Propionibacterium sp.P6 (190), P. acidipropionici 563 (864), Clostridium tyrobutiricum 3.5CT (651), C. tyrobutiricum 1754 (839), C. perfringens 376 (352), C. botulinum 551 (574), Listeria monocytogenes 4032 (662), L. ivanovii 913 (1-020), L. seeligeri 917 (684), L. grayi 931 (742), L. welshimeri 919 (452), Brochothrix thermosphacta 847 (283), Streptococcus pneumoniae FQ26 (590), S. pneumoniae 67620 (596), S. pneumoniae 15M-1047 (790). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 21057028 Appl Environ Microbiol. 2011 Jan;77(1):369-373. Borrero J, Brede DA, Skaugen M, Diep DB, Herranz C, Nes IF, Cintas LM, Hern¡ndez PE. Characterization of Garvicin ML, a Novel Circular Bacteriocin Produced by Lactococcus garvieae DCC43, Isolated from Mallard Ducks (Anas platyrhynchos). DRAMP18337 ATQSHQ 6 S. amritsarensis lipopeptide (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Streptomyces amritsarensis Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25006539 AMB Express. 2014 Jun 28;4:50. Sharma D, Mandal SM, Manhas RK. Purification and characterization of a novel lipopeptide from Streptomyces amritsarensis sp. nov. active against methicillin-resistant Staphylococcus aureus. DRAMP18338 STNCFCYICCSCSS 14 Thiocillin GE37468 (Bacteriocin) P0C8P9 Belongs to the class I bacteriocin getA Streptomyces ATCC 55365 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Has bacteriocidal activity against both aerobic and anaerobic Gram-positive bacteria. Has poor activity against Gram-negative bacteria, with the exception of B.fragilis. Inhibits bacterial protein biosynthesis by acting on elongation factor Tu. Full antibiotic activity depends on the presence of the modified residue Ile-50. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Elongation Factor Tu (EF-Tu) 21788474 Proc Natl Acad Sci U S A. 2011 Aug 9;108(32):13053-8. Young TS, Walsh CT. Identification of the thiazolyl peptide GE37468 gene cluster from Streptomyces ATCC 55365 and heterologous expression in Streptomyces lividans. DRAMP00175 MGAIAKLVAKFGWPIVKKYYKQIMQFIGEGWAINKIIEWIKKHI 44 Enterocin L50A (EntL50A; Bacteriocin) D4QP39 Belongs to the class IId bacteriocin Not found Enterococcus faecium E980/L50 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Function: Expression in vivo and in vitro transcription/translation experiments demonstrated that entL50A and entL50B are the only genes required to obtain antimicrobial activity, strongly indicating that their bacteriocin products are not posttranslationally modified. Both bacteriocins possess antimicrobial activity on their own, with EntL50A being the most active. In addition, when the two bacteriocins were combined, a considerable synergism was observed, especially with some indicator strains. Non-hemolytic activity [Ref.9555877]Gram-positive bacteria: Pediococcus acidilactici 347(2400AU/ml), Enterococcus faecium T136(1200AU/ml), Lactococcus lactis subsp.cremoris CNRZ 177(4800AU/ml), Lactobacillus sake 148(600AU/ml). [Ref:9555877]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9555877##20398277 Bacteriol. 1998 Apr;180(8):1988-1994.##BMC Genomics. 2010 Apr 14;11:239. Cintas LM, Casaus P, Holo H, Hernandez PE, Nes IF, H¥varstein LS.##van Schaik W, Top J, Riley DR, Boekhorst J, Vrijenhoek JE, Schapendonk CM, Hendrickx AP, Nijman IJ, Bonten MJ, Tettelin H, Willems RJ. Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins.##Pyrosequencing-based comparative genome analysis of the nosocomial pathogen Enterococcus faecium and identification of a large transferable pathogenicity island. DRAMP00176 MGAIAKLVTKFGWPLIKKFYKQIMQFIGQGWTIDQIEKWLKRH 43 Enterocin L50B (EntL51B; Bacteriocin) D4QP38 Belongs to the class IId bacteriocin Not found Enterococcus faecium E980/L50 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Function: Expression in vivo and in vitro transcription/translation experiments demonstrated that entL50A and entL50B are the only genes required to obtain antimicrobial activity, strongly indicating that their bacteriocin products are not posttranslationally modified. Both bacteriocins possess antimicrobial activity on their own, with EntL50A being the most active. In addition, when the two bacteriocins were combined, a considerable synergism was observed, especially with some indicator strains. Non-hemolytic activity. [Ref.9555877]Gram-positive bacteria: Pediococcus acidilactici 347(200AU/ml), Enterococcus faecium T136(100AU/ml), Lactococcus lactis subsp.cremoris CNRZ 177(1200AU/ml), Lactobacillus sake 148(100AU/ml). [Ref:9555877]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9555877##20398277 Bacteriol. 1998 Apr;180(8):1988-1994.##BMC Genomics. 2010 Apr 14;11:239. Cintas LM, Casaus P, Holo H, Hernandez PE, Nes IF, H¥varstein LS.##van Schaik W, Top J, Riley DR, Boekhorst J, Vrijenhoek JE, Schapendonk CM, Hendrickx AP, Nijman IJ, Bonten MJ, Tettelin H, Willems RJ. Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins.##Pyrosequencing-based comparative genome analysis of the nosocomial pathogen Enterococcus faecium and identification of a large transferable pathogenicity island. DRAMP00179 MNFLKNGIAKWMTGAELQAYKKKYGCLPWEKISC 34 Enterocin Q (EntQ; Bacteriocin) Q7WYZ9 Belongs to the class IId bacteriocin entqA Enterococcus faecium L50 (Gram-positive bacteria) Antimicrobial, Antibacterial Predicted Not found Not found Enterococcus faecium L50 produces, in addition to EntL50, the sec-dependent pediocin-like enterocin P (EntP), and an unmodified non-pediocin-like bacteriocin, termed enterocin Q (EntQ), synthesized without an N-terminal leader sequence or signal peptide. (Ref.1) A broad antimicrobial spectrum against the most relevant beer-spoilage lactic acid bacteria (LAB) (i.e., Lactobacillus brevis and Pediococcus damnosus). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11073927##17021217 J Bacteriol. 2000 Dec;182(23):6806-6814.##Appl Environ Microbiol. 2006 Oct;72(10):6653-6666. Cintas LM, Casaus P, Herranz C, H¢varstein LS, Holo H, Hern¡ndez PE, Nes IF.##Criado R, Diep DB, Aakra A, Guti©rrez J, Nes IF, Hern¡ndez PE, Cintas LM. Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q.##Complete sequence of the enterocin Q-encoding plasmid pCIZ2 from the multiple bacteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity. DRAMP00180 SLQYVMSAGPYTWYKDTRTGKTICKQTIDTASYTFGVMAEGWGKTFH 47 Lactococcin-B (LCN-B; Bacteriocin) P35518 Belongs to the class IId bacteriocin lcnB Lactococcus lactis subsp (Streptococcus cremoris) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found MOA: Kills Lactococci by dissipating the membrane potential of the cells. Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 1610182##8885398 Appl Environ Microbiol. 1992 Feb;58(2):572-577.##Microbiology. 1996 Oct;142 (Pt 10):2825-2830. van Belkum MJ, Kok J, Venema G.##Venema K, Dost MH, Venema G, Kok J. Cloning, sequencing, and expression in Escherichia coli of lcnB, a third bacteriocin determinant from the lactococcal bacteriocin plasmid p9B4-6.##Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis. DRAMP00181 KLTFIQSTAAGDLYYNTNTHKYVYQQTQNAFGAAANTIVNGWMGGAAGGFGLHH 54 Lactococcin-A (LCN-A; Bacteriocin) P0A313, Q00563 Belongs to the class IId bacteriocin lcnA Lactococcus lactis subsp (Streptococcus cremoris) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Domain: Contains one Transmembrane helix at position 9-31 (Potential). Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1901707##1904860 Appl Environ Microbiol. 1991 Feb;57(2):492-498.##J Bacteriol. 1991 Jun;173(12):3879-3887. van Belkum MJ, Hayema BJ, Jeeninga RE, Kok J, Venema G.##Holo H, Nilssen O, Nes IF. Organization and nucleotide sequences of two lactococcal bacteriocin operons.##Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. DRAMP00182 DWTXWSXLVXAACSVELL 18 Thuricin-S (Bacteriocin) P84763 Belongs to the class IId bacteriocin Not found Bacillus thuringiensis subsp. entomocidus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by Bacillus thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subBelongs to the class IId bacteriocin. Gram-positive bacteria: Listeria monocytogenes, Bacillus subtilis and other Bacillus, Enterobacter cloacae, L. acidophilus, Lactococcus lactis, Pediococcus acidilactici, S. thermophilus;##Gram-negative bacteria: S. cholerae, Shigella flexneri and Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17496978 Can J Microbiol. 2007 Feb;53(2):284-290. Chehimi S, Delalande F, Sabl© S, Hajlaoui MR, Van Dorsselaer A, Limam F, Pons AM. Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis. DRAMP00183 DWTCWSCLVCAACSVELLNLVTAATGASTAS 31 Thuricin-17 (Thurincin H; Bacteriocin) B5U2V4 Belongs to the class IId bacteriocin tucA1 Bacillus thuringiensis (strain SF361/NEB17) (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (2 helices; 18 residues) Not found 2LBZ resolved by NMR. Function: The bacteriocin thurincin H, which is produced by Bacillus thuringiensis SF361, exhibits strong activity against a spectrum of Bacillus and Listeria spp. , including the human pathogen Listeria monocytogenes. The application of this bacteriocin to leaves (spray) or roots (drench) directly stimulates the growth of both a C(3) dicot (soybean) and a C(4) monocot (corn). This growth stimulation is similar in nature to that previously seen when plants are treated with Nod factors. Strain NEB17 contains three copies of the gene for thuricin 17 that code for identical amino acid sequences. These two lines of evidence suggest that the dual functions of these proteins may have constrained their evolution. This is the first report of direct plant growth enhancement by a bacteriocin. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (++), Bacillus subtilis ATCC 6537 (+), Bacillus subtilis CU1065 5(WT) (+++), Bacillus subtilis LRB90 (+), Bacillus subtilis LRB91 (+), Bacillus cereus F4552 (+++++), Bacillus cereus F4810 (+++++), Bacillus cereus Northview P2E018 (+++++), Geobacillus stearothermophilus ATCC 12980 (+++++), Bacillus thuringiensis EG10368 (+++++), Bacillus megaterium LRB89 (+++++), Listeria mo nocytogenes F2 586 1053 (++++), Listeria monocytogenes 2289 (++++), Listeria innocua ATCC 2283 (+++++), Listeria ivanovii ATCC 19119 (+++++), Micrococcus luteus (+), Staphylococcus aureus ATCC 9144 (+), Staphylococcus aureus ATCC 8095 (+), Carnobacterium piscicola CU216 (+++++) [NOTE: + (weakly activity) to +++++ (highest activity)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1908301##216478494##19732155##21786372 Planta. 2009 Mar;229(4):747-755.##J Appl Microbiol. 2006 Mar;100(3):545-554.##FEMS Microbiol Lett. 2009 Oct;299(2):205-213.##Angew Chem Int Ed Engl. 2011 Sep 5;50(37):8718-8721. Lee KD, Gray EJ, Mabood F, Jung WJ, Charles T, Clark SR, Ly A, Souleimanov A, Zhou X, Smith DL.##Gray EJ, Lee KD, Souleimanov AM, Di Falco MR, Zhou X, Ly A, Charles TC, Driscoll BT, Smith DL.##Lee H, Churey JJ, Worobo RW.##Sit CS, van Belkum MJ, McKay RT, Worobo RW, Vederas JC. The Belongs to the class IId bacteriocin thuricin-17 increases plant growth.##A novel bacteriocin, thuricin 17, produced by plant growth promoting rhizobacteria strain Bacillus thuringiensis NEB17: isolation and classification.##Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361.##The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks. DRAMP00184 EGTWQHGYGVSSAYSNYHHGSKTHSATVVNNNTGRQGKDTQRAGVWAKATVGRNLTEKASFYYNFW 66 Lactococcin 972 (Lcn972; homodimer; Bacteriocin) O86283 Belongs to the class IId bacteriocin lcn972 Lactococcus lactis subsp. lactis IPLA 972 (Streptococcus lactis) (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Beta strand (6 strands; 45 residues) Not found 2LGN resolved by NMR. Comment: No comments found on DRAMP database Lactococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 10589723##21818877##PubMed ID is not available Microbiology. 1999 Nov;145 (Pt 11):3155-3161.##Microbiology. 1996 Sep;142 (Pt 9):2393-2398.##Submitted (JUL-2011) to the PDB data bank. Mart­nez B, Fern¡ndez M, Su¡rez JE, Rodr­guez A.##Mart­nez B, Su¡rez JE, Rodr­guez A.##Turner D.L, Lamosa P, Martinez B. Synthesis of lactococcin 972, a bacteriocin produced by Lactococcus lactis IPLA 972, depends on the expression of a plasmid-encoded bicistronic operon.##Lactococcin 972: a homodimeric lactococcal bacteriocin whose primary target is not the plasma membrane.##Structure and properties of lactococcin 972 from Lactococcus lactis. DRAMP00185 KGKGFWSWASKATSWLTGPQQPGSPLLKKHR 31 Leucocin-B (Leu B; Leucocin B-TA33a; Bacteriocin) P81052 Belongs to the class IId bacteriocin Not found Leuconostoc mesenteroides TA33a (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Inhibits a wide spectrum of lactic acid bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9611809 Microbiology. 1998 May;144 (Pt 5):1343-1348. Papathanasopoulos MA, Dykes GA, Revol-Junelles AM, Delfour A, von Holy A, Hastings JW. Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a. DRAMP00186 KRKCPKTPFDNTPGAWFAHLILGC 24 LSEI_2163 (m2163; Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Lactobacillus casei ATCC 334 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: mature LSEI_2163 peptide was a class IId bacteriocin that exhibited antimicrobial activity against some lactobacilli and several Listeria species. The activities of both peptides tolerat 121°C for 30 min but not treatment with proteinase K or trypsin. Gram-negative bacteria: Lactobacillus casei ATCC 393 (++), L. casei ATCC 27139 (++), Lactobacillus rhamnosus ATCC 21052 (+++++), L. rhamnosus ATCC 14957 (+), Lactobacillus plantarum ATCC 8014 (+), Listeria innocua ATCC 33091 (++), L. innocua CIP 78.44 (++), Listeria monocytogens ATCC 19112 (+++), Listeria welshimeri ATCC 43551 (++), Listeria seeligeri CIP79.46 (++++).##Note: + indistinct inhibit zone with diameter 8-12 mm, ++ indistinct inhibit zone with diameter ≥12 mm, +++ clear inhibit zone with diameter 12-16 mm, ++++ clear inhibit zone with diameter 16-20 mm, and +++++ clear inhibit zone with diameter ≥20 mm. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22688903 Appl Microbiol Biotechnol. 2012 Jun 12. Kuo YC, Liu CF, Lin JF, Li AC, Lo TC, Lin TH. Characterization of putative class II bacteriocins identified from a non-bacteriocin-producing strain Lactobacillus casei ATCC 334. DRAMP00187 DSIRDVSPTFNKIRRWFDGLFK 22 LSEI_2386 (m2386; Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Lactobacillus casei ATCC 334 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: mature LSEI_2386 was a putative pheromone peptide that also had significant bacteriocin activity against several Listeria species. The activities of both peptides tolerat 121°C for 30 min but not treatment with proteinase K or trypsin. Gram-negative bacteria: Listeria innocua ATCC 33091 (++++), L. innocua CIP 78.44 (++++), Listeria monocytogens ATCC 19112 (+++++), Listeria welshimeri ATCC 43551 (+++++), Listeria seeligeri CIP79.46 (+++++).##Note: ++++ clear inhibit zone with diameter 16-20 mm, and +++++ clear inhibit zone with diameter ≥20 mm. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22688903 Appl Microbiol Biotechnol. 2012 Jun 12. Kuo YC, Liu CF, Lin JF, Li AC, Lo TC, Lin TH. Characterization of putative class II bacteriocins identified from a non-bacteriocin-producing strain Lactobacillus casei ATCC 334. DRAMP00188 APAGLVAKFGRPIVKKYYKQIMQFIGEGSAINKIIPWIARMWRT 44 Enterocin RJ-11 (EntRJ-11; Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Enterococcus faecalis RJ-11 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Enterococcus faecalis RJ-11, Enterococcus sp. strain RB-3, Enterococcus sp. strain RJ-10, Enterococcus sp. strain SJ-16, Enterococcus sp. strain YJ-35, Enterococcus durans KB-60, Lactococcus lactis IFO12007, Leuconostoc mesenteroides IFO3426, Bacillus subtilis JCM1465, Bacillus amyloliquefaciens B1, Bacillus cereus B3, Listeria monocytogenes SUB635, Staphylococcus aureus SUB511. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14532021 Appl Environ Microbiol. 2003 Oct;69(10):5746-5753. Yamamoto Y, Togawa Y, Shimosaka M, Okazaki M. Purification and characterization of a novel bacteriocin produced by Enterococcus faecalis strain RJ-11. DRAMP00192 MRTGNAN 7 Microcin C7 (MccC7; Microcin C51, MccC51; Bacteriocin) Q47505 Belongs to the class I microcin mccA Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Beta strand Not found 3H5R, 3H9J, 3H9Q, 3H9G resolved by X-ray. Function: Inhibits protein translation by blocking aspartyl-tRNA synthetase Function: and inhibiting production of aminoacetylated tRNA-Asp. PTM: The peptide moiety allows entry into the bacterial cell, where it undergoes proteolytic cleavage to release the aspartyl adenylate analog, which is responsible for aspartyl-tRNA synthetase inhibition. Can be processed by the non-specific oligopeptidases pepA, pepB and pepN. Gram-negative bacteria: Enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, strains of Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet It targets the aspartyl-tRNA synthetase 17827970##17711420##19494832 J Mol Microbiol Biotechnol. 2007;13(4):200-209.##Mol Microbiol. 2007 Sep;65(6):1380-1394.##EMBO J. 2009 Jul 8;28(13):1953-1964. Duquesne S, Petit V, Peduzzi J, Rebuffat S.##Severinov K, Semenova E, Kazakov A, Kazakov T, Gelfand MS.##Regni CA, Roush RF, Miller DJ, Nourse A, Walsh CT, Schulman BA. Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.##Low-molecular-weight post-translationally modified microcins.##How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic. DRAMP00193 VGIGGGGGGGGGGSCGGQGGGCGGCSNGCSGGNGGSGGSGSHI 43 Microcin B17 (MccB17; Bacteriocin) P05834, Q7M024 Belongs to the class I microcin mcbA Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: This glycine-rich peptide antibiotic inhibits DNA replication in many enteric bacteria, that leads to induction of the SOS repair system, massive DNA degradation and cell death. B17 inhibits type II topoisomerase by trapping an enzyme - DNA cleavable complex. PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1846808##3329729 EMBO J. 1991 Feb;10(2):467-476.##Proteins. 1986 Nov;1(3):230-238. Viz¡n JL, Hern¡ndez-Chico C, del Castillo I, Moreno F.##Davagnino J, Herrero M, Furlong D, Moreno F, Kolter R. The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by Escherichia coli DNA gyrase.##The DNA replication inhibitor microcin B17 is a forty-three-amino-acid protein containing sixty percent glycine. DRAMP00194 GTPGFQTPDARVISRFGFN 19 Capistruin (Bacteriocin) No entry found Belongs to the class I microcin Not found Burkholderia thailandensis E264 (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Beta strand Not found Discovered by genome mining based on the known MccJ25-gene coding cluster McjABCD. Capistruin is endoded by the capABCD gene cluster, where capA encodes the precursor polypeptide, capB cleaves the presursor and is likely to promote the cyclization, capC encodes an enzyme that activates the side chain of Asp9 for cyclization, and capD encodes a immunity protein. Showed activity against closely related Burkholderia and Pseudomonas strains. Different from the lasso structure of MccJ25, where the N-terminal Gly forms an amide bond with the carboxyl group of Glu8, capistruin forms a 9-residue macrolactam ring formed between NH of Gly1 and the carboxylic side chain of Asp9. In addition, Arg15 is reponsible for the trapping of the tail in the ring structure. Burkholderia and Pseudomonas strains No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18671394 J Am Chem Soc. 2008 Aug 27;130(34):11446-11454. Knappe TA, Linne U, Zirah S, Rebuffat S, Xie X, Marahiel MA. Isolation and structural characterization of capistruin, a lasso peptide predicted from the genome sequence of Burkholderia thailandensis E264. DRAMP00195 ASGRDIAMAIGTLSGQFVAGGIGAAAGGVAGGAIYDYASTHKPNPAMSPSGLGGTIKQKPEGIPSEAWNYAAGRLCNWSPNNLSDVCL 88 Colicin-V (Microcin-V; Bacteriocin) P22522 Belongs to the class IIa microcin cvaC Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Colicin V kills sensitive cells by disrupting the membrane potential. It targets bacterial membranes and induces ion channel formation, leading to the disruption of the proton-motive force and hence ATP production. PTM: Contains one disulfide bond between 76-87." Gram-negative bacteria: Escherichia coli (also closely related bacteria), Enterobacteriaceae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8204625##7952189##2249654 Biochemistry. 1994 Jun 7;33(22):6911-6917.##Microbiology. 1994 Sep;140 (Pt 9):2383-2389.##EMBO J. 1990 Dec;9(12):3875-3884. Fath MJ, Zhang LH, Rush J, Kolter R.##H¥varstein LS, Holo H, Nes IF.##Gilson L, Mahanty HK, Kolter R. Purification and characterization of colicin V from Escherichia coli culture supernatants.##The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by Gram-positive bacteria.##Genetic analysis of an MDR-like export system: the secretion of colicin V. DRAMP00196 GDVNWVDVGKTVATNGAGVIGGAFGAGLCGPVCAGAFAVGSSAAVAALYDAAGNSNSAKQKPEGLPPEAWNYAEGRMCNWSPNNLSDVCL 90 Microcin L (MccL; Bacteriocin) Q841V4 Belongs to the class IIa microcin mclC Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Predicted Not found Not found It targets bacterial membranes and induces ion channel formation, leading to the disruption of the proton-motive force and hence ATP production. Gram-negative bacteria: Escherichia coli, Klebsiella oxytoca CIP666, Salmonella enterica serovar Agon, S. enterica serovar Braenderup, S. enterica serovar Brandenburg, S. enterica serovar Bredeney, S. enterica serovar Derby, S. enterica serovar Dublin, S. enterica serovar Enteritidis ATCC 13076, S. enterica serovar Hadar, S. enterica serovar Heildeberg, S. enterica serovar Indiana, S. enterica serovar Kottbus, S. enterica serovar Newport, S. enterica serovar St.Paul, S. enterica serovar Typhimurium CIP5858, S. enterica serovar Virchow, Shigella sonnei CIP5236, Shigella flexneri CIP5236, Pseudomonas aeruginosa CIP100720T, Pseudomonas aeruginosa ATCC 27853. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 14742202##12897830 Antimicrob Agents Chemother. 2004 Feb;48(2):505-513.##Can J Microbiol. 2003 May;49(5):357-361. Pons AM, Delalande F, Duarte M, Benoit S, Lanneluc I, Sabl© S, Van Dorsselaer A, Cottenceau G.##Sabl© S, Duarte M, Bravo D, Lanneluc I, Pons AM, Cottenceau G, Moreno F. Genetic analysis and complete primary structure of microcin L.##Wild-type Escherichia coli producing microcins B17, D93, J25, and L; cloning of genes for microcin L production and immunity. DRAMP00197 AGDPLADPNSQIVRQIMSNAAWGPPLVPERFRGMAVGAAGGVTQTVLQGAAAHMPVNVPIPKVPMGPSWNGSKG 74 Microcin 24 (Mcc24; Bacteriocin) Q46971 Belongs to the class IIa microcin mtfS Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Homology Not found Not found MOA: It targets bacterial membranes and induces ion channel formation, leading to the disruption of the proton-motive force and hence ATP production. Gram-negative bacteria: Escherichia coli, Salmonella typhimurium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. O'Brien G.J, Mahanty H.K. Complete nucleotide sequence of microcin 24 genetic region and analysis of a new ABC transporter. DRAMP00198 GGAPATSANAAGAAAIVGALAGIPGGPLGVVVGAVSAGLTTGIGSTVGSGSASSSAGGGS 60 Microcin H47 (MccH47; Bacteriocin) P62530, P62531, Q9RM53 Belongs to the class IIb microcin mchB Escherichia coli (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bactericidal antibiotic. Active on bacteria phylogenetically related to the producing strain. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10471561##11181394 Antimicrob Agents Chemother. 1999 Sep;43(9):2176-2182.##Antimicrob Agents Chemother. 2001 Mar;45(3):969-972. Rodr­guez E, Gaggero C, Lavi±a M.##Azpiroz MF, Rodr­guez E, Lavi±a M. The structural gene for microcin H47 encodes a peptide precursor with antibiotic activity.##The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V. DRAMP00199 MNLNGLPASTNVIDLRGKDMGTYIDANGACWAPDTPSIIMYPGGSGPSYSMSSSTSSANSGS 62 Microcin I47 (MccI47; Bacteriocin) No entry found Belongs to the class IIb microcin Not found Escherichia coli H47 (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16569859 Antimicrob Agents Chemother. 2006 Apr;50(4):1411-1418. Poey ME, Azpiroz MF, Lavi±a M. Comparative analysis of chromosome-encoded microcins. DRAMP00200 DGNDGQAELIAIGSLAGTFISPGFGSIAGAYIGDKVHSWATTATVSPSMSPSGIGLSSQFGSGRGTSSASSSAGSGS 77 Microcin M (MccM; Bacteriocin) No entry found Belongs to the class IIb microcin Not found Escherichia coli MC4100 (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Not found Not found All Belongs to the class IIb microcins such as MccE492 have a Ser-rich C-terminal region and they may carry a siderophore-type PTM. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Nat Prod Rep. 2007 Aug;24(4):708-734. Duquesne S, Destoumieux-Garz³n D, Peduzzi J, Rebuffat S. Microcins, gene-encoded antibacterial peptides from enterobacteria. DRAMP00202 SCTTCVCTCSCCTT 14 Thiocillin (Bacteriocin) P0C8P7, P0C8P6, Q812G9 Belongs to the thiocillin family Not found Bacillus cereus); also Bacillus badius Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has bacteriocidal activity against Gram-positive bacteria, but not against Gram-negative bacteria. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu). PTM: Maturation of thiazole and oxazole containing antibiot" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 819410##7328054 J Antibiot (Tokyo). 1976 Apr;29(4):366-374.##J Antibiot (Tokyo). 1981 Sep;34(9):1126-1136. Shoji J, Kato T, Yoshimura Y, Tori K.##Shoji J, Hinoo H, Wakisaka Y, Koizumi K, Mayama M. Structural studies on thiocillins I, II and III (studies on antibiotics from the genus Bacillus XXIX).##Isolation of three new antibiotics, thiocillins I, II and III, related to micrococcin P. Studies on antibiotics from the genus Bacillus. VIII. DRAMP00203 SCNCVCGFCCSCSP 14 Thiocillin GE2270 (Antibiotic GE2270; Bacteriocin) Q7M0J8 Belongs to the thiocillin family Not found Planobispora rosea (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: inhibits bacterial protein biosynthesis by preventing the formation of a stable complex between the elongation factor Tu (EF-Tu), GTP and tRNA, hindering the activation of EF-Tu. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1908853 J Antibiot (Tokyo). 1991 Jul;44(7):693-701. Selva E, Beretta G, Montanini N, Saddler G.S, Gastaldo L, Ferrari P, Lorenzetti R, Landini P, Ripamonti F, Goldstein B.P, Berti M, Montanaro L, Denaro M. Antibiotic GE2270 A: a novel inhibitor of bacterial protein synthesis. I. Isolation and characterization. DRAMP00205 CLGIGSCNDFAGCGYAVVCFW 21 Tricyclic peptide RP 71955 (Bacteriocin) P37046, Q7M104 Belongs to the class 1 lasso peptide Not found Streptomyces sp. (strain SP9440) (Gram-positive bacteria) Antimicrobial, Antiviral Protein level Beta strand Not found 1RPB, 1RPC resolved by NMR. Function: Active against HIV-1 virus in vitro. Virus: HIV-1 No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal between Cys1 and Asp9 Free Disulfide bonds between Cys1 and Cys 13,Cys 7 and Cys19. L No cytotoxicity information found Not found 8270499##8286361 J Antibiot (Tokyo). 1993 Nov;46(11):1756-1757.##Biochemistry. 1994 Jan 11;33(1):42-50. Helynck G, Dubertret C, Mayaux JF, Leboul J.##Fréchet D, Guitton JD, Herman F, Faucher D, Helynck G, Monegier du Sorbier B, Ridoux JP, James-Surcouf E, Vuilhorgne M. Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite.##Solution structure of RP 71955, a new 21 amino acid tricyclic peptide active against HIV-1 virus. DRAMP00206 KTYYGTNGVHCTKKSLWGKVRLKNVIPGTLCRKQSLPIKQDLKILLGWATGAFGKTFH 58 Acidocin A (Bacteriocin) Q48496 Not found acdA Lactobacillus acidophilus TK9201 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found Function: Acidocin A is active against closely related lactic acid bacteria and food-borne pathogens including Listeria monocytogenes. Gram-positive bacteria: Listeria monocytogenes, Clostridium sporogenes, Brochothrix thermosphacta, Lactobacillus fermentum, Lactobacillus delbrueckii subsp. Bulgaricus. Inmost other Lactobacillus species. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7793908 Appl Environ Microbiol. 1995 Mar;61(3):1061-1067. Kanatani K, Oshimura M, Sano K. Isolation and characterization of acidocin A and cloning of the bacteriocin gene from Lactobacillus acidophilus. DRAMP00207 IYWIADQFGIHLATGTARKLLDAVASGASLGTAFAAILGVTLPAWALAAAGALGATAA 58 Acidocin B (Bacteriocin) Q48499 Not found acdB Lactobacillus acidophilus M46 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Predicted Not found Not found 2MWR Function: Acidocin B is active against Listeria monocytogenes, Clostridium sporogenes, Brochothrix thermosphacta, Lactobacillus fermentum and Lactobacillus delbrueckii subsp. bulgaricus, but inactive against most other Lactobacillus species. Gram-positive bacteria: Listeria monocytogenes, Clostridium sporogenes, Brochothrix thermosphacta, Lactobacillus fermentum, Lactobacillus delbrueckii subsp. Bulgaricus. Inmost other Lactobacillus species. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 7551031 Microbiology. 1995 Jul;141 (Pt 7):1629-1635. Leer RJ, van der Vossen JM, van Giezen M, van Noort JM, Pouwels PH. Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus. DRAMP00208 KTHYPTNAWKSLWKGFWESLRYTDGF 26 Acidocin 8912 (Bacteriocin) Q48501, Q9R5H2 Not found acdT Lactobacillus acidophilus TK8912 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has a bactericidal effect on sensitive cells but not a bacteriolytic effect. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8554765##1368836 Lett Appl Microbiol. 1995 Dec;21(6):384-386.##Biosci Biotechnol Biochem. 1992 Aug;56(8):1212-1215. Kanatani K, Tahara T, Oshimura M, Sano K, Umezawa C.##Tahara T, Kanatani K, Yoshida K, Miura H, Sakamoto M, Oshimura M. Cloning and nucleotide sequence of the gene for acidocin 8912, a bacteriocin from Lactobacillus acidophilus TK8912.##Purification and some properties of acidocin 8912, a novel bacteriocin produced by Lactobacillus acidophilus TK8912. DRAMP00209 ANCSCSTASDYCPILTFCTTGTACSYTPTGCGTGWVYCACNGNFY 45 Fulvocin C (Bacteriocin) P01547 Not found Not found Myxococcus fulvus (Gram-negative bacteria) Unknown Protein level Not found Not found Function: Bacteriocin. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6783114 Biochim Biophys Acta. 1981 Jan 30;667(1):213-217. Tsai H, Hirsch HJ. The primary structure of fulvocin C from Myxococcus fulvus. DRAMP18336 ADRGWIKTLTKDCPNVISSICAGTIITACKNCA 33 Thermophilin 1277 (Bacteriocin) A7M695 Belongs to the lantibiotics family (Class I bacteriocin) tepA Streptococcus thermophilus SBT1277 Antimicrobial, Antibacterial, Anti-Gram+ Rich Peptide sequence analysis following chemical modification of thermophilin 1277 revealed that the Cys21 and Cys29 residues form a disulfide bridge and that Thr8 or Thr10 forms two 3-methyllanthionines with Cys13 or Cys32 via thioether bridges. Antimicrobial activity was disrupted by ethanethiol or reductive agent treatments, indicating that the internal amino acid modifications are crucial for the activity. It shares the same sequence with bovicin HJ50 prior to post-translational modifications. A followup study concluded at two rings and one disulfide bond . Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17381740 J Appl Microbiol. 2007 Apr;102(4):971-80. Kabuki T, Uenishi H, Watanabe M, Seto Y, Nakajima H. Characterization of a bacteriocin, Thermophilin 1277, produced by Streptococcus thermophilus SBT1277. DRAMP00211 GLGKAQCAALWLQCASGGTIGCGGGAVACQNYRQFCR 37 Sublancin-168 (Bacteriocin) P68578, O34781, O64033 Not found sunA Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta) Unknown Homology Not found Not found 2MIJ "Function: Bacteriocin active against Gram-positive bacteria. Inhibits B. cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells. Inhibits B.subtilis strain ATCC 6633 (By similarity). PTM: Production of active sublancin-168 requires at least one thiol-disulfide oxidoreductase (BdbB or, in its absence, BdbC). Membrane translocation and cleavage of the precursor are probably performed by SunT (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10376821 Microbiology. 1999 May;145 ( Pt 5):1055-1067. Lazarevic V, Düsterhöft A, Soldo B, Hilbert H, Mauël C, Karamata D. Nucleotide sequence of the Bacillus subtilis temperate bacteriophage SPbetac2. DRAMP00212 AVPAVRKTNETLD 13 Rhamnosin A (Bacteriocin) P86526 Not found Not found Lactobacillus rhamnosus strain 68 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against the Gram-positive bacterium: M. lysodeikticus, but not against Lactobacillus plantarum 8014 or Lact. plantarum 39268. It may act as a pore-forming protein, creating a channel in the cell membrane. Classification: Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin." Gram-positive bacterium: Micrococcus lysodeikticus ATCC 4698. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 19796123 J Appl Microbiol. 2009 Dec 1;107(6):2108-2015. Dimitrijević R, Stojanović M, Zivković I, Petersen A, Jankov RM, Dimitrijević L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. DRAMP00213 STPVLASVAVSMELLPTASVLYSDVAGCFKYSAKHHC 37 Lactocin S (Bacteriocin) P23826, Q48848, Q48858 Not found lasA Lactobacillus sakei L45 (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "MOA: The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor." Leuconostoc, Carnobacteria, Lactobacilli, Pediococci, Lactococci, Listeria monocytogenes, Listeria innocua, Staphylococcus, Bacillus cereus, Clostridium spp. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Deaminated Cyclization between S32 and C37 Two lanthionines(S32-C37,S23-C28) Mixed(D-Ala) No cytotoxicity information found Cell membrane 1872611##7961627 Appl Environ Microbiol. 1991 Jun;57(6):1829-1834.##J Biol Chem. 1994 Nov 4;269(44):27183-27185. M¸rtvedt CI, Nissen-Meyer J, Sletten K, Nes IF.##Skaugen M, Nissen-Meyer J, Jung G, Stevanovic S, Sletten K, Inger C, Abildgaard M, Nes IF. Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45.##In vivo conversion of L-serine to D-alanine in a ribosomally synthesized polypeptide. DRAMP00214 MVPTTFTLTTNNFLSDYQQLFI 22 Lactococcin K (Bacteriocin) No entry found Not found Not found Lactococcus lactis subsp. lactis MY23 Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16614924 Biotechnol Lett. 2006 Mar;28(5):357-362. Kim YS, Kim MJ, Kim P, Kim JH. Cloning and production of a novel bacteriocin, lactococcin K, from Lactococcus lactis subsp. lactis MY23. DRAMP00215 NRWYCNSAAGGVGGAAGCVLAGYVGEAKENIAGEVRKGWGMAGGFTHNKACKSFPGSGWASG 62 Enterocin E-760 (Bacteriocin) No entry found Not found Not found Enterococcus durans/faecium/hirae NRRL B-30745 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found The enterocin demonstrated thermostability by retaining activity after 5 min at 100 degrees C and was stable at pH values between 5.0 and 8.7. However, activity was lost below pH 3.0 and above pH 9.5. Gram-positive bacteria: Salmonella enterica serovar Enteritidis, S. enterica serovar Choleraesuis, S. enterica serovar Typhimurium, S. enterica serovar Gallinarum, Escherichia coli O157:H7, Yersinia enterocolitica, Citrobacter freundii, Klebsiella pneumoniae, Shigella dysenteriae, Pseudomonas aeruginosa, Proteus mirabilis, Morganella morganii, Staphylococcus aureus, Staphylococcus epidermidis, Listeria monocytogenes, Campylobacter jejuni, 20 other Campylobacter species isolates. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18086839 Antimic Agents Chemother 2008 Mar;52(3):1094-1100. Line JE, Svetoch EA, Eruslanov BV, Perelygin VV, Mitsevich EV, Mitsevich IP, Levchuk VP, Svetoch OE, Seal BS, Siragusa GR, Stern NJ. Isolation and purification of enterocin E-760 with broad antimicrobial activity against gram-positive and gram-negative bacteria DRAMP00216 AIKLVQSPNGNFAASFVLDGTKWIFKSKYYDSSKGYWVGIYEVWDRK 47 Antimicrobial peptide LCI (Bacteriocin) P82243 Not found Not found Bacillus subtilis (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Beta strand (4 strands; 27 residues) The solution structure of LCI has a novel topology, containing a four-strand antiparallel beta-sheet as the dominant secondary structure. 2B9K resolved by NMR. "Function: Has antibacterial activity against X.oryzae pv oryzae and R.solanacearum. May bind DNA or mRNA. Miscellaneous: Heat stable. Resistant to proteolysis by tryspin and pepsin, but susceptible to pronase E and proteinase K." X. oryzae pv oryzae, R. solanacearum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet DNA or mRNA PubMed ID is not available##21449609 Rice Genet. Newsl. 1990;7:151-154.##iochemistry. 2011 May 10;50(18):3621-3627. Liu JY, Pan NS, Chen ZL.##Xia, B, Gong, W, Lu, G. Characterization of an anti-rice bacterial blight polypeptide LCI.##Solution structure of LCI, an AMP from Bacillus subtilis. DRAMP00217 ASILTNAS 8 Bacteriocin P84703 Not found Not found Rhizobium leguminosarum bv. Viciae (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Function: Narrow spectrum bacteriocin, active against closely related bacterial species. Closely related bacterial species. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2005) to UniProtKB. Naeem F.I, Khan S.A, Mukhtar Z, Zafar Y, Malik K.A, Hafeez F.Y. Isolation and characterization of bacteriocin like protein from Rhizobium leguminosarum bv. viciae. DRAMP00219 YSLQMGATAIKQVKKLFKKWGW 22 PlnA-22 (Bacteriocin) No entry found Not found Not found Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Lactobacillus sake NCDO 2714 (IC50=40 nM), Lactobacillus plantarum 965 (IC50=300 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15805109 J Biol Chem. 2005 Jun 17;280(24):22945-22950. Kristiansen PE, Fimland G, Mantzilas D, Nissen-Meyer J. Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A. DRAMP00220 GATAIKQVKKLFKKWGW 17 PlnA-17 (Bacteriocin) No entry found Not found Not found Lactobacillus plantarum (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Lactobacillus sake NCDO 2714 (IC50=15 nM), Lactobacillus plantarum 965 (IC50=400 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15805109 J Biol Chem. 2005 Jun 17;280(24):22945-22950. Kristiansen PE, Fimland G, Mantzilas D, Nissen-Meyer J. Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A. DRAMP00221 DQMSDGVNYGKGSSLSKGGAKCGLGIVGGLATIPSGPLGWLAGAAGVINSCMK 53 Carnobacteriocin-A (Piscicolin-61; Bacteriocin) P38578 Not found cbnBA Carnobacterium piscicola (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity. PTM: Contains one disulfide bond 22-51." Gram-positive bacteria: Carnobacterium, Enterococcus, Listeria monocytogenes, Clostridium perfringens. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8012574##7764997 Microbiology. 1994 Mar;140 (Pt 3):517-526.##Curr Microbiol. 1994 Aug;29(2):63-68. Worobo RW, Henkel T, Sailer M, Roy KL, Vederas JC, Stiles ME.##Holck AL, Axelsson L, Schillinger U. Characteristics and genetic determinant of a hydrophobic peptide bacteriocin, carnobacteriocin A, produced by Carnobacterium piscicola LV17A.##Purification and cloning of piscicolin 61, a bacteriocin from Carnobacterium piscicola LV61. DRAMP18335 GNGVFKTISHECHLNTWAFLATCCS 25 Salivaricin G32(Bacteriocin) H6VLK4 Belongs to the lantibiotics family (Class I bacteriocin) slnA Streptococcus salivarius strain G32 Antimicrobial, Antibacterial, Anti-Gram+ Not found The first modified amino acid was found to be a dehydrobutyrine (Dhb) at position 8 that could form a beta-methyl-lanthionine bond with Cys13. A second beta-methyl-lanthionine formation between Dhb and Cys was found at positions 10 and 32, respectively. A disulfide bridge was between the two Cys residues at positions 21 and 29. The data is in accordance with the sequence analysis of bovicin HJ50 and thermophilin 1277. The inhibitory peptide differs from the Streptococcus pyogenes-produced SA-FF22 in the absence of lysine in position 2. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22567013##23122510 Int J Microbiol. 2012;2012:738503.##Food Microbiol. 2013 Feb;33(1):124-30. Wescombe PA, Dyet KH, Dierksen KP, Power DA, Jack RW, Burton JP, Inglis MA, Wescombe AL, Tagg JR.##Georgalaki M, Papadimitriou K, Anastasiou R, Pot B, Van Driessche G, Devreese B, Tsakalidou E. Salivaricin G32, a Homolog of the Prototype Streptococcus pyogenes Nisin-Like Lantibiotic SA-FF22, Produced by the Commensal Species Streptococcus salivarius.##Macedovicin, the second food-grade lantibiotic produced by Streptococcus macedonicus ACA-DC 198. DRAMP00224 KQQLATEAESAGPIL 15 BTL (Bacteriocin) No entry found Not found Not found Bacillus subtilis B-TL2 (Gram-positive bacteria) Antimicrobial, Antifungal Not found Not found Not found "Function: The peptide exhibits strong inhibitory activity against mycelial growth of Bipolaris maydis, Alternaria brassicae, Aspergillus niger, Cercospora personata. Biophysicochemical properties: The purified BTL displays thermostability, almost retaining 100% activity at 100 degrees C for 15 min." Fungi: Bipolaris maydis, Alternaria brassicae, Aspergillus niger, Cercospora personata. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18241956 Peptides. 2008 Mar;29(3):350-355. Zhang B, Xie C, Yang X. A novel small antifungal peptide from Bacillus strain B-TL2 isolated from tobacco stems. DRAMP00225 ILFSYLLFYVLKENSKREDKYQNIIEELTELLPKIKEDVEDIKEKLNK 48 Bacteriocin UviB P15936 Not found uviB Clostridium perfringens (Gram-positive bacteria) Antimicrobial, Antibacterial Transcript level Not found Not found Function: May have a role in bacteriocin secretion or immunity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2901768##2460717 Plasmid. 1988 Mar;19(2):134-150.##Mol Microbiol. 1988 Sep;2(5):607-614. Garnier T, Cole ST.##Garnier T, Cole ST. Complete nucleotide sequence and genetic organization of the bacteriocinogenic plasmid, pIP404, from Clostridium perfringens.##Studies of UV-inducible promoters from Clostridium perfringens in vivo and in vitro. DRAMP00226 NIPQLTPTP 9 Bioactive peptide 3 (BAP3; Curvalicin-28c; Bacteriocin) P84711 Not found Not found Lactobacillus curvatus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacteria and the Gram-positive bacteria. Has no antifungal activity against S.cerevisiae, Penicillium sp BKS-TAN2 or A.niger. PTM: Contains one disulfide bond." Gram-positive bacteria: Listeria monocytogenes, Lactococcus lactis subsp lactis and Lactobacillus curvatus H28. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Food Res. Intern. 2010;43:33-39. Ghalfi H, Benkerroum N, Ongena M, Bensaid M, Thonart P. Production of three anti-listerial peptides by Lactobacillus curvatus in MRS broth. DRAMP00227 VAPFPEQFLX 10 Bioactive peptide 2 (BAP2;Curvalicin-28b; Bacteriocin) P84710 Not found Not found Lactobacillus curvatus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has antibacterial activity. Has no antifungal activity against S. cerevisiae, Penicillium sp BKS-TAN2 or A. niger. Gram-positive bacteria: Listeria monocytogenes, Lactococcus lactis subsp lactis and Lactobacillus curvatus H28. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Food Res. Intern. 2010;43:33-39. Ghalfi H, Benkerroum N, Ongena M, Bensaid M, Thonart P. Production of three anti-listerial peptides by Lactobacillus curvatus in MRS broth. DRAMP00228 TPVVNPPFLQQT 12 Bioactive peptide 1 (BAP1; Curvalicin-28a; Bacteriocin) P84709 Not found Not found Lactobacillus curvatus (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has antibacterial activity. Has no antifungal activity against S. cerevisiae, Penicillium sp BKS-TAN2 or A. niger. Gram-positive bacteria: Listeria monocytogenes, Lactococcus lactis subsp lactis and Lactobacillus curvatus H28. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Food Res. Intern. 2010;43:33-39. Ghalfi H, Benkerroum N, Ongena M, Bensaid M, Thonart P. Production of three anti-listerial peptides by Lactobacillus curvatus in MRS broth. DRAMP00229 KPAWCWYTLAMCGAGYDSGTCDYMYSHCFGVKHSSGGGGSYHC 43 Bacteriocin plantarican ASM1 (PASM1; Bacteriocin) C7G1H4 Not found bactA1 Lactobacillus plantarum A-1 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found 2MVI "Function: Bacteriocin with a narrow antibacterial spectrum. Has Antibacterial activity. Biophysicochemical properties: pH dependence (Stable from pH 5.5-8.5); Temperature dependence (Thermostable, activity is retained after incubation at 90degrees Celsius for 15 minutes). PTM: Contains two disulfide bonds." Gram-positive bacteria: Lactobacillus plantarum, L. pentosus, L. curvatus, L. lindneri, Leuconostoc mesenteroides and Enterococcus faecalis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19939484 Int J Food Microbiol. 2010 Jan 31;137(1):94-99. Hata T, Tanaka R, Ohmomo S. Isolation and characterization of plantaricin ASM1: a new bacteriocin produced by Lactobacillus plantarum A-1. DRAMP00230 GSQLVYREWVGHSNVIKP 18 Lariatins A (lasso peptide; Bacteriocin) No entry found Not found Not found Rhodococcus jostii K01-B0171 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Mycobacterium smegmatis and Mycobacterium tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16756302 J Am Chem Soc. 2006 Jun 14;128(23):7486-7891. Iwatsuki M, Tomoda H, Uchida R, Gouda H, Hirono S, Omura S. Lariatins, antimycobacterial peptides produced by Rhodococcus sp. K01-B0171, have a lasso structure. DRAMP00231 GSQLVYREWVGHSNVIKGPP 20 Lariatins B (lasso peptide; Bacteriocin) No entry found Not found Not found Rhodococcus jostii K01-B0171 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Mycobacterium smegmatis and Mycobacterium tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16756302 J Am Chem Soc. 2006 Jun 14;128(23):7486-7891. Iwatsuki M, Tomoda H, Uchida R, Gouda H, Hirono S, Omura S. Lariatins, antimycobacterial peptides produced by Rhodococcus sp. K01-B0171, have a lasso structure. DRAMP00233 ISLEICXIFHDN 12 Lichenin (Bacteriocin-like) P82907 Not found Not found Bacillus licheniformis (Gram-positive bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Residue A7 is uncertain. Has antibacterial activity only against strictly anaerobic rumen bacteria. Biophysicochemical properties: pH dependence (Optimum pH is 6.8); Temperature dependence (Optimum temperature is 39 degrees Celsius)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11576300##15881839 J Appl Microbiol. 2001 Oct;91(4):636-645.##Microbiol Res. 2005;160(2):213-218. Pattnaik P, Kaushik JK, Grover S, Batish VK.##Pattnaik P, Grover S, Batish VK. Purification and characterization of a bacteriocin-like compound (Lichenin) produced anaerobically by Bacillus licheniformis isolated from water buffalo.##Effect of environmental factors on production of lichenin, a chromosomally encoded bacteriocin-like compound produced by Bacillus licheniformis 26L-10/3RA. DRAMP00234 DIGGSRQGCVA 11 Trifolitoxin (TFX; Bacteriocin) P42723 Not found tfxA Rhizobium leguminosarum bv. Trifolii T24 (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibiotic whose production provides the bacteria a mechanism of host root nodule competitiveness with other invading inefficient strains. PTM: Synthesized ribosomally as a prepeptide that is post-translationally modified to the active peptide. TfxB, TfxD and TfxF are all required for this processing.The chromophore is probably a six-membered ring derived from the cyclization of Gln-38. Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings. Biophysicochemical properties: pH dependence (Sensitive to extremes of pH); Temperature dependence (Thermostable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8509324 J Bacteriol. 1993 Jun;175(12):3693-3702. Breil BT, Ludden PW, Triplett EW. DNA sequence and mutational analysis of genes involved in the production and resistance of the antibiotic peptide trifolitoxin. DRAMP00235 MINRTDCNENSYLEIHNNEGRDTLCFANAGTMPVAIYGVNWVESGNNVVTLQFQRNLSDPRLETITLQKWGSWNPGHIHEILSIRIY 87 AFP1 (Bacteriocin) No entry found Not found Not found Streptomyces tendae Tu901 (Gram-positive bacteria) Antimicrobial, Antifungal Not found Combine helix and strand structure Mature AFP1 comprises 86 residues and contains two antiparallel beta-sheets (five and four beta-strands each), that pack against each other in a parallel beta-sandwich. 1G6E resolved by NMR. Function: AFP1 is a recently discovered anti-fungal, chitin-binding protein. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10601197##11350173 J Bacteriol. 1999 Dec;181(24):7421-7429.##J Mol Biol. 2001 May 11;308(4):765-782. Bormann C, Baier D, Hörr I, Raps C, Berger J, Jung G, Schwarz H.##Campos-Olivas R, Hörr I, Bormann C, Jung G, Gronenborn AM. Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae T¼901 that interferes with growth polarity.##Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901. DRAMP00236 SDCNINSNTAADVILCFNQVGSCALCSPTLVGGPVP 36 Halocin-S8 (HalS8; Bacteriocin) Q9HHA8 Not found halS8 Haloarchaeon S8a Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity. Miscellaneous: Halocin-S8 is quite robust, as it can be desalted, boiled, subjected to organic solvents, and stored at 4 degrees Celsius for extended periods without losing activity." Gram-positive bacteria: Halobacterium salinarum NRC817, Halobacterium GRB and Haloferax gibbonsii. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10940040 J Bacteriol. 2000 Sep;182(17):4951-4958. Price LB, Shand RF. Halocin S8: a 36-amino-acid microhalocin from the haloarchaeal strain S8a. DRAMP00237 DIDITGCSACKYAAG 15 Halocin-C8 (HalC8; Bacteriocin) P83716 Not found Not found Halobacterium sp. (strain AS7092) Antimicrobial, Antibacterial Protein level Not found Not found MOA: Causes cell lysis and death, possibly by disrupting the cell wall. boiled, subjected to organic solvents, and stored at 4 degrees Celsius for extended periods without losing activity. A wide variety of haloarchaeons. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell wall 12811620 Extremophiles. 2003 Oct;7(5):401-407. Li Y, Xiang H, Liu J, Zhou M, Tan H. Purification and biological characterization of halocin C8, a novel peptide antibiotic from Halobacterium strain AS7092. DRAMP00238 YTAKQCLQAIGSCGIAGTGAGAAGGPAGAFVGAXVVXI 38 Curvaticin FS47 (Bacteriocin) P80323 Not found Not found Lactobacillus curvatus FS47 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has bacteriocin activity. Gram-positive bacteria: Listeria monocytogenes, Pediococcus, Enterococcus, Lactobacilli and Bacilli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8031103 Appl Environ Microbiol. 1994 Jun;60(6):2191-2195. Garver KI, Muriana PM. Purification and partial amino acid sequence of curvaticin FS47, a heat-stable bacteriocin produced by Lactobacillus curvatus FS47. DRAMP00239 TPGGIDFISGGPHVAQDVLNAIKNFFK 27 Enterocin NKR-5-3D (Bacteriocin) No entry found Not found Not found Enterococcus faecium NKR-5-3 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22738965 Biosci Biotechnol Biochem. 2012 May 23;76(5):947-953. Ishibashi N, Himeno K, Fujita K, Masuda Y, Perez RH, Zendo T, Wilaipun P, Leelawatcharamas V, Nakayama J, Sonomoto K. Purification and characterization of multiple bacteriocins and an inducing peptide produced by Enterococcus faecium NKR-5-3 from Thai fermented fish. DRAMP00240 MRKEFHNVLSSGQLLADKRPARDYNRK 27 Pep27 (Bacteriocin) No entry found Not found Not found Streptococcus pneumoniae (Gram-negative bacteria) Antibacterial, Anti-cancer, Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of Anti-cancer peptide Pep27 analogues. DRAMP00241 KKXXKKVAXTWGNAATAAASGAVKGILG 28 Brevicin 27 (Bacteriocin) No entry found Not found Not found Lactobacillus brevis SB27 (Gram-positive bacteria) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9009071 Curr Microbiol. 1997 Mar;34(3):173-179. Benoit V, Lebrihi A, Milli¨re JB, Lefebvre G. Purification and partial amino acid sequence of brevicin 27, a bacteriocin produced by Lactobacillus brevis SB27. DRAMP00242 XXKEIXHIFHDN 12 Subpeptin JM4-B (Bacteriocin) P83879 Not found Not found Bacillus subtilis JM4 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive and Gram-negative bacteria. Developmental stage: Expressed from the mid-exponential phase, maximum activity is reached at the stationary phase." Gram-positive bacteria: Salmonella, Bacillus cereus, Bacillus megaterium, Lactobacillus casei, Leptostylus viridescens, Myotis flavus, Corynebacterium glutamicum, Corynebacterium crenatum, Leuconostoc mesenteroides, Enterococcus faecalis, Shigella flexneri, Staphylococcus aureus and Bacillus thuringiensis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16211432 Curr Microbiol. 2005 Nov;51(5):292-296. Wu S, Jia S, Sun D, Chen M, Chen X, Zhong J, Huan L. Purification and characterization of two novel antimicrobial peptides Subpeptin JM4-A and Subpeptin JM4-B produced by Bacillus subtilis JM4. DRAMP00243 XXKEIXWIFHDN 12 Subpeptin JM4-A (Bacteriocin) P83878 Not found Not found Bacillus subtilis JM4 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive and Gram-negative bacteria. Developmental stage: Expressed from the mid-exponential phase, maximum activity is reached at the stationary phase. Biophysicochemical properties: pH dependence (Active from pH 2.0 to 8.0. Retains some activity up to pH 12.0); Temperature dependence (Active from 20 to 100 degrees Celsius)." Gram-positive bacteria: Salmonella, Bacillus cereus, Bacillus megaterium, Lactobacillus casei, Leptostylus viridescens, Lactobacillus plantarum CGMCC 1.3, Myotis flavus, Corynebacterium glutamicum, Corynebacterium crenatum, Leuconostoc mesenteroides, Bacillus thuringiensis, Streptococcus faecalis CGMCC. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16211432 Curr Microbiol. 2005 Nov;51(5):292-296. Wu S, Jia S, Sun D, Chen M, Chen X, Zhong J, Huan L. Purification and characterization of two novel antimicrobial peptides Subpeptin JM4-A and Subpeptin JM4-B produced by Bacillus subtilis JM4. DRAMP00245 VGALAVVVWLWLWLW 15 Gramicidin A (GA; Nonribosomally synthesized bacteriocin) No entry found Not found Not found Bacillus brevis (soil bacterium) (Gram-positive bacteria) Antimicrobial, Antbacterial, Antiviral Not found Beta strand (1 strands; 13 residues) Amino acids 4, 6, 8, 10, and 12 are D-amino acids, allowing the formation of a special helical structure that head-to-head dimerizes into a cation channel in lipid bilayer with the C-terminus exposed. Structures solved in organic solvents by x-ray diffraction are believed to be non-channel forms. 1MAG resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19870884##8810522 J Exp Med. 1939 Jun 30;70(1):1-10.##J Biomol NMR. 1996 Jul;8(1):1-14. Dubos RJ.##Ketchem RR, Lee KC, Huo S, Cross TA. STUDIES ON A BACTERICIDAL AGENT EXTRACTED FROM A SOIL BACILLUS : I. PREPARATION OF THE AGENT. ITS ACTIVITY IN VIT.##Macromolecular structural elucidation with solid-state NMR-derived orientational constraints. DRAMP00246 VGALAVVVWLFLWLW 15 Gramicidin B (GB; Bacteriocin) No entry found Not found Not found Bacillus brevis (soil bacterium) (Gram-positive bacteria) Antimicrobial, Antbacterial, Antiviral Not found Beta strand (1 strands; 13 residues) Not found 1JO3 resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11570868 Biochemistry 2001; 40: 11676-11686. Townsley, L.E, Tucker, W.A, Sham, S, Hinton, J.F. Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. DRAMP00247 VGALAVVVWLYLWLW 15 Gramicidin C (GC; Bacteriocin) No entry found Not found Not found Bacillus brevis (soil bacterium) (Gram-positive bacteria) Antimicrobial, Antbacterial, Antiviral Not found Beta strand (1 strands; 13 residues) Not found 1JO4 resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11570868 Biochemistry 2001; 40: 11676-11686. Townsley, L.E, Tucker, W.A, Sham, S, Hinton, J.F. Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. DRAMP00248 KPAWCWYTLAMCGAGYDSGTCDYMYSHCFGIKHHSSGSSSYHC 43 Glycocin F (GccF; S-glycosylated bacteriocin) E9K9Z1 Not found gccF Lactobacillus plantarum KW30 (Gram-positive bacteria) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (2 helices; 16 residues) Glycocin F is a 43-amino acid bacteriocin, which contains two beta-linked N-acetylglucosamine moieties, attached via side chain linkages to a serine via oxygen, and to a cysteine via S-linked sugar. The peptide conformation consists primarily of two alpha-helices held together by a pair of nested disulfide bonds. 2KUY resolved by NMR. "Function: Has antibacterial activity. PTM: Contains two disulfide bonds 5-28; 12-21." Gram-positive bacterium: Lactobacillus plantarum ATCC 8014 (IC50=2 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21395300##21251913 Biochemistry. 2011 Apr 12;50(14):2748-2755.##FEBS Lett. 2011 Feb 18;585(4):645-650. Venugopal H, Edwards PJ, Schwalbe M, Claridge JK, Libich DS, Stepper J, Loo T, Patchett ML, Norris GE, Pascal SM.##Stepper J, Shastri S, Loo TS, Preston JC, Novak P, Man P, Moore CH, Havl­?ek V, Patchett ML, Norris GE. Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin.##Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. DRAMP00249 YSLQMGATAIKQVKKLFKKKGG 22 Pln149 (Plantaricin 149; Bacteriocin; Derivatives: Pln149a) No entry found Not found Not found Lactobacillus plantarum NRIC 149 (Gram-positive bacteria) Antimicrobial, Antibacterial, Antifungal Not found Alpha helix Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 17266050 J. Fermentation Bioeng. 1994;77(3):277-282. Kato T, Matsuda T, Ogawa E, Ogawa H, Kato H, Doi U. Plantaricin-149, a bacteriocin produced by Lactobacillus plantarum NRIC 149. DRAMP00250 DYHHGVRVL 9 Bacteriocin serracin-P 43 kDa subunit (Bacteriocin) P83375 Not found Not found Serratia plymuthica (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Major component of a prophage tail sheath. Antibacterial activity against Gram-negative bacteria E.amylovora. Gram-negative bacterium: Erwinia amylovora. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12406768 Appl Environ Microbiol. 2002 Nov;68(11):5704-5710. Jabrane A, Sabri A, Comp¨re P, Jacques P, Vandenberghe I, Van Beeumen J, Thonart P. Characterization of serracin P, a phage-tail-like bacteriocin, and its activity against Erwinia amylovora, the fire blight pathogen. DRAMP00251 ALPKKLKYLNLFNDGFNYMGVV 22 Bacteriocin serracin-P 23 kDa subunit (Bacteriocin) P83378 Not found Not found Serratia plymuthica J7 (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Major component of a prophage tail tube. Antibacterial activity against Gram-negative bacteria E.amylovora. Gram-negative bacterium: Erwinia amylovora. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12406768 Appl Environ Microbiol. 2002 Nov;68(11):5704-5710. Jabrane A, Sabri A, Comp¨re P, Jacques P, Vandenberghe I, Van Beeumen J, Thonart P. Characterization of serracin P, a phage-tail-like bacteriocin, and its activity against Erwinia amylovora, the fire blight pathogen. DRAMP00252 VNPSYRLDPESRPQCEAHCGQLGMRLGAIVIMGTATGCVCEPKEAATPESR 51 AdDLP (A. dehalogenans defensin-like peptide; Bacteriocin) No entry found Not found Not found Anaeromyxobacter dehalogenans (Gram-negative bacteria) Antibacterial, Antifungal, Antiparasitic, Antimicrobial Not found Not found Circular dichroism (CD) analysis indicates that recombinant AdDLP adopts a typical structural feature of eukaryotic defensins, which is also consistent with an ab initio structure model predicted using I-TASSER algorithm. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19615342 Biochem Biophys Res Commun. 2009 Sep 18;387(2):393-398. Gao B, Rodriguez MD, Lanz-Mendoza H, Zhu S. AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity. DRAMP00253 DAPGHPGKHYLQVNVPSDVRTIGVAGGGVQQCFRVTPGAWNDTRALVSNGAQVEVWGYTVADCANRTTANQKYYDKAAAPSDSSTYFWFTLKNLRV 96 Ipomicin (Bacteriocin) No entry found Not found Not found sweet potato pathogen); also Streptomyces ipomoeae (Gram-negative bacteria) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12676701 Appl Environ Microbiol. 2003 Apr;69(4):2201-2208. Zhang X, Clark CA, Pettis GS. Interstrain inhibition in the sweet potato pathogen Streptomyces ipomoeae: purification and characterization of a highly specific bacteriocin and cloning of its structural gene. DRAMP00256 KGILGKLGVVQAGVDFVSGVWAGIKQSAKDHPNA 34 Divergicin 750 (Bacteriocin) Q46597 Not found dvn750 Carnobacterium divergens (Lactobacillus divergens) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8869500 FEMS Microbiol Lett. 1996 Feb 15;136(2):163-168. Holck A, Axelsson L, Schillinger U. Divergicin 750, a novel bacteriocin produced by Carnobacterium divergens 750. DRAMP00257 MAAFMKLIQFLATKGQKYVSLAWKHKGTILKWINAGQSFEWIYKQIKKLWA 51 Bacteriocin O85756 Not found brcA Brochothrix campestris Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9835559 Appl Environ Microbiol. 1998 Dec;64(12):4757-4766. McCormick JK, Poon A, Sailer M, Gao Y, Roy KL, McMullen LM, Vederas JC, Stiles ME, Van Belkum MJ. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. DRAMP00258 MAGFLKVVQILAKYGSKAVQWAWANKGKILDWINAGQAIDWVVEKIKQILGIK 53 Lacticin Z (Bacteriocin) A7M6Q0 Not found lnqZ Lactococcus lactis Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17690480 Biosci Biotechnol Biochem. 2007 Aug;71(8):1984-1992. Iwatani S, Zendo T, Yoneyama F, Nakayama J, Sonomoto K. Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14. DRAMP00259 MQKPEIISADLGLCAVNEFVALAAIPGGAATFAVCQMPNLDEIVSNAAYV 50 Bacteriocin boticin B Q9KGZ4 Not found btcB Clostridium botulinum Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11097932 Appl Environ Microbiol. 2000 Dec;66(12):5480-5483. Dineen SS, Bradshaw M, Johnson EA. Cloning, nucleotide sequence, and expression of the gene encoding the bacteriocin boticin B from Clostridium botulinum strain 213B. DRAMP00260 TYYGNGLYCNKEKCWVDWNQAKGEIGKIIVNGWVNH 36 Bacteriocin (Class IIa sec-dependent bacteriocin) Q27HG2 Belongs to the Class IIa sec-dependent bacteriocin bacA Enterococcus faecium (Streptococcus faecium) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16820469 Appl Environ Microbiol. 2006 Jul;72(7):4761-4766. De Kwaadsteniet M, Fraser T, Van Reenen CA, Dicks LM. Bacteriocin T8, a novel class IIa sec-dependent bacteriocin produced by Enterococcus faecium T8, isolated from vaginal secretions of children infected with human immunodeficiency virus. DRAMP00261 GSGPTYCWNEANNPGGPNRCSNNKQCDGARTCSSSGFCQGTSRKPDPGPKGPTYCWDEAKNPGGPNRCSNSKQCDGARTCSSSGFCQGTAGHAAA 95 Antiviral lectin scytovirin (SVN) P86041 Not found Not found Scytonema varium (cyanobacterium) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 2QT4 resolved by X-ray. "Function: Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin. PTM: Contains five disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12614152##16647158##17965185 Biochemistry. 2003 Mar 11;42(9):2578-2584.##Peptides. 2006 Jul;27(7):1668-1675.##Protein Sci. 2007 Dec;16(12):2756-2760. Bokesch HR, O'Keefe BR, McKee TC, Pannell LK, Patterson GM, Gardella RS, Sowder RC 2nd, Turpin J, Watson K, Buckheit RW Jr, Boyd MR.##Xiong C, O'Keefe BR, Byrd RA, McMahon JB.##Moulaei T, Botos I, Ziółkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A. A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium.##Potent anti-HIV activity of scytovirin domain 1 peptide.##Atomic-resolution crystal structure of the antiviral lectin scytovirin. DRAMP00262 LGKFSQTCYNSAIQGSVLTSTCERTNGGYNTSSIDLNSVIENVDGSLKWQPSNFIETCRNTQLAGSSELAAECKTRAQQFVSTKINLDDHIANIDGTLKYE 101 Cyanovirin-N (CV-N) P81180 Belongs to the cyanovirin-N family Not found Nostoc ellipsosporum (cyanobacterium) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 2EZM resolved by NMR. "Function: Mannose-binding lectin. Biotechnological use: Overexpression of this protein to provide quantities adequate for medical use as a topical microbiocide has been attempted in a number of systems including E.coli, Lactobacillus jensenii, the yeast Pichia pastoris and Nicotiana tabacum. One fusion construct for overexpression of this protein can be found in entry AC D1WFZ2. Miscellaneous: Its activity in situ is Not found, however it acts as a viral entry inhibitor, inhibiting HIV-1, HIV-2 and simian immunodeficiency virus (and some other viruses such as feline immunodeficiency virus, measles virus and human herpesvirus) infection and replication. It prevents essential interactions between the envelope glycoprotein and target cell receptors by binding to carbohydrates on viral protein gp120 and possibly by other mechanisms as well. Addition to cells must occur before or shortly after virus addition. It also inhibits cell-to-cell fusion, and virus-to-cell and cell-to-cell transmission of a viral infection. Is remarkably stabile; the protein can withstand multiple freeze-thaw cycles, dissolution in organic solvents, treatment with salt, detergent, H2O2 and boiling without significant loss of anti-HIV activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9210678##9665171 Antimicrob Agents Chemother. 1997 Jul;41(7):1521-1530.##Nat Struct Biol. 1998 Jul;5(7):571-578. Boyd MR, Gustafson KR, McMahon JB, Shoemaker RH, O'Keefe BR, Mori T, Gulakowski RJ, Wu L, Rivera MI, Laurencot CM, Currens MJ, Cardellina JH 2nd, Buckheit RW Jr, Nara PL, Pannell LK, Sowder RC 2nd, Henderson LE.##Bewley CA, Gustafson KR, Boyd MR, Covell DG, Bax A, Clore GM, Gronenborn AM. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development.##Solution structure of cyanovirin-N, a potent HIV-inactivating protein. DRAMP00263 GWWNSWGKCVAGTIGGAGTGGLGGAAAGSAVPVIGTGIGGAIGGVSGGLTGAATFC 56 Bacteriocin cerein 7B Q2MDB2 Not found cer7B Bacillus cereus Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16451187 FEMS Microbiol Lett. 2006 Jan;254(1):108-115. Oscáriz JC, Cintas L, Holo H, Lasa I, Nes IF, Pisabarro AG. Purification and sequencing of cerein 7B, a novel bacteriocin produced by Bacillus cereus Bc7. DRAMP00264 EQCREEEDDR 10 Coconut antifungal peptide (Plants) No entry found Not found Not found Cocos nucifera Antimicrobial, Antifungal, Antiviral Not found Not found Not found Function: Also has HIV-1 reverse transcriptase activity (IC50=52.5 µM) Fungi: Fusarium oxysporum, Mycosphaerella arachidicola (IC50=1.2 µM), Physalospora piricola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16308082 Peptides. 2005 Dec;26(12):2392-2396. Wang HX, Ng TB. An antifungal peptide from the coconut. DRAMP00265 EALYNSEDLYEETSDSDD 18 Putative antimicrobial protein 1 (Ls-AMP1; Plant defensin) P86895 Not found Not found Lippia sidoides (Pepper-rosmarin) Antimicrobial, Antifungal Protein level Not found Not found "Function: May possess antifungal activity. Caution: Antifungal activity was tested using a fraction containing a number of different peptides. It is not clear which peptide actually has antifungal activity." Fungi: Botrytis cinerea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21210197 Protein J. 2011 Jan;30(1):32-38. Moreira JS, Almeida RG, Tavares LS, Santos MO, Viccini LF, Vasconcelos IM, Oliveira JT, Raposo NR, Dias SC, Franco OL. Identification of botryticidal proteins with similarity to NBS-LRR proteins in rosemary pepper (Lippia sidoides Cham.) flowers. DRAMP00266 SPPEAAYGPGNTNSDSGDK 19 Putative antimicrobial protein 2 (Ls-AMP2; Plant defensin) P86896 Not found Not found Lippia sidoides (Pepper-rosmarin) Antimicrobial, Antifungal Protein level Not found Not found "Function: May possess antifungal activity. Caution: Antifungal activity was tested using a fraction containing a number of different peptides. It is not clear which peptide actually has antifungal activity." Fungi: Botrytis cinerea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21210197 Protein J. 2011 Jan;30(1):32-38. Moreira JS, Almeida RG, Tavares LS, Santos MO, Viccini LF, Vasconcelos IM, Oliveira JT, Raposo NR, Dias SC, Franco OL. Identification of botryticidal proteins with similarity to NBS-LRR proteins in rosemary pepper (Lippia sidoides Cham.) flowers. DRAMP00267 ESGINLQGDATLANN 15 Antifungal lectin AMML (AMML; Plant defensin) P85004 Not found Not found Astragalus mongholicus (Huang qi) (Astragalus membranaceus varmongholicus) Antimicrobial, Antifungal Protein level Not found Not found "Function: Lectin that binds strongly to galactose, lactose, D-raffinose, L-rhamnose and cellobiose, and less strongly to D-glucose, D-xylose and L-arabinose. Does not bind D-galacturonic acid, D-fructose, D-mannose, D-ribose, L-sorbose, maltose and sucrose. Has hemagglutinating activity towards human type O and rabbit erythrocytes. Has strong antifungal activity against B. cinera, and weaker antifungal activity against D. turcia, F. oxysporum and Colletorichum sp. but not against Rhizoctonia solani and Mycosphaerella arachidicola. Miscellaneous: Hemagglutinating activity stable when incubated at 65 degrees Celsius for 30 minutes. Hemagglutinating activity is reduced by 50% when incubated at 75 degrees Celsius for 30 minutes and is abolished by incubation at 85 degrees Celsius for 30 minutes. Hemagglutinating activity is stable between pH 4.5 and 7.5, but is completely inhibited by incubation below pH 3.0 or above pH 10." Fungi: Botrytis cinerea (IC50=1.2 µM), Drechslera turcia, Fusarium oxysporum and Colletorichum sp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Galactose and Glucose 16140255 Arch Biochem Biophys. 2005 Oct 1;442(1):72-81. Yan Q, Jiang Z, Yang S, Deng W, Han L. A novel homodimeric lectin from Astragalus mongholicus with antifungal activity. DRAMP00268 QGIGVGDNDGKRGKR 15 Antifungal protein Pr-2 (Pr-2; Plant defensin) P86796 Not found Not found Cucurbita maxima (Pumpkin) (Winter squash) Antimicrobial, Antifungal Protein level Not found Not found Function: Has strong antifungal activity. Lacks antifungal activity against P.verrucosum var. verrucosum. Lacks antibacterial activity against the Gram-negative bacterium E.coli and against the Gram-positive bacterium S.aureus. Has very low hemolytic activity against human erythrocytes. Increases fungal cell membrane permeability, probably by disrupting the membrane structure. [Ref.19807165]Fungi: Botrytis cinerea (EC50=20 µM), Candida albicans (EC50=20 µM), Colletotrichum coccodes (EC50=10 µM), Fusarium oxysporum (EC50=10 µM), Fusarium solani (EC50=10 µM), Trichoderma harzianum (EC50=20 µM), Trichoderma viride (EC50=20 µM), Aspergillus fumigatus EC50=40 µM), Aspergillus parasiticus (EC50=80 µM), Didymella bryoniae (EC50=40 µM). [Ref:19807165]0% hemolytic activity at 80 µM and 8% hemolytic activity at 160 µM against huamn red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19807165 J Agric Food Chem. 2009 Oct 14;57(19):9299-9304. Park SC, Kim JY, Lee JK, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y. Antifungal mechanism of a novel antifungal protein from Pumpkin rinds against various fungal pathogens. DRAMP00269 LDSLSFSYNNFEEDD 15 Antifungal protein 1 (GAFP-1; Plant defensin) P86920 Not found Not found Arachis hypogaea (Peanut) Antimicrobial, Antifungal Protein level Not found Not found Function: Has strong antifungal activity against fungal phytopathogens. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2011) to UniProtKB Indira S. GAFP-1 from roots of Arachis hypogeae L. DRAMP00270 ATFTIRNNCPYTIWAAAVPGGGRRLNSGGTWTINVAPGTA 40 Osmotin (CpOsm; Plant defensin) P86363 Belongs to the thaumatin family Not found Calotropis procera (Roostertree) (Asclepias procera) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity. Miscellaneous: On the 2D-gel the determined pI of isoform 1 is: 8.9, its MW is: 22 kDa. On the 2D-gel the determined pI of isoform 2 is: 9.1, its MW is: 22 kDa." Fungi: Fusarium solani (IC50=67.0 µg/ml), Colletotrichum gloeosporioides (IC50=32.1 µg/ml), Neurospora isolate (IC50=57.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21334906 Plant Physiol Biochem. 2011 Jul;49(7):738-743. de Freitas CD, Nogueira FC, Vasconcelos IM, Oliveira JT, Domont GB, Ramos MV. Osmotin purified from the latex of Calotropis procera: Biochemical characterization, biological activity and role in plant defense. DRAMP00271 ATFTIRNNXPYTVWAAASPGGGRRLDMARIWGRTNXNFD 39 Osmotin-like protein (Thaumatin-like protein; Plant defensin) P83491 Belongs to the thaumatin family Not found Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) Antimicrobial, Antifungal Protein level Not found Not found "Function: May be an important antifungal protein. PTM: Contains intrachain disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Physiol. Biochem. 2001;39:1047-1055. Subroto T, de Vries H, Schuringa J.J, Soedjanaatmadja U.M.S, Hofsteenge J, Jekel P.A, Beintema J.J. Enzymic and structural studies on processed proteins from the vacuolar (lutoid-body) fraction of latex of Hevea brasiliensis. DRAMP00272 AKITFTNNHPRTIWP 15 Thaumatin-like protein (Plants) P83957 Belongs to the thaumatin family Not found Castanopsis chinensis (Chinese chinquapin) (Kweilin chestnut) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Botrytis cinerea, Fusarium oxysporum (IC50=0.5 µM), Mycosphaerella arachidicola, Psylla piricola.##HIV-1 reverse transcriptase (IC50=1.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12565869 Biochem Biophys Res Commun. 2003 Feb 7;301(2):364-370. Chu KT, Ng TB. Isolation of a large thaumatin-like antifungal protein from seeds of the Kweilin chestnut Castanopsis chinensis. DRAMP00273 ANFEIVNNCPYTVWAAASPGGGRRLDRGQT 30 Thaumatin-like protein (Plants) P83959 Belongs to the thaumatin family Not found Phaseolus vulgaris (Kidney bean) (French bean) Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Coprinus comatus, Fusarium oxysporum, Pleurotus ostreatus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10486265 Biochem Biophys Res Commun. 1999 Sep 16;263(1):130-134. Ye XY, Wang HX, Ng TB. First chromatographic isolation of an antifungal thaumatin-like protein from French bean legumes and demonstration of its antifungal activity. DRAMP00274 QKIQEIDLQTYLQPQ 15 Amaryllin (Plant defensin) P86781 Not found Not found Amaryllis belladonna (Naked lady lily) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Fungi: Aspergillus flavus and Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19478451 Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):635-637. Kumar S, Singh N, Sinha M, Kaur P, Srinivasan A, Sharma S, Singh TP. Isolation, purification, crystallization and preliminary crystallographic studies of amaryllin, a plant pathogenesis-related protein from Amaryllis belladonna. DRAMP00276 YSYKKIDCGGACAARCRLSSRPRLCNRACGTCCARCNCVPPGTSGNTETCPCYASLTTHGNKRKCP 66 Snakin-2 (StSN2; Cys-rich; Plant defensin) Q93X17, A1YN11, Q948Z5 Not found SN2 Solanum tuberosum (Potato) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Function: Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria. Tissue specificity: Expressed in tubers, stems, flowers, shoot apex and leaves, but not in roots or stolons. Induction: Locally up-regulated by abscisic acid, wounding and infection with compatible fungus. Down-regulated by gibberellic acid or infection with virulent bacteria. No responses to ethylene or abiotic stresses. PTM: Six disulfide bonds may be present." Gram-positive bacteria: Clavibacter michiganensis (EC50=4 µM), Ralstonia solanacearum (EC50=15 µM).##Fungi: pathogens Rhizobium meliloti (EC50=8 µM), Botrytis cinerea (EC50=2 µM), Fusarium solani (EC50=2 µM), Fusarium culmorum (EC50=2 µM), Fusarium oxysporum f.sp. conglutinans (EC50=10 µM), Fusarium oxysporum f.sp.lycopersici (EC50=20 µM), Plectosphaerella cucumerina (EC50=10 µM), Colletotrichum graminicola (EC50=10 µM), Colletotrichum lagenarium (EC50=10 µM), Bipolaris maydis (EC50=20 µM), Aspergillus flavus (EC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11891250 Plant Physiol. 2002 Mar;128(3):951-961. Marta Berrocal-Lobo, Ana Segura, Manuel Moreno, Gemma López, Francisco García-Olmedo, Antonio Molina Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. DRAMP00277 DICTNCCAGTKGCNTTSANGAFICEGQSDPKKPKACPLNCDPHIAYA 47 Potamin-1 (PT-1; Plants) P84813 Belongs to the protease inhibitor I20 Not found Solanum tuberosum (Potato) Antimicrobial, Antifungal, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Inhibitor of serine proteases chymotrypsin, papain and trypsin. Has strong antifungal activity against C. albicans and R.solani. Has antibacterial activity against the Gram-positive bacterium C.michiganense, but Non-antibacterial activity against the Gram-positive bacterium S. aureus. Lacks hemolytic activity against human erythrocytes. PTM: Contains four disulfide bonds (By similarity)." [Ref.15809084]Fungi: Candida albicans(MIC =100μM) and Rhizoctonia solani(MIC =100μM);##Gram-positive bacterium: Clavibacter michiganensis(MIC =50μM) [Ref:15809084]Non-hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15809084 Biochem Biophys Res Commun. 2005 May 13;330(3):921-927. Kim JY, Park SC, Kim MH, Lim HT, Park Y, Hahm KS. Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato. DRAMP00278 LPSDATLVLDQTGKELDARL 20 Antifungal protein J (AFP-J; Plants) P84794 Belongs to the protease inhibitor I3 Not found Solanum tuberosum (Potato) Antimicrobial, Antifungal Protein level Not found Not found Function: Inhibitor of serine proteases chymotrypsin, pepsin and trypsin. Has strong antifungal activity. Non-hemolytic activity against human erythrocytes. [Ref.16076139]Fungi: Candida albicans TIMM 1768(MIC=6.25μg/mL)), Saccharomyces cerevisiae KCTC 7296(MIC=6.25μg/mL)), Trichosporon beigelii KCTC 7707(MIC=6.25μg/mL)) [Ref:16076139]Non-hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16076139 J Agric Food Chem. 2005 Aug 10;53(16):6491-6496. Park Y, Choi BH, Kwak JS, Kang CW, Lim HT, Cheong HS, Hahm KS. Kunitz-type serine protease inhibitor from potato (Solanum tuberosum L. cv. Jopung). DRAMP00279 AQIVKLGGDDGSLAFVPSKISVAAGEAIEFVNNAGFPHNIVFDEDAVPAGVDADAISYDDYLNSKGETVVRKLSTPGVYGVYCEPHAGAGMKMTITVQ 98 Plastocyanin (Plants) P56274 Not found PETE Ulva pertusa (Sea lettuce) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 1IUZ resolved by X-ray. "Function: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. Has antiviral activity against Potato virus Y (strain N). Domain: Contains 1 plastocyanin-like domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9933621##PubMed ID is not availbale J Biol Chem. 1999 Feb 12;274(7):4225-4230.##Submitted (JUN-2003) to UniProtKB. Shibata N, Inoue T, Nagano C, Nishio N, Kohzuma T, Onodera K, Yoshizaki F, Sugimura Y, Kai Y.## Novel insight into the copper-ligand geometry in the crystal structure of Ulva pertusa plastocyanin at 1.6-A resolution. Structural basis for regulation of the copper site by residue 88.## DRAMP00280 LIYAKVECLTTGVRTYVGKQSWPELVGTKGKTAAATIDKENTHVTAVLCPPLTTLAACRTFDFRCDRVRVLINRIGGVVTKTPTVG 86 Trypsin inhibitor (FtTI; Plant defensin) P86971 Not found Not found Fagopyrum tataricum (Tartarian buckwheat) (Polygonum tataricum) Antimicrobial, Antifungal Protein level Not found Not found "Function: Serine protease inhibitor which is active against trypsin. Displays strong antifungal activity against a number of phytopathogenic fungi. Biophysicochemical properties: pH dependence (Optimum pH is 8.0 at 37 degrees Celsius. Maintains over 90% of its inhibitory activity from pH 3 to 10); Temperature dependence (Active between 10 and 60 degrees Celsius. 84% activity retained when heated for 30 minutes at 80 degrees Celsius. Incubation at temperatures above 80 degrees Celsius rapidly decreases inhibitory activity). PTM: Contains two disulfide bonds 8-65; 49-58." Fungi: M. melonis, A. cucumerina, A. solani, C. glaeosporioides and P. capsici. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21544554 Appl Biochem Biotechnol. 2011 May 5. Ruan JJ, Zhou ML, Chen H, Shao JR. Identification and Characterization of a Trypsin Inhibitor from Fagopyrum tataricum Seeds. DRAMP00281 NTCENLAGSYKGVCFGGCDRHCRTQEGAISGRCRDDFRCWCTKNC 45 Defensin-like protein 230 (Disease resistance response protein 230; Plant defensin) Q01783 Belongs to the DEFL family PI230 Pisum sativum (Garden pea) Unknown Transcript level Not found Not found "Function: Has antifungal activity (By similarity). Induction: Upon contact with the plant pathogen fungus Fusarium solani. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1799696 Mol Plant Microbe Interact. 1991 Jul-Aug;4(4):324-331. Chiang CC, Hadwiger LA. The Fusarium solani-induced expression of a pea gene family encoding high cysteine content proteins. DRAMP00282 GPMRIAEARHCESLSHRFKGPCTRDSNCASVCETERFSGGNCHGFRRRCFCTKPC 55 Defensin-like protein P322 (Probable protease inhibitor P322; Plant defensin) P20346 Belongs to the DEFL family Not found Solanum tuberosum (Potato) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Molecular Biology. 1988, 11(3):255-269. Stiekema WJ, Heidekamp F, Dirkse WG, van Beckum J, de Haan P, ten Bosch C, Louwerse JD. Molecular cloning and analysis of four potato tuber mRNAs. DRAMP00283 RECQSQSHRYKGACVHDTNCASVCQTEGFSGGKCVGFRGRCFCTKAC 47 Defensin Ec-AMP-D1 (Plant defensin) P86518 Belongs to the DEFL family Not found Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity. Inhibits hyphal development in P. infestans (IC50=25.5 µg/ml), but not release of zoospores. At concentrations above 100 µg/ml, induces morphological changes such as lysis of hyphae and sporangia in P. infestans. PTM: Contains four disulfide bonds (By similarity)." Fungi: Fusarium graminearum (IC50=15 µg/ml), Fusarium oxysporum (IC50=102 µg/ml), F. verticillioides (IC50=8.5 µg/ml), Diplodia maydis (IC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18625284 Biochimie. 2008 Nov-Dec;90(11-12):1667-1673. Odintsova TI, Rogozhin EA, Baranov Y, Musolyamov AKh, Yalpani N, Egorov TA, Grishin EV. Seed defensins of barnyard grass Echinochloa crusgalli (L.) Beauv. DRAMP00284 RVCMGKSQHHSFPCISDRLCSNECVKEEGGWTAGYCHLRYCRCQKAC 47 Defensin-like protein 1 (SI alpha-1; Plant defensin) P21923 Belongs to the DEFL family Not found Sorghum bicolor (Sorghum) (Sorghum vulgare) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds 3-47; 14-36; 20-41; 24-43." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1995329##7705336 FEBS Lett. 1991 Feb 11;279(1):101-104.##Eur J Biochem. 1995 Mar 1;228(2):250-256. Bloch C Jr, Richardson M.##Nitti G, Orrù S, Bloch C Jr, Morhy L, Marino G, Pucci P. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins.##Amino acid sequence and disulphide-bridge pattern of three gamma-thionins from Sorghum bicolor. DRAMP00285 RVCMGKSAGFKGLCMRDQNCAQVCLQEGWGGGNCDGVMRQCKCIRQCW 48 Defensin-like protein 2 (SI alpha-2; Plant defensin) P21924 Belongs to the DEFL family Not found Sorghum bicolor (Sorghum) (Sorghum vulgare) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1995329 FEBS Lett. 1991 Feb 11;279(1):101-104. Bloch C Jr, Richardson M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins. DRAMP00286 RVCRRRSAGFKGLCMSDHNCAQVCLQEGWGGGNCDGVIRQCKCIRQC 47 Defensin-like protein 3 (SI alpha-3; Plant defensin) P21925 Belongs to the DEFL family Not found Sorghum bicolor (Sorghum) (Sorghum vulgare) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1995329##7705336 FEBS Lett. 1991 Feb 11;279(1):101-104.##Eur J Biochem. 1995 Mar 1;228(2):250-256. Bloch C Jr, Richardson M.##Nitti G, Orrù S, Bloch C Jr, Morhy L, Marino G, Pucci P. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins.##Amino acid sequence and disulphide-bridge pattern of three gamma-thionins from Sorghum bicolor. DRAMP00287 RVCRRRSAGFKGLCMSDHNCAQVCLQEGWGGGNCDGVMRQCKCIRQC 47 Defensin-like protein 21 (SI alpha-2.1; Plant defensin) Q09198 Belongs to the DEFL family Not found Sorghum bicolor (Sorghum) (Sorghum vulgare) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7705336 Eur J Biochem. 1995 Mar 1;228(2):250-256. Nitti G, Orrù S, Bloch C Jr, Morhy L, Marino G, Pucci P. Amino acid sequence and disulphide-bridge pattern of three gamma-thionins from Sorghum bicolor. DRAMP00288 RECQSQSHRYKGACVHDTNCASVCQTEGFSGGKCVGFRGRCFCTKHC 47 Defensin Ec-AMP-D2 (Plant defensin) P86519 Belongs to the DEFL family Not found Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity. Inhibits spore germination in Fusarium oxysporum (IC(50)=102 μg/ml). Inhibits hyphal development in P. infestans (IC(50)=50 μg/ml). Does not induce morphological changes such as lysis of hyphae and sporangia in P. infestans. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18625284 Biochimie. 2008 Nov-Dec;90(11-12):1667-1673. Odintsova TI, Rogozhin EA, Baranov Y, Musolyamov AKh, Yalpani N, Egorov TA, Grishin EV. Seed defensins of barnyard grass Echinochloa crusgalli (L.) Beauv. DRAMP00289 RLCRVRGTRGHCFNDHGCDKVCTREGFVRGKCNGILRRCICDRQC 45 Defensin-like protein (Gamma-thionin; Plant defensin) B5LZ79 Belongs to the DEFL family Not found Gymnadenia conopsea (Fragrant orchid) (Orchis conopsea) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.##Submitted (JUL-2008) to UniProtKB. Not found##Mukherjee G, Sen SK. Not found##Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P(10). DRAMP00290 KTCENLSDSFKGPCIPDGNCNKHCKEKEHLLSGRCRDDFRCWCTRNC 47 Defensin Lc-def (Plant defensin) B3F051, P85530 Belongs to the DEFL family Not found Lens culinaris subsp. culinaris (Cultivated lentil) (Lens esculenta) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 2LJ7 resolved by NMR. "Function: Has antifungal activity against the phytopathogenic fungus Aspergillus niger VKM F-2259, but not against A.alternatia VKM F- 3047. Does not inhibit trypsin or chymotrypsin. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18468512##PubMed ID is not available Biochem Biophys Res Commun. 2008 Jul 11;371(4):860-865.##To be Published. Finkina EI, Shramova EI, Tagaev AA, Ovchinnikova TV.##Shenkarev Z, Mineev K, Gizatullina A, Finkina E, Arseniev A, Ovchinnikova T. A novel defensin from the lentil Lens culinaris seeds.##Solution structure of defensin Lc-def from germinated lentil (Lens Culinaris) seeds. DRAMP00291 RTCESQSHRFKGACLSDTNCASVCQTEGFPAGDCKGARRRCFCVKPC 47 Defensin-like protein (Gamma-thionin homolog; Plant defensin) A3FPF2 Belongs to the DEFL family Not found Nelumbo nucifera (Sacred lotus) Antimicrobial, Antifungal Homology Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##16972135 Submitted (FEB-2007) to the EMBL/GenBank/DDBJ database##Curr Microbiol. 2006 Oct;53(4):265-269. Not found##Mukherjee G, Sen SK. Not found##Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P(10). DRAMP00292 RVCESQSHGFHGLCNRDHNCALVCRNEGFSGGRCKRSRRCFCTRIC 46 Defensin-like protein (8.4 kDa sulfur-rich protein; Plant defensin) Q07502 Belongs to the DEFL family Not found Glycine max (Soybean) (Glycine hispida) Antimicrobial, Antifungal Homology Not found Not found "Function: Has antifungal activity (By similarity). PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8278516 Plant Physiol. 1993 Feb;101(2):699-700. Choi Y, Choi YD, Lee JS. Nucleotide sequence of a cDNA encoding a low molecular weight sulfur-rich protein in soybean seeds. DRAMP00293 RICRRRSAGFKGPCVSNKNCAQVCMQEGWGGGNCDGPLRRCKCMRRC 47 Gamma1-hordothionin (Gamma 1-H; Plant defensin) P20230 Belongs to the DEFL family Not found Hordeum vulgare (Barley) Antimicrobial, Antifungal Protein level Combine helix and strand structure Gamma 1-H adopts a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. 1GPT resolved by NMR. "Function: Inhibits protein translation in cell-free systems. PTM: Contains four disulfide bonds 3-47; 14-34; 20-21; 24-43. Caution: Was initially thought to be a thionin." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2176600##8380707 Eur I Biochem 1990;194:533-539.##Biochemistry. 1993 Jan 19;32(2):715-724. Mendez E, Moreno A, Colilla F.J, Pelaez F, Limas G.G, Mendez R, Soriano F, Salinas M, de Haro C.##Bruix M, Jim©nez MA, Santoro J, Gonz¡lez C, Colilla FJ, M©ndez E, Rico M. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-hordothionin, from barley endosperm.##Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. DRAMP00294 YKRGGGGWGGGGGWKGGGGGGGGWKGGGGGGKGGGG 36 Glycine-rich protein GWK (Plants) P84064 Not found Not found Cucumis melo (Muskmelon) Antimicrobial, Antifungal Protein level Not found Not found Function: Possesses antifungal activity against a number of phytopathogenic fungi. Fungi: Hordeum sativum and F. culmorum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2004) to UniProtKB Vassilevski AA, Egorov TA, Grishin EV. Unknown DRAMP00295 ADPTFGFTPLGLSEKANLQIMKAYD 25 Soybean toxin 27 kDa chain (SBTX 27 kDa chain; Plant defensin) P86520 Not found Not found Glycine max (Soybean) (Glycine hispida) Antimicrobial, Antifungal Protein level Not found Not found "Function: Involved in plant defense. Has antifungal activity against C. sojina but not A. niger and F. solani. Does not have urease or hemagglutination activities. Does not inhibit trypsin. Injection into mice produces toxic effects such as dyspnea, tonic-clonic convulsion and death. Subunit structure Heterodimer of a 27 kDa subunit and a 17 kDa subunit; disulfide-linked. Tissue specificity: Expressed in seeds, leaves, roots and stem (at protein level). Induction: In seeds, induced by jasmonate. Post-translational modification: SBTX is known to be glycosylated but it is not known which one of its two subunits is modified; contains 5% carbohydrates. Toxic dose: LD50 is 5.6 mg/kg by intraperitoneal injection into mice. Miscellaneous: On the 2D-gel the determined pI of SBTX is: 8.2, its MW is: 44 kDa. Biophysicochemical properties: pH dependence (Activity decreases below pH 5.5 and above pH 8.0)." Fungi: C. sojina. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18328522 Toxicon. 2008 May;51(6):952-963. Vasconcelos IM, Morais JK, Siebra EA, Carlini CR, Sousa DO, Beltramini LM, Melo VM, Oliveira JT. SBTX, a new toxic protein distinct from soyatoxin and other toxic soybean [Glycine max] proteins, and its inhibitory effect on Cercospora sojina growth. DRAMP00296 PNPKVFFDMTIGGQSAGRIVMEEYA 25 Soybean toxin 17 kDa chain (SBTX 17 kDa chain; Plant defensin) P86548 Not found Not found Glycine max (Soybean) (Glycine hispida) Antimicrobial, Antifungal, Cytotoxic Protein level Not found Not found "Function: Involved in plant defense. Has antifungal activity against C.sojina but not A.niger and F.solani. Does not have urease or hemagglutination activities. Does not inhibit trypsin. Injection into mice produces toxic effects such as dyspnea, tonic-clonic convulsion and death. Subunit structure: Heterodimer of a 27 kDa subunit and a 17 kDa subunit; disulfide-linked. Tissue specificity: Expressed in seeds, leaves, roots and stem (at protein level). Induction: In seeds, induced by jasmonate. Post-translational modification: SBTX is known to be glycosylated but it is not known which one of its two subunits is modified; contains 5% carbohydrates. Toxic dose: LD50 is 5.6 mg/kg by intraperitoneal injection into mice. Miscellaneous: On the 2D-gel the determined pI of SBTX is: 8.2, its MW is: 44 kDa. Biophysicochemical properties: pH dependence (Activity decreases below pH 5.5 and above pH 8.0). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18328522 Toxicon. 2008 May;51(6):952-963. Vasconcelos IM, Morais JK, Siebra EA, Carlini CR, Sousa DO, Beltramini LM, Melo VM, Oliveira JT. SBTX, a new toxic protein distinct from soyatoxin and other toxic soybean [Glycine max] proteins, and its inhibitory effect on Cercospora sojina growth. DRAMP00297 ACGILHDNCVYVPAQNPCCRGLQCRYGKCLVQV 33 U1-theraphotoxin-Pc1a (U1-TRTX-Pc1a; Psalmopeotoxin-1; PcFK1; Plants) P0C201 Not found Not found Psalmopoeus cambridgei (Trinidad chevron tarantula) Antiplasmodial, Cytotoxic Protein level Combine helix and strand structure Not found 1X5V resolved by NMR. "Function: Possess strong antiplasmodial activity against the intra-erythrocyte stage of Plasmodium falciparum in vitro. Interacts with infected and healthy erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity. Tissue specificity: Expressed by the venom gland. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds and C-terminal amidation." Plasmodium falciparum (IC50=1.59 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15304333##16452619 FEBS Lett. 2004 Aug 13;572(1-3):109-117.##Protein Sci. 2006 Mar;15(3):628-634. Choi SJ, Parent R, Guillaume C, Deregnaucourt C, Delarbre C, Ojcius DM, Montagne JJ, C©l©rier ML, Phelipot A, Amiche M, Molgo J, Camadro JM, Guette C.##Pimentel C, Choi SJ, Chagot B, Guette C, Camadro JM, Darbon H. Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei.##Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum. DRAMP00298 RCLPAGKTCVRGPMRVPCCGSCSQNKCT 28 U1-theraphotoxin-Pc1a (U2-TRTX-Pc1a; Psalmopeotoxin-2; PcFK2; Plants) P0C202 Not found Not found Psalmopoeus cambridgei (Trinidad chevron tarantula) Antiplasmodial, Cytotoxic Protein level Not found Not found "Function: Possess strong antiplasmodial activity against the intra-erythrocyte stage of P.falciparum in vitro. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity. Tissue specificity: Expressed by the venom gland. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin By similarity. Miscellaneous: Usually endopeptidases cleave the propeptide at the C-terminus of the basic doublet (Arg-37-38-Arg), but here, it seems that the endopeptidase cleaves the precursor within the doublet. PTM: Contains three disulfide bonds (By similarity)." Plasmodium falciparum (IC50=1.15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15304333 FEBS Lett. 2004 Aug 13;572(1-3):109-117. Choi SJ, Parent R, Guillaume C, Deregnaucourt C, Delarbre C, Ojcius DM, Montagne JJ, C©l©rier ML, Phelipot A, Amiche M, Molgo J, Camadro JM, Guette C. Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei. DRAMP00299 DADIAVWAPPVNAQN 15 Ribonuclease (Plants) P84784 Not found Not found Thelephora ganbajun (Mushroom) Antimicrobial, Antiviral Protein level Not found Not found "Function: Inhibits HIV-1 reverse transcriptase. Miscellaneous: Inhibits HIV-1 reverse transcriptase with an IC50 of 300 nM. Biophysicochemical properties: pH dependence (Optimum pH is 6-7); Temperature dependence (Optimum temperature is 45 degrees Celsius. Activity decreases sharply above 50 degrees Celsius and below 40 degrees Celsius)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15474506 Biochem Biophys Res Commun. 2004 Nov 12;324(2):855-859. Wang HX, Ng TB. Purification of a novel ribonuclease from dried fruiting bodies of the edible wild mushroom Thelephora ganbajun. DRAMP00300 PGAGSQEERMQGQMEGQDFSHEERFLSMVRE 31 Antifungal protein 1 (Pa-AFP1; Plant defensin) B3EWF0 Not found Not found Passiflora alata (Winged-stem passion flower) (Fragrant granadilla) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity against C. gloeosporioides but not against Botrytis cinerea and Fusarium sp. or against various yeasts. Has no antibacterial activity. Subunit structure: Heterodimer; disulfide-linked. PTM: Disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20955745 Peptides. 2011 May;32(5):868-874. Ribeiro SM, Almeida RG, Pereira CA, Moreira JS, Pinto MF, Oliveira AC, Vasconcelos IM, Oliveira JT, Santos MO, Dias SC, Franco OL. Identification of a Passiflora alata Curtis dimeric peptide showing identity with 2S albumins. DRAMP00301 DYPKLTFTTS 10 Malanin chain A (Plant defensin) P86600 Not found Not found Malania oleifera Anti-cancer, Cytotoxic Protein level Not found Not found "Function: Significantly inhibits growth and induces an apoptotic response in HeLa cells through cell-cycle arrest at S-phase. Exhibits highly cytotoxic activities against cancer cell and non-cancer cell lines. Subunit structure: Heterodimer of an A chain and a B chain, which are crosslinked by one or more disulfide bonds. Toxic dose: LD50 values are 26.22 µg/kg by intraperitoneal injection and 43.11 mg/kg by intragingival injection into IRC strain mice." Cancer cell lines: HeLa (IC50=0.15±0.08 nM), PC-12 (IC50=7.71±0.24 nM), MCF-7 (IC50=11.20±0.02 nM), K562 (IC50=15.80±0.09 nM).##Non-cancer cell lines: Vero (IC50=2.79±0.05 nM) and Madin-Darby canine kidney cells (IC50=3.92±0.01 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19341757 Toxicon. 2009 Aug;54(2):121-127. Yuan Y, Dai X, Wang D, Zeng X. Purification, characterization and cytotoxicity of malanin, a novel plant toxin from the seeds of Malania oleifera. DRAMP00302 DETXTDEEFN 10 Malanin chain B (Plant defensin) P86601 Not found Not found Malania oleifera Anti-cancer, Cytotoxic Protein level Not found Not found "Function: Significantly inhibits growth and induces an apoptotic response in HeLa cells through cell-cycle arrest at S-phase. Exhibits highly cytotoxic activities against cancer cell and non-cancer cell lines. Subunit structure: Heterodimer of an A chain and a B chain, which are crosslinked by one or more disulfide bonds. Toxic dose: LD50 values are 26.22 µg/kg by intraperitoneal injection and 43.11 mg/kg by intragingival injection into IRC strain mice." Cancer cell lines: HeLa (IC50=0.15±0.08 nM), PC-12 (IC50=7.71±0.24 nM), MCF-7 (IC50=11.20±0.02 nM), K562 (IC50=15.80±0.09 nM).##Non-cancer cell lines: Vero (IC50=2.79±0.05 nM) and Madin-Darby canine kidney cells (IC50=3.92±0.01 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19341757 Toxicon. 2009 Aug;54(2):121-127. Yuan Y, Dai X, Wang D, Zeng X. Purification, characterization and cytotoxicity of malanin, a novel plant toxin from the seeds of Malania oleifera. DRAMP00303 ACGGGGGDVGSLISASLFDQMLKYRNDPRCCXXGF 35 Basic endochitinase CH1 (Plant defensin) P29137 Belongs to the glycosyl hydrolase 19 family (Chitinase class I subfamily) Not found Castanea sativa (Sweet chestnut) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16653058 Plant Physiol. 1992 Oct;100(2):778-783. Collada C, Casado R, Fraile A, Aragoncillo C. Basic Endochitinases Are Major Proteins in Castanea sativa Cotyledons. DRAMP00304 SIGFDGLNDPDIVAR 15 Endochitinase 1 (Plant defensin) P86078 Belongs to the glycosyl hydrolase 20 family (Chitinase class I subfamily) Not found Capsicum annuum var. annuum (Red pepper) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Submitted (JUL-2008) to UniProtKB Belchi-Navarro S, Almagro L, Pedreno M.A. Not found DRAMP00305 NNFYSYNAFITAAKSFPGFGTTGDTAVRGPIQISYNYNYGPCGR 44 Endochitinase 1 (Plant defensin) P86081 Belongs to the glycosyl hydrolase 21 family (Chitinase class I subfamily) Not found Capsicum chinense (Scotch bonnet) (Bonnet pepper) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Submitted (JUL-2008) to UniProtKB Gomez Ros L.V, Almagro L, Ros Barcelo A, Pedreno M.A. Not found DRAMP00306 GPLQLSWNYNYGAAGK 16 Endochitinase 1 (Plant defensin) P85343 Belongs to the glycosyl hydrolase 22 family (Chitinase class I subfamily) Not found Ginkgo biloba (Ginkgo) (Maidenhair tree) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-843. Uzal EN, Gómez-Ros LV, Hernández JA, Pedreño MA, Cuello J, Ros Barceló A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00307 EQCGNQAGGXVPPNG 15 Endochitinase A1 (Plant defensin) P21225 Belongs to the glycosyl hydrolase 23 family (Chitinase class I subfamily) Not found Pisum sativum (Garden pea) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By infection with the fungal pathogen Ascochyta pisi." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Planta 184:24-29(1991). Vad K, Mikkelsen JD, Collinge DB. Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi. DRAMP00308 AIGFDGLNDPDIVAR 15 Endochitinase 1 (Plant defensin) P85337 Belongs to the glycosyl hydrolase 24 family (Chitinase class I subfamily) Not found Taxus baccata (English yew) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-843. Uzal EN, Gómez-Ros LV, Hernández JA, Pedreño MA, Cuello J, Ros Barceló A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00309 MTEQKPKPSCHNVMVGNYVPTASDRAANRTLGFGLVTNIINGGLDC 46 Endochitinase 2 (CHIT 2; Plant defensin) Q06014 Belongs to the glycosyl hydrolase 25 family (Chitinase class I subfamily) Not found Arachis hypogaea (Peanut) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense against chitin containing fungal and bacterial pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By glucan and Phytophthora megasperma elicitors." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1980004 Mol Gen Genet. 1990 Dec;224(3):469-476. Herget T, Schell J, Schreier PH. Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. DRAMP00310 SAIWFWMTPQSPK 13 Endochitinase 2 (Plant defensin) P86079 Belongs to the glycosyl hydrolase 26 family (Chitinase class I subfamily) Not found Capsicum annuum var. annuum (Red pepper) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Submitted (JUL-2008) to UniProtKB Gomez Ros L.V, Almagro L, Ros Barcelo A, Pedreno M.A. Not found DRAMP00311 GPIQISYNYNYGPCGRYCGILGVSPGDNLDCGNQR 35 Endochitinase 2 (Plant defensin) P86082 Belongs to the glycosyl hydrolase 27 family (Chitinase class I subfamily) Not found Capsicum chinense (Scotch bonnet) (Bonnet pepper) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Submitted (JUL-2008) to UniProtKB Sabater Jara A.B, Almagro L, Pedreno M.A. Not found DRAMP00312 TAGFGVFTNIINGGLECGK 19 Endochitinase 2 (Plant defensin) P85338 Belongs to the glycosyl hydrolase 28 family (Chitinase class I subfamily) Not found Taxus baccata (English yew) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. PTM: Contians one disulfide bond (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-843. Uzal EN, Gómez-Ros LV, Hernández JA, Pedreño MA, Cuello J, Ros Barceló A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00313 MTPQGNKPSSHDVITGRWTPSDADRAAGRVSGFGVITNIINGGLDC 46 Endochitinase 3 (CHIT 3; Plant defensin) Q06015 Belongs to the glycosyl hydrolase 29 family (Chitinase class I subfamily) Not found Arachis hypogaea (Peanut) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Defense against chitin containing fungal and bacterial pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: Constitutively expressed at low levels." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1980004 Mol Gen Genet. 1990 Dec;224(3):469-476. Herget T, Schell J, Schreier PH. Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. DRAMP00314 MYDESTGYSSALK 13 Endochitinase 3 (Plant defensin) P85355 Belongs to the glycosyl hydrolase 30 family (Chitinase class I subfamily) Not found Taxus baccata (English yew) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-843. Uzal EN, Gómez-Ros LV, Hernández JA, Pedreño MA, Cuello J, Ros Barceló A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00315 MTPQGNKPSCHDVITNAWRPTATDSAAGRAPGYGVITNIINGGLDC 46 Endochitinase 4 (CHIT 4; Plant defensin) Q06016 Belongs to the glycosyl hydrolase 31 family (Chitinase class I subfamily) Not found Arachis hypogaea (Peanut) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Defense against chitin containing fungal and bacterial pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By glucan elicitor, and to a lesser extent by yeast extract, Phytophthora megasperma elicitor, UV light and dilution." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1980004 Mol Gen Genet. 1990 Dec;224(3):469-476. Herget T, Schell J, Schreier PH. Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. DRAMP00316 MTAQGNKPSSHDVITGRWTPSAADRAAGRVSGFGVITNIINGGLDC 46 Endochitinase 1A (CHIT 1A; Plant defensin) Q06012 Belongs to the glycosyl hydrolase 32 family (Chitinase class I subfamily) Not found Arachis hypogaea (Peanut) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Defense against chitin containing fungal and bacterial pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By yeast extract and dilution. Slight induction by glucan elicitor." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1980004 Mol Gen Genet. 1990 Dec;224(3):469-476. Herget T, Schell J, Schreier PH. Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. DRAMP00317 MTAQGNKPSSHDVITGRWTPSAADKAAGRVSGFGVITNIINGGLDC 46 Endochitinase 1B (CHIT 1B; Plant defensin) Q06013 Belongs to the glycosyl hydrolase 33 family (Chitinase class I subfamily) Not found Arachis hypogaea (Peanut) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Defense against chitin containing fungal and bacterial pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By yeast extract and dilution. Slight induction by glucan elicitor." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1980004 Mol Gen Genet. 1990 Dec;224(3):469-476. Herget T, Schell J, Schreier PH. Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. DRAMP00318 EQCGRQAGGATCPNNLCCSQYGY 23 Endochitinase B (Plant defensin) P21227 Belongs to the glycosyl hydrolase 34 family (Chitinase class I subfamily) Not found Pisum sativum (Garden pea) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Induction: By infection with the fungal pathogen Ascochyta pisi." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding PubMed ID is not availbale Planta 184:24-29(1991). Vad K, Mikkelsen JD, Collinge DB. Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi. DRAMP00319 ENCGRQAG 8 Endochitinase (Plant defensin) P86473 Belongs to the glycosyl hydrolase 35 family (Chitinase class I subfamily) Not found Actinidia chinensis (Kiwi) (Yangtao) Antimicrobial, Antifungal Protein level Not found Not found "Function: Defense against chitin containing fungal pathogens (By similarity). Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Allergenic properties: Causes an allergic reaction in human. Domian: Contains 1 chitin-binding type-1 domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 1553642 Tidsskr Nor Laegeforen. 1992 Jan 10;112(1):38-42. Rygnestad T. Suicide in Norway. Changes in the 20th century with special emphasis on the development during the last 20 years. DRAMP00320 MARVNSLKCALCFIVLILFVQLNCIPETRVMAVELSRVFLQTSSTDCGEPCVYIPCTITALLGCSCLNKVCVRP 74 Acyclotide phyb-K (Plant defensin) B3EWH6 Belongs to the cyclotide family (Bracelet subfamily) Not found Petunia hybrida (Petunia) Unknown Protein level Not found Not found "Function: Probably participates in a plant defense mechanism (By similarity). Tissue specificity: Expressed in midvein, lamina and periphery of leaves (at protein level). Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21143680##22700981 Plant J. 2010 Dec;64(6):1002-1017.##J Biol Chem. 2012 Aug 3;287(32):27033-46. Breuillin F, Schramm J, Hajirezaei M, Ahkami A, Favre P, Druege U, Hause B, Bucher M, Kretzschmar T, Bossolini E, Kuhlemeier C, Martinoia E, Franken P, Scholz U, Reinhardt D.##Poth AG, Mylne JS, Grassl J, Lyons RE, Millar AH, Colgrave ML, Craik DJ. Phosphate systemically inhibits development of arbuscular mycorrhiza in Petunia hybrida and represses genes involved in mycorrhizal functioning.##Cyclotides associate with leaf vasculature and are the products of a novel precursor in petunia (Solanaceae). DRAMP00321 QSISCAESCVWIPCATSLIGCSCVNSRCIYSK 32 Acyclotide phyb-M (Plant defensin) B3EWH7 Belongs to the cyclotide family (Bracelet subfamily) Not found Petunia hybrida (Petunia) Unknown Protein level Not found Not found "Function: Probably participates in a plant defense mechanism (By similarity). Tissue specificity: Expressed in midvein, lamina and periphery of leaves (at protein level). Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22700981 J Biol Chem. 2012 Aug 3;287(32):27033-46. Poth AG, Mylne JS, Grassl J, Lyons RE, Millar AH, Colgrave ML, Craik DJ. Cyclotides associate with leaf vasculature and are the products of a novel precursor in petunia (Solanaceae). DRAMP00322 SEPQXGRDAGGAL 13 Insecticidal protein LA-a (Latex abundant protein a; Plant defensin) P86799 Not found Not found Morus alba (White mulberry) Insecticidal Protein level Not found Not found "Function: Has insecticidal activity when consumed by D. melanogaster larvae. Has low chitinase and chitosanase activity. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan. PTM: Glycosylated; contains galactose." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 20109180 BMC Biochem. 2010 Jan 28;11:6. Kitajima S, Kamei K, Taketani S, Yamaguchi M, Kawai F, Komatsu A, Inukai Y. Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity. DRAMP00323 SEQQXGRDVGGAL 13 Insecticidal protein LA-b (Latex abundant protein b; Plant defensin) P86800 Not found Not found Morus alba (White mulberry) Insecticidal Protein level Not found Not found "Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan. PTM: Glycosylated; contains galactose." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20109180 BMC Biochem. 2010 Jan 28;11:6. Kitajima S, Kamei K, Taketani S, Yamaguchi M, Kawai F, Komatsu A, Inukai Y. Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity. DRAMP00324 GIFTFEDESTSTVAPAKLYK 20 Protein PR-L1 (Plant defensin) P83363 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00325 SVFAFENEQSSTIAPARLYK 20 Protein PR-L2 (Plant defensin) P83364 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00326 GIFTFEDESTTTVAPAKLYK 20 Protein PR-L3 (Plant defensin) P83365 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00327 SVFAFQDESTSTIAQARLFI 20 Protein PR-L4 (Plant defensin) P83366 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00328 SIFAFQDESPSAIAQAKLFK 20 Protein PR-L5 (Plant defensin) P83367 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00329 GVFTFEDESTSTVAPAKLYK 20 Protein PR-L6 (Plant defensin) P83368 Belongs to the BetVI family Not found Lupinus luteus (European yellow lupin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Pathogenesis-related protein. May have antifungal or antibacterial activity. Induction: By heavy metal ions." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale J. Plant Physiol. 1999;154:703-708. Przymusinski R, Gwozdz E.A. Heavy metal-induced polypeptides in lupin roots are similar to pathogenesis-related proteins. DRAMP00330 DFVDAHNAARAQVGVGPVHWTVDAYARQYANDRNLVHSATR 41 Pathogenesis-related protein (PR-1; Plant defensin) P83834 Belongs to the CRISP family Not found Cucumis melo (Muskmelon) Unknown Protein level Not found Not found Function: Probably involved in the defense reaction of plants against pathogens (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15480331 J Allergy Clin Immunol. 2004 Oct;114(4):896-899. Asensio T, Crespo JF, Sanchez-Monge R, Lopez-Torrejon G, Somoza ML, Rodriguez J, Salcedo G. Novel plant pathogenesis-related protein family involved in food allergy. DRAMP00331 GVQKSEVVITSA 12 Pathogenesis-related protein (PRP; Plant defensin) C0HJB6 Belongs to the BetVI family Not found Foeniculum vulgare (Fennel) Unknown Protein level Not found Not found "Function: Probably involved in the defense reaction of plants against pathogens (By similarity). Allergenic properties: Causes an allergic reaction in human." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 23210484 J Agric Food Chem. 2013 Jan 23;61(3):740-746. Pastorello EA, Farioli L, Stafylaraki C, Scibilia J, Giuffrida MG, Mascheri A, Piantanida M, Baro C, Primavesi L, Nichelatti M, Schroeder JW, Pravettoni V. Fennel allergy is a lipid-transfer protein (LTP)-related food hypersensitivity associated with peach allergy. DRAMP00332 DLDVNVFNR 9 Pathogenesis-related protein (Plant defensin) P85494 Not found Not found Ephedra distachya (Joint-fir) (Ephedra vulgaris) Antimicrobial Protein level Not found Not found "Function: Probably involved in the defense reaction of plants against pathogens. Domain: Contains 1 barwin domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-843. Uzal EN, Gómez-Ros LV, Hernández JA, Pedreño MA, Cuello J, Ros Barceló A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00333 AVKTITLNLVSPSANRYATFLTEIRDNVRXRSLDYSHSGIDVIGAPSSRDSXLNINFQSP 60 Antiviral protein DAP-32 (Ribosome-inactivating protein; Plant defensin) P24477 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Dianthus caryophyllus (Carnation) (Clove pink) Antimicrobial, Antiviral Protein level Not found Not found "Function: Single-chain ribosome-inactivating protein, possessing high antiviral potency and low toxicity to normal cells in culture and to intact animals. Capable of inhibiting HIV-1 infection and replication. Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA." Syncytkia (IC50=0.76 nM), viral coreprotein P24 (IC50=0.71 nM), HIV-RT (IC50=0.76 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1936243 FEBS Lett. 1991 Oct 7;291(1):139-144. Lee-Huang S, Kung HF, Huang PL, Huang PL, Li BQ, Huang P, Huang HI, Chen HC. A new class of anti-HIV agents: GAP31, DAPs 30 and 32. DRAMP00334 GLDTVSFSTKGATYITYVNFLNELRVKTKPEGNSHGIPSLRKSSDDPGSSFVVAG 55 Antiviral protein GAP-31 (Ribosome-inactivating protein; Plant defensin) P24475 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Suregada multiflora (False lime) (Gelonium multiflorum) Antimicrobial, Antiviral Protein level Not found Not found "Function: Single-chain ribosome-inactivating protein, possessing high antiviral potency and low toxicity to normal cells in culture and to intact animals. Capable of inhibiting HIV-1 infection and replication. Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1936243 FEBS Lett. 1991 Oct 7;291(1):139-144. Lee-Huang S, Kung HF, Huang PL, Huang PL, Li BQ, Huang P, Huang HI, Chen HC. A new class of anti-HIV agents: GAP31, DAPs 30 and 32. DRAMP00335 NVRFDLSGATSSSYKTFIKN 20 Ribosome-inactivating protein (rRNA N-glycosidase; Plant defensin) P80750 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Cucurbita pepo (Vegetable marrow) (Summer squash) Unknown Protein level Not found Not found Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S Rrna. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022685 Eur J Biochem. 1996 Dec 15;242(3):585-591. Yoshinari S, Yokota S, Sawamoto H, Koresawa S, Tamura M, Endo Y. Purification, characterization and subcellular localization of a type-1 ribosome-inactivating protein from the sarcocarp of Cucurbita pepo. DRAMP00339 GADFQECMKEHSQKQHQHQG 20 Alpha-basrubrin (Fragment; Plants) P83186 Not found Not found Basella alba (Malabar spinach) (Basella rubra) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Inhibits HIV-1 reverse transcriptase and cell-free translation. Fungi: Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11688973 Biochem Biophys Res Commun. 2001 Nov 9;288(4):765-770. Wang H, Ng T.B. Novel antifungal peptides from ceylon spinach seeds. DRAMP00340 KIMAKPSKFYEQLRGR 16 Beta-basrubin (Plants) P83187 Not found Not found Basella alba (Malabar spinach) (Basella rubra) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Possesses antifungal activity. Inhibits HIV-1 reverse transcriptase and cell-free translation. Fungi: Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11688973 Biochem Biophys Res Commun. 2001 Nov 9;288(4):765-770. Wang H, Ng T.B. Novel antifungal peptides from ceylon spinach seeds. DRAMP00341 ANTAFVSSAHNTQKIPAGAPFNRNLRAMLADLRQNAAFAG 40 Antifungal protein ginkbilobin-1 (Ginkbilobin, GNL; Plants) P83171 Not found GNK1 Ginkgo biloba (Ginkgo) (Maidenhair tree) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Protein level Not found Not found Function: Also inhibits HIV-1 reverse transcriptase and proliferation of murine splenocytes. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Pseudomonas aeruginosa, Escherichia coli.##Fuungi: Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum, Rhizoctonia solani, Coprinus comatus, No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11118300 Biochem Biophys Res Commun. 2000 Dec 20;279(2):407-411. Wang H, Ng T.B. Ginkbilobin, a novel antifungal protein from Ginkgo biloba seeds with sequence similarity to embryo-abundant protein. DRAMP00342 ATITVVNRCSYTVWPGALPGGGVRLDPGQRWALNMPAGTAGAAV 44 Antifungal protein R (Plant defensin) P33044 Not found Not found Hordeum vulgare (Barley) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Inhibits the growth of Trichoderma viridae and Candida albicans. Fungi: Trichoderma viridae, Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1936240 FEBS Lett. 1991 Oct 7;291(1):127-131. Hejgaard J, Jacobsen S, Svendsen I. Two antifungal thaumatin-like proteins from barley grain. DRAMP00343 ATFTVINKCQYTVWAAAVPAGGGQKLDAGQTWSIXXP 37 Antifungal protein S (Plant defensin) P33045 Not found Not found Hordeum vulgare (Barley) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Inhibits the growth of Trichoderma viridae and Candida albicans. Fungi: Trichoderma viridae, Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1936240 FEBS Lett. 1991 Oct 7;291(1):127-131. Hejgaard J, Jacobsen S, Svendsen I. Two antifungal thaumatin-like proteins from barley grain. DRAMP00344 AISYDQVKSSLLPCVGYVRGNNARPAPPNYCKGIRSLKSAARIRLDRQAACKCIKSLAADISDINYGVAAGLPGQCNVHIPYKISPSIDCKRVK 94 Non-specific lipid-transfer protein 6 (LTP; Plants) O24418 Belongs to the plant LTP family LTP6 Gossypium hirsutum (Upland cotton) (Gossypium mexicanum) Not found Transcript level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). Tissue specificity: Specifically expressed in fiber cells." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 9030188 Biochim Biophys Acta. 1997 Jan 21;1344(2):111-114. Ma DP, Liu HC, Tan H, Creech RG, Jenkins JN, Chang YF. Cloning and characterization of a cotton lipid transfer protein gene specifically expressed in fiber cells. DRAMP00345 ACEPAQLAVCASAILGGTKPSGECCGNLRAQQGCLCQYVKDPNYGHYVSSPHARDTLNLCGIPVPHC 67 Probable non-specific lipid-transfer protein (LTP; B-FABP; Plants) P20145 Belongs to the plant LTP family LTP2 Hordeum vulgare (Barley) Not found Transcript level Not found Not found "Function: Potential phospholipid transfer protein. Tissue specificity: Aleurone. Developmental stage: Maximum mRNA abundance around mid-phase of grain development. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 7849757 Plant J. 1994 Dec;6(6):849-860. Kalla R, Shimamoto K, Potter R, Nielsen PS, Linnestad C, Olsen OA. The promoter of the barley aleurone-specific gene encoding a putative 7 kDa lipid transfer protein confers aleurone cell-specific expression in transgenic rice. DRAMP00346 AITCGQVSSALGPCAAYAKGSGTSPSAGCCSGVKRLAGLARSTADKQATCRCLKSVAGAYNAGRAAGIPSRCGVSVPYTISASVDCSKIH 90 Non-specific lipid-transfer protein Cw18 (LTP Cw-18; PKG2316; Plants) Q43871 Belongs to the plant LTP family CW18 Hordeum vulgare (Barley) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Tissue specificity: Highly expressed in leaves and coleoptiles. No expression in roots. Induction: By NaCl, abscisic acid and inoculation with the fungal pathogen E. graminis. PTM: Contains four disulfide bonds 4-52; 14-29; 30-72; 50-86." Fungi: Fusarim solani (EC50=3-20×10-6 M), Pseudomonas solanacearum (EC50=3-6×10-7 M), Pythium aphanidermatum, Clavibacter michiganensis subsp. Sepedonicus (EC50=l-3×10-7 M). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8420795##8281190 FEBS Lett. 1993 Jan 25;316(2):119-122.##Plant J. 1993 Dec;4(6):983-991. Molina A, Segura A, García-Olmedo F.##Molina A, Garc­a-Olmedo F. Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens.##Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. DRAMP00347 AISCGQVSSALSPCISYARGNGAKPPVACCSGVKRLAGAAQSTADKQAACRCLKSLATSIKGINMGKVSGVPGKCGVSVPFPISMSTDCNKVH 93 Non-specific lipid-transfer protein 3 (LTP 3; CW-19; CW-20; Plants) Q43766 Belongs to the plant LTP family LTP3 Hordeum vulgare (Barley) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." Fungi: Fusarim solani (EC50=3-20×10-6 M), Pseudomonas solanacearum (EC50=3-6×10-7 M), Pythium aphanidermatum, Clavibacter michiganensis subsp. Sepedonicus (EC50=l-3×10-7 M). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8420795##8281190 FEBS Lett. 1993 Jan 25;316(2):119-122.##Plant J. 1993 Dec;4(6):983-991. Molina A, Segura A, García-Olmedo F.##Molina A, Garc­a-Olmedo F. Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens.##Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. DRAMP00348 AISCGQVSSALSPCISYARGNGAKPPAACCSGVKRLAGAAQSTADKQAACKCIKSAAGGLNAGKAAGIPSMCGVSVPYAISASVDCSKIR 90 Non-specific lipid-transfer protein 4.1 (LTP 4.1; CW-21; Plants) Q43767 Belongs to the plant LTP family LTP4.1 Hordeum vulgare (Barley) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-52; 14-29; 30-72; 50-86." Fungi: Fusarim solani (EC50=3-20×10-6 M), Pseudomonas solanacearum (EC50=3-6×10-7 M), Pythium aphanidermatum, Clavibacter michiganensis subsp. Sepedonicus (EC50=l-3×10-7 M). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8420795##8281190 FEBS Lett. 1993 Jan 25;316(2):119-122.##Plant J. 1993 Dec;4(6):983-991. Molina A, Segura A, García-Olmedo F.##Molina A, Garc­a-Olmedo F. Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens.##Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. DRAMP00349 AISCGQVSSALSPCISYARGNGAKPPVACCSGVKRLAGAAQSTADKQAACKCIKSAAGGLNAGKAAGIPSMCGVSVPYAISASVDCSKIR 90 Non-specific lipid-transfer protein 4.2 (LTP 4.2; Low-temperature-responsive protein 4.9; Plants) Q43875 Belongs to the plant LTP family LTP4.2 Hordeum vulgare (Barley) Not found Transcript level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Induction: By cold. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8804389 Mol Gen Genet. 1996 Aug 27;252(1-2):162-168. Molina A, Diaz I, Vasil IK, Carbonero P, Garc­a-Olmedo F. Two cold-inducible genes encoding lipid transfer protein LTP4 from barley show differential responses to bacterial pathogens. DRAMP18333 STPACAIGVVGITVAVTGISTACTSRCINK 30 BHT-Ab(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Streptococcus rattus BHT Antimicrobial, Antibacterial, Anti-Gram+ Not found The amino acid sequence is identical to SmbA. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16194596##18220976 FEMS Microbiol Lett. 2005 Nov 15;252(2):235-41.##Mini Rev Med Chem. 2007 Dec;7(12):1236-47. Hyink O, Balakrishnan M, Tagg JR.##Lawton EM, Ross RP, Hill C, Cotter PD. Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin.##Two-peptide lantibiotics: a medical perspective. DRAMP18334 MWGRILAFVAKYGTKAVQWAWKNKWFLLSLGEAVFDYIRSIWGG 44 BHT-B (Bacteriocin) No entry found Belongs to the class IId bacteriocin bht-b Streptococcus rattus BHT Antimicrobial, Antibacterial, Anti-Gram+ Not found BHT-B is a non-modi?ed 5195 Da peptide with some similarity to the tryptophan-rich Staphylococcus aureus bacteriocin, aureocin A53. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16194596 FEMS Microbiol Lett. 2005 Nov 15;252(2):235-41.##Mini Rev Med Chem. 2007 Dec;7(12):1236-47. Hyink O, Balakrishnan M, Tagg JR. Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin. DRAMP00351 AITCGQVTSNLAPCLAYLRNTGPLGRCCGGVKALVNSARTTEDRQIACTCLKSAAGAISGINLGKAAGLPSTCGVNIPYKISPSTDCSKVQ 91 Non-specific lipid-transfer protein 1 (LTP 1; PR-14; Plant defensin) Q42952 Belongs to the plant LTP family LTP1 Nicotiana tabacum (Common tobacco) Not found Protein level Alpha helix (5 helices; 50 residues) The overall fold of tobacco LTP 1 includes four α-helices: H1 (Cys4-Leu18), H2 (Cys27-Val37), H3 (Glu42-Ala55) and H4 (Leu63-Thr72), followed by a C-terminal segment involving three γ-turns. 1T12 resolved by NMR. "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. Binds cis-unsaturated fatty acids and jasmonic acid with a higher affinity than linear chain fatty acids. Formation of the complex with jasmonic acid results in a conformational change facilitating the LPT1 binding on the elicitin plasma membrane receptor that is known to be involved in plant defense induction. May also play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Tissue specificity: High expression in leaf epidermis and shoot apex, and also in root epidermis during seedling germination. PTM: Contains four disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8883375##15726627 Plant Physiol. 1996 Oct;112(2):513-524.##Proteins. 2005 May 1;59(2):356-367. Canevascini S, Caderas D, Mandel T, Fleming AJ, Dupuis I, Kuhlemeier C.##Da Silva P, Landon C, Industri B, Marais A, Marion D, Ponchet M, Vovelle F. Tissue-specific expression and promoter analysis of the tobacco Itp1 gene.##Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features. DRAMP00352 VDCGQVNSSLASCIPFLTGGVASPSASCCAGVQNLKTLAPTSADRRAACECIKAAAARFPTIKQDAASSLPKKCGVDINIPISKTTNCQAIN 92 Non-specific lipid-transfer protein A (NS-LTP A; PLTP; Plants) P10973 Belongs to the plant LTP family Not found Ricinus communis (Castor bean) Not found Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Biochim. Biophys. Acta 1986;870:248-255. Takishima K, Watanabe S, Yamada M, Mamiya G. The amino-acid sequence of the nonspecific lipid transfer protein from germinated castor bean endosperms. DRAMP00353 VNCGQVNKALSSCVPFLTGFDTTPSLTCCAGVMELKRLAPTVKDKRIACECVKTAAARYPNIREDAASSLPYKCGVVINVPISKTTNCHEIN 92 Non-specific lipid-transfer protein B (NS-LTP B; PLTP; Plants) P10974 Belongs to the plant LTP family Not found Ricinus communis (Castor bean) Not found Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 3191918 Eur J Biochem. 1988 Nov 1;177(2):241-249. Takishima K, Watanabe S, Yamada M, Suga T, Mamiya G. Amino acid sequences of two nonspecific lipid-transfer proteins from germinated castor bean. DRAMP00354 AVPCSTVDMKAAACVGFATGKDSKPSQACCTGLQQLAQTVKTVDDKKAICRCLKASSKSLGIKDQFLSKIPAACNIKVGFPVSTNTNCETIH 92 Non-specific lipid-transfer protein C, cotyledon-specific isoform (NS-LTP C; PLTP; Plants) P10975, Q43120 Belongs to the plant LTP family Not found Ricinus communis (Castor bean) Not found Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 1783615 J Biochem. 1991 Nov;110(5):823-831. Tsuboi S, Suga T, Takishima K, Mamiya G, Matsui K, Ozeki Y, Yamada M. Organ-specific occurrence and expression of the isoforms of nonspecific lipid transfer protein in castor bean seedlings, and molecular cloning of a full-length cDNA for a cotyledon-specific isoform. DRAMP00355 AVPCSTVDMKAAACVGFATGKDSKPSSACCTGLQQLAQTVKSVDDKKAICRCLKASSKSLGIKDQFLSKIPAACNIKVGFPVSTATNCETIH 92 Non-specific lipid-transfer protein D, cotyledon-specific isoform (NS-LTP D; Plants) Q43119 Belongs to the plant LTP family Not found Ricinus communis (Castor bean) Not found Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Planta 1992;187:367-371. Weig A, Komor E. The lipid-transfer protein C of Ricinus communis L.: isolation of two cDNA sequences which are strongly and exclusively expressed in cotyledons after germination. DRAMP00356 GITCGMVSSKLAPCIGYLKGGPLGGGCCGGIKALNAAAATTPDRKTACNCLKSAANAIKGINYGKAAGLPGMCGVHIPYAISPSTNCNAVH 91 Non-specific lipid-transfer protein (LTP; PLTP; Plants) P10976 Belongs to the plant LTP family Not found Spinacia oleracea (Spinach) Not found Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16667945##3609015 Plant Physiol. 1991 Jan;95(1):164-170.##Eur J Biochem. 1987 Jul 15;166(2):387-391. Bernhard WR, Thoma S, Botella J, Somerville CR.##Bouillon P, Drischel C, Vergnolle C, Duranton H, Kader JC. Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway.##The primary structure of spinach-leaf phospholipid-transfer protein. DRAMP00357 TTSEAAISCGQVSSAIALCLSYARGQGFAPSAGCCSGVRSLNSAARTTADRRAACNCLKNAARGISGLNAGNAASIPSKCGVSVPYTISTSTDCSRVS 98 Non-specific lipid-transfer protein 1 (LTP 1; Plants) Q43193, Q43195 Belongs to the plant LTP family LTP1 Sorghum bicolor (Sorghum) (Sorghum vulgare) Not found Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 7958959 Gene. 1994 Oct 21;148(2):305-308. Pel¨se-Siebenbourg F, Caelles C, Kader JC, Delseny M, Puigdom¨nech P. A pair of genes coding for lipid-transfer proteins in Sorghum vulgare. DRAMP00358 ATTSEAAVTCGQVSSAIGPCLSYARGQGSGPSAGCCSGVRSLNSAARTTADRRAACNCLKNAARGIRGLNVGKAASIPSKCGVSIPYTISTSTDCSRVS 99 Non-specific lipid-transfer protein 2 (LTP 2; Plants) Q43194 Belongs to the plant LTP family LTP2 Sorghum bicolor (Sorghum) (Sorghum vulgare) Not found Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 7958959 Gene. 1994 Oct 21;148(2):305-308. Pel¨se-Siebenbourg F, Caelles C, Kader JC, Delseny M, Puigdom¨nech P. A pair of genes coding for lipid-transfer proteins in Sorghum vulgare. DRAMP00359 AISCGQVASAIAPCISYARGQGSGPSAGCCSGVRSLNNAARTTADRRAACNCLKNAAAGVSGLNAGNAASIPSKCGVSIPYTISTSTDCSRVN 93 Non-specific lipid-transfer protein (LTP; PLTP; Plants) P19656 Belongs to the plant LTP family Not found Zea mays (Maize) Not found Protein level Alpha helix (6 helices; 53 residues) The global fold involving four helical fragments connected by three loops and a C-terminal tail without regular secondary structures is stabilized by four disulfide bridges. The most striking feature of this structure is the existence of an internal hydrophobic cavity running through the whole molecule. (Ref.3) 1AFH resolved by NMR.##1FK0, 1FK1, 1FK2, 1FK3 resolved by X-ray "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Allergenic properties: Causes an allergic reaction in human. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 2022320##7735835##8845747 Gene. 1991 Mar 1;99(1):133-136.##Structure. 1995 Feb 15;3(2):189-199.##Protein Sci. 1996 Apr;5(4):565-577. Arondel V, Tchang F, Baillet B, Vignols F, Grellet F, Delseny M, Kader JC, Puigdom¨nech P.##Shin DH, Lee JY, Hwang KY, Kim KK, Suh SW.##Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M. Multiple mRNA coding for phospholipid-transfer protein from Zea mays arise from alternative splicing.##High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings.##Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds. DRAMP00360 ISCQDVKQSLAPCLPYVTGRAPKPA 25 Non-specific lipid-transfer protein 1 (LTP 1; Plants) P86527 Belongs to the plant LTP family Not found Nigella sativa (Black cumin) Antimicrobial, Antifungal Protein level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Fungi: Fusarium oxysporum and Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 19621049 Bioorg Khim. 2009 May-Jun;35(3):344-349. Oshchepkova IuI, Veshkurova ON, Rogozhin EA, Musoliamov AKh, Smirnov AN, Odintsova TI, Egorov TsA, Grishin EV, Salikhov ShI. Isolation of the lipid-transporting protein Ns-LTP1 from seeds of the garden fennel flower (Nigella sativa). DRAMP00361 ITCPQVTQSLAPCVPYLISG 20 Non-specific lipid-transfer protein (LTP; Harmalin; Plants) B3EWH4 Belongs to the plant LTP family Not found Peganum harmala (Syrian rue) (Harmal peganum) Antimicrobial, Antifungal, Antiviral, Anti-cancer Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Inhibits cell proliferation of cervical carcinoma cell line HeLa (IC50=2.74 µM), gastric carcinoma cell line MGC-7 (IC50=3.13 µM), esophageal carcinoma cell line Eca-109 (IC50=0.7 µM) and melanoma B16 cells (IC50=1.47 µM). Has antifungal activity. Induces caspase-dependent apoptosis in cell line Eca-109. Demonstrates inhibitory effect on HIV-1 reverse transcriptase (IC50=1.26 µM). Biophysicochemical properties: pH dependence (Stable between pH 4 and 10); Temperature dependence (Thermostable. Retains antifungal activity between 4 degrees Celsius and 60 degrees Celsius. Activity reduced after 30 min at 80 degrees Celsius)." Fungi: Penicillium digitatum (IC50=37.5 µM), Alternaria alternata (IC50=1.5 µM), Rhizopus stolonifer (IC50=8.44 µM) and Magnaporthe grisea (IC50=12.19 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (MAR-2012) to UniProtKB Ma XJ, Liu DL, Tang HS, Wang Y, Sun SR. Purification and characterization of a novel protein from Peganum harmala seeds with antifungal, antiproliferation and anti-HIV-1 reverse transcriptase activities. DRAMP00362 AISCGTVSGALVPCLTYLKGGPGPSPQCCGGVKRLNGAARTTIDRRAACNCLKSSAGSISGLKPGNVATLPGKCGVRLPYTISTSTNCNTIRF 93 Non-specific lipid-transfer protein 1 (Lc-LTP1; Plants) A0AT28 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00363 AISCGAVTSDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCLKSAAGSITKLNTNNAAALPGKCGVNIPYKISTTTNCNTVKF 93 Non-specific lipid-transfer protein 2 (Lc-LTP2; Plants) A0AT29, P84255 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Protein level Alpha helix (6 helices; 57 residues) Not found 2LJO resolved by NMR. "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608##17511608##PubMed ID is not available Biochemistry (Mosc). 2007 Apr;72(4):430-438.##Biochemistry (Mosc). 2007 Apr;72(4):430-438.##To be Published. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV.##Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV.##Shenkarev, Z, Mineev, K, Gizatullina, A, Finkina, E, Arseniev, A, Ovchinnikova, T. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds.##Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds.##Solution structure of lipid transport protein Lc-LTP2 from germinated lentil (Lens Culinaris) seeds. DRAMP00364 AISCGAVTSDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCLKSAAGSITKLNTNNAAALPGKCGVNIPYKISTSTNCNTVKF 93 Non-specific lipid-transfer protein 4 (Lc-LTP4; Plants) A0AT33, P84255 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00365 AISCGAVTGDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCMKSAASSITKLNTNNAAALPGKCGVNIPYKISTSTNCNTVK 92 Non-specific lipid-transfer protein 5 (Lc-LTP5; Plants) A0AT31 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Homology Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00366 AISCGAVTSDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCLKSAAGSITKLNTNNAAALPGKCGVDIPYKISTSTNCNTVKF 93 Non-specific lipid-transfer protein 6 (Lc-LTP6; Plants) A0AT32 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00367 AISCGAVTSDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCLKSAAGSITKLNTNNAAALPGKCGVNIPYKISTTTNCNTVK 92 Non-specific lipid-transfer protein 7 (Lc-LTP7; Plants) A0AT29, P84255 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Protein level Not found Not found 2MAL##5LQV "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00368 AISCGAVTSDLSPCLTYLTGGPGPSPQCCGGVKKLLAAANTTPDRQAACNCLKSAAGSITKLNTNNAAALPGKCGVNIPYKISTSTNCNTVK 92 Non-specific lipid-transfer protein 8 (Lc-LTP8; Plants) A0AT33, P84255 Belongs to the plant LTP family Not found Lens culinaris (Lentil) (Cicer lens) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 4-51; 14-28; 29-74; 49-88." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 17511608 Biochemistry (Mosc). 2007 Apr;72(4):430-438. Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV. Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. DRAMP00369 ITCGLVASKLAPCIGYLQGAPGPSAACCGGIKSLNSAAASPADRKTACTCLKSAATSIKGINYGKAASLPRQCGVSVPYAISPNTNCNAIH 91 IWF1 (Bv-LTP1; Plant defensin) Q43748 Belongs to the plant LTP family IWF1' Beta vulgaris (Sugar beet) Antimicrobial, Antifungal Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Also has fungicide activity. Fungi: Cercospora beticola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8790287 Plant Mol Biol. 1996 Jun;31(3):539-552. Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD. New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. DRAMP00370 ITCGQVTSQVAGCLSYLQRGGAPAPXXXXGIRNLXXMA 38 Antifungal protein 5 (CW-5; Plants) P83139 Belongs to the plant LTP family Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses potent antifungal activity against F. graminearum but not P. infestans. Miscellaneous: Under low salt conditions, possesses potent antifungal activity but activity is drastically reduced under high salt conditions." Fungi: Fusarium graminearum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11302747 Biochem Biophys Res Commun. 2001 Apr 20;282(5):1224-1228. Wang X, Bunkers GJ, Walters MR, Thoma RS. Purification and characterization of three antifungal proteins from cheeseweed (Malva parviflora). DRAMP00371 GPLGGCCGGIKKSAAAGISGINYGIAAGLPGKCGVNIPYKISPSTDCSKVQ 51 Non-specific lipid-transfer protein (LTP; Plant defensin) B3A0N2 Belongs to the plant LTP family Not found Lycium barbarum (Matrimony vine) Unknown Protein level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). Miscellaneous: Causes an allergic reaction." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not availbale Submitted (SEP-2011) to UniProtKB Carnes J, Lopez-matas M.A, Saez R. Allergic sensitization to Goji berries is mediated by a 7 kDa band (LTP). DRAMP00372 AVSCGDVTSSIAPCLSYVMGRESSPSSSCCSGVRTLNGKASSSADRRTACSCLKNMASSFRNLNMGNAASIPSKCGVSVAFPISTSVDCSKIN 93 Non-specific lipid-transfer protein 3 (Os-LTP3) Q2QYL3, Q42976, Q8GZV1 Belongs to the plant LTP family LTP110-A Oryza sativa Japonica Group Antimicrobial, Antifungal Transcript level Not found Not found "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. May possess an antifungal activity and protect the plant against pathogens. PTM: Problely contains four disulfide bonds 4-52; 14-29; 30-75; 50-89. " Pyricularia oryzae, Xanthomonas oryzae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14659081 J Biochem Mol Biol. 2003 Nov 30;36(6):603-607. Ge X, Chen J, Li N, Lin Y, Sun C, Cao K. Resistance Function: of rice lipid transfer protein LTP110. DRAMP00373 ALSCGTVNSNLAACIGYLTQNAPLARGCCTGVTNLNNMAXTTP 43 Seed non-specific lipid transfer protein-like (ns-LTP; Plants) P29420 Belongs to the plant LTP family Not found Raphanus sativus (Radish) Antimicrobial, Antifungal Protein level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. This isoform inhibits the hyphal growth of several fungi in vitro. Fungi: Alternaria brassicola (MUCL 20297) (IC50=48 µg/mL), Ascochyta pisi (MUCL 20164) (IC50=41 µg/mL), Botrytis cinerea (MUCL 30158) (IC50=45 µg/mL), Colletotrichum lindemuthianum (MUCL 9577) (IC50=25 µg/mL), Fusarium culmorum (IMI 180420) (IC50=20 µg/mL), Fusarium oxysporum f. sp. lycopersici (MUCL 909) (IC50=54 µg/mL), Fusarium oxysporum f. sp. pisi (IMI 236441) (IC50=58 µg/mL), Nectria haematococca (Collection Van Etten 26022) (IC50=100 µg/mL), Phoma betae (MUCL 9916) (IC50=18 µg/mL), Pyricularia oryzae (MUCL 30166) (IC50=10 µg/mL), Trichoderma hamatum (MUCL 29736) (IC50=30 µg/mL), Verticillium dahliae (MUCL 6963) (IC50=7 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16653017 Plant Physiol. 1992 Oct;100(2):1055-1058. Terras FR, Goderis IJ, Van Leuven F, Vanderleyden J, Cammue BP, Broekaert WF. In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to non-specific lipid transfer proteins. DRAMP00374 AVSCNTVIADLYPCLSYVTQGGPVPTLCCNGLTTLKSQAQTSVDRQGVCRCIKSAIGGLTLSPRTIQNALELPSKCGVDLPYKFSPSTDCDSIQ 94 Non-specific lipid-transfer protein 6 (LTP 6; Plants) Q9LDB4 Belongs to the plant LTP family LTP6 Arabidopsis thaliana (Mouse-ear cress) Not found Transcript level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). Their biological Function: is presently Comment: No comments found on DRAMP databasen. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 10940464 Plant Sci. 2000 Aug 8;157(1):1-12. Arondel12 V V, Vergnolle2 C, Cantrel C, Kader J. Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana. DRAMP00375 PAGPFRIPPRXRXEFQ 16 Antifungal protein 1 small subunit (CW-1; Plants) P83140 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses very potent antifungal activity against F. graminearum. Subunit structure: Heterodimer of a large and a small subunit. Miscellaneous: Antimicrobial activity is not affected by salt concentration." Fungi:##At low salt condition: Fusarium graminearum (IC50=2.5 ppm).##At high salt condition: Fusarium graminearum (IC50=10 ppm). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11118343 Biochem Biophys Res Commun. 2000 Dec 20;279(2):669-673. Wang X, Bunkers GJ. Potent heterologous antifungal proteins from cheeseweed (Malva parviflora). DRAMP00376 VAGPFRIPPLRREFQ 15 Antifungal protein 1 large subunit (CW-1; Plants) P83141 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity against P. infestans but not F. graminearum. Subunit structure: Heterodimer of a large and a small subunit. Miscellaneous: Antimicrobial activity is not affected by salt concentration." Fungi: Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11118343 Biochem Biophys Res Commun. 2000 Dec 20;279(2):669-673. Wang X, Bunkers GJ. Potent heterologous antifungal proteins from cheeseweed (Malva parviflora). DRAMP00377 SDYSRKRDPPQKYEEE 16 Antifungal protein 2 small subunit (CW-2; Plants) P83142 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity against P. infestans but not F. graminearum. Subunit structure: Heterodimer of a large and a small subunit. Miscellaneous: Antimicrobial activity is not affected by salt concentration." Fungi: Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11118343 Biochem Biophys Res Commun. 2000 Dec 20;279(2):669-673. Wang X, Bunkers GJ. Potent heterologous antifungal proteins from cheeseweed (Malva parviflora). DRAMP00378 PEDPQRRYQEXQREXRXQQE 20 Antifungal protein 2 large subunit (CW-2; Plants) P83143 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity against P. infestans but not F. graminearum. Subunit structure: Heterodimer of a large and a small subunit. Miscellaneous: Antimicrobial activity is not affected by salt concentration." Fungi: Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11118343 Biochem Biophys Res Commun. 2000 Dec 20;279(2):669-673. Wang X, Bunkers GJ. Potent heterologous antifungal proteins from cheeseweed (Malva parviflora). DRAMP00379 PEDPQRRYQEEQRRE 15 Antifungal protein 3 (CW-3; Plants) P83137 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity. Miscellaneous: Antimicrobial activity is not affected by salt concentration." Fungi: Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11302747 Biochem Biophys Res Commun. 2001 Apr 20;282(5):1224-1228. Wang X, Bunkers GJ, Walters MR, Thoma RS. Purification and characterization of three antifungal proteins from cheeseweed (Malva parviflora). DRAMP00380 DRQIDMEEQQLEKLNKQDRXPGLRYAAKQQMXTXRMG 37 Antifungal protein 4 (CW-4; Plants) P83138 Not found Not found Malva parviflora (Little mallow) (Cheeseweed mallow) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity. Miscellaneous: Antimicrobial activity is not affected by salt concentration. Biophysicochemical properties: Temperature dependence (Thermostable). Still active after heating at 100 degrees Celsius for 20 minutes." Fungi: Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11302747 Biochem Biophys Res Commun. 2001 Apr 20;282(5):1224-1228. Wang X, Bunkers GJ, Walters MR, Thoma RS. Purification and characterization of three antifungal proteins from cheeseweed (Malva parviflora). DRAMP00381 SGECNMYGRCPPGYCCSKFGYCGGVRAYCG 30 IWF4 (Plants) No entry found Not found Not found Beta vulgaris (Sugar beet) Antimicrobial, Antifungal Not found Not found Not found Tissue specificity: IWF4 mRNA is expressed in the aerial parts of the plant only, with a constitutive expression in young and mature leaves and in young flowers. Fungi: Cercospora beticola (IC50<2 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 9008390 Plant Physiol. 1997 Jan;113(1):83-91. Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD. Characterization of a new antifungal chitin-binding peptide from sugar beet leaves. DRAMP00382 TFPKCAPTRPPGPKPCDINNFKSKFWHIWRA 31 Datucin (Glycopeptide; Plants) No entry found Not found Not found Datura stramonium Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23193597 Biopolymers 2012; 98(4):332-337. Mandal SM. A Novel Hydroxyproline Rich Glycopeptide from Pericarp of Datura stramonium: Proficiently Eradicate the Biofilm of Antifungals Resistant Candida albicans. DRAMP00383 AKCIKNGKGCREDQGPPFCCSGFCYRQVGWARGYCKNR 38 Antimicrobial peptide 1 (Mc-AMP1; knottin-type peptide; Plant defensin) O81338 Belongs to the AMP family Not found Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Homology Bridge Not found "Function: Possesses antifungal and antibacterial activity. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds 3-20; 10-24; 18-35." Gram-positive bacteria: Bacillus megaterium (IC50=2 µg/mL), Sarcina lutea (IC50=50 µg/mL).##Fungi: Alternaria brassicola (IC50=6 µg/mL), Ascochyta pisi (IC50=6 µg/mL), Botrytis cinerea (IC50=2 µg/mL), Cercospora beticola (IC50=2 µg/mL), Colletotrichum lindemuthianum (IC50=1 µg/mL), Fusarium culmorum (IC50=3 µg/mL), Fusarium oxysporum f. sp. Pisi (IC50=5 µg/mL), Fusarium oxysporum f. sp. Lycopersici (IC50=10 µg/mL), Nectria haematococca (IC50=0.5 µg/mL), Phoma betae (IC50=6 µg/mL), Pyrenophora tritici-repentis (IC50=20 µg/mL), Pyricularia oryzae (IC50=0.5 µg/mL), Rhizoctonia solani (IC50=15 µg/mL), Verticiliium dahliae (IC50=0.5 µg/mL), Venturia inaequalis (IC50=1 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. Michalowski C.B, Bohnert H.J. Antimicrobial peptide 1 from the common ice plant. DRAMP00386 AISCGQVSSAIGPCLSYARGQGSAPSAGCC 30 EcLTP (E. crus-galli lipid transfer protein; Plants) No entry found Not found Not found Echinochloa crusgalli L. (seeds of weed cereal barnyard grass) Antimicrobial, Antifungal Not found Not found Not found Function: Possesses antifungal activity. Fungi: Phytophthora infestans (IC50=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22940285 Peptides. 2012 Nov;38(1):33-40. Rogozhin EA, Ryazantsev DY, Grishin EV, Egorov TA, Zavriev SK. Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds. DRAMP00387 GSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGD 37 Antimicrobial peptide 1 (EcAMP1; hairpin-like peptides; Plants) P86698 Not found Not found Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) Antimicrobial, Antifungal Protein level Alpha helix (3 helices; 20 residues) The peptide adopts a disulfide-stabilized alpha-helical hairpin structure in aqueous solution and thus represents a novel fold among naturally occurring antimicrobial peptides. 2L2R resolved by NMR. "Function: EcAMP1 can inhibit growth of several fungal phytopathogens. Does not destroy spores but rather inhibits hyphal growth during germination. Does not affect spore germination in A. niger, C. graminicola, D. maydis and T. album. Does not inhibit trypsin. Confocal microscopy revealed intensive EcAMP1 binding to the surface of fungal conidia followed by internalization and accumulation in the cytoplasm without disturbance of membrane integrity. Tissue specificity: Seed." Fungi: Alternaria alternata (EC50=16.0±2.3 µM), A. solani (EC50=14.0±2.1 µM), Aspergillus niger (EC50>32 µM), Bipolaris sorokiniana (EC50=18.2±2.7 µM), Colletotrichum graminicola (EC50>10 µM), Diplodia maydis (EC50>10 µM), Fusarium graminearum (EC50=4.5±1.4 µM), Fusarium oxysporum (EC50=8.5±1.6 µM), F. solani (EC50=4.0±1.2 µM), F. verticillioides (EC50=8.1±2.3 µM), Phoma betae (EC50=6.0±1.5 µM), Phytophthora infestans (EC50=16.3±2.5 µM), Pythium debaryanum (EC50=12.0±1.7 µM), P. ultimum (EC50=14.4±2.1 µM), Tritirachium album (EC50>32 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22940285##21561864 Peptides. 2012 Nov;38(1):33-40.##J Biol Chem. 2011 Jul 15;286(28):25145-25153. Rogozhin EA, Ryazantsev DY, Grishin EV, Egorov TA, Zavriev SK.##Nolde SB, Vassilevski AA, Rogozhin EA, Barinov NA, Balashova TA, Samsonova OV, Baranov YV, Feofanov AV, Egorov TA, Arseniev AS, Grishin EV. Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds.##Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli). DRAMP00388 DRCSQQCQHHRDPDRKQQCMRECRRHQGRSD 31 Antimicrobial peptide 2 (EcAMP2; Plants) B3EWR4 Not found Not found Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) Antimicrobial, Antifungal Protein level Not found Not found "Function: EcAMP2 inhibits spore germination of P. infestans with an IC50 of 24 µM but have no antibacterial activity. PTM: Contains two disulfide bonds (By similarity)." Fungi: Phytophthora infestans (IC50=24 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22940285 Peptides. 2012 Nov;38(1):33-40. Rogozhin EA, Ryazantsev DY, Grishin EV, Egorov TA, Zavriev SK. Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds. DRAMP00389 DRCSQQCQHHRDPDRKQQCMRECRRH 26 EcAMP2.1 (truncated EcAMP2 without five C-terminal residues) B3EWR4 Not found Not found Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) Antimicrobial, Antifungal Protein level Not found Not found "Function: EcAMP2.1 inhibits spore germination of P. infestans with an IC50 of 24 µM but have no antibacterial activity. PTM: Contains two disulfide bonds (By similarity)." Fungi: Phytophthora infestans (IC50=24 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22940285 Peptides. 2012 Nov;38(1):33-40. Rogozhin EA, Ryazantsev DY, Grishin EV, Egorov TA, Zavriev SK. Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds. DRAMP00390 ANKCIIDCMKVKTTCGDECKGAGFKTGGCALPPDIMKCCHNC 42 Antimicrobial peptide 3 (ToAMP3; Cys-rich; Plant defensin) B3EWQ3 Not found Not found Taraxacum officinale (Common dandelion) (Leontodon taraxacum) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity. Also active against bacterial species P. syringae, B. subtilis and X. campestris. Tissue specificity: Expressed in flowers but not in leaves, seeds or roots (at protein level)." Fungi: Aspergillus niger (IC50=1.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22640720 Peptides. 2012 Aug;36(2):266-271. Astafieva AA, Rogozhin EA, Odintsova TI, Khadeeva NV, Grishin EV, Egorov TsA. Discovery of novel antimicrobial peptides with unusual cysteine motifs in dandelion Taraxacum officinale Wigg. flowers. DRAMP00391 GGKCTVDWGGQGGGRRLPSPLFCCYKPTRICYLNQETCETETCP 44 Antimicrobial peptide 2 (ToAMP2; Cys-rich; Plant defensin) B3EWQ2 Not found Not found Taraxacum officinale (Common dandelion) (Leontodon taraxacum) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity. Also active against bacterial species P. syringae, B. subtilis and X. campestris. Tissue specificity: Expressed in flowers but not in leaves, seeds or roots (at protein level)." Fungi: Botrytis cinerea (IC50=5.2 µM), Aspergillus niger (IC50=2.6 µM), Bipolaris sorokiniana (IC50=5.2 µM), Pythium debaryanum (IC50=2.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22640720 Peptides. 2012 Aug;36(2):266-271. Astafieva AA, Rogozhin EA, Odintsova TI, Khadeeva NV, Grishin EV, Egorov TsA. Discovery of novel antimicrobial peptides with unusual cysteine motifs in dandelion Taraxacum officinale Wigg. flowers. DRAMP00392 VAKCTEESGGKYFVFCCYKPTRICYMNEQKCESTCIGK 38 Antimicrobial peptide 1 (ToAMP1; Cys-rich; Plant defensin) B3EWQ1 Not found Not found Taraxacum officinale (Common dandelion) (Leontodon taraxacum) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity. Also active against bacterial species P. syringae, B. subtilis and X. campestris. Tissue specificity: Expressed in flowers but not in leaves, seeds or roots (at protein level)." Fungi: Botrytis cinerea (IC50=5.8 µM), Aspergillus niger (IC50=5.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22640720 Peptides. 2012 Aug;36(2):266-271. Astafieva AA, Rogozhin EA, Odintsova TI, Khadeeva NV, Grishin EV, Egorov TsA. Discovery of novel antimicrobial peptides with unusual cysteine motifs in dandelion Taraxacum officinale Wigg. flowers. DRAMP00393 IQCGESCVWIPCISSAWGCSCKNKICSS 28 Hedyotide B2 (hB2; Uncyclotides; Plants) No entry found Not found Not found Hedyotis biflora (aerial tissues) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Possesses antifungal activity. Gram-negative bacterium: Escherichia coli (MIC>80 µM);##Gram-positive bacteria: Streptococcus salivarius(MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM), Streptococcus aureus (MIC>80 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21979955 J Biol Chem. 2011 Dec 30;286(52):44833-44844. Nguyen GK, Zhang S, Wang W, Wong CT, Nguyen NT, Tam JP. Discovery of a linear cyclotide from the bracelet subfamily and its disulfide mapping by top-down mass spectrometry. DRAMP00394 FSGSVNQACSGFGWK 15 Antimicrobial peptide1 (Plant defensin) P85484 Not found Not found Pinus halepensis (Aleppo pine) Antimicrobial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19157640 J Plant Physiol. 2009 May 15;166(8):831-143. Uzal EN, G³mez-Ros LV, Hern¡ndez JA, Pedre±o MA, Cuello J, Ros Barcel³ A. Analysis of the soluble cell wall proteome of gymnosperms. DRAMP00395 GIPCGESCVWIPCITSAIGCSCKSKVCYRN 30 Cyclotide vitri-A (Vbc6; Plant defensin) B1NRR3 Not found Not found Viola biflora (Yellow wood violet) Antimicrobial Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 4-20; 8-22; 13-27. This is a cyclic peptide." No MICs found in DRAMP database [Ref.20580652] HD50=8.91 µM against human type O red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys 4 and Cys20, Cys8 and Cys22, Cys13 and Cys27 . L [Ref.14987049] Cytotoxicity: U-937 GTB (lymphoma)(IC50 = 0.6 µM) and RPMI-8226/s (myeloma)(IC50 = 1 µM).##[Ref.20580652] Cytotoxicity: U251(IC50 = 6.03 μg/mL), MDA-MB-231(IC50 = 3.69 μg/mL), A549(IC50 = 3.90 μg/mL), DU145(IC50 = 3.07 μg/mL), BEL-7402(IC50 = 4.94 μg/mL). Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00396 NLCERASLTWTGNCGNTGHCDTQCRNWESAKHGACHKRGNWKCFCYFDC 49 Ct-AMP1 (CtAMP1, C. ternatea-antimicrobial peptide 1; Plant defensin) No entry found Not found Not found Clitoria ternatea Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Bacillus subtilis (IC50=15 µg/mL).##Medium A: Botrytis cinerea (IC50=20 µg/ml), Cladosporium sphaerospermum (IC50=6 µg/ml), Fusarium culmorum (IC50=10 µg/ml), Leptosphaeria maculans (IC50=6 µg/ml), Penicillium digitatum (IC50=20 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=2 µg/ml), Verticilium albo-atrum (IC50=2 µg/ml). NOTE: Medium B = 1/2 strength potato dextrose broth.##Medium B: Botrytis cinerea (IC50>100 µg/ml), Cladosporium sphaerospermum (IC50=100 µg/ml), Fusarium culmorum (IC50=50 µg/ml), Leptosphaeria maculans (IC50=20 µg/ml), Penicillium digitatum (IC50=80 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=80 µg/ml), Verticilium albo-atrum (IC50>100 µg/ml).##NOTE: Medium B = Medium A supplemented with 1 mM CaCl2 and 50 mM KCI. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7628617 FEBS Lett. 1995 Jul 17;368(2):257-262. Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. DRAMP00397 KFCEKPSGTWSGVCGNSGACKDQCIRLEGAKHGSCNYKPPAHRCICYYEC 50 Defensin D1 (Ns-D1; Plant defensin) P86972 Belongs to the DEFL family Not found Nigella sativa (Black cumin) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Antimicrobial peptide active against fungi, Gram-positive and Gram-negative bacteria. Has no effect on spore germination. Destroys spores in germinated conidia by disruption of cell walls and membranes in A. niger and B. sorokiniana. Causes vacuolization of germinated macro- and microconidia in F. oxysporum, F. graminearum and F. culmorum. Strongly inhibits growth of P. infestans on potato tubers above concentrations of 13.6 µg/ml. PTM: Contains four disulfide bonds." Fungi: Aspergillus niger (IC50=3.5 µg/ml), Bipolaris sorokiniana (IC50=3.0 µg/ml), Fusarium oxysporum (IC50=9.5 µg/ml), Fusarium graminearum (IC50=6.9 µg/ml), Fusarium culmorum (IC50=6.9 µg/ml) and Botrytis cinerea (IC50=27.4 µg/ml).##Gram-positive bacteria: Clavibacter michiganensis (1.4 cm) and Bacillus subtilis (1.3 cm);##Gram-negative bacteria: Pseudomonas syringae (0.9 cm), Erwinia carotovora (0.7 cm) and Escherichia coli (1.2 cm).##NOTE: Inhibition zone; Defensin concentration (11 µg in 50 μl). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21144761 Plant Physiol Biochem. 2011 Feb;49(2):131-137. Rogozhin EA, Oshchepkova YI, Odintsova TI, Khadeeva NV, Veshkurova ON, Egorov TA, Grishin EV, Salikhov SI. Novel antifungal defensins from Nigella sativa L. seeds. DRAMP00398 KFCEKPSGTWSGVCGNSGACKDQCIRLEGAKHGSCNYKLPAHRCICYYEC 50 Defensin D2 (Ns-D2; Plant defensin) P86973 Belongs to the DEFL family Not found Nigella sativa (Black cumin) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Antimicrobial peptide active against fungi, Gram-positive and Gram-negative bacteria. Has no effect on spore germination. Destroys spores in germinated conidia by disruption of cell walls and membranes in Aspergillus niger and B.sorokiniana. Causes vacuolization of germinated macro- and microconidia in Fusarium oxysporum, F.graminearum and F.culmorum. Strongly inhibits growth of P.infestans on potato tubers above concentrations of 3.4 µg/ml. PTM: Contains four disulfide bonds." Fungi: Aspergillus niger (IC50=3.5 µg/ml), Bipolaris sorokiniana (IC50=1.8 µg/ml), Fusarium oxysporum (IC50=5.3 µg/ml), Fusarium graminearum (IC50=6.9 µg/ml), Fusarium culmorum (IC50=6.9 µg/ml) and Botrytis cinerea (IC50=13.7 µg/ml).##Gram-positive bacteria: Clavibacter michiganensis (1.5 cm) and Bacillus subtilis (1.3 cm);##Gram-negative bacteria: Pseudomonas syringae (1.3 cm), Erwinia carotovora (0.7 cm) and Escherichia coli (1.4 cm).##NOTE: Inhibition zone; Defensin concentration (11 µg in 50 μl). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21144761 Plant Physiol Biochem. 2011 Feb;49(2):131-137. Rogozhin EA, Oshchepkova YI, Odintsova TI, Khadeeva NV, Veshkurova ON, Egorov TA, Grishin EV, Salikhov SI. Novel antifungal defensins from Nigella sativa L. seeds. DRAMP00399 NTCEHLADTYRGVCFTNASCDDHCKNKAHLISGTCHDWKCFCTQNC 46 Defensin-like protein 39 (Disease resistance response protein 39; Plant defensin) Q01784 Belongs to the DEFL family PI39 Pisum sativum (Garden pea) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Possesses antifungal activity (By similarity). Tissue specificity: Pods. Induction: Upon contact with the plant pathogen fungus Fusarium solani. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1799696 Mol Plant Microbe Interact. 1991 Jul-Aug;4(4):324-331. Chiang CC, Hadwiger LA. The Fusarium solani-induced expression of a pea gene family encoding high cysteine content proteins. DRAMP00400 NLCERASLTWTGNCGNTGHCDTQCRNWESAKHGACHKRGNWKCFCYFNC 49 Defensin-like protein 1 (Defensin AMP1, CtAMP1; Plant defensin) Q7M1F2 Belongs to the DEFL family Not found Clitoria ternatea (Butterfly pea) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Possesses antimicrobial activity sensitive to inorganic cations. Binds specifically to the fungal plasma membrane. Has no inhibitory effect on insect gut alpha-amylase. PTM: Contains four disulfide bonds (By similarity)." Fungi: Botrytis cinerea (IC50=20 µg/ml), Cladosporium sphaerospermum (IC50=6 µg/ml), Fusarium culmorum (IC50=10 µg/ml), Leptosphaeria maculans (IC50=6 µg/ml), Penicillium digitatum (IC50=20 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=2 µg/ml), Verticilium albo-atrum (IC50=2 µg/ml), Neurospora crassa (IC50<0.3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet fungal plasma membrane 7628617##10656585 FEBS Lett. 1995 Jul 17;368(2):257-262.##Mol Plant Microbe Interact. 2000 Jan;13(1):54-61. Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF.##Thevissen K, Osborn RW, Acland DP, Broekaert WF. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.##Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. DRAMP00401 DSECLKEYGGDVGFPFCAPRIFPTICYTRCRENKGAKGGRCIWGEGTNVKCLCDYCNDSPFDQ 63 Defensin-like protein 2 (MTI-2; Trypsin inhibitor 2; Plant defensin) P26780 Belongs to the DEFL family Not found Sinapis alba (White mustard) (Brassica hirta) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Inhibits bovine beta-trypsin and alpha-chymotrypsin on a 1:1 molar basis. PTM: Problely contains four disulfide bonds 4-56; 17-41; 26-51; 30-53." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7750566##1451776 FEBS Lett. 1995 May 8;364(2):179-181.##FEBS Lett. 1992 Apr 13;301(1):10-14. Ceci LR, Spoto N, de Virgilio M, Gallerani R.##Menegatti E, Tedeschi G, Ronchi S, Bortolotti F, Ascenzi P, Thomas RM, Bolognesi M, Palmieri S. The gene coding for the mustard trypsin inhibitor-2 is discontinuous and wound-inducible.##Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seed. DRAMP00402 XTCESPSHKFKGPCATNRNCES 22 Defensin D1 (So-D1; Antimicrobial peptide D1; Plant defensin) P81572 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide. Active against Gram-positive and Gram-negative bacterial pathogens. Gram-positive bacterium: Clavibacter michiganensis;##Gram-negative bacterium: Ralstonia solanacearum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garc­a-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00403 GIFSSRKCKTPSKTFKGICTRDSNCDTSCRYEGYPAGDCKGIRRRCMCSKPC 52 Defensin D2 (So-D2; Antimicrobial peptide D2; Plant defensin) P81571 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf. PTM: Contains four disulfide bonds (By similarity)." Gram-positive bacterium: Clavibacter michiganensis;##Gram-negative bacterium: Ralstonia solanacearum.##Fungi: Fusarium culmorum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garc­a-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00404 GIFSSRKCKTVSKTFRGICTRNANC 25 Defensin D3 (So-D3; Antimicrobial peptide D3; Plant defensin) P81570 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." Fungi: Fusarium spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00405 MFFSSKKCKTVSKTFRGPCVRNA 23 Defensin D4 (So-D4; Antimicrobial peptide D4; Plant defensin) P81569 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." Fungi: Fusarium spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00406 MFFSSKKCKTVXKTFRGPCVRNAN 24 Defensin D5 (So-D5; Antimicrobial peptide D5; Plant defensin) P81568 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." Gram-positive bacterium: Clavibacter michiganensis;##Gram-negative bacterium: Ralstonia solanacearum.##Fungi: Fusarium culmorum, Fusarium solani, Bipolaris maydis and Colletotrichum lagenarium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00407 GIFSNMYXRTPAGYFRGPXGYXXN 24 Defensin D6 (So-D6; Antimicrobial peptide D6; Plant defensin) P81567 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." Gram-positive bacterium: Clavibacter michiganensis (EC50=1 µM);##Gram-negative bacterium: Ralstonia solanacearum (EC50=6 µM).##Fungi: Fusarium solani (EC50=11 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00408 GIFSSRKCKTPSKTFKGYCTRDSNCDTSCRYEGYPAGD 38 Defensin D7 (So-D7; Antimicrobial peptide D7; Plant defensin) P81573 Belongs to the DEFL family Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." Fusarium spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9762899 FEBS Lett. 1998; 435: 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP00409 KTCENLADTY 10 Defensin-like protein (Sesquin; Plant defensin) P84868 Belongs to the DEFL family Not found Vigna unguiculata subsp. sesquipedalis (Yard-Long bean) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Protein level Not found Not found Function: Has antifungal and antibacterial activity. Has mitogenic activity towards murine splenocytes. Inhibits the proliferation of M1 leukemia and MCF-7 breast cancer cells in vitro. Inhibits human immunodeficiency virus-1 (HIV-1) reverse transcriptase. Fungi: Botrytis cinerea (IC50=2.5±0.01 µM), Fusarium oxysporum (IC50=1.4±0.02 µM), Mycosphaerella arachidicola (IC50=0.15±0.002 µM).##Gram-positive bacteria: Bacillus megaterium, Mycobacterium phlei;##Gram-negative bacteria: Escherichia coli, Proteus vulgaris. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15949629 Peptides. 2005 Jul;26(7):1120-1126. Wong JH, Ng TB Sesquin, a potent defensin-like antimicrobial peptide from ground beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase. DRAMP00410 QKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHK 44 Defensin-like protein 1 (Bn-AFP1; Plant defensin) P69240, P30225, Q41163 Belongs to the DEFL family AFP1 Brassica napus (Rape) Antimicrobial, Antifungal Protein level Rich Not found 1AYJ "Function: Possesses antifungal activity sensitive to inorganic cations. Subunit structure: Forms oligomers in its native state. PTM: Problely contains one disulfide bond." Fungi: Alternaria brassicola (IC50=3 µg/ml), Botrytis cinerea (IC50=1.50 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Fusarium oxysporum f.sp.lycopersici (IC50=1.80 µg/ml), Pyricularia oryzae (IC50=0.25 µg/ml), Verticiliium dahliae (IC50=0.80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949 FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP00411 QKLCERPSGTWSGVCGNNNACKN 23 Defensin-like protein 2 (Bn-AFP2; Plant defensin) P30226 Belongs to the DEFL family Not found Brassica napus (Rape) Antimicrobial, Antifungal Protein level Rich Not found "Function: Possesses antifungal activity sensitive to inorganic cations. Subunit structure: Forms oligomers in its native state." Fungi: Alternaria brassicola (IC50=75 µg/ml), Botrytis cinerea(IC50> 100 µg/ml), Fusarium culmorum (IC50=38 µg/ml), Fusarium oxysporum f.sp.lycopersici (IC50=42 µg/ml), Pyricularia oryzae (IC50=3 µg/ml), Verticiliium dahliae (IC50=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949 FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP00412 QKLCERPSGTWSGVCGNNNACKNQCIN 27 Defensin-like protein 1 (Br-AFP1; Plant defensin) P30227 Belongs to the DEFL family Not found Brassica rapa (Turnip) Antimicrobial, Antifungal Protein level Not found Not found "Function: Possesses antifungal activity sensitive to inorganic cations. Subunit structure: Forms oligomers in its native state." Fungi: Alternaria brassicola (IC50=3 µg/ml), Botrytis cinerea(IC50=1.5 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Fusarium oxysporum f.sp. lycopersici (IC50=1.8 µg/ml), Pyricularia oryzae (IC50=0.25 µg/ml), Verticiliium dahliae (IC50=0.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949 FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP00413 QKLCERPSGTXSGVCGNNNACKNQCIR 27 Defensin-like protein 2 (Br-AFP2; Plant defensin) P30228 Belongs to the DEFL family Not found Brassica rapa (Turnip) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). Fungi: Alternaria brassicola (IC50=75 µg/ml), Botrytis cinerea(IC50>100 µg/ml), Fusarium culmorum (IC50=38 µg/ml), Fusarium oxysporum f.sp. lycopersici (IC50=42 µg/ml), Pyricularia oryzae (IC50=3 µg/ml), Verticiliium dahliae (IC50=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949 FEBS Lett. 1993 Feb 1;316(3):233-240. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. DRAMP18331 GKNGVFKTISHECHLNTWAFLATCCS 26 Antibacterial peptide A-M49 (Bacteriocin) Q54957 Belongs to the lantibiotics family (Class I bacteriocin) scnA' AND scnA'' Streptococcus pyogenes serotype M49 Antimicrobial, Antibacterial, Anti-Gram+ Not found There are one 2,3-didehydrobutyrine at T23, two Beta-methyllanthionines (T8-C13; T17-C25) and one Lanthionine (S10-C24). There are two genes coding for lantibiotic streptococcin A-M49, their coding sequences only differ in the propeptide region. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7993103 Appl Environ Microbiol. 1994 Nov;60(11):4207-9. Hynes WL, Friend VL, Ferretti JJ. Duplication of the lantibiotic structural gene in M-type 49 group A streptococcus strains producing streptococcin A-M49. DRAMP18332 GTTVVNSTFSIVLGNKGYICTVTVECMRNCQ 31 BHT-Aa(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) bht-a Streptococcus rattus BHT Antimicrobial, Antibacterial, Anti-Gram+ tryptophan rich A variant of Smb, as evidenced by the fact that the two operons share 95% identity. The amino acid sequence of another chain (BhtA2) is STPACAIGVVGITVAVTGISTACTSRCINK, which is identical to SmbA. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16194596##18220976 FEMS Microbiol Lett. 2005 Nov 15;252(2):235-41.##Mini Rev Med Chem. 2007 Dec;7(12):1236-47. Hyink O, Balakrishnan M, Tagg JR.##Lawton EM, Ross RP, Hill C, Cotter PD. Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin.##Two-peptide lantibiotics: a medical perspective. DRAMP00415 QKLCQRPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC 51 Raphanus sativus Antifungal Protein 2 (Rs-AFP2; Plant defensin) P30230, Q003I2 Belongs to the DEFL family AFP2 Raphanus sativus (Radish) Antimicrobial, Antifungal Protein level Bridge Not found 2N2R PTM: Contains four disulfide bonds 4-51;15-36;21-45;25-47, and Pyrrolidone carboxylic acid at position 1. Fungi: Alternaria brassicola (IC50=2 µg/ml), Ascochyta pisi (IC50=4 µg/ml), Botrytis cinerea (IC50=2 µg/ml), Cercospora beticola (IC50=2 µg/ml), Colletotrichum lindemuthianum (IC50=3 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Fusarium oxysporum f.sp.lycopersici (IC50=2 µg/ml), Fusarium oxysporum f.sp.pisi (IC50=2 µg/ml), Mycosphaerella fijiensis var.fijiensis (IC50=1.5 µg/ml), Nectria haematococca (IC50=2 µg/ml), Phoma betae (IC50=1 µg/ml), Phytophthora infestans (IC50=25 µg/ml), Pyrenophora tritici-repentis (IC50=1.5 µg/ml), Pyricularia oryzae (IC50=0.4 µg/ml), Rhizoctonia solani (IC50>100 µg/ml), Sclerotinia sclerotiorum (IC50>100 µg/ml), Septoria nodorum (IC50=15 µg/ml), Trichoderma hamatum (IC50=2 µg/ml), Verticillium dahliae (IC50=1.5 µg/ml), Venturia inaequalis (IC50=25 µg/ml). [NOTE: Synthetic low ionic strength growth medium] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7780308 Plant Cell. 1995 May;7(5):573-588. Terras FR, Eggermont K, Kovaleva V, Raikhel NV, Osborn RW, Kester A, Rees SB, Torrekens S, Van Leuven F, Vanderleyden J, et al. Small cysteine-rich antifungal proteins from radish: their role in host defense. DRAMP00418 QKLCERPSGTWSGVCGNNGACRNQCIRLERARHGSCNYVFPAHKCICYFPC 51 Hc-AFP4 (Plant defensin) No entry found Not found Hc-AFP4 Heliophila coronopifolia (South African Brassicaceae species) Antimicrobial, Antifungal Not found Not found Not found "Function: Has antifungal activity. PTM: Contains four disulfide bonds." Fungi: Botrytis cinerea (IC50=15-20 µg/ml), Fusarium solani (IC50=5-10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22032337 BMC Res Notes. 2011 Oct 28;4:459. de Beer A, Vivier MA. Four plant defensins from an indigenous South African Brassicaceae species display divergent activities against two test pathogens despite high sequence similarity in the encoding genes. DRAMP00419 RYCERSSGTWSGVCGNTDKCSSQCQRLEGAAHGSCNYVFPAHKCICYYPC 50 Hc-AFP3 (Plant defensin) No entry found Not found Hc-AFP3 Heliophila coronopifolia (South African Brassicaceae species) Antimicrobial, Antifungal Not found Not found Not found "Function: Has antifungal activity. PTM: Contains four disulfide bonds." Fungi: Botrytis cinerea (IC50=20-25 µg/ml), Fusarium solani (IC50>25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22032337 BMC Res Notes. 2011 Oct 28;4:459. de Beer A, Vivier MA. Four plant defensins from an indigenous South African Brassicaceae species display divergent activities against two test pathogens despite high sequence similarity in the encoding genes. DRAMP00420 QKLCERPSGTWSGVCGNNNACRNQCINLEKARHGSCNYVFPAHKCICYFPC 51 Hc-AFP2 (Plant defensin) No entry found Not found Hc-AFP2 Heliophila coronopifolia (South African Brassicaceae species) Antimicrobial, Antifungal Not found Not found Not found "Function: Has antifungal activity. PTM: Contains four disulfide bonds." Fungi: Botrytis cinerea (IC50=10-15 µg/ml), Fusarium solani (IC50=10-15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22032337 BMC Res Notes. 2011 Oct 28;4:459. de Beer A, Vivier MA. Four plant defensins from an indigenous South African Brassicaceae species display divergent activities against two test pathogens despite high sequence similarity in the encoding genes. DRAMP00421 RYCERSSGTWSGVCGNSGKCSNQCQRLEGAAHGSCNYVFPAHKCICYYPC 50 Hc-AFP1 (Plant defensin) No entry found Not found Hc-AFP1 Heliophila coronopifolia (South African Brassicaceae species) Antimicrobial, Antifungal Not found Not found Not found "Function: Has antifungal activity. PTM: Contains four disulfide bonds." Fungi: Botrytis cinerea (IC50>25 µg/ml), Fusarium solani (IC50>25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22032337 BMC Res Notes. 2011 Oct 28;4:459. de Beer A, Vivier MA. Four plant defensins from an indigenous South African Brassicaceae species display divergent activities against two test pathogens despite high sequence similarity in the encoding genes. DRAMP00424 QKLCERSSGTWSGVCGNNNACKNQCINLEGARHGSCNYVFPYHRCICYFPC 50 Br-AFP1 (Defensin 1.2; Plant defensin) No entry found Not found Not found Brassica rapa subsp. Chinensis Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949##7628617 FEBS Lett. 1993 Feb 1;316(3):233-240.##FEBS Lett. 1995 Jul 17;368(2):257-262. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF.##Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species.##Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. DRAMP00426 DGVKLCDVPSGTWSGHCGSSSKCSQQCKDREHFAYGGACHYQFPSVKCFCKRQC 54 Defensin-like protein 1 (Hs-AFP1; Plant defensin) Q7M1F4, P0C8Y5 Belongs to the DEFL family Not found Heuchera sanguinea (Coralbells) Antimicrobial, Antifungal Protein level Bridge Not found 2N2Q "Function: Possesses antifungal activity insensitive to inorganic cations. Causes germ tubes and hyphae to swell and form multiple hyphal buds. Binds to the plasma membrane of the fungus. Has no inhibitory effect on insect gut alpha-amylase. PTM: Contains four disulfide bonds (By similarity)." Fungi: Botrytis cinerea (IC50=6 µg/ml), Cladosporium sphaerospermum (IC50=1 µg/ml), Fusarium culmorum (IC50=1 µg/ml), Leptosphaeria maculans (IC50=25 µg/ml), Penicillium digitatum (IC50=1µg/ml), Trichoderma viride (IC50=15 µg/ml), Septoria tritiei (IC50=0.5 µg/ml), Verticillium albo-atrum (IC50=0.5 µg/ml), Neurospora crassa (IC50=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet chitin, mannan, galactocerebrosides, and sphingomyelin (Mycopathologia. 1998-1999;144:87-91) 7628617##9405418##16284838 FEBS Lett. 1995 Jul 17;368(2):257-262.##J Biol Chem. 1997 Dec 19;272(51):32176-32181.##Mycopathologia. 1998-1999;144(2):87-91. Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF.##Thevissen K, Osborn RW, Acland DP, Broekaert WF.##De Lucca AJ, Jacks TJ, Broekaert WJ. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.##Specific, high affinity binding sites for an antifungal plant defensin on Neurospora crassa hyphae and microsomal membranes.##Fungicidal and binding properties of three plant peptides. DRAMP00427 AICKKPSKFFKGACGRDADCEKACDQENWPGGVCVPFLRCECQRSC 46 Defensin-like protein AX1 (Antifungal protein AX1; Plant defensin) P81493 Belongs to the DEFL family Not found Beta vulgaris (Sugar beet) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Not found Not found "Function: Strong inhibiting activity against C. beticola and other filamentous fungi. Little or no effect against bacteria. Tissue specificity: Leaves and flowers. PTM: Contains four disulfide bonds 3-46; 14-34; 20-40; 24-42 (By similarity)." Fungi: Cercospora beticola, Botrytis cinerea, Fusarium graminearum, Bipolaris maydis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7655063 Mol Plant Microbe Interact. 1995 May-Jun;8(3):424-434. Kragh KM, Nielsen JE, Nielsen KK, Dreboldt S, Mikkelsen JD. Characterization and localization of new antifungal cysteine-rich proteins from Beta vulgaris. DRAMP00428 ATCRKPSMYFSGACFSDTNCQKACNREDWPNGKCLVGFKCECQRPC 46 Defensin-like protein AX2 (Antifungal protein AX2; Cys-rich; Plant defensin) P82010, P81510 Belongs to the DEFL family Not found Beta vulgaris (Sugar beet) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Not found Not found "Function: Strong inhibiting activity against C. beticola and other filamentous fungi. Little or no effect against bacteria. Tissue specificity: Leaves and flowers. PTM: Contains four disulfide bonds 3-46; 14-34; 20-40; 24-42 (By similarity)." Fungi: Cercospora beticola, Botrytis cinerea, Fusarium graminearum, Bipolaris maydis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7655063 Mol Plant Microbe Interact. 1995 May-Jun;8(3):424-434. Kragh KM, Nielsen JE, Nielsen KK, Dreboldt S, Mikkelsen JD. Characterization and localization of new antifungal cysteine-rich proteins from Beta vulgaris. DRAMP00429 LCNERPSQTWSGNCGNTAHCDKQCQDWEKASHGACHKRENHWKCFCYFNC 50 Aesculus hippocastanum antimicrobial protein 1 (Ah-AMP1; Cys-rich; Plant defensin) Q7M1F3 Belongs to the DEFL family Not found Aesculus hippocastanum (Horse chestnut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Combine helix and strand structure Not found 1BK8 resolved by NMR. "Function: Possesses antimicrobial activity sensitive to inorganic cations. Binds specifically to the fungal plasma membrane. Has no inhibitory effect on insect gut alpha-amylase. PTM: Contains four disulfide bonds 2-50; 14-35; 20-44; 24-46 (By similarity)." Gram-positive bacterium: Bacillus subtilis (IC50=100 µg/mL).##Fungi: [MA: Botrytis cinerea (IC50=25 µg/mL), Cladosporium sphaerospermum (IC50=0.5 µg/mL), Fusarium culmorum (IC50=12 µg/mL), Leptosphaeria maculans (IC50=0.5 µg/mL), Penicillium digitatum (IC50=6 µg/mL), Trichoderma viride (IC50>100 µg/mL), Septoria tritiei (IC50=0.5 µg/mL), Verticilium albo-atrum (IC50=6 µg/mL). MA+: Botrytis cinerea (IC50>100 µg/mL), Cladosporium sphaerospermum (IC50=12 µg/mL), Fusarium culmorum (IC50>100 µg/mL), Leptosphaeria maculans (IC50=6 µg/mL), Penicillium digitatum (IC50=25 µg/mL), Trichoderma viride (IC50>100 µg/mL), Septoria tritiei (IC50=1.5 µg/mL), Verticilium albo-atrum (IC50>100 µg/mL)].##NOTE: MA+ = MA supplemented with 1 mM CaCl2 and 50 mM KCl. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binds specifically to the fungal plasma membrane. 7628617##10591099##10656585 FEBS Lett. 1995 Jul 17;368(2):257-262.##Proteins. 1999 Nov 15;37(3):388-403.##Mol Plant Microbe Interact. 2000 Jan;13(1):54-61. Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF.##Fant F, Vranken WF, Borremans FA.##Thevissen K, Osborn RW, Acland DP, Broekaert WF. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.##The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.##Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. DRAMP00430 RVCESQSHGFKGACTGDHNCALVCRNEGFSGGNCRGFRRRCFCTLKC 47 Defensin-like protein 1 (Cp-thionin I; Cp-thionin-1; Gamma-thionin I; Plant defensin) P83399 Belongs to the DEFL family Not found Vigna unguiculata (Cowpea) Not found Protein level Bridge Not found "Function: Inhibits trypsin but not chymotrypsin. Subunit structure: Monomer and homodimer. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12112698 Proteins. 2002 Aug 1;48(2):311-319. Melo FR, Rigden DJ, Franco OL, Mello LV, Ary MB, Grossi de S¡ MF, Bloch C Jr. Inhibition of trypsin by cowpea thionin: characterization, molecular modeling, and docking. DRAMP00432 RVCRRRSAGFKGVCMSDHNCAQVCLQEGYGGGNCDGIMRQCKCIRQC 47 Defensin-like protein 1 (Gamma-zeathionin-1; Plant defensin) P81008 Belongs to the DEFL family Not found Zea mays (Maize) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Sodium channel blocker. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Protein Pept. Lett. 1996;3:267-274. Castro M.S, Fontes W, Morhy L, Bloch C. Jr. Complete amino acid sequences of two gamma-thionins from maize (Zea mays L.) seeds. DRAMP00433 RVCMGKSQHHSFPCISDRLCSNECVKEDGGWTAGYCHLRYCRCQKAC 47 Defensin-like protein 2 (Gamma-zeathionin-2; Plant defensin) P81009 Belongs to the DEFL family Not found Zea mays (Maize) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Sodium channel blocker. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Protein Pept. Lett. 1996;3:267-274. Castro M.S, Fontes W, Morhy L, Bloch C. Jr. Complete amino acid sequences of two gamma-thionins from maize (Zea mays L.) seeds. DRAMP00434 KICRRRSAGFKGPCMSNKNCAQVCQQEGWGGGNCDGPFRRCKCIRQC 47 Defensin-like protein 1 (Gamma-1-purothionin; Plant defensin) P20158 Belongs to the DEFL family Not found Triticum aestivum (Wheat) Antimicrobial, Antifungal Protein level Bridge Gamma 1-P has a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. 1GPS PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2226781##8380707 FEBS Lett. 1990 Sep 17;270(1-2):191-194.##Biochemistry. 1993 Jan 19;32(2):715-724. Colilla FJ, Rocher A, Mendez E.##Bruix M, Jim©nez MA, Santoro J, Gonz¡lez C, Colilla FJ, M©ndez E, Rico M. Gamma-Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm.##Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. DRAMP00435 KVCRQRSAGFKGPCVSDKNCAQVCLQEGWGGGNCDGPFRRCKCIRQC 47 Defensin-like protein 2 (Gamma-2-purothionin; Plant defensin) P20159 Belongs to the DEFL family Not found Triticum aestivum (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2226781 FEBS Lett. 1990 Sep 17;270(1-2):191-194. Colilla FJ, Rocher A, Mendez E. Gamma-Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. DRAMP00438 KSTCKAESNTFPGLCITKPPCRKACLSEKFTDGKCSKILRRCICYKPCVFDGKMIQTGAENLAEEAETLAAALLEEEMMDN 81 Defensin-like protein 1 (Gamma-thionin 1; Plant defensin) O24115 Belongs to the DEFL family THIO1 Nicotiana paniculata Antimicrobial, Antifungal Transcript level Bridge Not found PTM: Contains four disulfide bonds 4-48; 15-35; 21-42; 25-44. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Gene Register PGR97-132. Komori T, Yamada S, Imaseki H. A cDNA clone for gamma-thionin from Nicotiana paniculata. DRAMP00439 RTCESQSHRFHGTCVRESNCASVCQTEGFIGGNCRAFRRRCFCTRNC 47 Defensin-like protein (Gamma-thionin homolog PPT; Plant defensin) Q40901 Belongs to the DEFL family Not found Petunia integrifolia (Violet-flowered petunia) Antimicrobial, Antifungal Transcript level Bridge Not found "Function: May be involved in the defense of the pistil against pathogen infection. Tissue specificity: Predominantly expressed in the pistil during all stages of flower development. PTM: Contains four disulfide bonds 3-47; 14-34; 20-21; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7948892 Plant Mol Biol. 1994 Oct;26(1):459-464. Karunanandaa B, Singh A, Kao TH. Characterization of a predominantly pistil-expressed gene encoding a gamma-thionin-like protein of Petunia inflata. DRAMP00440 NEMGGPLVVEARTCESQSHKFKGTCLSDTNCANVCHSERFSGGKCRGFRRRCFCTTHC 58 Defensin SD2 (Plant defensin) P82659 Belongs to the DEFL family SD2 Helianthus annuus (Common sunflower) Antimicrobial, Antifungal Transcript level Bridge Not found "Function:May play a protective role in flowers by protecting the reproductive organs from potential pathogen attack. Tissue specificity: Highest expression in flowers and to a lesser extent in leaves. Lower levels in hypocotyls. No expression in roots and cotyledons. Developmental stage:Expressed progressively during flower development reaching the highest level in the mature fertilized flower stage. PTM: Problely contains four disulfide bonds 14-57; 25-44; 31-52; 35-54." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Physiol. Biochem. 2000;38:253-258. Urdangarin M.C, de la Canal L. A defensin gene expressed in sunflower inflorescence. DRAMP00441 RTCQSQSHKFKGACFSDTNCDSVCRTENFPRGQCNQHHVERKCYCERDC 49 Defensin Tk-AMP-D1 (Plant defensin) P84963 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Has weak antifungal activity, but not against A. consortiale Botrytis cinerea, H. sativum, F. culmorum, C. graminicola and D. maydis. PTM: Contains four disulfide bonds 3-49; 14-34; 20-43; 24-45 (By similarity)." Fungi: Fusarium graminearum and Fusarium verticillioides (MIC<30 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030##18625284 Biochimie. 2007 May;89(5):605-612.##Biochimie. 2008 Nov-Dec;90(11-12):1667-1673. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV.##Odintsova TI, Rogozhin EA, Baranov Y, Musolyamov AKh, Yalpani N, Egorov TA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes.##Seed defensins of barnyard grass Echinochloa crusgalli (L.) Beauv. DRAMP00442 RDCESDSHKFHGACFSDTNCANVCQTEGFTAGKCVGVQRHCHCTKDC 47 Defensin Tk-AMP-D1.1 (Plant defensin) P84965 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00443 RTCESQSHKFKGPCFSDSNCATVCRTENFPRGQCNQHHVERKCYCERSC 49 Defensin Tk-AMP-D2 (Plant defensin) P84968 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-49; 14-34; 20-43; 24-45 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00444 RDCKSDSHKFHGACFSDTNCANVCQTEGFTRGKCDGIHCHCIKDC 45 Defensin Tk-AMP-D3 (Plant defensin) P84970 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-45; 14-34; 20-39; 24-41 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00445 RDCTSQSHKFVGLCLSDRNCASVCLTEYFTGGKCDHRRCVCTKGC 45 Defensin Tk-AMP-D4 (Plant defensin) P84971 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-45; 14-34; 20-39; 24-41 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00446 RECRSESKKFVGLCVSDTNCASVCLTERFPGGKCDGYRRCFCTKDC 46 Defensin Tk-AMP-D5 (Plant defensin) P84966 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-46; 14-34; 20-40; 24-42 (By similarity). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00447 RDCRSQSKTFVGLCVSDTNCASVCLTEHFPGGKCDGYRRCFCTKDC 46 Defensin Tk-AMP-D6 (Plant defensin) P84967 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-46; 14-34; 20-40; 24-42 (By similarity). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00448 RECRSQSKQFVGLCVSDTNCASVCLTEHFPGGKCDGYRRCFCTKDC 46 Defensin Tk-AMP-D6.1 (Plant defensin) P84969 Belongs to the DEFL family Not found Triticum kiharae (Wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-46; 14-34; 20-40; 24-42 (By similarity). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00449 RTCQSQSHKFKGACFSDTNCASVCRTENFPRGQCNQHHVERKCYCERDC 49 Defensin Tm-AMP-D1.2 (Plant defensin) P84964 Belongs to the DEFL family Not found Triticum monococcum (Einkorn wheat) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide (By similarity). PTM: Contains four disulfide bonds 3-49; 14-34; 20-43; 24-45 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17321030 Biochimie. 2007 May;89(5):605-612. Odintsova TI, Egorov TA, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. DRAMP00451 QKLCARPSGTWSSGNCRNNNACRNFCIKLEKSRHGSCNIPFPSNKCICYFPC 52 Defensin-like protein 2B (AFP2b; M2B; Plant defensin) Q10989 Belongs to the DEFL family Not found Sinapis alba (White mustard) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Possesses antifungal activity sensitive to inorganic cations. Subunit structure: Forms oligomers in its native state. PTM: Contains four disulfide bonds 4-52; 16-37; 22-46; 26-48 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8836771 Int J Pept Protein Res. 1996 Jun;47(6):437-446. Neumann GM, Condron R, Polya GM. Purification and mass spectrometry-based sequencing of yellow mustard (Sinapis alba L.) 6 kDa proteins. Identification as antifungal proteins. DRAMP00452 KICEALSGNFKGLCLSSRDCGNVCRREGFTDGSCIGFRLQCFCTKPCA 48 Defensin J1-1 (Plant defensin) Q43413 Belongs to the DEFL family Not found Capsicum annuum (Bell pepper) Antimicrobial, Antifungal Protein level Bridge Not found "Tissue specificity: Expressed in orange and red ripe fruit and to a lesser extent in mature, green fruit. Present in trace in young, green fruit. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." Fungi: Fusarium oxysporum, Botrytis cinerea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8883377 Plant Physiol. 1996 Oct;112(2):615-622. Meyer B, Houln© G, Pozueta-Romero J, Schantz ML, Schantz R. Fruit-specific expression of a defensin-type gene family in bell pepper. Upregulation during ripening and upon wounding. DRAMP00453 RTCESQSHRFKGLCFSKSNCGSVCHTEGFNGGHCRGFRRRCFCTRHC 47 Defensin J1-2 (Plant defensin) O65740 Belongs to the DEFL family Not found Capsicum annuum (Bell pepper) Antimicrobial, Antifungal Protein level Bridge Not found "Tissue specificity: Expressed in flowers and in young fruits. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." Fungi: Fusarium oxysporum, Botrytis cinerea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8883377##9790581 Plant Physiol. 1996 Oct;112(2):615-622.##Mol Gen Genet. 1998 Sep;259(5):504-510. Meyer B, Houln© G, Pozueta-Romero J, Schantz ML, Schantz R.##Houln© G, Meyer B, Schantz R. Fruit-specific expression of a defensin-type gene family in bell pepper. Upregulation during ripening and upon wounding.##Alteration of the expression of a plant defensin gene by exon shuffling in bell pepper (Capsicum annuum L.). DRAMP00455 LLGRCKVKSNRFNGPCLTDTHCSTVCRGEGYKGGDCHGLRRRCMCLC 47 Defensin-like protein 2 (Fabatin-2; Plant defensin) P81457 Belongs to the DEFL family Not found Vicia faba (Broad bean) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Fabatins have antibacterial activity against Gram-positive and Gram-negative bacteria, but were inactive against the yeasts Saccharomyces cerevisiae and Candida albicans. High activity against P. aeruginosa. PTM: Contains four disulfide bonds 5-47; 16-36; 22-43; 26-45." Gram-positive bacteria: Bacillus subtilis, Enterococcus hirae;##Gram-negative bacterium: Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 9103978 FEMS Microbiol Lett. 1997 Apr 1;149(1):59-64. Zhang Y, Lewis K. Fabatins: new antimicrobial plant peptides. DRAMP00456 LLGRCKVKSNRFHGPCLTDTHCSTVCRGEGYKGGDCHGLRRRCMCLC 47 Defensin-like protein 1 (Fabatin-1; Plant defensin) P81456 Belongs to the DEFL family Not found Vicia faba (Broad bean) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Fabatins have antibacterial activity against Gram-positive and Gram-negative bacteria, but were inactive against the yeasts Saccharomyces cerevisiae and Candida albicans. High activity against P. aeruginosa. PTM: Contains four disulfide bonds 5-47; 16-36; 22-43; 26-45." Gram-positive bacteria: Bacillus subtilis, Enterococcus hirae;##Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 9103978 FEMS Microbiol Lett. 1997 Apr 1;149(1):59-64. Zhang Y, Lewis K. Fabatins: new antimicrobial plant peptides. DRAMP00457 RTCESKSHRFKGPCVSTHNCANVCHNEGFGGGKCRGFRRRCYCTRHC 47 Defensin-like protein 1 (LCR68; Plant defensin 2.3; Plant defensin) Q9ZUL7, Q4VP02 Belongs to the DEFL family PDF2.3 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Bridge Not found "Tissue specificity: Expressed in the whole plant except roots. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637 Plant Biotechnol J. 2006 May;4(3):317-324. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations. DRAMP00458 RTCESQSHRFKGTCVSASNCANVCHNEGFVGGNCRGFRRRCFCTRHC 47 Defensin-like protein 2 (LCR69; Plant defensin 2.2; Plant defensin) Q39182, Q42011, Q4VP00, Q4VP03 Belongs to the DEFL family PDF2.2 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Bridge Not found "Function: Confers broad-spectrum resistance to pathogens. Tissue specificity: Broadly expressed. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##8281187 Plant Mol Biol. 2001 May;46(1):17-34.##Plant J. 1993 Dec;4(6):1051-1061.##Plant Physiol. Biochem. 1998;36:533-537. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Höfte H, Desprez T, Amselem J, Chiapello H, Rouz© P, Caboche M, Moisan A, Jourjon MF, Charpenteau JL, Berthomieu P, et al.##Thomma B.P.H.J, Broekaert W.F. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana.##Tissue-specific expression of plant defensin genes PDF2.1 and PDF2.2 in Arabidopsis thaliana. DRAMP00459 RICKSRSQKFKGPCVSEDNCANVCHTEGFPDGDCDGLLRRCYCNTHC 47 Defensin-like protein 3 (Protein LCR71; Plant defensin) P82781 Belongs to the DEFL family LCR71 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds 3-47;14-34;20-41;24-43. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00460 RTCASQSQRFKGKCVSDTNCENVCHNEGFPGGDCRGFRRRCFCTRNC 47 Defensin-like protein 4 (Protein LCR70; Plant defensin 2.1; Plant defensin) Q41914, Q541X5, Q9ZUL6 Belongs to the DEFL family PDF2.1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Bridge Not found "Function: Confers broad-spectrum resistance to pathogens. Tissue specificity: Expressed in roots, siliques and seeds. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##8281187 Plant Mol Biol. 2001 May;46(1):17-34.##Plant J. 1993 Dec;4(6):1051-1061. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Höfte H, Desprez T, Amselem J, Chiapello H, Rouz© P, Caboche M, Moisan A, Jourjon MF, Charpenteau JL, Berthomieu P, et al. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana. DRAMP00461 RTCETSSNLFNGPCLSSSNCANVCHNEGFSDGDCRGFRRRCLCTRPC 47 Defensin-like protein 5 (Protein LCR66; Plant defensin 2.4; Plant defensin) Q9C947, A0MED6, Q1PFI2, Q8LEG6 Belongs to the DEFL family PDF2.4 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds 4-51; 15-36; 21-45; 25-47, and Pyrrolidone carboxylic acid at position 1. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637 Plant Biotechnol J. 2006 May;4(3):317-324. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations. DRAMP00462 RTCQSKSHHFKYMCTSNHNCAIVCRNEGFSGGRCHGFHRRCYCTRLC 47 Defensin-like protein 6 (Protein LCR74; Plant defensin 2.5; Plant defensin) Q9FFP8, P82783 Belongs to the DEFL family PDF2.5 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds 4-47; 14-34; 20-41; 24-43. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00463 QQMCEAKSLDWKGMCLKWRNCRQVCISEGFTDGRCKGFTRKCICSKPCFVLPN 53 Defensin-like protein 7 (Protein LCR75; LCR79; Plant defensin) P82784, P82788 Belongs to the DEFL family LCR75 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Bridge Not found "Tissue specificity: Expressed in stems, roots, rosette leaves and flower buds. PTM: Contains four disulfide bonds 4-48;15-35;21-42;25-44." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00464 EVSPLDNKICKTRSDRFSGVCISTNNCAIICQQFEHFDGGHCEFDGAFRRCMCTKQC 57 Defensin-like protein 8 (Protein LCR73; Plant defensin) P82782, Q4VP01 Belongs to the DEFL family LCR73 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Bridge Not found PTM: Contains four disulfide bonds 10-57; 21-42; 27-51; 31-53. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00465 QPQLCETKSLNYRGLCLKWRSCKRVCISEGFPDGRCKGFFNNKCVCRKPCALLSTEN 57 Defensin-like protein 9 (Protein LCR76; Plant defensin) P82785 Belongs to the DEFL family LCR76 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds 5-50;16-36;22-44;26-46. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00466 RTCESPSNKFQGVCLNSQSCAKACPSEGFSGGRCSSLRCYCSKAC 45 Defensin-like protein 10 (Protein LCR72; Plant defensin 2.6; Plant defensin) Q9ZUL8, Q0IGN8 Belongs to the DEFL family PDF2.6 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00467 QKCEWECKLLPNFPCWLKGAGEGLCDNLCKYEGAISGVCVSDPHRCLCRNRKPGCS 56 Defensin-like protein 11 (Plant defensin) Q9M1V4, A0MF42 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00468 QMNDCDCDHDHRCGEWEDESHGNCKQHHLRVVCTCTLDCLDISSTSNA 48 Putative defensin-like protein 12 (Plant defensin) Q2V477 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00469 QKLCERPSGTWSGVCGNSNACKNQCINLEKARHGSCNYVFPAHKCICYFPC 51 Defensin-like protein 13 (At-AFP1; Protein LCR67; Plant defensin) P30224, Q42179 Belongs to the DEFL family PDF1.1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Protein level Rich Not found "Function: Confers broad-spectrum resistance to pathogens. Possesses antifungal activity sensitive to inorganic cations in vitro. Tissue specificity: Expressed predominantly in siliques and dry seeds. PTM: Contains four disulfide bonds 4-51; 15-36; 21-45; 25-47, and pyrrolidone carboxylic acid at Q1." Fungi: Alternaria brassicola (IC50=10 µg/ml), Botrytis cinerea (IC50=3.90 µg/ml), Fusarium culmorum (IC50=3 µg/ml), Fusarium oxysporum f.sp. lycopersici (IC50=3 µg/ml), Pyricularia oryzae (IC50=0.25 µg/ml), Verticiliium dahliae (IC50=1.50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8422949##17180735##8989885 FEBS Lett. 1993 Feb 1;316(3):233-240.##Transgenic Res. 2007 Aug;16(4):531-538.##Plant Cell. 1996 Dec;8(12):2309-2323. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF.##Sels J, Delaur© SL, Aerts AM, Proost P, Cammue BP, De Bolle MF.##Penninckx IA, Eggermont K, Terras FR, Thomma BP, De Samblanx GW, Buchala A, M©traux JP, Manners JM, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species.##Use of a PTGS-MAR expression system for efficient in planta production of bioactive Arabidopsis thaliana plant defensins.##Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway. DRAMP00470 QKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYFPC 51 Defensin-like protein 14 (Plant defensin 1.3; Plant defensin) O80995 Belongs to the DEFL family PDF1.3 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds 4-51;15-36;21-45;25-47, and Pyrrolidone carboxylic acid at position 1. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10617197 Nature. 1999 Dec 16;402(6763):761-768. Lin X, Kaul S, Rounsley S, Shea TP, Benito MI, Town CD, Fujii CY, Mason T, Bowman CL, Barnstead M, Feldblyum TV, Buell CR, Ketchum KA, Lee J, Ronning CM, Koo HL, Moffat KS, Cronin LA, Shen M, Pai G, Van Aken S, Umayam L, Tallon LJ, Gill JE, Adams MD, Carr Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. DRAMP00471 QKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYVPC 51 Defensin-like protein 15 (Putative plant defensin 1.2b; Plant defensin) O80994 Belongs to the DEFL family PDF1.2B Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found "Function: Confers broad-spectrum resistance to pathogens. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##12447532 Plant Physiol. 2005 Jun;138(2):600-610.##Planta. 2002 Dec;216(2):193-202. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Thomma BP, Cammue BP, Thevissen K. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Plant defensins. DRAMP18329 NSGGAAVVAALGCAAGGVKYGRLLGPWGAAIG 32 Pneumococin N(Bacteriocin) No entry found Belongs to the class IIb bacteriocin blpN Streptococcus pneumoniae?TIGR4 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comparison of the TIGR4 BlpM and -N amino acid sequences demonstrated that only ?ve amino acid differences were suf?cient to target the heterologous strain. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17074857 Infect Immun. 2007 Jan;75(1):443-51. Dawid S, Roche AM, Weiser JN. The blp bacteriocins of Streptococcus pneumoniae mediate intraspecies competition both in vitro and in vivo. DRAMP18330 CCCCCTTCCFSIATGSGNSQGGSGSYTPGK 30 streptolysin S(Bacteriocin) No entry found Belongs to the class I bacteriocin sagA Streptococcus pyogenes MGAS 8232 Unknown Not found Not found Streptolysin S (SLS) is a bacteriocin-like haemolytic and cytotoxic virulence factor that plays a key role in the virulence of Group A Streptococcus(GAS). The peptide contributes to the cytotoxicity, inflammatory activation and polymorphonuclear neutrophil (PMN) resistance of GAS, thereby playing a role in necrosis and systemic spread. It is also responsible for the associated characteristic beta-haemolytic activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18787690 PLoS Pathog. 2008 Sep 12;4(9):e1000144. Cotter PD, Draper LA, Lawton EM, Daly KM, Groeger DS, Casey PG, Ross RP, Hill C. Listeriolysin S, a novel peptide haemolysin associated with a subset of lineage I Listeria monocytogenes. DRAMP18328 KNNWQTNVLEGGGAAFGGWGLGTAICAASGVGAPFMGACGYIGAKFGVDLWAGVTGATGGF 61 Pneumococin M(Bacteriocin) No entry found Belongs to the class IIb bacteriocin blpM Streptococcus pneumoniae?TIGR4 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comparison of the TIGR4 BlpM and -N amino acid sequences demonstrated that only ?ve amino acid differences were suf?cient to target the heterologous strain. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17074857 Infect Immun. 2007 Jan;75(1):443-51. Dawid S, Roche AM, Weiser JN. The blp bacteriocins of Streptococcus pneumoniae mediate intraspecies competition both in vitro and in vivo. DRAMP00474 LCKRESETWSGRCVNDYQCRDHCINNDRGNDGYCAGGYPWYRSCFCFFSC 50 Defensin-like protein 18 (Plant defensin 1.5; Plant defensin) Q9FZ31 Belongs to the DEFL family PDF1.5 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Confers broad-spectrum resistance to pathogens. PTM: Contains four disulfide bonds 3-51; 14-35; 20-45; 24-47." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##12447532 Plant Physiol. 2005 Jun;138(2):600-610.##Planta. 2002 Dec;216(2):193-202. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Thomma BP, Cammue BP, Thevissen K. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Plant defensins. DRAMP00475 TEMMAVEGRICERRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC 58 Defensin-like protein 19 (Protein LCR78; Plant defensin 1.4; Plant defensin) P82787, Q8VZQ7, Q9FWR6 Belongs to the DEFL family PDF1.4 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Bridge Not found PTM: Contains four disulfide bonds 11-58;22-43;28-52;32-54. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00476 QKHIAPWIFEDKSICCKEHPSVGRCLPGIDDDAEKDGKCWKFCIEGCETGGFCKLFEHKHICHCNCSG 68 Putative defensin-like protein 20 (Plant defensin) Q2V2S1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00477 QKHTAPWIPEDNSICCKEHPSVGRCLPNIDDSAEKGGKCWKFCIEGCETGGFCKLFGHKHICHCNCSG 68 Defensin-like protein 21 (Plant defensin) P0CAX9, O23285, Q2V3I6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Bridge Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00478 YNVENGGSLCCNNHPKFGKCNTKNDDQRCNSWCLNGCDNGKGGYCKSMSHGGQCHCYC 58 Defensin-like protein 22 (Plant defensin) Q2V391 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00479 SGSSLCCNTHAKFGACNTYQDRKRCNKWCLDGCDNKKGGFCKRFAGGAKKCHCYC 55 Putative defensin-like protein 23 (Plant defensin) Q2V364 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00480 RKTVWPSSELDPKCCSNQPEFGICDSKEDDERCAQMCLDGCPTNKGGGCQPITEAPGAVCSCYCA 65 Defensin-like protein 24 (Plant defensin) Q2V371 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00481 YNVESGGSLCCNNHPKFGKCNTNNDNQRCNRWCHNGCGNGKGDYCKAMSHGGLCHCYC 58 Putative defensin-like protein 25 (Plant defensin) Q2V392 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00482 MIYNVESGGSLCCNSHPKFGKCNTNNDEQRCNRWCHNGCGNGKGGYYKSMSHGGQCHYYC 60 Putative defensin-like protein 26 (Plant defensin) Q2V4J2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found PTM: Problely contains two disulfide bonds. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00483 VMNEDSILSSNKGDSLCCNDHPEFGICTNKSCNKWCLQGCTRGGFCKRKICHCYC 55 Putative defensin-like protein 27 (Plant defensin) Q2L6T3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00484 KENITPWIYSMKQPVSCNREHSEIGICLSGIDDDIQNDGKCWKFCLMVAKSGGYNADK 58 Putative defensin-like protein 28 (Plant defensin) P0CAY0, F4JUP3, O23285 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00485 KSMVEVNAAHKWYIVEGLCSKFPDCNKHCKEQKFPGGTCLKLGVNMMCTCIYS 53 Putative defensin-like protein 29 (Plant defensin) Q2V3R9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##10907853 Plant Physiol. 2005 Jun;138(2):600-610.##DNA Res. 2000 Jun 30;7(3):217-221. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Kaneko T, Katoh T, Sato S, Nakamura A, Asamizu E, Tabata S. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones. DRAMP00486 KSMAKAQGGWYLVEGLCSKFPDCNKHCKEQGFLGGQCLKLGVNMLCFCIHT 51 Putative defensin-like protein 30 (Plant defensin) Q2V3S0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found Caution: Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##10907853 Plant Physiol. 2005 Jun;138(2):600-610.##DNA Res. 2000 Jun 30;7(3):217-221. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Kaneko T, Katoh T, Sato S, Nakamura A, Asamizu E, Tabata S. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones. DRAMP00487 EDRSKLIPIGPCSKIANCNQTCIESQFLGGKCIKWYPDSIKETCACLVKPSITHV 55 Putative defensin-like protein 31 (Plant defensin) Q2V3D7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00488 KDIDGRKPLLIGTCIEFPTEKCNKTCIESNFAGGKCVHIGQSLDFVCVCFPKYYI 55 Defensin-like protein 32 (Plant defensin) Q2V4I8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found 2MZ0 "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00489 QNPRGRKCEDPNGVDQKAKCYIYCNEQGFLGGSCQGYTNHYMCECYVG 48 Putative defensin-like protein 33 (Plant defensin) Q2V4D6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00490 QILTGIKCPDPNGHDKEDKCNIYCLNQNYMGGSCQGYKNHYMCECYVG 48 Defensin-like protein 34 (Plant defensin) Q2V4D7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00491 KSMNPTGRRCPDPNGVEKKSMCYSSCKTQGFMGGSCQGHKGNYMCECYEG 50 Defensin-like protein 35 (Plant defensin) Q2V4F3, Q9SH70 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00492 IESPIFTGNKCSDPTGMDKDGKCLDYCHAQGYPGGSCIGFIDQGYMCVCKVG 52 Putative defensin-like protein 36 (Plant defensin) Q2V4D5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00493 TTAGRRDGKSGRTEWLYVAGECAKLPRCNKYCVSNGFHLGGFCEKLSPQASYLSCVCKYT 60 Defensin-like protein 37 (Plant defensin) Q56XC2, F4JSA4, Q9SVQ4 Belongs to the DEFL family EDA21 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00494 YCERVRSRSAPHDICKKKNGNAVCKEKCWTIEKYQNGRCLILPKTTKLDCYCYHFDQC 58 Putative defensin-like protein 38 (Plant defensin) Q2V462 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00495 YCEKVRSKTAPRDVCKKSNGNALCKKTCWTIEKYVNGKCLILPKTTNLDCYCYHYDNGSACRA 63 Putative defensin-like protein 39 (Plant defensin) Q2V460 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00496 LGTSPYCEKVLSRFAPPGNCLKKNGNALCKESCANEQFREGVCLHLPKPQSKLNCYCSVLKCP 63 Putative defensin-like protein 40 (Plant defensin) Q2V325 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00497 MTQGKRKHPCDLKNPSKRAPPATCNKPNGAILCGDFCLHEGYNIGKCVMRRTGKACICSQCEGW 64 Defensin-like protein 41 (Plant defensin) Q3E8B0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00498 MNWELCDDYPSKAPPETCNKVDGARRCRTSCNNEGYGGANCNLKGKVKVCECTILRVCLPHHKRPPHVPKPPK 73 Putative defensin-like protein 42 (Plant defensin) P0CAY1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "PTM: Contains four disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved feature of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##10907853 Plant Physiol. 2005 Jun;138(2):600-610.##DNA Res. 2000 Jun 30;7(3):217-221. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Kaneko T, Katoh T, Sato S, Nakamura A, Asamizu E, Tabata S. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones. DRAMP00499 SEIKPTGRIDDQCKQMCSATYGDGKCASDCRKAGFSSGRCLTSSPFGNKCCCTK 54 Defensin-like protein 43 (Plant defensin) Q2V4J5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00500 SEIKPTGRVDNQCKEMCSATFGDGKCAADCRKAGFSSGRCLTSSPFGNKCCCT 53 Defensin-like protein 44 (Plant defensin) Q9M833 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00501 SDIKPTGRIDNQCKRMCSATYGNGKCAADCRSDGFSSGQCFTSPPFDNRCCCNN 54 Defensin-like protein 45 (Plant defensin) Q2V3Y8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00502 IDAGIKGFDTDHCDTRCYGRDECMNYCIKAGFPKGGQCGSLCIPCGFKCCCQK 53 Defensin-like protein 46 (Plant defensin) Q2V3V1, A0ME04 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00503 SDARIEGFSFDNCNIRCSEDYWNDECNKDCLRAGFQKGGQCGSPCIPCPVKCCCQK 56 Defensin-like protein 47 (Plant defensin) Q3E7C7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00504 AEIKKFSYDHCFHLCVAGEYGSNECFVDCAQKGFWHGDCANRTEKDPIRCCCYN 54 Putative defensin-like protein 48 (Plant defensin) Q2V365 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00505 AETTKFSYDHCFHLCVEGEYGSRECFVDCTQKGFWHGVCANKTTAKDPIHCCCYN 55 Defensin-like protein 49 (Plant defensin) Q2V366 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##14993207 Plant Physiol. 2005 Jun;138(2):600-610.##Genome Res. 2004 Mar;14(3):406-413. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Castelli V, Aury JM, Jaillon O, Wincker P, Clepet C, Menard M, Cruaud C, Qu©tier F, Scarpelli C, Schächter V, Temple G, Caboche M, Weissenbach J, Salanoubat M. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Whole genome sequence comparisons and full-length cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation. DRAMP00506 SEIKAKINGLECFNTCTPYYDDYKCNVDCLSSGYPAGDCHIVSPSQPKKCCCY 53 Defensin-like protein 50 (Protein LCR49; Plant defensin) P82764 Belongs to the DEFL family LCR49 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17229318##11437247##15955924 BMC Genomics. 2007 Jan 17;8:18.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Moskal WA Jr, Wu HC, Underwood BA, Wang W, Town CD, Xiao Y.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Experimental validation of novel genes predicted in the un-annotated regions of the Arabidopsis genome.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00507 SEIKAKINGLECFNTCTSYYDDHKCNVDCLSSGYPAGECYTVSPSQPKKCCCY 53 Defensin-like protein 51 (Protein LCR48; Plant defensin) P82763, A0MJW7, A7REH1 Belongs to the DEFL family LCR48 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17565583##11437247##15955924 Plant J. 2007 Jul;51(2):262-280.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00508 VSGPPKCIALCRPGYYERFECFHDCITEGYDDGSCVPGPTTAKCGIITKTTNKICYSFAFE 61 Putative defensin-like protein 52 (Plant defensin) Q2V433 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "PTM: Problely contains two disulfide bonds. Caution: Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00509 MFSQNICMWRDCFARCSPGYYERFECFHDCITKGYDDGNCVPGPKTGRCCCTR 53 Putative defensin-like protein 53 (Plant defensin) P0CAY2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "PTM: Contains four disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00510 ESVIEPAKYGACLFLCDARRDDHACFYDCTNVAIYRTGHCVGNPPRCCCIRG 52 Defensin-like protein 54 (Plant defensin) Q8GY39 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11910074##15955924##14993207 Science. 2002 Apr 5;296(5565):141-145.##Plant Physiol. 2005 Jun;138(2):600-610.##Genome Res. 2004 Mar;14(3):406-413. Seki M, Narusaka M, Kamiya A, Ishida J, Satou M, Sakurai T, Nakajima M, Enju A, Akiyama K, Oono Y, Muramatsu M, Hayashizaki Y, Kawai J, Carninci P, Itoh M, Ishii Y, Arakawa T, Shibata K, Shinagawa A, Shinozaki K.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Castelli V, Aury JM, Jaillon O, Wincker P, Clepet C, Menard M, Cruaud C, Qu©tier F, Scarpelli C, Schächter V, Temple G, Caboche M, Weissenbach J, Salanoubat M. Functional annotation of a full-length Arabidopsis cDNA collection.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Whole genome sequence comparisons and full-length cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation. DRAMP00511 LSNSDALASSVIETTKNDVCSTPCTIRYGTFECFQDCILDHFRDGNCINGRCCCKY 56 Putative defensin-like protein 55 (Plant defensin) Q2V2Q4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00512 DVLASSDIYICVTVIETTKNDVCSTPCTIRYGTFECFHDCILEHYRDGNCINGRCCCK 58 Putative defensin-like protein 56 (Plant defensin) Q2V4A6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00513 SSVIETTKNDVCSTPCTRRYGTYECWHDCLHERYNDGGCVDGRCCCKK 48 Putative defensin-like protein 57 (Plant defensin) Q2V4A8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00514 DVLVSSVIETSKNDVCFIPCTRRYGDWECYDDCLGKNFNDGGCVDGRCCCKK 52 Defensin-like protein 58 (Plant defensin) Q4VNZ9, F4IU82, F4IU83 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00515 LSNSDILVSSVIETSKYDVCFIPCTRRYEDRECNDDCLAKDFNDGGCVDGRCCCKY 56 Defensin-like protein 59 (Plant defensin) Q4VNZ8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00516 EVLVAPVIETAQNDVCFVPCTSRYGHYECAFDCMHKRYKDGGCVHGRCCCKT 52 Putative defensin-like protein 60 (Plant defensin) Q2V4A5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00517 YDRCIGPCLRFYGNHQCYKNCRKAKYDGGQCDFVKKGEKLPECCCYYNKN 50 Putative defensin-like protein 62 (Plant defensin) Q2V485 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00518 SYNIGQTRLVVIQEQEPHCIGPCEIAFGNRPCNEECTSQQYAYGFCDYQTKGEDNPQCCCYTS 63 Putative defensin-like protein 63 (Plant defensin) Q2V4G1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00519 ERIDICFIPCTRRYGDYECWFDCTYNRYKEGGCVEDVVVKHNRNRPTFRAVELCFFSIKFMYDFSMK 67 Putative defensin-like protein 64 (Plant defensin) Q2V4A7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found Caution: Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00520 FSVQIGISVQAAPPTCGRDCTEKFLTQDCDKYCVGLSYKKGVCILSEGLPPKTSTYRCCCS 61 Putative defensin-like protein 66 (Plant defensin) Q2V2Y6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00521 VEMGISVQALPPTCGPDCTGRFMNQDCSKYCAALSYKHGVCILFRGLPPRTSTLRCCCG 59 Putative defensin-like protein 67 (Plant defensin) Q3EBU2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00522 YDLFSEIGISAATLVIPTCFENCNATFQDPECNKWCALLAYKDGSCLYPPSEVDDLPPIKRPYIPRCCCNPITLSPPSP 79 Defensin-like protein 68 (Plant defensin) Q2V4L5, A0MJT8, Q9LR89 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##17147637##17229318 Plant Physiol. 2005 Jun;138(2):600-610.##Plant Biotechnol J. 2006 May;4(3):317-324.##BMC Genomics. 2007 Jan 17;8:18. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Moskal WA Jr, Wu HC, Underwood BA, Wang W, Town CD, Xiao Y. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Experimental validation of novel genes predicted in the un-annotated regions of the Arabidopsis genome. DRAMP00523 YDLFTGIGIDARTVPPTCYESCNATFQNPECNKMCVGLAYKDGSCIYPPPEVDGLPPKRPYFPRCCCNPIILSPPSP 77 Defensin-like protein 69 (Plant defensin) Q9FL73, A0MFP1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##15955924##17147637 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant Biotechnol J. 2006 May;4(3):317-324. Kaneko T, Kotani H, Nakamura Y, Sato S, Asamizu E, Miyajima N, Tabata S.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations. DRAMP00524 NFASGEASSQLCFNPCTPQLGNNECNTICMNKKYKEGSCVGFGIPPTSKYCCCKT 55 Putative defensin-like protein 70 (Protein LCR83; Plant defensin) P82792 Belongs to the DEFL family LCR83 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00525 LPSSVINGFGYDYCIVECSITFLDDACKPLCIDRGYSDGGCIGLSPHFKCCCKK 54 Defensin-like protein 71 (Plant defensin) P82793 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00526 MKLSILVKAMKRNNGFRYDYCIAECSEHFLDDVCKPVCIDKGYSDGGCIGLAPNFKCCCKK 61 Putative defensin-like protein 72 (Plant defensin) Q2V2S9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "PTM: Contains four disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide, which is a conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00527 EPQCIGSCEMLADCNTACIRMGYLFGQCVGWKTPDMCCCNH 41 Putative defensin-like protein 73 (Protein LCR44; Plant defensin) P82759 Belongs to the DEFL family LCR44 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00528 QKECIGPCDMFTDCQAACVGIRKGYNYGQCVAWKPKDDDPFTCCCYKLTP 50 Defensin-like protein 74 (Protein LCR43; Plant defensin) P82758 Belongs to the DEFL family LCR43 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00529 ITVQADCIGPCNDDCQQLCKSKGYTDWTCASFRTKSSCCCKPPRHQIFEQNAQLNN 56 Defensin-like protein 75 (Protein LCR45; Plant defensin) P82760 Belongs to the DEFL family LCR45 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247 Plant Mol Biol. 2001 May;46(1):17-34. Vanoosthuyse V, Miege C, Dumas C, Cock JM. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00530 IDVHDAMCYRSECTSVCDQICLSHGYTNGWYCGTFRLHTGCCCLKKKELNQIISPSKN 58 Defensin-like protein 76 (Protein LCR86; Plant defensin) P82795 Belongs to the DEFL family LCR86 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10470850##11437247 DNA Res. 1999 Jun 30;6(3):183-195.##Plant Mol Biol. 2001 May;46(1):17-34. Kaneko T, Katoh T, Sato S, Nakamura Y, Asamizu E, Kotani H, Miyajima N, Tabata S.##Vanoosthuyse V, Miege C, Dumas C, Cock JM. Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00531 RSNGIYDPMCPGVCGNLVKPDCNGLCHELGFPAGGYCKPGNTCCCKKKDSGPVDVPPTA 59 Defensin-like protein 78 (Plant defensin) Q9SL74, A0MJT1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00532 YQMLICLDLNISCADCQKQCDETSYGGMCLNGGRTCCCKKSPPPSYYDPRPPSS 54 Putative defensin-like protein 79 (Plant defensin) Q2V470 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00533 EVRDICPGVCHAGIEPDCDTLCISMGFTGGYCQGLTCCCNPKSSKSSIINRPI 53 Putative defensin-like protein 80 (Protein LCR81; Plant defensin) P82790 Belongs to the DEFL family LCR81 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00534 KSPVSCDGACTSTPQCNKICTSKGYKKGICHGSAHLFYICCCYAKFESQYDPSISSPPNY 60 Defensin-like protein 81 (Plant defensin) Q2V4G6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00535 RTQEHPCQDYRLGCKSRDVCNAKCLSLGYVKGGDCVTFAFPICCCKINFGFQDDSPISSPIFTD 64 Defensin-like protein 82 (Plant defensin) Q2V334 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14993207 Genome Res. 2004 Mar;14(3):406-413. Castelli V, Aury JM, Jaillon O, Wincker P, Clepet C, Menard M, Cruaud C, Qu©tier F, Scarpelli C, Schächter V, Temple G, Caboche M, Weissenbach J, Salanoubat M. Whole genome sequence comparisons and full-length cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation. DRAMP00536 QIITCLPGECTNPSECNAACKSNGYKGGACVSMSIGSTTGACCCKPNFKSQDSFKSNDIIINNN 64 Putative defensin-like protein 83 (Protein LCR46; Plant defensin) P82761 Belongs to the DEFL family LCR46 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10470850##11437247 DNA Res. 1999 Jun 30;6(3):183-195.##Plant Mol Biol. 2001 May;46(1):17-34 Kaneko T, Katoh T, Sato S, Nakamura Y, Asamizu E, Kotani H, Miyajima N, Tabata S.##Vanoosthuyse V, Miege C, Dumas C, Cock JM. Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00537 QSSKCTKGCTSTPECNIKCMKKGGGHCQAYIGRSHGRLAIENYCCCNNYSNSPISSPVMN 60 Putative defensin-like protein 84 (Plant defensin) Q2V2Y3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00538 LISDKCTEGCKSTIGCNTRCMMRGGGYCESAKIHGAVKIFCCCNNYSNSPISSPVIN 57 Defensin-like protein 85 (Plant defensin) Q8GXV6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11910074##9628582 Science. 2002 Apr 5;296(5565):141-145.##DNA Res. 1998 Feb 28;5(1):41-54. Seki M, Narusaka M, Kamiya A, Ishida J, Satou M, Sakurai T, Nakajima M, Enju A, Akiyama K, Oono Y, Muramatsu M, Hayashizaki Y, Kawai J, Carninci P, Itoh M, Ishii Y, Arakawa T, Shibata K, Shinagawa A, Shinozaki K.##Sato S, Kaneko T, Kotani H, Nakamura Y, Asamizu E, Miyajima N, Tabata S. Functional annotation of a full-length Arabidopsis cDNA collection.##Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones. DRAMP00539 QFRGIKQCEMKCYSTPECNATCLHEGYEEGKCLKSWDGGVECCCLGLLASSHQDSSPISSPHYIIFHGICILNI 74 Putative defensin-like protein 86 (Protein LCR82; Plant defensin) P82791 Belongs to the DEFL family LCR82 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found PTM: Contains four disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00540 QLKSTCRIAEAWKGAKECNAKCAALGTTRGGVCQKFLGDLYCCCWD 46 Defensin-like protein 87 (Plant defensin) Q3E7S1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Caution: Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00541 VEVIPCIAGSKCTNDMTYNELCRFKGFSKGGFCQKYVHQTIGRCCCHPTGLESQESSISGDTNVVITN 68 Putative defensin-like protein 88 (Plant defensin) Q2V3J1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00542 QTMQCYSGIACTDDGTCNDYCNPRNNNLGGVCLRRANCCCCYVSVVKSQESSLSKDTNNVFITN 64 Putative defensin-like protein 89 (Plant defensin) Q2V3J0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00543 SPEKYYDCKQDGCITTPPCWRKCVSMGYPKGGECRIYSYGGVCCCDLTSKPPN 53 Defensin-like protein 90 (Plant defensin) Q2V4G9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00544 FTIAEPYIHPCMKGFCSFKSECANKCIFMGHHKGGDCIGGLDGIYCCCLA 50 Defensin-like protein 91 (Protein LCR47; Plant defensin) P82762 Belongs to the DEFL family LCR47 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14993207##11437247##15955924 Genome Res. 2004 Mar;14(3):406-413.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Castelli V, Aury JM, Jaillon O, Wincker P, Clepet C, Menard M, Cruaud C, Qu©tier F, Scarpelli C, Schächter V, Temple G, Caboche M, Weissenbach J, Salanoubat M.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Whole genome sequence comparisons and full-length cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00545 WGKCDLRKGLCRLADTISTCDVPCRAVDSKYHGGECLNVGGGQGICWCCRDYDAAKSGAEKESM 64 Defensin-like protein 95 (Plant defensin) Q6NMS3, O49628 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00546 RQVCDYDKGECNSYEKSSTCIEPCKQLDSKFIGGRCIPVGGITGMGLCVCCRDVQRGAEKESM 63 Defensin-like protein 96 (Plant defensin) Q8L7G7, O49628, Q8H0Y6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Confers broad-spectrum resistance to pathogens. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00547 RRVCDSAAGLCSMLFSCNTQCNSLGRNFTGGECSDARFPGLSVCYCCHNVESSAEMESM 59 Defensin-like protein 97 (Protein LCR85; Plant defensin) P82794, O49626, Q1PE59 Belongs to the DEFL family LCR85 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00548 RLVCDTPAGTCTSSSTCNDQCNTWGGNYSGGECADSSFPGLSICYCCHYVGSSAEMESM 59 Defensin-like protein 98 (Plant defensin) Q94AZ8, O49626 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00549 SCDFPLGACTPFRDCKESCIKFKTRAGQTFFDGKCRPRDRPSVWTACFCCYYDSIGAQ 58 Defensin-like protein 100 (Plant defensin) Q3E6U0, A0MJT5, O49626 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00550 FPASDQSIYARCIGPCPRYAVPHWCENECLSRKYMAGGECAFIEGEGPTPRCCCINL 57 Putative defensin-like protein 101 (Plant defensin) Q2V337 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00551 RTTTGGSPGYGIGGRTKTCFTPALCIYRGVHGCDSYCKTKNFDYGYCRQEHCCCVNY 57 Putative defensin-like protein 102 (Plant defensin) Q2V3L0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00552 LPTTARSPGYEIGPQRRRRVTCFSFSFCKPARGLASCDLFCKRLKFESGLCTGDLEKCCCIDYIN 65 Defensin-like protein 103 (Plant defensin) Q8GXR4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11910074##15955924 Science. 2002 Apr 5;296(5565):141-145.##Plant Physiol. 2005 Jun;138(2):600-610. Seki M, Narusaka M, Kamiya A, Ishida J, Satou M, Sakurai T, Nakajima M, Enju A, Akiyama K, Oono Y, Muramatsu M, Hayashizaki Y, Kawai J, Carninci P, Itoh M, Ishii Y, Arakawa T, Shibata K, Shinagawa A, Shinozaki K.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Functional annotation of a full-length Arabidopsis cDNA collection.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00553 LPMTHGGKPGYGIERTIIRPEWRCYVDEGCPKGQGAPCEKNCKNVADYGICIGIKCCCFDVIPVPPT 67 Putative defensin-like protein 104 (Plant defensin) Q2V476 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00554 MLMACYSAGQLGCLVFCNEAEYSYGKCIGRGRCCCYDL 38 Putative defensin-like protein 105 (Plant defensin) P0CAY3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00555 HTTIASAPSSGEPTTYATGPALSKHSHDNDGICFVTPACFAPGQYEIGCIVYCHESHYKHYKCVNRSCCCYNTDKNASELK 81 Defensin-like protein 106 (Plant defensin) Q1G3Y1, A0MDJ9, Q9SYA4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00556 RMTTTTSPGFGIKQQDRQCFEHAPYLCRGGEGDCRMYCRDLDFSFGTCFSGVCCCQI 57 Defensin-like protein 107 (Plant defensin) Q2V413 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00557 RMTTASTPGYGIKQEDRLCIQGQEGTKLCSSGTSRDCLNFCLIRGYAGGSCYAYTLDQCCCRIPPPKLK 69 Defensin-like protein 108 (Protein LCR51; Plant defensin) A8MQN0, O80684 Belongs to the DEFL family LCR51 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00558 RPSFKPIPLFGEKLTQCFDTRPCLQGMLKCIEFCSSMGTADGQCNNENLCCCTHE 55 Defensin-like protein 109 (Plant defensin) Q2V390 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##15955924 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Physiol. 2005 Jun;138(2):600-610. Kaneko T, Kotani H, Nakamura Y, Sato S, Asamizu E, Miyajima N, Tabata S.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00559 RSTSDIVSGSGIKEDEHVCFKTSPCLPEVGGEKGCIAFCSRMKFTTGLCLGSVVCCCYT 59 Putative defensin-like protein 110 (Plant defensin) Q2V4N0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00560 SDDTQGFGIKQEYKQCYTPDPCRKGGNDECERFCVAKSGLLYGKCINDGSKDVCCCLTK 59 Putative defensin-like protein 111 (Protein LCR50; Plant defensin) P82765 Belongs to the DEFL family LCR50 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00561 SDRTSGVGINQEYAKCYDLADCQKPKVDDAACERFCGAKSFLLYGKCDTATNKCCCKSKTK 61 Defensin-like protein 112 (Plant defensin) Q2V488 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00562 SDSFPGLGLKKQAHKQCYSPDLCTGGDSKCDICCVLISGVYYGKCIQSKCHCLNKTK 57 Defensin-like protein 113 (Plant defensin) Q2V342 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00563 SELDNTSGFEIKQEDKCYGPEPCKNGYEGCLFFCVRIAYYLYGECTMKPDHQKHCCCVTK 60 Putative defensin-like protein 114 (Plant defensin) Q2V322 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00564 SDSTLGIGINQDWKKCFSPDPCKKAGTQGCMEFCRTISFLLFGECTSKPDQCCCVTK 57 Defensin-like protein 115 (Plant defensin) Q2V321 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00565 SDSALGIGIKEDWEVCFSIDPCLTGEGTLGCTKWCRNHINLSLVGYCRTDPEHCCCVAEK 60 Defensin-like protein 116 (Plant defensin) Q3E8I8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##15955924##14993207 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Physiol. 2005 Jun;138(2):600-610.##Genome Res. 2004 Mar;14(3):406-413. Kaneko T, Kotani H, Nakamura Y, Sato S, Asamizu E, Miyajima N, Tabata S.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Castelli V, Aury JM, Jaillon O, Wincker P, Clepet C, Menard M, Cruaud C, Qu©tier F, Scarpelli C, Schächter V, Temple G, Caboche M, Weissenbach J, Salanoubat M. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Whole genome sequence comparisons and full-length cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation. DRAMP00566 SDGTSGYGITEATKRCFTPAPCTRGLFYCQTFCSSLSAVLIGVCESGICCCILNQ 55 Defensin-like protein 117 (Plant defensin) Q2V4G3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00567 QEMCRDILMKAKNCDEGTCDTLCKQKWKGNGSCFPNVYTYRKSCLCTFPCKT 52 Putative defensin-like protein 118 (Protein LCR52; Plant defensin) P82766 Belongs to the DEFL family LCR52 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00568 QEMCRDLLMRAKNCDDSTCATLCKQKWKGNGSCFPNVYRKSCLCTFPCKT 50 Putative defensin-like protein 119 (Protein LCR53; Plant defensin) P82767 Belongs to the DEFL family LCR53 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00569 QEMCHDLIKKTDCDDATCVTLCKQKWNGNGGGSCFQIVNLKSCLCAFPCQV 51 Putative defensin-like protein 120 (Protein LCR56; Plant defensin) P82770 Belongs to the DEFL family LCR56 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00570 QETCHDLIMKRDCDEATCVNMCQQKWKGSGGSCFQNFNVMSCICNFPCQV 50 Putative defensin-like protein 121 (Protein LCR55; Plant defensin) P82769 Belongs to the DEFL family LCR55 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00571 QELCHDYMSGTELCEEDKCVAKCIWMHGTAAKGTCMPKPSKQCVCTYSCNA 51 Defensin-like protein 122 (Protein LCR30; Plant defensin) P82745 Belongs to the DEFL family LCR30 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. Tissue specificity: Expressed in flower buds, but not in stems, roots or rosette leaves. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00572 MRPRSRAGDKFMSQGQELCHEYFQLTAPCEKQPCIDMCSSKYKTGKGVCGPAVHQCFCTFSCTV 64 Defensin-like protein 123 (Plant defensin; Uncertain) Q0WN71 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924##17565583 Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00573 ANCVNYFEITFPEVCEANWCAAECLKAYKNGKGTCWQKFCQCVYDC 46 Defensin-like protein 124 (Protein LCR16; Plant defensin) P82731, A0MJV4 Belongs to the DEFL family LCR16 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP00574 EEKQCYDYLLTPQENCEGLICAHECTMQHGGNGVCVDTTSTVCICTYDCTS 51 Defensin-like protein 125 (Protein LCR54; Plant defensin) P82768 Belongs to the DEFL family LCR54 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00575 QHAMCHEILPETDCGAGSCTALCLQLWRGTGKCVRTNDQKLICLCNFECIV 51 Putative defensin-like protein 126 (Protein LCR6; Plant defensin) P82721 Belongs to the DEFL family LCR6 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##11437247##15955924 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00576 QNAICQKFLSETDCGAGSCTALCLQLWKGIGKCIKTDDHKLLCLCKYECIV 51 Defensin-like protein 127 (Protein LCR20; Plant defensin) P82734, Q4VP05, Q4VP06 Belongs to the DEFL family LCR20 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##11437247##15955924 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00577 QHICHQILLNNNCDGATCTSLCDKQLQGTGQCYKTVDKRFICLCNYLCRT 50 Putative defensin-like protein 128 (Protein LCR8; Plant defensin) P82723 Belongs to the DEFL family LCR8 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00578 DTCHEYLYPEKCENNQCNSECATKFKEVGVFGFCVPPRSEPTEQFCICSYNC 52 Putative defensin-like protein 129 (Protein LCR13; Plant defensin) P82728 Belongs to the DEFL family LCR13 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00579 SIFIKYSDRTCHVYIKAENCEIDQCNWECGTKYKRVGVQGLCVPPGFDPIDQACLCSFNC 60 Defensin-like protein 130 (Protein LCR28; Plant defensin) P82743, Q2V320 Belongs to the DEFL family LCR28 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##11437247##15955924 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00580 HICHDYLEGDHCDPKDCNLDCRDKWKGTGTCEPPTGTPLTRTCYCTYDC 49 Putative defensin-like protein 131 (Protein LCR29; Plant defensin) P82744 Belongs to the DEFL family LCR29 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00581 NDEQLRGNRCFQIKFKTGKCVPKECQTACQEKLRKPKLKGEGFCMKECTCCFYT 54 Putative defensin-like protein 133 (Protein LCR33; Plant defensin) P82748 Belongs to the DEFL family LCR33 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00582 FSPEDCLDDVGWILICTKPTCKFSCWTSRSVNKGRKMQDYWCSDSNTCHCVFCTGD 56 Putative defensin-like protein 134 (Plant defensin) P0CAY4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00583 QRRKCDEKIVLQFCNGRNRCYEYCDTKECVAACKKKRNGEGICNGDVFSVSAQCLCLYKC 60 Putative defensin-like protein 135 (Plant defensin) Q2V3K1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00584 NMSVDQKRCWATLKENNCVHDECRSMCLKKNPKGHGRCIKSSKGRIICLCGYDCP 55 Putative defensin-like protein 137 (Protein LCR14; Plant defensin) P82729 Belongs to the DEFL family LCR14 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00585 QPLGTMERCYDMLTWGECVPDNCAFSCALKRHGKGGCIKAYDNRPACVCYYTCLRS 56 Putative defensin-like protein 139 (Protein LCR7; Plant defensin) P82722 Belongs to the DEFL family LCR7 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00586 QPLEEMVECKEVLWPEECKYDACAFACALKRHGKGGCLEGPDYRSACICQYACKRS 56 Defensin-like protein 140 (Protein LCR15; Plant defensin) P82730 Belongs to the DEFL family LCR15 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00587 QQQQQRCEEALTEIDCGAGNCNALCLQKRKGLGRCVQRTPCDKLKCMCYYPCSS 54 Defensin-like protein 141 (Protein LCR3; Plant defensin) P82718 Belongs to the DEFL family LCR3 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9679202##11437247##15955924 DNA Res. 1998 Apr 30;5(2):131-145.##Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00588 EKLTTCSRFLSQKSGKCVKEDCDRMCKQKWPGKYTVGHCYGQFKDAKRCLCSVCGPDRQPP 61 Putative defensin-like protein 142 (Protein LCR34; Plant defensin) P82749 Belongs to the DEFL family LCR34 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00589 MVNGQCSFPQPVGPNGKCVPKDCKSLCHKKYKGGSICTTGKPNICMCLVCRRRSPEV 57 Defensin-like protein 144 (Protein LCR10; Plant defensin) Q8S8H9, A0MJT0, P82725, Q1PF66 Belongs to the DEFL family LCR10 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147637##15955924##17565583##11437247 Plant Biotechnol J. 2006 May;4(3):317-324.##Plant Physiol. 2005 Jun;138(2):600-610.##Plant J. 2007 Jul;51(2):262-280.##Plant Mol Biol. 2001 May;46(1):17-34. Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA.##Vanoosthuyse V, Miege C, Dumas C, Cock JM. Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants.##Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response. DRAMP00590 NLQQRRQMNQTWCSRPLLTHKQTGKCVIEDCESKCRQKWKGNGTQATCRNQCNCHFRCPWIQGQP 65 Putative defensin-like protein 145 (Protein LCR2; Plant defensin) P82717 Belongs to the DEFL family LCR2 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00591 NVQQVKREQCHTVIPNKSGKCIFTECKSACEKLKKPVASLCLPPKTCRCYHFCS 54 Putative defensin-like protein 146 (Protein LCR9; Plant defensin) P82724 Belongs to the DEFL family LCR9 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00592 NVQQKRSNRCIDFPVNPKTGLCVLKDCESVCKKTSKGLEGICWKFNAKGKDPKQCKCCGLWPPLY 65 Defensin-like protein 147 (Protein LCR1; Plant defensin) P82716 Belongs to the DEFL family LCR1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00593 NVEQKSQDWCWSIVNKDRCLQKECESLCSKKHPKGKFMCIPSTPGGPFQCHCRHPCR 57 Putative defensin-like protein 148 (Protein LCR4; Plant defensin) P82719 Belongs to the DEFL family LCR4 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00594 NEGLGKPKKQCNEILKQSNCVAAECDSMCVKKRGKGAGYCSPSKKCYCYYHCP 53 Defensin-like protein 149 (Protein LCR5; Plant defensin) Q8S8H3, P82720, Q8LGD4 Belongs to the DEFL family LCR5 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00595 DVDQGYKQQCYKTIDVNLCVTGECKKMCVRRFKQAAGMCIKSVPSAPAPNRCRCIYHC 58 Putative defensin-like protein 150 (Protein LCR32; Plant defensin) P82747 Belongs to the DEFL family LCR32 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00596 QAPSTCFEALKDASKGASCDSELCASLCKKKSGGGVGTCRTKTTQPSKGQPECHCRFWCKSDGTPYK 67 Defensin-like protein 151 (Protein LCR17; Plant defensin) Q9T0E3, Q6GKX9 Belongs to the DEFL family LCR17 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00597 KQRLCIKVLTNASHVSKGASTCDSKLCTSLCEKISPQGVSFCKPIATTGQSKKGNPVCNCRYWCRSDGTPHTT 73 Putative defensin-like protein 152 (Protein LCR11; Plant defensin) P82726 Belongs to the DEFL family LCR11 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00598 KVPCLSRMFNKNNTCSFLRCEANCARKYKGYGDCRPGDRPHDKKDSLFCFCNYPC 55 Defensin-like protein 153 (Protein LCR31; Plant defensin) P82746, A0MJV0 Belongs to the DEFL family LCR31 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00599 VVEKAKGDGSCTIIIDPKAPSCDIIQCRLSCITDYNGLAECIASRIGSPPNCVCTYDC 58 Putative defensin-like protein 154 (Protein LCR35; Plant defensin) P82750 Belongs to the DEFL family LCR35 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00600 DKRCSIIIDLSPCYPIECRLSCITERNGDGECVVSKVGSTPNCLCTYDC 49 Defensin-like protein 155 (Protein LCR36; Plant defensin) P82751 Belongs to the DEFL family LCR36 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00601 KRHCSTIILPESPCVPQDCVEYCFEEYNGGGTCIASKTGRTTNCMCTYNCHGNNL 55 Defensin-like protein 156 (Protein LCR21; Plant defensin) P82735 Belongs to the DEFL family LCR21 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00602 DERCTIIIHPGSPCDPSDCVQYCYAEYNGVGKCIASKPGRSANCMCTYNC 50 Putative defensin-like protein 157 (Protein LCR22; Plant defensin) Q9M0F3 Belongs to the DEFL family LCR22 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00603 DQTDKYCTIIIDPRTPCDLVDCRLSCYTGYNGVGKCIASKASRTPNCVCTYNC 53 Putative defensin-like protein 158 (Protein LCR23; Plant defensin) P82737 Belongs to the DEFL family LCR23 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00604 KRCHLTIDKATACSLSDCRLSCYSGYNGVGKCFDDPKVAGPSNCGCIYNC 50 Defensin-like protein 159 (Protein LCR25; Plant defensin) P82739, A0MJW9 Belongs to the DEFL family LCR25 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00605 DEGKRCHTTIDKGNFCDLVDCRLSCFSGYNGVGKCFDDPKVPGRSNCGCLYNC 53 Putative defensin-like protein 160 (Protein LCR26; Plant defensin) Q9M0F2 Belongs to the DEFL family LCR26 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00606 EECRLTIDKATPCHLSDCRLSCYTGYNGVGECFDDPNVPGPDNCGCRYNC 50 Defensin-like protein 161 (Protein LCR27; Plant defensin) Q9M0F1 Belongs to the DEFL family LCR27 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00607 GATIKKCVVDVKLSKPCTFQECQPLCLQKYNGNGLCPGDDNNICACVYNC 50 Putative defensin-like protein 162 (Protein LCR37; Plant defensin) P82752 Belongs to the DEFL family LCR37 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00608 ADIKRCVVDVKLSKPCTFQECIPLCFQRYNGNGVCTGKKNEICTCAYNC 49 Defensin-like protein 163 (Protein LCR24; Plant defensin) Q8LFM0, P82738, Q0V821 Belongs to the DEFL family LCR24 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00609 KQLKTCTSVIKLGHPCDIESCLNECFRVYNTGFATCRGDKYSQLCTCEYNC 51 Defensin-like protein 164 (Protein LCR38; Plant defensin) P82753 Belongs to the DEFL family LCR38 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00610 QKRCRQELEPGKQCVLAKCRELCFKQLKGFGSCIEKPPGSSKYTCNCFYNCGPPGFF 57 Putative defensin-like protein 165 (Protein LCR12; Plant defensin) P82727 Belongs to the DEFL family LCR12 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00611 LYMCVSSTCVIQWCAIQCKRKEANGIGTCKPRPNQGKIQYRKLKEECHCVYKCS 54 Defensin-like protein 166 (Plant defensin) P0CAY5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00612 RNRICRTSEKYYREFCGHAGNDDCLSKSTKKPKPFKCVCHDNRSQNITSINDRYNNCICTFYC 63 Putative defensin-like protein 168 (Plant defensin) Q2V3Q1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00613 LMDSMPQRHPVEGWCKRPLPNQKPGPCNNDRCSARCKEQKQFEFKGGKAMGICSSENRCLCTFRCR 66 Putative defensin-like protein 169 (Plant defensin) Q2V3K0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00614 NMGCMAVLGSCGVITDCSGSCKTKFGQDASGDCDRDGGQGTCMCGYPCPHDKLHM 55 Putative defensin-like protein 170 (Protein LCR62; Plant defensin) P82776 Belongs to the DEFL family LCR62 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00615 NMGCMAVLGSCGVITDCSGECISRFGPQARGYCDRDGGSGTCVCVYPCPADKPHM 55 Defensin-like protein 171 (Protein LCR61; Plant defensin) P82775, Q4VNZ4 Belongs to the DEFL family LCR61 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00616 NMGCTATMGPCEKDKSCSATCRATFGDRANGFCDYSTSTSPGGECTCVYHCPPVVPHESHL 61 Defensin-like protein 172 (Protein LCR60; Plant defensin) P82774 Belongs to the DEFL family LCR60 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00617 NMGCIQIIGRCIKIPDCSASCRKFLGPHASGYCDNDGAGGTCICTYPCQTKEIHM 55 Defensin-like protein 173 (Protein LCR63; Plant defensin) P82777, Q4VNZ3 Belongs to the DEFL family LCR63 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00618 NTGCFDYDVYQPCDHCRERCLKYYPVTRKAICRKNHCVCIGPCPNDKAIPNVKLFKNVKEQILS 64 Defensin-like protein 175 (Plant defensin) Q2V4H7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00619 NTGCFDYDVYQPCDHCRERCLKYYPVTRKAICRKNHCVCIGPCPDDKAIPDVKLFKNVKEQILS 64 Defensin-like protein 176 (Protein LCR65; Plant defensin) P82779, A0MJW1 Belongs to the DEFL family LCR65 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00620 NMGCNDYIVGDVCVHCRERCLRYYPVTRKAECYRNHCLCIGPCPDDRPHKRFQMLNSSKNVKAQILS 67 Defensin-like protein 178 (Protein LCR64; Plant defensin) P82778, A0MJW0 Belongs to the DEFL family LCR64 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00621 QTCDENLSSCENCDQRCKAKHGPSSVSKCNGPDGTCGCASFKPAKLCIGATDMCTDKCPTSCCDRQCAIKYKNGKGGCVDYAGYRMCICEYTC 93 Putative defensin-like protein 179 (Protein LCR57; Plant defensin) P82771 Belongs to the DEFL family LCR57 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains seven disulfide bonds (By similarity). Caution: Contains 7 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00622 SICNDRLGLCDGCDQRCKAKHGPSCESKCDGPVGMLLCTCTYECGPTKLCNGGLGNCGESCNEQCCDRNCAQRYNGGHGYCNTLDDFSLCLCKYPC 96 Defensin-like protein 181 (Protein LCR80; Plant defensin 3.1; Plant defensin) P82789, A0MJT6, Q1PDQ7 Belongs to the DEFL family PDF3.1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Confers broad-spectrum resistance to pathogens. PTM: Contains eight disulfide bonds (By similarity). Caution: Contains 8 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00623 NTCIEGIGNCQQCDVRCKARHGPAAKGACDSKFQLCTCNYPCGQGPSPPQPKKCYGGAGICSDRCGAQCCNQNCAQKYNQGSGFCDSIGNTSLCKCQYNC 100 Defensin-like protein 183 (Protein LCR19; Plant defensin) P82733, Q4VNZ2 Belongs to the DEFL family LCR19 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains eight disulfide bonds (By similarity). Caution: Contains 8 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00624 NKKMVGEAKKCDQTWTCEGEDKCREKCLTLHNGVGVCDLYTAPLVPKQCFCHYDC 55 Putative defensin-like protein 184 (Protein LCR18; Plant defensin) P82732 Belongs to the DEFL family LCR18 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00625 KTCSDGWTCLGPKEEDKCKENCMAKHKGVGTCNLYTIPEFPAPITYYMCDCMFDC 55 Putative defensin-like protein 185 (Protein LCR39; Plant defensin) P82754 Belongs to the DEFL family LCR39 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00626 KTCSDGWTCVGEDKCKVNCMAKHKGVGTCTLYIIPSFPAPITSYICDCMFDC 52 Putative defensin-like protein 186 (Protein LCR40; Plant defensin) P82755 Belongs to the DEFL family LCR40 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00627 ENQKMVGEAKQCKTGWACFGEDACKEKCMAKYKGVGTVTYFPFPPETIIIYCECLYDC 58 Putative defensin-like protein 187 (Protein LCR42; Plant defensin) P82757 Belongs to the DEFL family LCR42 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00628 ENGIMIGEAKKCSNSWICEGDEKCKEKCMADYKGNGTCYYPSPPSKQHPEFFYPTCWCGFDC 62 Putative defensin-like protein 188 (Protein LCR41; Plant defensin) P82756 Belongs to the DEFL family LCR41 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00629 MSNGMPRTVPCIEGRILWNRTLPCSSILCGDHCVPHGYRAGTCDIVNDRAICKCSRCR 58 Putative defensin-like protein 189 (Plant defensin) Q2V468 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00630 MRMTQKVSCIEGRTLWARPPKFFYCSSTLCEDNCINTGAYRGGTCDMEDEVAICRCHRCKKII 63 Putative defensin-like protein 190 (Plant defensin) Q2V467 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00631 KKPPCLEGRTAYVSPGPCSNSLCTQDCRPAGYHTGKCKVEWSTPICKCYGCRKV 54 Putative defensin-like protein 191 (Plant defensin) Q2V466 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00632 YDRKCLKEYGGDVGFSYCAPRIFPTFCDQNCRKNKGAKGGVCRWEENNAIGVKCLCNFCSEEPSDQTLSRI 71 Defensin-like protein 192 (Trypsin inhibitor ATTI-7; Plant defensin) Q42330, Q9SX84 Belongs to the DEFL family O22866 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00633 QGSKCLKEYGGNVGFSYCAPRIFPSFCYRNCRKNKGAKGGRCRSGGAGAGSMICLCDYCSDKP 63 Defensin-like protein 193 (Trypsin inhibitor ATTI-2; Plant defensin) O22866, Q67YC6, Q6ZZT9 Belongs to the DEFL family ATTI2 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00634 KDKECLKGYIDAPLSYCMARIYPSLCYRNCRFYKGAKGGKCDGLKCFCDFCSDKPF 56 Defensin-like protein 194 (Trypsin inhibitor ATTI-3; Plant defensin) O22867, B9DGH7, F4IR67, Q6ZZP9, Q6ZZQ4, Q6ZZQ9, Q6ZZR4, Q6ZZR9, Q6ZZT8 Belongs to the DEFL family ATTI3 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00635 QGNECLKEYGGDVGFGFCAPRIFPTICYTRCRENKGAKGGRCRWGQGSNVKCLCDFCDDTPQ 62 Defensin-like protein 195 (Trypsin inhibitor ATTI-1; diDi 4T-1; Plant defensin) Q42328, O22865, Q6ZZP6 Belongs to the DEFL family ATTI1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Protein level Combine helix and strand structure The protein contains one alpha-helix and two strands of antiparallel beta-sheet, with a type IV beta-turn connecting the two strands. The alpha-helix and the inhibitory loop are connected to the beta-sheet through three disulfide bridges; a fourth disulfide bridge connects the N- and C-termini. (Ref.3) 1JXC resolved by NMR. "Function: Defense response to fungus. PTM: Contains four disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924##12369816 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610.##Biochemistry. 2002 Oct 15;41(41):12284-96. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA.##Zhao Q, Chae YK, Markley JL. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis.##NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor. DRAMP00636 HDSECLKEYGGDVGFGFCAPKIFPTICYRNCQKDKGANGGKCLWGEGGKVKCLCDFCSNESFNQFISLT 69 Defensin-like protein 196 (Trypsin inhibitor ATTI-4; Plant defensin) Q8RYE7, Q6ZZS3 Belongs to the DEFL family ATTI4 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00637 KDDKFICVVEYGGDVGPTFCNPKFFPTLCRQNCRSFKGAKGGKCVKQPKHKHIKCFCDYCKDD 63 Defensin-like protein 197 (Trypsin inhibitor ATTI-6; Plant defensin) O22869, F4IR70, Q6ZZS7, Q6ZZU1, Q8GWN0 Belongs to the DEFL family ATTI6 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity). Caution: Was initially thought (PubMed:15082560) to be a protease inhibitor." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00638 RTTTSGYGMLFDSVACEGGFEYCPRGGGNDKCTTFCRSLPNKYDFGVCDKIYACCCHINV 60 Defensin-like protein 199 (Plant defensin) Q2V4G5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00639 RETRMMEQTCPVFWPMVPCDANKCEQMCRDYYGSVPSYCNRIGTPIAECACSLTPC 56 Defensin-like protein 201 (Plant defensin) Q2V4N2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00640 KTCKLFRGECPVDPCEPEKCDECCKATFGKQICGKCEQESTELHCHCRR 49 Putative defensin-like protein 202 (Plant defensin) Q2V3J6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00641 QTCFKGEAQEGVCVKVDGSKLCDLLCRATNTTWFGACEVEDNETHCHCYGPC 52 Putative defensin-like protein 203 (Plant defensin) Q2V424 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00642 HCDHFLGEAPVYPCKEKACKSVCKEHYHHACKGECEYHGREVHCHCYGDYH 51 Defensin-like protein 204 (Plant defensin) Q56XB0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found 7JN6 "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00643 NCDTYLGEVTVYYPCRERDCEAQCYEHYPHSCKGECEHHDHVVHHDNEEEHCHCYGR 57 Defensin-like protein 205 (His-rich; Plant defensin) Q9M9M3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00644 ACFTFLGECGPEPFTGSNADCLACCVALYKSPPVCAGRVEGVPAHCHCYKS 51 Defensin-like protein 206 (Plant defensin) Q94JR6, Q9M1Y2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP18327 ESISVAGGTWNYGYGVGQAYSHYKHDYNNHGAKVVNSNNGVKDYKNAGPGVWAKASIGTVWDPATFYYNPTGFYSN 76 Sil(Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Streptococcus iniae SF1 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found SIL is secreted by S. iniae into the extracellular milieu. Although it displayed antibacterial activity against B. subtilis, SIL showed no effect on 22 other Gram+ and Gram- bacteria tested. It can attach to the B. subtilis surface without killing (bacteriostatic). Activity is lost by heating at 50oC (heat-sensitive). SIL may serve as a virulent factor for infection. This dual role as antimicrobial and immune modulator suggests that a good understanding of the functions of an AMP is essential. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24781647 PLoS One. 2014 Apr 29;9(4):e96222. Li MF, Zhang BC, Li J, Sun L. Sil: a Streptococcus iniae bacteriocin with dual role as an antimicrobial and an immunomodulator that inhibits innate immune response and promotes S. iniae infection. DRAMP00646 ACFKFLGECGAVPFPGTNADCTSCCVGNFGSAVCAGRVEVEGGVKHCHCYGTS 53 Defensin-like protein 208 (Plant defensin) Q2V2Q8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00647 IITKTMNSKETIYLDNPAVSPSIDQNLVDIHLGHSFVQGVMSFCYDCGKACFRRGKNLARCQKFVCRCTISKLR 74 Defensin-like protein 209 (Plant defensin) Q2V3K2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00648 IITKTMNSKETTYLDSPAVSPSIDQYLVDIHLGHSFLQGVMSFCYDCGKACFRRGKNLARCKKFVCRCTKSGIK 74 Defensin-like protein 210 (Plant defensin) Q2V3K4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00649 IVMKSSNSKERTYPVTPALNPLTGQHSLRQRQLIFCDECANACFRRKKPVRSCQRFICRCAIRDVGY 67 Putative defensin-like protein 211 (Plant defensin) Q2V3K7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00650 VLINGSSDEERTYSFSPRASPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRYSISDIK 71 Defensin-like protein 212 (Plant defensin) A8MRC6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: Defense response to fungus. PTM: Contains two disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00651 TLINGSSDEERTYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISDIK 71 Defensin-like protein 213 (Plant defensin) Q4VP08, Q9LSW1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00652 ILINESSDEERTYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISGIK 71 Defensin-like protein 214 (Plant defensin) Q4VP10 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00653 ILINESSDEQRIYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISGIK 71 Defensin-like protein 215 (Plant defensin) Q4VP07 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00654 ILINESSDEQRIYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISDIK 71 Defensin-like protein 216 (Plant defensin) P0CAY6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00655 ILIKESSEEERIYPFNPVASPFDPRSLNQILKIGKIGYCFDCARACMRRDRYIRTCSFERKLCRCSYSHIHHTHG 75 Defensin-like protein 217 (Plant defensin) Q4VP09 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00656 KNKKVVIIPGPKGERPDIKVVEGPSTVEDDFCYDCVRRCMVKGVGFYFRSCKGFVCRCYYPFMGGYGP 68 Defensin-like protein 218 (Plant defensin) Q2V370 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00657 FFKKLFLRASNIMIKSISEGKSQFSGPALSPNIDPADEHIGHSPEDMKIIFCQQCAFHCIEKKKNIAHCENSICRCTLEDIL 82 Defensin-like protein 219 (Plant defensin) Q2V305 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00658 NIMTKSISQVKSQFFSPALSPNVDPADEHIGHSPDDMKIIFCQQCAFHCIEKKKNIGNCENSICRCTLEDIL 72 Defensin-like protein 220 (Plant defensin) Q2V304 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00659 NIMTKSILEGKTQFSIPSLSSTIDPAYEHIGHFPDDMKIIFCQQCAFHCIEKKKNIPHCENSICRCTLENIL 72 Putative defensin-like protein 221 (Plant defensin) Q2V306 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00660 TVKSYSEEKTHSFDLTANPPIDLNIVDELPRDEHLGVSHADNVIGFCQECAHHCLQRKRVLGECRWFTCHCSRITIGVGL 80 Defensin-like protein 222 (Plant defensin) Q2V300 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00661 VVPSSFKRVEGPVTAASADFCYKCSRGCYRRYRRPVFCQGSICRCSSFIDDGY 53 Defensin-like protein 223 (Plant defensin) Q2V369 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00662 MKKFGCNTTHPFPGKCGNNGKSSWVSDMKKLPSAPKNRDIRCECSDRPSLARGMPGERVCRCDYDC 66 Putative defensin-like protein 225 (Protein SCRL1; SCR-like protein 1; Plant defensin) P82620 Belongs to the DEFL family SCRL1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00663 KTKWGCDMNRPFPGKCGTNGKDTCISDIKKMPGAPKDLVVRCECSQRFVWKGYPPERLCKCQYDC 65 Defensin-like protein 226 (Protein SCRL2; SCR-like protein 2; Plant defensin) P82621 Belongs to the DEFL family SCRL2 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00664 IHVEQAGVCEFTGEFPGKCGNNGRKMCVEAMNKKNKGSPGENKKNLRCECFDNPVVILGRPKRICRCRNNC 71 Putative defensin-like protein 227 (Protein SCRL28; SCR-like protein 28; Plant defensin) P82647 Belongs to the DEFL family SCRL28 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00665 ANKRCHLNQMFTGKCGNDGNKACLGDFKNKRFRYDLCQCTDATQISPSLPPQRVCNCSRPC 61 Putative defensin-like protein 228 (Protein SCRL3; SCR-like protein 3; Plant defensin) P82622 Belongs to the DEFL family SCRL3 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00666 HVREVKSVETKAKRVKKVCEKAQVFEQNCGWDGNKTCIRGFNKIKEYPFHCECGIYDAPNSRRICKCKFPYSPC 74 Defensin-like protein 229 (Protein SCRL27; SCR-like protein 27; Plant defensin) P82646 Belongs to the DEFL family SCRL27 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity). Tissue specificity: Flower buds. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00667 EKLCTTIGDLDGKCSQDGEKLCMRYMTDQSKKKFLSCTCNNVVMLHKYKHYCECQSHCTPKQT 63 Putative defensin-like protein 230 (Protein SCRL24; SCR-like protein 24; Plant defensin) P82643 Belongs to the DEFL family SCRL24 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00668 KELCNRIEDIDGNCDFEGEKGCLKFMTNKYKKERHVSCTCTNLYMLHKTKRFCDCKHRCSG 61 Putative defensin-like protein 231 (Protein SCRL25; SCR-like protein 25; Plant defensin) P82644 Belongs to the DEFL family SCRL25 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00669 GAPPVECWSEILFSGKCGFHGKKKCYKEMESKLKQRVLKCRCEDVKKDSNTSKDEHYCGCQRENPYECN 69 Defensin-like protein 232 (Protein SCRL23; SCR-like protein 23; Plant defensin) P82642 Belongs to the DEFL family SCRL23 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity). Tissue specificity: Flower buds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00670 GAPPQDCWNLVTFPAKCGIHGKKKCFKEMESKYQQRFLQCTCKNLKPEPKSPKDEHDCTCQRANPYECNS 70 Putative defensin-like protein 233 (Protein SCRL22; SCR-like protein 22; Plant defensin) P82641 Belongs to the DEFL family SCRL22 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity). Tissue specificity: Expressed at least in stem, root, rosette leaves and flower buds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00671 VLKPMDQCGRKDIFLGGCGSNGSKTCINDFVKKGGVAAKPSSCECDDFGEEHLCRCYVPC 60 Putative defensin-like protein 234 (Protein SCRL14; SCR-like protein 14; Plant defensin) P82633 Belongs to the DEFL family SCRL14 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00672 GLDPMAANLRVRKDIFIGGCGRDGNKTCMKDFVKKGGVMNKPISCECDNLGYEHLCRCNFS 61 Putative defensin-like protein 235 (Protein SCRL26; SCR-like protein 26; Plant defensin) P82645 Belongs to the DEFL family SCRL26 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: Defense response to fungus. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00673 QGKKKPPCPLGLSANGKCGHDGPKLCFSEMERKFNKDVVKTITHCKCWDDRRNNVDKHRCTCYLKHGFPCTNG 73 Putative defensin-like protein 236 (Protein SCRL20; SCR-like protein 20; Plant defensin) P82639 Belongs to the DEFL family SCRL20 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00674 QAKKKRCPIGLHTYGKCGTDRAKFCFSEIESKLSFSKQVLNTISSCRCDDDRQGNKDLYWCQCDRREGRPCPAN 74 Putative defensin-like protein 237 (Protein SCRL21; SCR-like protein 21; Plant defensin) P82640, F4JMF8 Belongs to the DEFL family SCRL21 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00675 QVKPTGCQGGQRYRGKCGTNGTKTCVKDMMLPKLFKTKRCDCQDMLGTFKGWHFCTCYSGRPGC 64 Putative defensin-like protein 238 (Protein SCRL16; SCR-like protein 16; Plant defensin) P82635 Belongs to the DEFL family SCRL16 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00676 GLIRECDYTMEGYGPCGPNGRSLCLDTFWKTPPSPGLSKNLEGCRCEDRGKRPPIFTGLSHTCRCCWSYGGGSDD 75 Putative defensin-like protein 239 (Protein SCRL17; SCR-like protein 17; Plant defensin) P82636 Belongs to the DEFL family SCRL17 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00677 GLVRICNHRIEGYGTCGPNGRKICLDAFWKNQPSPGLSKNLEGCQCEDRRKRPQFKGLSHSCSCCWSYQGNSDE 74 Putative defensin-like protein 240 (Protein SCRL18; SCR-like protein 18; Plant defensin) P82637 Belongs to the DEFL family SCRL18 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00678 RTIRICDRKVEGNGTCGPNSNNICLDEFWKNPPSPRLAKSLEGCTCEPRGKRPKFKGLSHVCWCCWSYNSSNPAG 75 Defensin-like protein 241 (Protein SCRL19; SCR-like protein 19; Plant defensin) P82638 Belongs to the DEFL family SCRL19 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00679 HEEPKVAPTEELMFAPSNQPRYCRSRQVFDGSCTDRGTPRTTCFLDFLGARSASEMPKNCDCTPQPNNKRLCECSVICTDCCVKN 85 Defensin-like protein 242 (Protein SCRL10; SCR-like protein 10; Plant defensin) P82629, Q6GKW3 Belongs to the DEFL family SCRL10 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00680 HLSHEEPMKEPEYCRWTNAFNGTCSDRGNPQTMCFFDFLDAHTARVMPKNCACNDLPGNKRYCECSFVCNS 71 Putative defensin-like protein 243 (Protein SCRL9; SCR-like protein 9; Plant defensin) P82628 Belongs to the DEFL family SCRL9 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00681 KELKWCPSKDVFNGSCTDTGSPSYTCFLDLLGSKSASAMPKNCKCTPLPHNRRQCDCFVVCDSN 64 Putative defensin-like protein 244 (Protein SCRL11; SCR-like protein 11; Plant defensin) P82630 Belongs to the DEFL family SCRL11 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00682 EESSMNIDAQRRPWCPSKKQVFGGSCGNDGAQQCLNNLLSTWDPSVRLSPVSCNCTPQPNNNILCSCPNMICP 73 Defensin-like protein 245 (Protein SCRL4; SCR-like protein 4; Plant defensin) P82623, A0MJS7, A7RED2 Belongs to the DEFL family SCRL4 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity). Tissue specificity: Flower buds and roots." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00683 EESRMNINAERRPWCPSKIQMFDTNCEVDGAKQCLDLLISTWDPSVRLTRVSCICSDFPYRNMMCSCPNMICP 73 Defensin-like protein 246 (Protein SCRL5; SCR-like protein 5; Plant defensin) P82624, Q1PFI3, Q5XVH8 Belongs to the DEFL family SCRL5 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity). Tissue specificity: Flower buds and stems." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00684 EKLSMDPTRRPWCPSKKQMFGGNCGNDGDSLCLMLLAASWDESLRHSSISCNCTTYPNYKILCSCPNMICP 71 Defensin-like protein 247 (Protein SCRL6; SCR-like protein 6; Plant defensin) P82625, Q570C5, Q8L952 Belongs to the DEFL family SCRL6 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00685 EAAGERRQWCPSKQQVFRGSCSDDGGQKCLNDLLWTWNPSVRLSPIYCDCTPKRHNKRLCDCPSMICL 68 Defensin-like protein 249 (Protein SCRL7; SCR-like protein 7; Plant defensin) P82626, A7RED3 Belongs to the DEFL family SCRL7 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00686 EKRPWCPTRKQIFDGSCNRTDYTQCFNDLRNTWDDIGDLCPTDCTCTPQPQNKRLCYCRYLPCPST 66 Defensin-like protein 250 (Protein SCRL8; CR-like protein 8; Plant defensin) P82627 Belongs to the DEFL family SCRL8 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00687 QRLVPLCKTIGYENPGKCPADGNKFCRRKLDDRYVKYKRCDCQDTKGRKQNHHRCICYMKLPCNQ 65 Putative defensin-like protein 251 (Protein SCRL12; SCR-like protein 12; Plant defensin) P82631 Belongs to the DEFL family SCRL12 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00688 QRRKPVCKLTGVLNPGKCPTAIHDASNLCSRKLASPNMTFKRCDCQNTEWRGKDHYQCTCYIKLPCNQ 68 Putative defensin-like protein 252 (Protein SCRL13; SCR-like protein 13; Plant defensin) P82632 Belongs to the DEFL family SCRL13 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00689 EVEPVPYCKVITWYDVKCGADGNKTCVDHLIKGHIYDVPVCDCSELTTSGILCTCQHRFPCKEPPPLHRISIRKQIRG 78 Putative defensin-like protein 253 (Protein SCRL15; SCR-like protein 15; Plant defensin) P82634 Belongs to the DEFL family SCRL15 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00690 VRHNLAVGDVCATNEECRINCQCDAAYCDLSCNMCVYMLHVMDTIDANIPNQPCISEYQNCGKKTSSLQ 69 Putative defensin-like protein 254 (Plant defensin) Q2V318 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains two disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00691 YEDSCSTDEECRRNCLCDVAYCDKSRDKCDYGFMNRVDVRFPKHPYISKNKDGSGR 56 Defensin-like protein 255 (Plant defensin) Q2V3Q8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains two disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks 2 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00692 VADYCNRDADCKRVCLRPYACNLTRHLCMCHPNDVSSSKQHCIPEHKGFGEGGPPPQRLKLYR 63 Putative defensin-like protein 256 (Plant defensin) Q2V483 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00693 RELAGVNEIFEIAARSSNNAGTARALQQAPPCKRDVDCSFECPKGGFCNDRLGTCDCF 58 Putative defensin-like protein 257 (Plant defensin) Q2V3S8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00694 RELTGAGKKLEVATRSSNYAGTARTLLQARPCQRDVDCNFQCPRIQGGQCNNHHGTCDCF 60 Putative defensin-like protein 258 (Plant defensin) Q2V3S7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00695 RKLTGVADVIVEGEAASPQYGIIDENDTLNKSPSCKRDIDCTFQCRRGGFCNLILQKCECL 61 Defensin-like protein 259 (Plant defensin) Q9LV55, A0MEY0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00696 IQNSETSVNQNSCMPNEPRCTGCPGGGSGGYRGPPPPCCKNDSDCKAHCPEGGYCSNQCDCVCNLVKVMNNDVRCQVDTDCNMKCSKQGYCKLAS 95 Defensin-like protein 260 (Plant defensin) Q9LMX3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00697 REMVKAEVNCIGGKCPEGKKNCNCMPPIAHVMDDIRPCNTDGDCYKFCPRECELGTCYCRCDYGCTCTC 69 Putative defensin-like protein 262 (Plant defensin) Q2V4E0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00698 REMAKEEVNCIGGHCPDGKKDCNCLPLIAPTMDIYETNESCRTDNECIKYCPKGCKIVDCNFGTCLCEYC 70 Putative defensin-like protein 263 (Plant defensin) Q2V4D9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00699 LEGESKVSGQVRDETPHTWYCKYDDNCRENCPGCTITKCNYGVCICSNCYHQQSDLGVESHM 62 Putative defensin-like protein 264 (Plant defensin) Q2V2W3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00700 SKGEEKTSGELRDVTPQRGGPCSYDNLCHNHCPGCKITQCVNGECVCLICYTPPL 55 Putative defensin-like protein 265 (Plant defensin) Q2V2W2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00701 SEQRTRVSEVVREAEIHDGGQCTDDDICNKNCLDCIARQCIFQQCVCSKRFFPPNSQPNLRVKKH 65 Defensin-like protein 267 (Plant defensin) Q2V354 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00702 IPRGWQEPCFCPSKNPYCDCGDDLQVPTTSVISPKPIIEQCARCERNSQCNKVCPATCKYKVCIFNRTCEFSTCHCYRC 79 Defensin-like protein 268 (Plant defensin) Q2V4N6, A0MJU3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00703 RMSGDVTIQRGGSCNNDNTCHDTCPGCRITQCIFRQCVCTRCNTPRSSLRIESHM 55 Defensin-like protein 266 (Plant defensin) Q2V4F0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00704 RQMQRPQNVECVGGECQPKHPQQYFGSCFRDSDCRNSCFPYCRYQKCHHHECICSLCSSEVAPSPK 66 Defensin-like protein 269 (Plant defensin) Q2V4F4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00705 TRIMDDSSDCVFKGPCQRRSDCYERCGLKPPSRAALCQPMGLQGRVCCCL 50 Putative defensin-like protein 270 (Plant defensin) Q2V2Z3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00706 TRIMDASSDCEFKGPCHKKEDCYDSCGVNKPPFNNAICVPGRDSFQCCCILS 52 Putative defensin-like protein 271 (Plant defensin) Q2V352 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00707 TREILSAEICGWNDPAVHCKTKEDCFEKCGGRPAKKVFCVRPGDHSYDRLCCCRA 55 Defensin-like protein 272 (Plant defensin) Q2V2W8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00708 NSVEKDVMDGPCRLRGTCNNDGDCDKHCHRSTDAAAMDGHCLFDKPTGPVCCCLFD 56 Putative defensin-like protein 274 (Plant defensin) Q2V2W7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00709 KIVKRMQVGPSECVYRGRCRDSYECRSRCGPPEFSHETLGLCMFDYDDYEYFCCCTTNY 59 Defensin-like protein 275 (Plant defensin) Q2V4I9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00710 SGCNFKGSCRTDDQCKRICRGHGLDPSFQLCVPYSSKGGKCCCLHYEGAPLSSEVI 56 Defensin-like protein 276 (Plant defensin) Q2V328 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00711 IVCNFEGHCVTSDDCINVCKSGEDPFLCVRSGPHKGMCCCLKTNGSVLE 49 Putative defensin-like protein 277 (Plant defensin) Q2V329 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00712 ARIQESTNDILKPITCNTNADCAKFCKGPIHNCVYHTCQCVPGNPHCC 48 Defensin-like protein 278 (Plant defensin) Q2V4F7 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00713 QESKKGILLKPKTCNTNADCAKFCKGPIQNCLYHTCACVPGNPHCC 46 Putative defensin-like protein 279 (Plant defensin) Q2V4F6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00714 DYKFHVCDPSFDEKDCDFECKEFGHPGGYCRPDRVQPRIRMCYCTDR 47 Putative defensin-like protein 280 (Plant defensin) Q2V4C4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00715 TDPVPTPPGLHIPCGKGFTSKECNKYCTGVGYRRGYCAPDEEYPQISSCYCKWRI 55 Defensin-like protein 281 (Plant defensin) Q2V4C3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00716 NRQCVQAMDCTNVCSHGGLCTKNGKCVCWSPNVVINSGPPCWSDEMCFSTCGGNGGYCNYDIGGCFCQ 68 Putative defensin-like protein 282 (Plant defensin) Q2V2Y0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00717 TAARENLHHQCFCESPSKCDCFPTTPTPPTSVNKSRKGGPLCTTDGDCKHFCRPKKGVCNIDFETCICQ 69 Putative defensin-like protein 283 (Plant defensin) Q2L6T1 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00718 KEDKECNDSKCLPNPSRINLEEGNIKRIDVNHGGICDTYLECGGLACSDYRRACCVNGKCVCRKQGQTLPDCPN 74 Defensin-like protein 285 (Plant defensin) Q2V315, F4KBR3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00719 LDEPNMDTISKSREYKCKIDLDCSNHIACRHCSYRNCKCDHGTCKCMP 48 Defensin-like protein 286 (Plant defensin) Q2L6T6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00720 AEEMGKGEVTISLRCKTKTECLKNIACEACVDCRCDKGICKCHGFTAETNNPTV 54 Defensin-like protein 287 (Plant defensin) Q2V4N4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00721 KPRGKRPQSNFHAKRIRTVLQTLLVMLCTDYRCDKGLCKCHGFGGEKENPTAAPLTA 57 Putative defensin-like protein 288 (Plant defensin) Q2V4N5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00722 DASCLTTKECVVRCSDEDAQCIHGECHCPHLKVDIEPTKAIRCKTDLDCPDPHQCPKYDYYACLNNGECTCISV 74 Defensin-like protein 289 (Plant defensin) Q2V4I2 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains six disulfide bonds (By similarity). Caution: Contains 6 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00723 TSSTLKESLTAEIKPTKVDRCKTDRDCPQSHRCQKDFYYGCVVGECICRAV 51 Defensin-like protein 291 (Plant defensin) Q2V472 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00724 MLLETDASRNKPSSYIPLCGSDNSCGGLWCPRKGGKYSCISMTCDIQEDCPKLVRCKDSPGPYCMEGFCTC 71 Defensin-like protein 292 (Plant defensin; Uncertain) P0CAY8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide and 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00725 SRNKLSSYIPLCGSNTYCGGLWCPKKGGKYSCISMSCDIQEDCPKLVRCKNSPGPYCMEGFCTC 64 Defensin-like protein 293 (Plant defensin) Q2V4A3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00726 SKNKSRSDLPLCGFREHCDGLWCPGEGGKYSCINWSCNFIEDCEKRIRCEKTGPCCFDGLCDCTNF 66 Defensin-like protein 294 (Plant defensin) Q2V4A4 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00727 HNFLPCVITNDCEYHHCSSGTVLCVNRQCHCSRSSTHQTKLDNLKKMDYAKKCKWTKDCDPRMRFTCVSGSYMCFDGLCTCTN 83 Defensin-like protein 295 (Plant defensin) Q4VNZ6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains six disulfide bonds (By similarity). Caution: Contains 6 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00728 ELVLPCKTTYDCVNLPCLGRPPLCINGQCKCTTTLTHQAKLDNLRTMNDAKTCKYTSDCDPRMRYSCVSGSYICLNGFCTCT 82 Defensin-like protein 296 (Plant defensin) Q4VNZ5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains six disulfide bonds (By similarity). Caution: Contains 6 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00729 QLIVPCKTSEQCKSIRCSNGSAQCVNKQCQCPSLKQIYSVTDVSCKTVSDCVASHQCPTGLSACIEGKCICLP 73 Putative defensin-like protein 298 (Plant defensin) Q2V459 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains six disulfide bonds (By similarity). Caution: Contains 6 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00730 QFRCKSVAECDSRGCRVGTHVICNEHHICTCAHGSPIGGQCDGVEDCDLSGCPPNSHVICDRIGGNFCTCVPN 73 Defensin-like protein 301 (Plant defensin) Q3E715 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains six disulfide bonds (By similarity). Caution: Contains 6 disulfide bonds instead of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00731 MLRFVLVYIPVSVVSHTLCISLFIICSTRHTCFSKRYTCLLNICFCFFISSRIRNYF 57 Defensin-like protein 302 (Plant defensin) Q2V3W5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide and 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00732 RCYTNDDCKDGQPCPVPLACLFGSCICPWKSQSKLPICQIICANLD 46 Putative defensin-like protein 303 (Plant defensin) Q2V311 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00733 VRLTENMCFKDDDCINQGEWCPVLRVCSYAECICPWGTRSKLPSCQIICAHLDKKSVNSYNPCGCNYK 68 Putative defensin-like protein 304 (Plant defensin) Q2V309 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00734 KTNFDCVNLKCPTPFVTPKCVSGGCECPLKELLTLLSDTNYGVAACIDYCKAKGENAYTCILNHCYCRKPSM 72 Putative defensin-like protein 305 (Plant defensin) Q2V493 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00735 QSCNNDSDCTNLKCATKNIKCEQNKCQCLDERYIRAISLNTRSPRCNVQSCIDHCKAIGEVIYVCFTYHCYCRKPPM 77 Defensin-like protein 306 (Plant defensin) Q2V3H6 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00736 RTGYVSCKTNSDCVKLKCPTPFGGPKCISGSCECPFKELMTLPNDTNYGVAACIDYCKAKGEIVYACILNHCYSYKPPM 79 Putative defensin-like protein 307 (Plant defensin) Q2V3H5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00737 MIMGVSYHENRCHDWVDCAIWCKQWVPQPKCINRVCDCKPKSLPTNDEIPKSASSSSKN 59 Defensin-like protein 308 (Plant defensin) Q4VP04 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00738 MIMGVHYHEYRCHDWVDCAIWCKQWVPQPKCINRVCDCKPKSLPTNEEVPQSAYSSNSNY 60 Putative defensin-like protein 309 (Plant defensin) Q2V310 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00739 DICQTDRDCVEIGIPRCKRTGKMPICYNGYCCCICSAKRLPASTTRKPPSPSTSKLV 57 Defensin-like protein 311 (Plant defensin) Q2V3X3 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Transcript level Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00740 QSPLSQSSHEFTVVSPYLSCFGIEECLFYLYFKLYDLCVILLCTWFDLSE 50 Putative defensin-like protein 312 (Plant defensin) Q2V3K9 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found Caution: Could be the product of a pseudogene. Lacks 3 of the 4 disulfide bonds, which are conserved features of the family. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00741 HVCLMSFGSSYRVGVHITHEKVAACPRQNQRLYSCDSLRILYHYSCLTTRDLLYICDCSDFENIICLIRLLLNLDFVEVKLV 82 Defensin-like protein 316 (Plant defensin) Q2V4J8 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00742 FKIHEVPEPTGKWCGYSVPMKPCINDDRVKRCIAENTHGWLMATGMCTSIPSLKDCYCMHQCP 63 Putative defensin-like protein 317 (Plant defensin) Q2V3Y5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00743 DCKHPVGPYTDSCFTDCVSGKYGYNYESAFCSRDETGTCKICCCELINE 49 Defensin-like protein 313 (Plant defensin) Q3E8K0, Q1PDQ0 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Homology Not found Not found "Function: May have antifungal activity. PTM: Contains three disulfide bonds (By similarity). Caution: Lacks 1 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11437247##15955924 Plant Mol Biol. 2001 May;46(1):17-34.##Plant Physiol. 2005 Jun;138(2):600-610. Vanoosthuyse V, Miege C, Dumas C, Cock JM.##Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Two large Arabidopsis thaliana gene families are homologous to the Brassica gene superfamily that encodes pollen coat proteins and the male component of the self-incompatibility response.##Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00744 MYLSSRTGSRLLFLVKASFNTFEKVATISSTLIYFVSHKLVSSRSCSHNFRNICGYIRHNCRKCIRFCFCTFSIKISLPLVIARRIEY 88 Putative defensin-like protein 315 (Plant defensin) Q2V3R5 Belongs to the DEFL family Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Not found Not found Not found "PTM: Contains two disulfide bonds (By similarity). Caution: Could be the product of a pseudogene. Lacks the signal peptide and 2 of the 4 disulfide bonds, which are conserved features of the family." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15955924 Plant Physiol. 2005 Jun;138(2):600-610. Silverstein KA, Graham MA, Paape TD, VandenBosch KA. Genome organization of more than 300 defensin-like genes in Arabidopsis. DRAMP00745 GTCKAECPTWEGICINKAPCVKCCKAQPEKFTDGHCSKILRRCLCTKPC 49 Floral defensin-like protein 2 (PhD2; Plant defensin) Q8H6Q0 Belongs to the DEFL family D2 Petunia hybrida (Petunia) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Plant defense peptide with antifungal activity against F. oxysporum and Botrytis cinerea. Tissue specificity: Petals. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin (By similarity). Biophysicochemical properties: pH dependence (Stable under extremes of pH); Temperature dependence (Stable under extremes of temperature). PTM: Contains five disulfide bonds 3-49; 7-23; 14-36; 20-43; 24-45 (By similarity)." Fungi: Fusarium oxysporum (86% inhibition at 10 µg/ml), Botrytis cinerea (41% inhibition at 10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644678 Plant Physiol. 2003 Mar;131(3):1283-1293. Lay FT, Brugliera F, Anderson MA. Isolation and properties of floral defensins from ornamental tobacco and petunia. DRAMP00746 RECKTESNTFPGICITKPPCRKACISEKFTDGHCSKILRRCLCTKPC 47 Flower-specific defensin (NaD1; Plant defensin) Q8GTM0 Belongs to the DEFL family D1 Nicotiana alata (Winged tobacco) (Persian tobacco) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure NaD1 adopts the cysteine-stabilized αβ (CSαβ) motif formed by a triple-stranded antiparallel β-sheet and a single α-helix that is tethered to the sheet via three disulfide bonds. The fourth disulfide bond reinforces the N- and C-terminal regions of the molecule. 4AAZ, 4AB0 resolved by X-ray. "Function: NaD1 is a member of a family of cationic peptides that displays growth inhibitory activity against several filamentous fungi, including Fusarium oxysporum. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43. Tissue specificity: Most abundant in the epidermal cell layers of the petals and sepals, within the connective cells of the anthers, and the cortical cells of the style. Not detected in the tapetum, pollen mother cells, the transmitting tissue, the vascular bundles of the anther and style or in leaves. Expressed also in ovaries, but barley detectable in roots. Biophysicochemical properties: pH dependence (Stable under extremes of pH); Temperature dependence (Stable under extremes of temperature." Fungi: Fusarium oxysporum f. sp. Vasinfectum (IC50=1 µM), Thielaviopsis basicola (IC50=0.80 µM), Verticillium dahliae (IC50=0.75 µM), Leptosphaeria maculans (IC50=0.80 µM), Aspergillus nidulans (IC50=0.80 µM), Candida albicans (IC50>10 µM), Pichia pastoris (IC50>10 µM), Saccharomyces cerevisiae (IC50>10 µM).##Gram-negative bacteria: Escherichia coli (IC50>10 µM), Pseudomonas aeruginosa (IC50>10 µM);##Gram-positive bacteria: Staphylococcus aureus (IC50>10 µM), Bacillus cereus (IC50>10 µM).##HeLa cells (IC50>10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644678##12473460##22511788##18339623 Plant Physiol. 2003 Mar;131(3):1283-1293.##J Mol Biol. 2003 Jan 3;325(1):175-188.##J Biol Chem. 2012 Jun 8;287(24):19961-72.##J Biol Chem. 2008 May 23;283(21):14445-52. Lay FT, Brugliera F, Anderson MA.##Lay FT, Schirra HJ, Scanlon MJ, Anderson MA, Craik DJ.##Lay FT, Mills GD, Poon IK, Cowieson NP, Kirby N, Baxter AA, van der Weerden NL, Dogovski C, Perugini MA, Anderson MA, Kvansakul M, Hulett MD.##van der Weerden NL, Lay FT, Anderson MA. Isolation and properties of floral defensins from ornamental tobacco and petunia.##The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP.##Dimerization of plant defensin NaD1 enhances its antifungal activity.##The plant defensin, NaD1, enters the cytoplasm of Fusarium oxysporum hyphae. DRAMP00747 RECKTESNTFPGICITKPPCRKACISEKFTDGHCSKLLRRCLCTKPCVFDEKMIKTGAETLVEEAKTLAAALLEEEIMDN 80 Defensin-like protein (Flower-specific gamma-thionin; Plant defensin) P32026 Belongs to the DEFL family FST Nicotiana tabacum (Common tobacco) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 1MR4 resolved by NMR. "Function: Involved in floral organogenesis. May play a protective role in flowers by protecting the reproductive organs from potential pathogen attack. Tissue specificity: Found in petals, stamen and pistils, but not in sepals. In particular, accumulation in a configuration surrounding the inner reproductive whorls. Developmental stage: Accumulates in developing flowers and its level drops as flowers mature. PTM: Contains four disulfide bonds 3-47; 14-34; 20-41; 24-43." Fungi: Fusarium oxysporum and Botrytis cinerea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1495489##12473460 Mol Gen Genet. 1992 Jul;234(1):89-96.##J Mol Biol. 2003 Jan 3;325(1):175-188. Gu Q, Kawata EE, Morse MJ, Wu HM, Cheung AY.##Lay FT, Schirra HJ, Scanlon MJ, Anderson MA, Craik DJ. A flower-specific cDNA encoding a novel thionin in tobacco.##The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP. DRAMP00748 QDKCKKVYENYPVSKCQLANQCNYDCKLDKHARSGECFYDEKRNLQCICDYCEY 54 Defensin-like protein(Brazzein; Plants) P56552 Belongs to the DEFL family Not found Pentadiplandra brazzeana Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Combine helix and strand structure The brazzein fold, which contains one alpha-helix and three strands of antiparallel beta-sheet. 1BRZ resolved by NMR.##4HE7 resolved by X-ray. "Function: Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis. Has a pH-specific antimicrobial activity against bacteria and fungi. PTM: Contains four disulfide bonds 4-52; 16-37; 22-47; 26-49." Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus.##Gram-positive bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15118082##9628478 Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-7368.##Nat Struct Biol. 1998 Jun;5(6):427-431. Yount NY, Yeaman MR.##Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G, Markley JL. Multidimensional signatures in antimicrobial peptides.##Solution structure of the thermostable sweet-tasting protein brazzein. DRAMP00749 ELCEKASKTWSGNCGNTGHCDNQCKSWEGAAHGACHVRNGKHMCFCYFNC 50 Defensin-like protein 1 (Dm-AMP1; Plant defensin) P0C8Y4 Belongs to the DEFL family Not found Dahlia merckii (Bedding dahlia) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Function: Possesses antimicrobial activity sensitive to inorganic cations. Has no inhibitory effect on insect gut alpha-amylase. Induces potential changes in fungal membranes and increased K+ efflux and Ca2+ uptake. Interacts with sphingolipids and ergosterols found in fungal plasma membranes. Biotechnological use: DmAMP1 expression in heterologous plants such as rice or papaya may provide a broad-spectrum disease resistance. PTM: Problely contains four disulfide bonds 3-50;14-35;20-44;24-46." Gram-positive bacterium: Bacillus subtilis (IC50=150 µg/mL).##Medium A: Botrytis cinerea (IC50=12 µg/ml), Cladosporium sphaerospermum (IC50=3 µg/ml), Fusarium culmorum (IC50=5 µg/ml), Leptosphaeria maculans (IC50=1.5 µg/ml), Penicillium digitatum (IC50=2 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=1 µg/ml), Verticilium albo-atrum (IC50=4 µg/ml). NOTE: Medium B = 1/2 strength potato dextrose broth.##Medium B: Botrytis cinerea (IC50>100 µg/ml), Cladosporium sphaerospermum (IC50=12 µg/ml), Fusarium culmorum (IC50=8 µg/ml), Leptosphaeria maculans (IC50=15 µg/ml), Penicillium digitatum (IC50=70 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=4 µg/ml), Verticilium albo-atrum (IC50>100 µg/ml).##NOTE: Medium B = Medium A supplemented with 1 mM CaCl2 and 50 mM KCI. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrabce 13129623##7628617##8663029##17216480 FEMS Microbiol Lett. 2003 Sep 12;226(1):169-173.##FEBS Lett. 1995 Jul 17;368(2):257-262.##Plant Physiol. 2002 Apr;128(4):1346-1358.##J Biol Chem. 1996 Jun 21;271(25):15018-15025.##Planta. 2007 Jun;226(1):87-97 Thevissen K, Fran§ois IE, Takemoto JY, Ferket KK, Meert EM, Cammue BP.##Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF.##Fran§ois IE, De Bolle MF, Dwyer G, Goderis IJ, Woutors PF, Verhaert PD, Proost P, Schaaper WM, Cammue BP, Broekaert WF.##Thevissen K, Ghazi A, De Samblanx GW, Brownlee C, Osborn RW, Broekaert WF.##Zhu YJ, Agbayani R, Moore PH. DmAMP1, an antifungal plant defensin from dahlia (Dahlia merckii), interacts with sphingolipids from Saccharomyces cerevisiae.##Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.##Fungal membrane responses induced by plant defensins and thionins.##Ectopic expression of Dahlia merckii defensin DmAMP1 improves papaya resistance to Phytophthora palmivora by reducing pathogen vigor. DRAMP00750 EVCEKASKTWSGNCGNTGHC 20 Defensin-like protein 2 (Dm-AMP2; Plant defensin) No entry found Belongs to the DEFL family Not found Dahlia merckii (Bedding dahlia) Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Medium A: Botrytis cinerea (IC50=10 µg/ml), Cladosporium sphaerospermum (IC50=3 µg/ml), Fusarium culmorum (IC50=5 µg/ml), Leptosphaeria maculans (IC50=1 µg/ml), Penicillium digitatum (IC50=2 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=1 µg/ml), Verticilium albo-atrum (IC50=2 µg/ml). NOTE: Medium A = 1/2 strength potato dextrose broth.##Medium B: Botrytis cinerea (IC50>100 µg/ml), Cladosporium sphaerospermum (IC50=12 µg/ml), Fusarium culmorum (IC50=12 µg/ml), Leptosphaeria maculans (IC50=20 µg/ml), Penicillium digitatum (IC50=50 µg/ml), Trichoderma viride (IC50>100 µg/ml), Septoria tritiei (IC50=2 µg/ml), Verticilium albo-atrum (IC50>100 µg/ml).##NOTE: Medium B = Medium A supplemented with 1 mM CaCl2 and 50 mM KCI. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrabce 8422949##7628617 FEBS Lett. 1993 Feb 1;316(3):233-240.##FEBS Lett. 1995 Jul 17;368(2):257-262. Terras FR, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BP, Broekaert WF.##Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF. A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species.##Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. DRAMP00751 RMCKTPSAKFKGYCVSSTNCKNVCRTEGFPTGSCDFHITSRKCYCYKPCP 50 Defensin-2 (Plant defensin) A4L7R8 Belongs to the DEFL family Def2 Pinus sylvestris (Scots pine) Antimicrobial, Antifungal Homology Not found Not found 7LNS "Function: Plant defense peptide. Has antifungal activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19253756 Tsitol Genet. 2008 Nov-Dec;42(6):55-60. Koval'ova VA, Hut RT. Molecular cloning and characterization of Scotch pine Defensin-2. DRAMP00752 RMCKTPSGKFKGYCVNNTNCKNVCRTEGFPTGSCDFHVAGRKCYCYKPCP 50 PsDef1 (P. sylvestris defensin 1, p1; Plant defensin) A4L7R7 Belongs to the DEFL family Def1 Pinus sylvestris (Scots pine) Antimicrobial, Antifungal Protein level Not found Not found 5NCE "Function: Plant defense peptide. Has antifungal activity. PTM: Contains four disulfide bonds (By similarity)." Fungi: Botrytis cinerea (IC50=0.4 µg/ml), Fusarium oxysporum (IC50=2.9 µg/ml), Fusarium solani (IC50=0.9 µg/ml), Heterobasidion annosum (IC50=1.4 µg/ml), Candida albicans and Trichoderma reesei. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19683554 Peptides. 2009 Dec;30(12):2136-2143. Kovaleva V, Kiyamova R, Cramer R, Krynytskyy H, Gout I, Filonenko V, Gout R. Purification and molecular cloning of antimicrobial peptides from Scots pine seedlings. DRAMP00753 ATKVKAKQRGKEKVSSGRPGQHN 23 Elicitor peptide 1 (AtPep1; Plant defensin) Q9LV87, Q8LCK9 Belongs to the brassicaceae elicitor peptide family PEP1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Protein level Not found Sequential removal of N-terminal amino acids has little effect on activity. Activity is completely abolished when nine C-terminal amino acids remained. Removal of the C-terminal asparagine from AtPep1(9-23), resultes in a decrease in activity (12 max approximately 100 nM). "Function: Elicitor of plant defense. Induces the production of plant defensin (PDF1.2) and of H2O2. Promotes resistance to the root fungal pathogen P. irregulare. Subunit structure: Interacts with its receptor PEPR1. Induction: By wounding, methyl jasmonate (MeJA), ethylene. The expression of the peptide PEP1 precursor is induced by the mature peptide PEP1." Pythium irregulare No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##16785433##18824048 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10104-9.##Peptides. 2008 Dec;29(12):2083-9. Huffaker A, Pearce G, Ryan CA.##The cell surface leucine-rich repeat receptor for AtPep1, an endogenous peptide elicitor in Arabidopsis, is functional in transgenic tobacco cells.##Pearce G, Yamaguchi Y, Munske G, Ryan CA. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##The cell surface leucine-rich repeat receptor for AtPep1, an endogenous peptide elicitor in Arabidopsis, is functional in transgenic tobacco cells.##Structure-activity studies of AtPep1, a plant peptide signal involved in the innate immune response. DRAMP00754 DNKAKSKKRDKEKPSSGRPGQTNSVPNAAIQVYKED 36 Elicitor peptide 2 (AtPep2; Plant defensin) Q9LV88, Q8L902 Belongs to the brassicaceae elicitor peptide family PEP2 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. DRAMP00755 EIKARGKNKTKPTPSSGKGGKHN 23 Elicitor peptide 3 (AtPep3; Plant defensin) Q8LAX3 Belongs to the brassicaceae elicitor peptide family PEP3 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. DRAMP00756 GLPGKKNVLKKSRESSGKPGGTNKKPF 27 Elicitor peptide 4 (AtPep4; Plant defensin) Q9FIA9, Q8L9J1 Belongs to the brassicaceae elicitor peptide family PEP4 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. DRAMP00757 SLNVMRKGIRKQPVSSGKRGGVNDYDM 27 Elicitor peptide 5 (AtPep5; Plant defensin) Q8LD63, Q9FIA8 Belongs to the brassicaceae elicitor peptide family PEP5 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. DRAMP00758 ITAVLRRRPRPPPYSSGRPGQNN 23 Elicitor peptide 6 (AtPep6; Plant defensin) Q9SIZ9 Belongs to the brassicaceae elicitor peptide family PEP6 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones. DRAMP00759 VSGNVAARKGKQQTSSGKGGGTN 23 Elicitor peptide 7 (AtPep7; Plant defensin) P0C1T5, Q1G3G0 Belongs to the brassicaceae elicitor peptide family PEP7 Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: Elicitor of plant defense (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16785434##10718197##17147637 Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones.##Plan Huffaker A, Pearce G, Ryan CA.##Sato S, Nakamura Y, Kaneko T, Katoh T, Asamizu E, Kotani H, Tabata S.##Underwood BA, Vanderhaeghen R, Whitford R, Town CD, Hilson P. An endogenous peptide signal in Arabidopsis activates components of the innate immune response.##Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones.##Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations. DRAMP00760 RECKAQGRHGTCFRDANCVQVCEKQAGWSHGDCRAQFKCKCIFEC 45 NmDef02 (Plants) No entry found Belongs to the defensin family Not found Nicotiana megalosiphon Antimicrobial, Antifungal Not found Not found Not found Transgenic plants: Constitutive expression of NmDef02 gene in transgenic tobacco and potato plants enhanced resistance against various plant microbial pathogens, including the oomycete Phytophthora infestans, causal agent of the economically important pot No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20626828 Plant Biotechnol J. 2010 Aug;8(6):678-690. Portieles R, Ayra C, Gonzalez E, Gallo A, Rodriguez R, Chac³n O, L³pez Y, Rodriguez M, Castillo J, Pujol M, Enriquez G, Borroto C, Trujillo L, Thomma BP, Borr¡s-Hidalgo O. NmDef02, a novel antimicrobial gene isolated from Nicotiana megalosiphon confers high-level pathogen resistance under greenhouse and field conditions. DRAMP00762 GLPVCGETCFGGTCNTPGCTCDPWPVCTRN 30 Vaby D (Plant defensin) No entry found Not found Not found Viola abyssinica (Ethiopian highlands) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Bridge Not found PTM: Contains three disulfide bonds No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21434649 J Nat Prod. 2011 Apr 25;74(4):727-731. Yeshak MY, Burman R, Asres K, Göransson U. Cyclotides from an extreme habitat: characterization of cyclic peptides from Viola abyssinica of the Ethiopian highlands. DRAMP00763 GLPVCGETCAGGTCNTPGCSCSWPICTRN 29 Vaby A (Plant defensin) No entry found Not found Not found Viola abyssinica (Ethiopian highlands) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Bridge Not found PTM: Contains three disulfide bonds No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21434649 J Nat Prod. 2011 Apr 25;74(4):727-731. Yeshak MY, Burman R, Asres K, Göransson U. Cyclotides from an extreme habitat: characterization of cyclic peptides from Viola abyssinica of the Ethiopian highlands. DRAMP00767 GDACGETCFTGICFTAGCSCNPWPTCTRN 29 ChaC1 (Chassatide C1; Plant defensin) No entry found Belongs to the cyclotide family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found IC50=9.8 µM, HD50=51.9 µM.##Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells). Gram-negative bacterium: Escherichia coli (MIC>80 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50=51.9 µM against human type A red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys 4 and Cys18, Cys8 and Cys20, Cys13 and Cys26 . L [Ref.22467870] Cytotoxicity: HeLa cells (IC50=9.8 µM). Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00768 GIPCAESCVWIPPCTITALMGCSCKNNVCYNN 32 ChaC2 (Chassatide C2; Plant defensin) No entry found Belongs to the cyclotide family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found IC50=2.4 µM, HD50>25 µM.##Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells). Gram-negative bacterium: Escherichia coli (MIC>80 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50>25 µM against human type A red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys 4 and Cys21, Cys8 and Cys23, Cys13 and Cys28. L [Ref.22467870] Cytotoxicity: HeLa cells (IC50=2.4 µM). Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00769 GASCGETCFTGICFTAGCSCNPWPTCTRN 29 ChaC4 (Chassatide C4; Plant defensin) No entry found Belongs to the cyclotide family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found IC50=9.8 µM, HD50=51.9 µM.##Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells). Gram-negative bacterium: Escherichia coli (MIC>80 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50=51.9 µM against human type A red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys 4 and Cys18, Cys8 and Cys20, Cys13 and Cys26 . L [Ref.22467870] Cytotoxicity: HeLa cells (IC50=9.8 µM). Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00770 GEYCGESCYLIPCFTPGCYCVSRQCVNKN 29 ChaC10 (Chassatide C10; Plant defensin) No entry found Belongs to the cyclotide family Not found Chassalia chartacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found IC50=5.0 µM, HD50>25 µM.##Note: IC50 (concentration that gives a survival index of 50%) and HD50 (concentration that causes 50% lysis of red blood cells). Gram-negative bacterium: Escherichia coli (MIC>80 µM);##Gram-positive bacteria: Staphylococcus aureus (MIC>80 µM), Staphylococcus epidermidis (MIC>80 µM). [Ref.22467870] HD50>25 µM against human type A red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys 4 and Cys18, Cys8 and Cys20, Cys13 and Cys25 . L [Ref.22467870] Cytotoxicity: HeLa cells (IC50=5.0 µM). Not found 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GK, Lim WH, Nguyen PQ, Tam JP. Novel Cyclotides and Uncyclotides with Highly Shortened Precursors from Chassalia chartacea and Effects of Methionine Oxidation on Bioactivities. DRAMP00771 GIACGESCVFLGCFIPGCSCKSKVCYFN 28 Psyle A (Cyclotides; Plants) No entry found Belongs to the cyclotide family Not found Psychotria leptothyrsa Antimicrobial, Anti-HIV, Anti-cancer Not found Not found Not found Function: Cyclotide cytotoxicity on the human lymphoma cell line U-937 GTB (IC50=26 µM). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys I and CysIV, CysII and CysV, CysIII and CysVI . L [Ref.20575512] Cytotoxicity: the human lymphoma cell line U-937 GTB (IC50 = 26 µM). Not found 20575512 J Nat Prod. 2010 Jul 23;73(7):1207-1213. Gerlach SL, Burman R, Bohlin L, Mondal D, Göransson U. Isolation, characterization, and bioactivity of cyclotides from the Micronesian plant Psychotria leptothyrsa. DRAMP00772 KLCGETCFKFKCYTPGCSCSYPFCK 25 Psyle C (uncyclotides; Plants) No entry found Not found Not found Psychotria leptothyrsa Anti-cancer Not found Not found Not found Cyclotide cytotoxicity on the human lymphoma cell line U-937 GTB (IC50=3.5 µM). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20575512 J Nat Prod. 2010 Jul 23;73(7):1207-1213. Gerlach SL, Burman R, Bohlin L, Mondal D, Göransson U. Isolation, characterization, and bioactivity of cyclotides from the Micronesian plant Psychotria leptothyrsa. DRAMP00773 GVIPCGESCVFIPCISSVLGCSCKNKVCYRD 31 Psyle E (Cyclotides; Plants) No entry found Belongs to the cyclotide family Not found Psychotria leptothyrsa Anti-cancer Not found Not found Not found Function: Cyclotide cytotoxicity on the human lymphoma cell line U-937 GTB (IC50=0.76 µM). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys I and CysIV, CysII and CysV, CysIII and CysVI . L [Ref.20575512] Cytotoxicity: the human lymphoma cell line U-937 GTB (IC50=0.76 µM). Not found 20575512 J Nat Prod. 2010 Jul 23;73(7):1207-1213. Gerlach SL, Burman R, Bohlin L, Mondal D, Göransson U. Isolation, characterization, and bioactivity of cyclotides from the Micronesian plant Psychotria leptothyrsa. DRAMP00775 GIPCGESCVFIPCLTSAIDCSCKSKVCYRN 30 Mram 8 (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Cancer cell lines: BGC-823 (IC50=1.75±0.05 µM), MM96L (IC50=4.91±0.04 µM), HeLa (IC50=15.5±0.06 µM).##Non-cancer cell line: HFF-1 (IC50=3.19±0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00776 GSIPCEGSCVFIPCISAIIGCSCSNKVCYKN 31 Viphi G (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Note: Activity tested together with Viphi F. Cancer cell lines: BGC-823 (IC50=2.91±0.06 µM), MM96L (IC50=1.03±0.03 µM), HeLa (IC50=6.35±0.31 µM).##Non-Cancer cell line: HFF-1 (IC50=1.76±0.12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00777 GSIPCGESCVFIPCISAIIGCSCSSKVCYKN 31 Viphi F (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Note: Activity tested together with Viphi G. Cancer cell lines: BGC-823 (IC50=2.91±0.06 µM), MM96L (IC50=1.03±0.03 µM), HeLa (IC50=6.35±0.31 µM)##Non-Cancer cell line: HFF-1 (IC50=1.76±0.12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00778 GSIPCGESCVFIPCISAVIGCSCSNKVCYKN 31 Viphi E (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Note: Activity tested together with Viphi D. Cancer cell lines: MM96L (IC50=2.51±0.03 µM), HeLa (IC50=5.24±0.40 µM).##Non-Cancer cell line: HFF-1 (IC50=1.55±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00779 GIPCGESCVFIPCISSVIGCSCSSKVCYRN 30 Viphi D (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Note: Activity tested together with Viphi E. Cancer cell lines: MM96L (IC50=2.51±0.03 µM), HeLa (IC50=5.24±0.40 µM).##Non-Cancer cell line: HFF-1 (IC50=1.55±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00780 GSIPCGESCVFIPCISSVIGCACKSKVCYKN 31 Viphi A (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Cancer cell lines: BGC-823 (IC50=1.75±0.05 µM), MM96L (IC50=4.91±0.04 µM), HeLa (IC50=15.5±0.06 µM).##Non-cancer cell line: HFF-1 (IC50=3.19±0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00781 GLPVCGETCVGGTCNTPGCGCSWPVCTRN 29 Viba 17 (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Note: Activity tested together with Viba 15. Cancer cell lines: BGC-823 (IC50=1.32±0.15 µM), MM96L (IC50=3.10±0.06 µM), HeLa (IC50=10.21±0.43 µM).##Non-Cancer cell line: HFF-1 (IC50=2.38±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP00782 GLPVCGETCVGGTCNTPGCACSWPVCTRN 29 Viba 15 (Plants) No entry found Belongs to the cyclotide family Not found Viola philippica Anti-cancer Not found Not found Not found Function: The novel cyclotides show cytotoxic activity against several cancer cell lines. Activity tested together with Viba 17. Cancer cell lines: BGC-823 (IC50=1.32±0.15 µM), MM96L (IC50=3.10±0.06 µM), HeLa (IC50=10.21±0.43 µM).##Non-Cancer cell line: HFF-1 (IC50=2.38±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21723349 Peptides. 2011 Aug;32(8):1719-1723. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica. DRAMP18326 NGEWGYVVTKGAFQATTDVIANGWVSSLGGGYFGKP 36 Bovicin 255(Bacteriocin) No entry found Belongs to the class II bacteriocin Not found Streptococcus bovis Antimicrobial, Antibacterial, Anti-Gram+ Not found The prepeptide shares homology with the nonlantibiotic bacteriocins lactococcin A of Lactobacillus lactis (identities, 29%; positives, 48%) and thermophilin A of Streptococcus thermophilus (identities, 35%; positives, 42%). However, the homology with thermophilin A seems to reside primarily in the leader sequence (identities, 65%; positives, 73%), whereas homology with lactococcin A is distributed along the length of the prepeptide. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11157218 Appl Environ Microbiol. 2001 Feb;67(2):569-74. Whitford MF, McPherson MA, Forster RJ, Teather RM. Identification of bacteriocin-like inhibitors from rumen Streptococcus spp. and isolation and characterization of bovicin 255. DRAMP00784 GLPVCGETCVGGTCNTPGCSCSWPVCTRN 29 Varv peptide A (Varv A; Plant defensin) Q5USN7, P58446 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity against a variety of drug-resistant and drug-sensitive human tumor cell lines, and against primary chronic lymphocytic leukemia cells. Has weak cytotoxic activity against primary ovarian carcinoma cells or normal lymphocytes. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." Human tumor cell lines: RPMI-8226/s (IC50=3.24 µM), RPMI-8226/Dox40 (IC50=2.73 µM), RPMI-8226/LR-5 (IC50=3.19 µM), U-937GTB (IC50=6.35 µM), U-937Vcr (IC50=4.84 µM), ACHN (IC50=4.19 µM), CCRF-CEM (IC50=3.56 µM), CCRF-CEM/VM-1 (IC50=4.97 µM), NCI-H69 (IC50=4.88 µM), NCI-H69AR (IC50=4.89 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L [Ref.20580652] Cytotoxicity: U251(IC50 = 37.8μg/mL), MDA-MB-231(IC50>10μg/mL), A549(IC50>10μg/mL), DU145(IC50>10μg/mL), BEL-7402(IC50>10μg/mL).##[Ref.14987049] Cytotoxicity: U-937 GTB (lymphoma)(IC50 = 6µM) and RPMI-8226/s (myeloma)(IC50 = 3µM). Not found 20580652##14987049##12477048 "Peptides . 2010 Aug;31(8):1434-1440.##J Nat Prod. 2004 Feb;67(2):144-147.##Mol Cancer Ther . 2002 Apr;1(6):365-9." Jun Tang, Conan K Wang, Xulin Pan, He Yan, Guangzhi Zeng, Wenyan Xu, Wenjun He, Norelle L Daly, David J Craik, Ninghua Tan. ##Erika Svangård, Ulf Göransson, Zozan Hocaoglu, Joachim Gullbo, Rolf Larsson, Per Claeson, Lars Bohlin. ##Petra Lindholm, Ulf Göransson, Senia Johansson, Per Claeson, Joachim Gullbo, Rolf Larsson, Lars Bohlin, Anders Backlund Isolation and characterization of cytotoxic cyclotides from Viola tricolor. ##Cytotoxic cyclotides from Viola tricolor.##Cyclotides: a novel type of cytotoxic agents. DRAMP00785 GLPVCGETCFGGTCNTPGCSCDPWPMCSRN 30 Varv peptide B (Varv B; Plant defensin) P58447 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No Cytotoxicity information found Not found 10075760 J Nat Prod. 1999 Feb;62(2):283-286. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. DRAMP00786 GVPICGETCVGGTCNTPGCSCSWPVCTRN 29 Varv peptide C (Varv C; Plant defensin) P58448 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10075760 J Nat Prod. 1999 Feb;62(2):283-286. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. DRAMP00787 GLPICGETCVGGSCNTPGCSCSWPVCTRN 29 Varv peptide D (Varv D; Plant defensin) P58449 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10075760 J Nat Prod. 1999 Feb;62(2):283-286. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. DRAMP00788 GLPICGETCVGGTCNTPGCSCSWPVCTRN 29 Varv peptide E (Varv E; Plant defensin) P83835 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer, Antiviral Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity against human lymphoma U-937 GTB and human myeloma RPMI-8226/s cell lines. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." [Ref.14987049]Human cancer cell lines: U-937 GTB (lymphoma) (IC50=4 µM), RPMI-8226/s (myeloma) (IC50=4 µM).##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=350 nM). [Ref.20580652] HD50=6.96µM against human type O red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L [Ref.20580652] Cytotoxicity: U251(IC50=38.84μg/mL), MDA-MB-231(IC50>10μg/mL), A549(IC50>10μg/mL), DU145(IC50>10μg/mL), BEL-7402(IC50>10μg/mL).##[Ref.14987049] Cytotoxicity: U-937 GTB (lymphoma)(IC50 = 4 µM) and RPMI-8226/s (myeloma)(IC50 = 4 µM).##[Ref.18008336]CEM-SS cells:IC50=3980 nM. Not found 18008336##10075760##14987049##20580652 Biopolymers. 2008;90(1):51-60.##J Nat Prod. 1999 Feb;62(2):283-286.##J Nat Prod. 2004 Feb;67(2):144-147.##Peptides. 2010 Aug;31(8):1434-40. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. ##Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P.Svang.##Svangård E, Göransson U, Hocaoglu Z, Gullbo J, Larsson R, Claeson P, Bohlin L.##Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Cyclotides as natural anti-HIV agents.##Seven novel macrocyclic polypeptides from Viola arvensis.##Cytotoxic cyclotides from Viola tricolor.##Isolation and characterization of cytotoxic cyclotides from Viola tricolor. DRAMP00789 GVPICGETCTLGTCYTAGCSCSWPVCTRN 29 Varv peptide F (Varv F; Plant defensin) P58451 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Combine helix and strand structure Not found 2K7G resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity against a variety of drug-resistant and drug-sensitive human tumor cell lines. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." Human tumor cell lines: RPMI-8226/s (IC50=5.90 µM), RPMI-8226/Dox40 (IC50=3.14 µM), RPMI-8226/LR-5 (IC50=6.31 µM), U-937GTB (IC50=7.07 µM), U-937Vcr (IC50=7.45 µM), ACHN (IC50=2.63 µM), CCRF-CEM (IC50=7.13 µM), CCRF-CEM/VM-1 (IC50=7.15 µM), NCI-H69 (IC50=7.49 µM), NCI-H69AR (IC50=7.12 µM). [Ref.20580652] HD50=33.04µM against human type O red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L [Ref.20580652] Cytotoxicity: U251(IC50=44.49μg/mL), MDA-MB-231(IC50>10μg/mL), A549(IC50>10μg/mL), DU145(IC50>10μg/mL), BEL-7402(IC50>10μg/mL). Not found 10075760##12477048##19211551 J Nat Prod. 1999 Feb;62(2):283-286.##Mol Cancer Ther. 2002 Apr;1(6):365-369.##J Biol Chem. 2009 Apr 17;284(16):10672-83. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P.##Lindholm P, Göransson , Johansson S, Claeson P, Gullbo J, Larsson R, Bohlin L, Backlund A.##Wang CK, Hu SH, Martin JL, Sjögren T, Hajdu J, Bohlin L, Claeson P, Göransson U, Rosengren KJ, Tang J, Tan NH, Craik DJ. Seven novel macrocyclic polypeptides from Viola arvensis.##Cyclotides: a novel type of cytotoxic agents.##Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold. DRAMP00790 GVPVCGETCFGGTCNTPGCSCDPWPVCSRN 30 Varv peptide G (Varv G; Plant defensin) P58452 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10075760 J Nat Prod. 1999 Feb;62(2):283-286. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. DRAMP00791 GLPVCGETCFGGTCNTPGCSCETWPVCSRN 30 Varv peptide H (Varv H; Plant defensin) P58453 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Anti-cancer Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref.20580652] HD50=7.52µM against human type O red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L [Ref.20580652] Cytotoxicity: U251(IC50=44.70μg/mL), MDA-MB-231(IC50>10μg/mL), A549(IC50>10μg/mL), DU145(IC50>10μg/mL), BEL-7402(IC50>10μg/mL). Not found 10075760 J Nat Prod. 1999 Feb;62(2):283-286. Göransson U, Luijendijk T, Johansson S, Bohlin L, Claeson P. Seven novel macrocyclic polypeptides from Viola arvensis. DRAMP00792 GLPVCGETCTLGKCYTAGCSCSWPVCYRN 29 Vodo peptide N (Plant defensin) P83838 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Not found Protein level Not found Forms a head-to-tail cyclic backbone and that six cysteine residues are involved in three disulphide bonds. 2AKS "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12946412 Phytochemistry. 2003 Sep;64(1):135-142. Svang¥rd E, Göransson , Smith D, Verma C, Backlund A, Bohlin L, Claeson P. Primary and 3-D modelled structures of two cyclotides from Viola odorata. DRAMP00793 GAPICGESCFTGKCYTVQCSCSWPVCTRN 29 Vodo peptide M (Plant defensin) P83839 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Not found Protein level Not found Forms a head-to-tail cyclic backbone and that six cysteine residues are involved in three disulphide bonds. 1ZLO "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12946412 Phytochemistry. 2003 Sep;64(1):135-142. Svang¥rd E, Göransson , Smith D, Verma C, Backlund A, Bohlin L, Claeson P. Primary and 3-D modelled structures of two cyclotides from Viola odorata. DRAMP18325 MAADIISTIGDLVKLIINTVKKFQK 25 delta-lysin I (Bacteriocin) No entry found Not found Not found Staphylococcus warneri RK Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Warnericin RK and delta-lysin I displayed the same antibacterial spectrum, which is almost restricted to the Legionella genus. Also, both peptides have a hemolytic activity. [Ref.18339450]Gram-positive bacteria: Bacillus megaterium F04(+), Bacillus subtilis(–), Enterococcus faecalis V583(–), Listeria monocytogenes EGDe(–), Micrococcus luteus(–), Pediococcus acidilactici 583(–), Staphylococcus aureus 971(–), Staphylococcus chromogenes(–), Staphylococcus cohnii 898(–), Staphylococcus epidermidis 567(-), Staphylococcus haemolyticus 694(-), Staphylococcus hominis 373(-), Staphylococcus lentus 982(-), Staphylococcus lugdunensis 967(-), Staphylococcus saprophyticus 715(-), Staphylococcus warneri 447(-), Staphylococcus warneri RK(-);## Gram-negative bacteria:  Enterobacter cloacae D03(-), Escherichia coli MG1655(-), Hafnia alvei(-), Klebsiella pneumoniae 0502083(-), Legionella bozemanii ATCC 33217(+),  Legionella dumofii ATCC 33279(+), Legionella feeleii ATCC 35072(+), Legionella like bacteria (LLAP10)(+), Legionella longbeachae ATCC 33484(+), Legionella micdadei ATCC 33218(+), Legionella oakridgensis ATCC 33761(+), Legionella pneumophila Corby (sg1)(+), Legionella pneumophila Lens (sg1)(+), Legionella pneumophila Paris (sg1)(+), Legionella pneumophila ATCC 33155 (sg3)(+), Legionella pneumophila ATCC 33216 (sg5)(+), Legionella pneumophila ATCC 33215 (sg6)(+), Proteus mirabilis ATCC 35659(-), Pseudomonas aeruginosa DSMZ1128(-), Pseudomonas aeruginosa 910704(-), Salmonella typhimurium(-) [Ref.18339450]10% hemolytic activity at 1.56 μM, 40% hemolytic activity at 6.25 μM, 62% hemolytic activity at 25 μM, 80% hemolytic activity at 50 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18339450 Peptides. 2008 Jun;29(6):978-84. Verdon J, Berjeaud JM, Lacombe C, H Characterization of anti-Legionella activity of warnericin RK and delta-lysin I from Staphylococcus warneri. DRAMP00796 GEFLKCGESCVQGECYTPGCSCDWPICKKN 30 Cliotide T2 (cT2; Plant defensin) No entry found Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found Function: Cliotide T2 shows stronger antimicrobial activity against the Gram-negative bacteria than the Gram-positive bacteria. Cliotide T2 was relatively nonhemolytic (HD50>100 µM) . [Ref.21596752]Gram-positive bacteria: Staphylococcus aureus ATCC12600, Enterococcus faecalis ATCC 47077 (less active);##Gram-negative bacteria: Escherichia coli ATCC 700926 (MIC>100 µM), Pseudomonas aeruginosa ATCC 39018 (MIC>100 µM), Klebsiella pneumonia ATCC 13883 (MIC>100 µM). [Ref:21596752] HD50>100 µM against human type A erythrocytes Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys I and CysIV, CysII and CysV, CysIII and CysVI. L [Ref.21596752] Cytotoxicity: HeLa Cells (IC50=8.0 µM). Not found 21596752 J Biol Chem. 2011 Jul 8;286(27):24275-24287. Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, Hardjojo A, Tam JP. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. DRAMP00797 GLPTCGETCTLGTCYVPDCSCSWPICMKN 29 Cliotide T3 (cT3; Plant defensin) No entry found Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found 2LAM "Function: Cliotide T3 shows stronger antimicrobial activity against the Gram-negative bacteria than the Gram-positive bacteria. It also has hemolytic activity against human type A erythrocytes (HD50=13.1 µM) and cytotoxicity against HeLa Cells (IC50=2.0 µM). [Note: HD50 refers to the peptide concentration that causes 50% lysis of red blood cells; IC50 refers to the peptide concentration that causes 50% death of HeLa cells]. " [Ref.21596752]Gram-positive bacteria: Staphylococcus aureus ATCC12600, Enterococcus faecalis ATCC 47077 (less active);##Gram-negative bacteria: Escherichia coli ATCC 700926 (MIC>100 µM), Pseudomonas aeruginosa ATCC 39018 (MIC>100 µM), Klebsiella pneumonia ATCC 13883 (MIC>100 µM). [Ref:21596752] HD50=13.1 µM against human type A erythrocytes Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys I and CysIV, CysII and CysV, CysIII and CysVI. L [Ref.21596752] Cytotoxicity: HeLa Cells (IC50=2.0 µM). Not found 21596752 J Biol Chem. 2011 Jul 8;286(27):24275-24287. Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, Hardjojo A, Tam JP. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. DRAMP00799 GVIPCGESCVFIPCISAAIGCSCKNKVCYRN 31 Cycloviolin-A (Plant defensin) P84637 Belongs to the cyclotide family Not found Leonia cymosa (Sacha uba) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has anti-HIV activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21;9-23;14-28." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys5 and Cys21, Cys9 and Cys23,Cys14 and Cys28. L [Ref.18008336]CEM-SS cells:IC50=560 nM. Not found 10813905##18008336 J Org Chem. 2000 Jan 14;65(1):124-128.##Biopolymers. 2008;90(1):51-60. Hallock YF, Sowder RC 2nd, Pannell LK, Hughes CB, Johnson DG, Gulakowski R, Cardellina JH 2nd, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa.##Cyclotides as natural anti-HIV agents. DRAMP00800 GTACGESCYVLPCFTVGCTCTSSQCFKN 28 Cycloviolin-B (Plant defensin) P84638 Belongs to the cyclotide family Not found Leonia cymosa (Sacha uba) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has anti-HIV activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-18;8-20;13-25." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys18, Cys8 and Cys20,Cys13 and Cys25. L [Ref.18008336]CEM-SS cells:IC50=560 nM. Not found 10813905##18008336 J Org Chem. 2000 Jan 14;65(1):124-128.##Biopolymers. 2008;90(1):51-60. Hallock YF, Sowder RC 2nd, Pannell LK, Hughes CB, Johnson DG, Gulakowski R, Cardellina JH 2nd, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa.##Cyclotides as natural anti-HIV agents. DRAMP00801 GIPCGESCVFIPCLTTVAGCSCKNKVCYRN 30 Cycloviolin-C (Plant defensin) P84639 Belongs to the cyclotide family Not found Leonia cymosa (Sacha uba) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has anti-HIV activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20;8-22;13-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=560 nM. Not found 10813905##18008336 J Org Chem. 2000 Jan 14;65(1):124-128.##Biopolymers. 2008;90(1):51-60. Hallock YF, Sowder RC 2nd, Pannell LK, Hughes CB, Johnson DG, Gulakowski R, Cardellina JH 2nd, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa.##Cyclotides as natural anti-HIV agents. DRAMP00802 GFPCGESCVFIPCISAAIGCSCKNKVCYRN 30 Cycloviolin-D (Plant defensin) P84640 Belongs to the cyclotide family Not found Leonia cymosa (Sacha uba) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has anti-HIV activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=130 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=560 nM. Not found 10813905##18008336 J Org Chem. 2000 Jan 14;65(1):124-128.##Biopolymers. 2008;90(1):51-60. Hallock YF, Sowder RC 2nd, Pannell LK, Hughes CB, Johnson DG, Gulakowski R, Cardellina JH 2nd, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa.##Cyclotides as natural anti-HIV agents. DRAMP00803 GDPTFCGETCRVIPVCTYSAALGCTCDDRSDGLCKRN 37 Palicourein (Cyclotides; Plants) P84645 Belongs to the cyclotide family Not found Palicourea condensata (Cappel) Antimicrobial, Antiviral Protein level Combine helix and strand structure Palicourein has an atypical size and composition within one of the surface-exposed loops. 1R1F resolved by NMR. "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. In vitro activity: Palicourein inhibits the cytopathic effects of HIV-1RF infection of CEM-SS cells with an EC50 value of 0.1 µM and an IC50 value of 1.5 µM. PTM: This is a cyclic peptide which may contain three disulfide bonds 6-24; 10-26; 16-34." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=100 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys1 and Cys19; Cys5 and Cys21; Cys11 and Cys28;hydrogen bonds between the oxygen atoms of the Glu3 carboxyl group and the backbone amides of residues Thr12, Thr13, and Ser14, and the side chain of Ser14. L [Ref.11430013] Cytotoxicity: human T-lymphoblastoid cell line (CEM-SS)(EC50=0.10 Μm, IC50=1.5 μM) . ##[Ref.18008336]CEM-SS cells:IC50=1500 nM. Not found 11430013##14725768##18008336 J Nat Prod. 2001 Feb;64(2):249-250.##Structure. 2004 Jan;12(1):85-94.##Biopolymers. 2008;90(1):51-60. Bokesch HR, Pannell LK, Cochran PK, Sowder RC 2nd, McKee TC, Boyd MR.##Barry DG, Daly NL, Bokesch HR, Gustafson KR, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. A novel anti-HIV macrocyclic peptide from Palicourea condensata.##Solution structure of the cyclotide palicourein: implications for the development of a pharmaceutical framework.##Cyclotides as natural anti-HIV agents. DRAMP00804 GIPCAESCVYIPCTVTALLGCSCSNRVCYN 30 Cycloviolacin-O1 (Plant defensin) P82230 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Combine helix and strand structure Not found 1NBJ resolved by NMR. "Function: Probably participates in a plant defense mechanism. It shows haemolytic activity. PTM: This is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L [Ref.20575512] Cytotoxicity on the human lymphoma cell line U-937 GTB(IC50 around 1 µM). Not found 16872274##10600388##12482868 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##J Biol Chem. 2003 Mar 7;278(10):8606-8616. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. DRAMP00805 GIPCGESCVWIPCISSAIGCSCKSKVCYRN 30 Cycloviolacin-O2 (Plant defensin) P58434, P85526 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) & Viola odorata (Sweet violet) Insecticidal Protein level Combine helix and strand structure Not found 2KCG, 2KNM, 2KNN resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has strong cytotoxic activity against a variety of drug-resistant and drug-sensitive human tumor cell lines, and against primary chronic lymphocytic leukemia and ovarian carcinoma cells. Has weaker cytotoxic activity against normal lymphocytes. Has hemolytic activity. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." [Ref.16872274]Human tumor cell lines: RPMI-8226/s (IC50=0.12 µM), RPMI-8226/Dox40 (IC50=0.12 µM), RPMI-8226/LR-5 (IC50=0.12 µM), U-937GTB (IC50=0.26 µM), U-937Vcr (IC50=0.20 µM), ACHN (IC50=0.22 µM), CCRF-CEM (IC50=0.11 µM), CCRF-CEM/VM-1 (IC50=0.14 µM), NCI-H69 (IC50=0.12 µM), NCI-H69AR (IC50=0.26 µM). [Ref:16872274] It has 35% hemolytic activity at 1.0 μM and 60% hemolytic activity at 1.5 μM against human type A red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L [Ref.20580652] Cytotoxicity: U251(IC50=17.05μg/mL), MDA-MB-231(IC50=4.81μg/mL), A549(IC50=5.99μg/mL), DU145(IC50=5.08μg/mL), BEL-7402(IC5=6.07μg/mL). Not found 16872274##10600388##16872274 "Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Biochem J . 2006 Nov 15;400(1):1-12. " Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##David C Ireland 1, Michelle L Colgrave, David J Craik A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability DRAMP00806 GIPCGESCVWIPCLTSAIGCSCKSKVCYRN 30 Cycloviolacin-O3 (Plant defensin) P58435 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00807 GIPCGESCVWIPCISSAIGCSCKNKVCYRN 30 Cycloviolacin-O4 (Plant defensin) P58436 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00808 GTPCGESCVWIPCISSAVGCSCKNKVCYKN 30 Cycloviolacin-O5 (Plant defensin) P58437 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00809 GTLPCGESCVWIPCISAVGCSCKSKVCYKN 30 Cycloviolacin-O6 (Plant defensin) P58438 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00810 SIPCGESCVWIPCTITALAGCKCKSKVCYN 30 Cycloviolacin-O7 (Plant defensin) P58439 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00811 GTLPCESCVWIPCISSVVGCSCKSKVCYKN 30 Cycloviolacin-O8 (Cyclotide c1; Plant defensin) P58440, Q5USN9 Belongs to the cyclotide family Voc1 Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L [Ref.29734037] Cytotoxicity against three cancer cell lines: MDA-MB-231 breast (IC50=1.15 μM), PC-3 prostate (IC50=1.05 μM), and OVCAR-3 ovarian (IC50=0.80 μM). Cytotoxicity against non-cancerous human dermal fibroblast cells was determined to be ∼3× less (3.13 μM) than cancer cell lines Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00812 GIPCGESCVWIPCLTSAVGCSCKSKVCYRN 30 Cycloviolacin-O9 (Vbc5; Plant defensin) P58441, B1NRR2 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) & Viola biflora (Yellow wood violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388##18191970 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Phytochemistry. 2008 Feb;69(4):939-952. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00813 GIPCGESCVYIPCLTSAVGCSCKSKVCYRN 30 Cycloviolacin-O10 (Plant defensin) P58442 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00814 GTLPCGESCVWIPCISAVVGCSCKSKVCYKN 31 Cycloviolacin-O11 (Cyclotide c2; Plant defensin) P58443, Q5USP0 Belongs to the cyclotide family Voc2 Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP18324 MQFITDLIKKAVDFFKGLFGNK 22 Warnericin RK (Bacteriocin) No entry found Not found Not found Staphylococcus warneri RK Antimicrobial, Antibacterial, Anti-Gram- Alpha Helix Not found Warnericin RK acts as a specific anti-Legionella AMP by permeabilizing the bacterial membrane. Gram-negative(Narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18339450##19804724 Peptides. 2008 Jun;29(6):978-84.##Biophys J. 2009 Oct 7;97(7):1933-40. Verdon J, Berjeaud JM, Lacombe C, H Characterization of anti-Legionella activity of warnericin RK and delta-lysin I from Staphylococcus warneri.##Detergent-like activity and alpha-helical structure of warnericin RK, an anti-Legionella peptide. DRAMP00816 GIPCGESCVWIPCISAAIGCSCKSKVCYRN 30 Cycloviolacin-O13 (Cyclotide c3; Plant defensin) Q5USN8 Belongs to the cyclotide family Voc3 Viola odorata (Sweet violet) Antiviral,Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=320 nM). [Ref:16872274] It has 50% hemolytic activity at 1.0 μM and 75% hemolytic activity at 1.5 μM against human type A red blood cells Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=6400 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents. DRAMP00817 GSIPACGESCFKGKCYTPGCSCSKYPLCAKN 31 Cycloviolacin-O14 (Plant defensin) P85177 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Antiviral,Insecticidal Protein level Combine helix and strand structure Cycloviolacin O14 is shown to contain the CCK motif. 2GJ0 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 6-20; 10-22; 15-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=440 nM). [Ref:16872274] It has 3% hemolytic activity at 1.0 μM and 13% hemolytic activity at 1.5 μM against human type A red blood cells Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=4800 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents. DRAMP00818 GLVPCGETCFTGKCYTPGCSCSYPICKKN 29 Cycloviolacin-O15 (Plant defensin) P85178 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database [Ref:16872274] It has 6% hemolytic activity at 1.0 μM and 26% hemolytic activity at 1.5 μM against human type A red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00819 GLPCGETTCFTGKCYTPGCSCSYPICKKIN 30 Cycloviolacin-O16 (Plant defensin) P85179 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-18; 8-20; 13-25." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys18; Cys8 and Cys20; Cys13 and Cys25. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00820 GIPCGESCVWIPGISAAIGCSCKNKVCYRN 30 Cycloviolacin-O17 (Plant defensin) P85180 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00821 GIPCGESCVYIIPCTVTALAQCKCKSKVCYN 31 Cycloviolacin-O18 (Plant defensin) P85181 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00822 GTLPCGESCVWIPCISSVVGCSCKSKVCYKD 31 Cycloviolacin-O19 (Plant defensin) P85182 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00823 GIPCGESCVWIPCLTSAIGCSCKSKVCYKD 30 Cycloviolacin-O20 (Plant defensin) P85183 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00824 GLPVCGETCVTGSCYTPGCTCSWPVCTRN 29 Cycloviolacin-O21 (Plant defensin) P85184 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00825 GLPICGETCVGGTCNTPGCTCSWPVCTRN 29 Cycloviolacin-O22 (Plant defensin) P85185 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP00826 GLPTCGETCFGGTCNTPGCTCDSSWPICTHN 31 Cycloviolacin-O23 (Plant defensin) P85186 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. DRAMP18197 INNWVRVPPCDQVCSRSNPEKDECCRAHGHAFHAHCNGGMNCYRR 45 Diapausin-1 No entry found Belongs to the diapausin family of peptides Not found hemolymph, tobacco hornworm, Manduca sexta Antimicrobial, Antifungal Not found Not found Function: Active against FUNGI such as S. cerevisiae (IC50 12 uM) but not bacteria. S. cerevisiae(IC50 12 uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26976231 Dev Comp Immunol.61:258-68(2016) Al Souhail Q, Hiromasa Y, Rahnamaeian M, Giraldo MC, Takahashi D, Valent B, Vilcinskas A, Kanost MR. Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta. DRAMP18196 GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1A P40843 Belongs to the frog skin active peptide (FSAP) family Not found Pelophylax esculentus (Edible frog) (Rana esculenta) Antimicrobial, Antibacterial, Antibiotic Not found Not found 2N6M Function: Antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. No MICs found in DRAMP database [Swiss_Prot Entry P40843]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J. Biol. Chem. 269:11956-11961(1994) Simmaco M., Mignogna G., Barra D., Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta.Molecular cloning of cDNAs encoding esculentin and brevinins andisolation of new active peptides. DRAMP00829 GIPCGESCVYIPCLTSAIGCSCKSKVCYRN 30 Cycloviolacin-H1 (Plant defensin) P58433 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 10600388 J Mol Biol. 1999 Dec 17;294(5):1327-1336. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00830 SAIACGESCVYIPCFIPGCSCRNRVCYLN 29 Cycloviolacin-H2 (Plant defensin) P85233 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." Virus: HIV. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 10600388 J Mol Biol. 1999 Dec 17;294(5):1327-1336. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00831 GLPVCGETCFGGTCNTPGCICDPWPVCTRN 30 Cycloviolacin-H3 (Plant defensin) P85232 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." Virus: HIV. No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 10600388 J Mol Biol. 1999 Dec 17;294(5):1327-1336. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00832 GIPCAESCVWIPCTVTALLGCSCSNNVCYN 30 Cycloviolacin-H4 (Plant defensin) P85234 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database [Ref.16441062] HD50=5.5 µM against human type A red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 10600388 J Mol Biol. 1999 Dec 17;294(5):1327-1336. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP00833 GGTIFDCGETCFLGTCYTPGCSCGNYGFCYGTN 33 Cycloviolacin-Y1 (Plants) No entry found Belongs to the cyclotide family Not found Viola yedoensis (Chinese herb) Antimicrobial, Antiviral Not found Bridge Not found Function: Has anti-HIV activity. PTM: Contains three disulfide bonds. [Ref.18081258] Anti-HIV activity:EC50=1.2μM, IC50>4.5μM. ##NOTE:EC50 refers to the values for HIV-infected cell cultures, IC50 refers to the values for uninfected cell cultures.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=1210 nM). [Ref.18081258] It has hemolytic activity. Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys7 and Cys21; Cys11 and Cys23; Cys16 and Cys29. L [Ref.18008336]CEM-SS cells:IC50>4470 nM. Not found 18081258##18008336 J Nat Prod. 2008 Jan;71(1):47-52.##Biopolymers. 2008;90(1):51-60. Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ.##David C Ireland, Conan K L Wang, Jennifer A Wilson, Kirk R Gustafson, David J Craik Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis.##Cyclotides as natural anti-HIV agents DRAMP00834 GGTIFDCGESCFLGTCYTAGCSCGNWGLCYGTN 33 Cycloviolacin-Y2 (Plants) No entry found Belongs to the cyclotide family Not found Viola yedoensis (Chinese herb) Antimicrobial, Antiviral Not found Bridge Not found Function: Has anti-HIV activity. PTM: Contains three disulfide bonds. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys7 and Cys21; Cys11 and Cys23; Cys16 and Cys29. L No cytotoxicity information found Not found 18081258 J Nat Prod. 2008 Jan;71(1):47-52. Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ. Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. DRAMP00835 GGTIFDCGETCFLGTCYTAGCSCGNWGLCYGTN 33 Cycloviolacin-Y3 (Plants) No entry found Belongs to the cyclotide family Not found Viola yedoensis (Chinese herb) Antimicrobial, Antiviral Not found Bridge Not found Function: Has anti-HIV activity. PTM: Contains three disulfide bonds. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys7 and Cys21; Cys11 and Cys23; Cys16 and Cys29. L No cytotoxicity information found Not found 18081258 J Nat Prod. 2008 Jan;71(1):47-52. Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ. Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. DRAMP00836 GVPCGESCVFIPCITGVIGCSCSSNVCYLN 30 Cycloviolacin-Y4 (Plants) No entry found Belongs to the cyclotide family Not found Viola yedoensis (Chinese herb) Antimicrobial, Antiviral Not found Bridge Not found Function: Has anti-HIV activity. Cycloviolacins Y4 is more hemolytic than cycloviolacin Y1. PTM: Contains three disulfide bonds. [Ref.18618891]Effects: H. contortus( IC50=2.01μM, IC99=6.73μM) and T. colubriformis(IC50=2.27μM, IC99=5.26μM).##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=120 nM). [Ref:18081258] HD50=9.3 μM against human type A red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=1720 nM. Not found 18081258##18008336##18618891 J Nat Prod. 2008 Jan;71(1):47-52.##Biopolymers. 2008;90(1):51-60.##Chembiochem. 2008 Aug 11;9(12):1939-45. doi: 10.1002/cbic.200800174. Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ.##David C Ireland, Conan K L Wang, Jennifer A Wilson, Kirk R Gustafson, David J Craik##Michelle L Colgrave, Andrew C Kotze, David C Ireland, Conan K Wang, David J Craik Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis.##Cyclotides as natural anti-HIV agents##The anthelmintic activity of the cyclotides: natural variants with enhanced activity DRAMP00837 GIPCAESCVWIPCTVTALVGCSCSDKVCYN 30 Cycloviolacin-Y5 (Plants) No entry found Belongs to the cyclotide family Not found Viola yedoensis (Chinese herb) Antimicrobial, Antiviral Not found Bridge Not found "Function: Has anti-HIV activity. Cycloviolacin Y5 is the most hydrophobic of the cyclotides from V. yedoensis, and is more hemolytic than cycloviolacin Y1. PTM: Contains three disulfide bonds. " [Ref.18618891]Effects: H. contortus( IC50=2.28μM, IC99=22.24μM) and T. colubriformis(IC50=2.40μM, IC99=10.97μM).##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=40 nM). [Ref:18081258] HD50=8.7 μM against human type A red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L [Ref.18008336]CEM-SS cells:IC50=1760 nM. Not found 18081258##18008336##18618891 J Nat Prod. 2008 Jan;71(1):47-52.##Biopolymers. 2008;90(1):51-60.##Chembiochem. 2008 Aug 11;9(12):1939-45. doi: 10.1002/cbic.200800174. Wang CK, Colgrave ML, Gustafson KR, Ireland DC, Goransson U, Craik DJ.##David C Ireland, Conan K L Wang, Jennifer A Wilson, Kirk R Gustafson, David J Craik##Michelle L Colgrave, Andrew C Kotze, David C Ireland, Conan K Wang, David J Craik Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis.##Cyclotides as natural anti-HIV agents##The anthelmintic activity of the cyclotides: natural variants with enhanced activity DRAMP00838 GIGCGESCVWIPCVSAAIGCSCSNKICYRN 30 Cyclotide phyb-A (Plant defensin) B3EWH5 Belongs to the cyclotide family Not found Petunia hybrida (Petunia) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism (By similarity). Tissue specificity: Expressed in midvein, lamina and periphery of leaves (at protein level). Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-2; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found PubMed ID is not available J. Biol. Chem. 2012;287:27033-27046. Poth A.G, Mylne J.S, Grassl J, Lyons R.E, Millar A.H, Colgrave M.L, Craik D.J. Cyclotides associate with leaf vasculature and are the products of a novel precursor in Petunia (Solanaceae). DRAMP00839 GVIPCGESCVFIPCISTVIGCSCKNKVCYRN 31 Cyclotide cter-A (Plant defensin) P86841 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21; 9-23; 14-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00840 GVPCAESCVWIPCTVTALLGCSCKDKVCYLN 31 Cyclotide cter-B (Plant defensin) P86842 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00841 GVPCAESCVWIPCTVTALLGCSCKDKVCYLD 31 Cyclotide cter-C (Plant defensin) P86843 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00842 GIPCAESCVWIPCTVTALLGCSCKDKVCYLN 31 Cyclotide cter-D (Plant defensin) P86844 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00843 GIPCAESCVWIPCTVTALLGCSCKDKVCYLD 31 Cyclotide cter-E (Plant defensin) P86845 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00844 GIPCGESCVFIPCISSVVGCSCKSKVCYLD 30 Cyclotide cter-F (Plant defensin) P86846 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00845 GLPCGESCVFIPCITTVVGCSCKNKVCYNN 30 Cyclotide cter-G (Plant defensin) P86847 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00846 GLPCGESCVFIPCITTVVGCSCKNKVCYND 30 Cyclotide cter-H (Plant defensin) P86848 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00847 GTVPCGESCVFIPCITGIAGCSCKNKVCYIN 31 Cyclotide cter-I (Plant defensin) P86849 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21; 9-23; 14-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00848 GTVPCGESCVFIPCITGIAGCSCKNKVCYID 31 Cyclotide cter-J (Plant defensin) P86850 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21; 9-23; 14-28. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00849 HEPCGESCVFIPCITTVVGCSCKNKVCYN 29 Cyclotide cter-K (Plant defensin) P86851 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00850 HEPCGESCVFIPCITTVVGCSCKNKVCYD 29 Cyclotide cter-L (Plant defensin) P86852 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00851 GIPCGESCVFIPCITGIAGCSCKSKVCYRN 30 Cyclotide cter-O (Plant defensin) P86901 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21593408 Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10127-32. Poth AG, Colgrave ML, Lyons RE, Daly NL, Craik DJ. Discovery of an unusual biosynthetic origin for circular proteins in legumes. DRAMP18323 KKKSGVIPTVSHDCHMNSFQFVFTCCS 27 Nukacin ISK-1(Bacteriocin) Q9KWM4 Belongs to the lantibiotics family (Class I bacteriocin) nukA Staphylococcus warneri ISK-1 Antimicrobial, Antibacterial, Anti-Gram+ Not found There are one didehydrobutyrine (Dhb): T24; two lanthionines: S11-C25, S18-C26; and one Beta-methyllanthionine: T9-C14. Nukacin 3299, produced by Staphylococcus simulans 3299, is identical to nukacin ISK-1.Partial known sequence of Warnericin RB4 matches nukacin ISK-1, suggesting a possible identical peptide also produced by Staphylococcus warneri RB4. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 11193411##20627619 Biosci Biotechnol Biochem. 2000 Nov;64(11):2420-8.##Vet Microbiol. 2010 Nov 20;146(1-2):124-31. Sashihara T, Kimura H, Higuchi T, Adachi A, Matsusaki H, Sonomoto K, Ishizaki A.##Ceotto H, Holo H, da Costa KF, Nascimento Jdos S, Salehian Z, Nes IF, Bastos Mdo C. A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: cloning of the structural gene and identification of the structure.##Nukacin 3299, a lantibiotic produced by Staphylococcus simulans 3299 identical to nukacin ISK-1. DRAMP00853 GIPCGESCVFIPCISTVIGCSCKNKVCYRN 30 Cyclotide cter-Q (Plant defensin) P86904 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00854 GIPCGESCVFIPCTVTALLGCSCKDKVCYKN 31 Cyclotide cter-R (Plant defensin) P86903 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00855 GSAFCGETCVLGTCYTPDCSCTALVCLKN 29 Cyclotide cter-N (Plant defensin) P86900 Belongs to the cyclotide family Not found Clitoria ternatea (Butterfly pea) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21194241 ACS Chem Biol. 2011 Apr 15;6(4):345-355. Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, Anderson MA, Craik DJ. Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. DRAMP00857 GLPVCGETCFGGTCNTPGCSCTWPICTRD 29 Kalata-B2 (Plant defensin) P58454 Belongs to the cyclotide family OAK4 Oldenlandia affinis Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Inhibitory effect on the growth and development of Helicoverpa armigera larvae suggests a role for the cyclotides in plant defense. Has hemolytic activity. PTM: Kalata-B2 is a cyclic peptide which contains three disulfide bonds 5-19; 9-21; 14-26." [Ref.17534989]Insects: Helicoverpa armigera [Ref.20564013] HD50=3.3±1.9 μM against Human red blood cells . Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26. L No cytotoxicity information found Not found 10600388##15654741##17534989##20564013 "J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Biochemistry. 2005 Jan 25;44(3):851-860.##Chembiochem. 2007 Jun 18;8(9):1001-1011.##Biopolymers . 2010;94(5):647-58." Craik DJ, Daly NL, Bond T, Waine C.##Jennings CV, Rosengren KJ, Daly NL, Plan M, Stevens J, Scanlon MJ, Waine C, Norman DG, Anderson MA, Craik DJ.##Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.##Manuel R Plan, K Johan Rosengren, Lillian Sando, Norelle L Daly, David J Craik Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do Möbius strips exist in nature?##The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.##Structural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinis DRAMP00858 GLPTCGETCFGGTCNTPGCTCDPWPICTRD 30 Kalata-B3 (Plant defensin) P58455 Belongs to the cyclotide family OAK2 Oldenlandia affinis Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: Kalata-B3 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref:11535828] It has hemolytic activity Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L No cytotoxicity information found Not found 11535828 Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10614-9. Jennings C, West J, Waine C, Craik D, Anderson M. Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. DRAMP00859 GLPVCGETCVGGTCNTPGCTCSWPVCTRD 29 Kalata-B4 (Plant defensin) P83938 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Beta strand (4 strands; 10 residues) The charged residues (Glu3 and Arg24), along with the cation-binding site (near Glu3) are segregated on the other side of the molecule and in contact with polar head groups of detergent. The spatial structure of kalata B1 is only slightly changed during incorporation into micelles and represents a distorted triple-stranded beta-sheet cross-linked by a cystine knot. Detailed structural analysis and comparison with other knottins revealed 1ZNU resolved by NMR. "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B4 is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Binds to the micelle surface 10600388##16817894 J Mol Biol. 1999 Dec 17;294(5):1327-1336.##FEBS J. 2006 Jun;273(12):2658-2672. Craik DJ, Daly NL, Bond T, Waine C.##Shenkarev ZO, Nadezhdin KD, Sobol VA, Sobol AG, Skjeldal L, Arseniev AS. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle. DRAMP00860 TPCGESCVYIPCISGVIGCSCTDKVCYLN 29 Kalata-B5 (Plant defensin) P58456 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Combine helix and strand structure It displays a typical tightly folded cyclic Scystine knot structure. A range of pH and temperature titrations reveal that a conserved glutamic acid in loop 1 Sof the structure forms a key hydrogen bond network, similar to that reported previously for other cyclotides. 2KUX resolved by NMR. "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B5 is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database [Ref.20564013] HD50=27.4±1.2 μM against Human red blood cells . Cyclic No specific N-terminal No specific C-terminal "Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27.Hydrogen bonds between the side chain carboxyl group of Glu6 and the backbone amide protons of Ile14 and Ser15, as well as the side chain hydroxyl proton of Ser15. " L No cytotoxicity information found Not found 10600388##17534989##20564013 J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Chembiochem. 2007 Jun 18;8(9):1001-1011.##Biopolymers. 2010;94(5):647-658. Craik DJ, Daly NL, Bond T, Waine C.##Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.##Plan MR, Rosengren KJ, Sando L, Daly NL, Craik DJ. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.##Structural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinis. DRAMP00861 GLPVCGETCFGGTCNTPGCSCSSWPICTRN 30 Kalata-B6 (Plant defensin) P58455 Belongs to the cyclotide family OAK2 Oldenlandia affinis Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: Kalata-B6 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref.20564013] HD50=7.7±1.3 μM against Human red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found cell membrabce 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00862 GLPVCGETCTLGTCYTQGCTCSWPICKRN 29 Kalata-B7 (Plant defensin) P58457 Belongs to the cyclotide family OAK3 Oldenlandia affinis Not found Protein level Bridge Not found 2M9O##2JWM "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: Kalata-B7 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref.20564013] HD50=55.2±1.3 μM against Human red blood cells . Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found cell membrabce 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00863 GSVLNCGETCLLGTCYTTGCTCNKYRVCTKD 31 Kalata-B8 (Plant defensin) P85175 Belongs to the cyclotide family Not found Oldenlandia affinis Antimicrobial, Antiviral Protein level Beta strand (3 strands; 7 residues) Not found 2B38 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. Has no hemolytic activity. PTM: Kalata-B8 is a cyclic peptide which contains three disulfide bonds 6-20; 10-22; 15-28." [Ref.16207177]Virus: Human T-lymphoblast (CEM-SS) cells (EC50=2.5 µM).##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=2500 nM). [Ref.20564013] It produced 7% hemolysis at the 62μM. Cyclic Cyclization (N termini to C termini) Cyclization (C termini to N termini) Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys28. L [Ref.16207177] Kalata B8 inhibited the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells with an antiviral cytoprotective concentration (EC50) of approx. 2.5 μM, while the cytotoxic concentration (IC50) was >11 μM. ##[Ref.18008336]CEM-SS cells:IC50>11000 nM. Not found 18008336##16207177##17534989 Biopolymers. 2008;90(1):51-60.##Biochem J. 2006 Feb 1;393(Pt 3):619-626.##Chembiochem. 2007 Jun 18;8(9):1001-1011. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. ##Daly NL, Clark RJ, Plan MR, Craik DJ.##Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. Cyclotides as natural anti-HIV agents.##Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif.##The cyclotide fingerprint in Oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00864 GSVFNCGETCVLGTCYTPGCTCNTYRVCTKD 31 Kalata-B9 (Plant defensin) P85127 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B9 is a cyclic peptide which contains three disulfide bonds 6-20; 10-22; 15-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys28. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00865 ESEFDRQEYEECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQE 49 Vicilin-like Antimicrobial peptide 2a (MiAMP2a; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database. Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml).##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP00866 GLPTCGETCFGGTCNTPGCSCSSWPICTRD 30 Kalata-B10 (Plant defensin) P85128 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B10 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00867 GLPVCGETCFGGTCNTPGCSCTDPICTRD 29 Kalata-B11 (Plant defensin) P85129 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B11 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00868 GSLCGDTCFVLGCNDSSCSCNYPICVKD 28 Kalata-B12 (Plant defensin) P85130 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Beta strand (3 strands; 11 residues) Not found 2KVX resolved by NMR. "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B12 are cyclic peptides which may contain three disulfide bonds 4-18; 8-20; 13-25." No MICs found in DRAMP database [Ref.21466163] It has almost negligible hemolytic activity. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys18,Cys8 and Cys20,Cys13 and Cys25. L No cytotoxicity information found Not found 17534989##21466163 Chembiochem. 2007 Jun 18;8(9):1001-1011.##Biochemistry. 2011 May 17;50(19):4077-4086. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.##Wang CK, Clark RJ, Harvey PJ, Rosengren KJ, Cemazar M, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.##The role of conserved Glu residue on cyclotide stability and activity: a structural and functional study of kalata B12, a naturally occurring Glu to Asp mutant. DRAMP00869 GLPVCGETCFGGTCNTPGCACDPWPVCTRD 30 Kalata-B13 (Plant defensin) P85131 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B13 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00870 GLPVCGESCFGGTCNTPGCACDPWPVCTRD 30 Kalata-B14 (Plant defensin) P85132 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B14 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00871 GLPVCGESCFGGSCYTPGCSCTWPICTRD 29 Kalata-B15 (Plant defensin) P85133 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B15 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00872 GIPCAESCVYIPCTITALLGCKCQDKVCYD 30 Kalata-B16 (Plant defensin) P85134 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B16 are cyclic peptides which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21,Cys8 and Cys23,Cys13 and Cys28. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00873 GIPCAESCVYIPCTITALLGCKCKDQVCYN 30 Kalata-B17 (Plant defensin) P85135 Belongs to the cyclotide family Not found Oldenlandia affinis Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Kalata-B16 are cyclic peptides which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21,Cys8 and Cys23,Cys13 and Cys28. L No cytotoxicity information found Not found 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. DRAMP00875 SISCGESCAMISFCFTEVIGCSCKNKVCYLN 31 Leaf cyclotide 1 (Vhl-1; Plant defensin) P84522 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial, Antiviral Protein level Combine helix and strand structure Vhl-1 adopts a compact and well defined structure including a distorted triple-stranded beta-sheet, a short 3(10) helical segment and several turns. It is stabilized by three disulfide bonds, which, together with backbone segments, form a cyclic cystine knot motif. The three-disulfide bonds are almost completely buried into the protein core, and the six cysteines contribute only 3.8% to the molecular surface. 1ZA8 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has anti-human immunodeficiency virus activity. Tissue specificity: Expressed in leaves. PTM: Vhl-1 is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 14-28." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=870 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found in the reference(s) presented Not found 18008336##15824119 Biopolymers. 2008;90(1):51-60.##J Biol Chem. 2005 Jun 10;280(23):22395-22405. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. ##Chen B, Colgrave ML, Daly NL, Rosengren KJ, Gustafson KR, Craik DJ. Cyclotides as natural anti-HIV agents.##Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide. DRAMP00876 GLPVCGETCFTGTCYTNGCTCDPWPVCTRN 30 Leaf cyclotide 2 (Vhl-2; Plant defensin) P85231 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Antimicrobial, Antiviral Protein level Beta strand (5 strands; 6 residues) Analysis of surface hydrophobicity and haemolytic activity for a range of cyclotides indicates a correlation between them, with increasing hydrophobicity resulting in increased haemolytic activity. 2KUK resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. Tissue specificity: Expressed in leaves. PTM: This is a cyclic peptide which contains three disulfide bonds 5-19; 9-21; 14-27." [Ref.15824119]Virus: HIV(EC50= 0.87 μM) [Ref:15824119]Has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrabce 15824119##Pubmed ID is not available J Biol Chem. 2005 Jun 10;280(23):22395-22405.##Aust. J. Chem. 2010;63:771-778. Chen B, Colgrave ML, Daly NL, Rosengren KJ, Gustafson KR, Craik DJ.##Daly NL, Chen B, Nguyencong P, Craik DJ. Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide.##Structure and activity of the leaf-specific cyclotide vhl-2. DRAMP00879 GIPCGESCVFIPCITSVAGCSCKSKVCYRN 30 Circulin-C (CIRC; Plant defensin) P84641 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.10691702]Virus: HIV-1 (EC50= 50-275 nM).##NOTE: EC50 = concentration that is 50% effective.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 10691702##18008336 J Nat Prod. 2000 Feb;63(2):176-178.##Biopolymers. 2008;90(1):51-60. Gustafson KR, Walton LK, Sowder RC Jr, Johnson DG, Pannell LK, Cardellina JH Jr, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. New circulin macrocyclic polypeptides from Chassalia parvifolia.##Cyclotides as natural anti-HIV agents. DRAMP00880 KIPCGESCVWIPCVTSIFNCKCKENKVCYHD 31 Circulin-D (CIRD; Plant defensin) P84642 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.10691702]Virus: HIV-1 (EC50= 50-275 nM).##NOTE: EC50 = concentration that is 50% effective.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 10691702##18008336 J Nat Prod. 2000 Feb;63(2):176-178.##Biopolymers. 2008;90(1):51-60. Gustafson KR, Walton LK, Sowder RC Jr, Johnson DG, Pannell LK, Cardellina JH Jr, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. New circulin macrocyclic polypeptides from Chassalia parvifolia.##Cyclotides as natural anti-HIV agents. DRAMP00881 KIPCGESCVWIPCLTSVFNCKCENKVCYHD 30 Circulin-E (CIRE; Plant defensin) P84643 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.10691702]Virus: HIV-1 (EC50= 50-275 nM).##NOTE: EC50 = concentration that is 50% effective.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 10691702##18008336 J Nat Prod. 2000 Feb;63(2):176-178.##Biopolymers. 2008;90(1):51-60. Gustafson KR, Walton LK, Sowder RC Jr, Johnson DG, Pannell LK, Cardellina JH Jr, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. New circulin macrocyclic polypeptides from Chassalia parvifolia.##Cyclotides as natural anti-HIV agents. DRAMP00882 KVCYRAIPCGESCVWIPCISAAIGCSCKN 29 Circulin-F (CIRF; Plant defensin) P84644 Belongs to the cyclotide family Not found Chassalia parviflora Antimicrobial, Antiviral Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.10691702]Virus: HIV-1 (EC50= 50-275 nM).##NOTE: EC50 = concentration that is 50% effective.##[Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 10691702##18008336 J Nat Prod. 2000 Feb;63(2):176-178.##Biopolymers. 2008;90(1):51-60. Gustafson KR, Walton LK, Sowder RC Jr, Johnson DG, Pannell LK, Cardellina JH Jr, Boyd MR.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. New circulin macrocyclic polypeptides from Chassalia parvifolia.##Cyclotides as natural anti-HIV agents. DRAMP00883 SCVYIPCTITALLGCSCKNKVCYNGIPCAE 30 Cyclotide hypa-A (hypa-A; Plant defensin) P58445 Belongs to the cyclotide family Not found Hybanthus parviflorus (Violetilla) (Viola parvifloria) Not found Protein level Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. "Function: Probably participates in a plant defense mechanism. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: This is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11524112 Phytochemistry. 2001 Sep;58(1):47-51. Broussalis AM, Göransson U, Coussio JD, Ferraro G, Martino V, Claeson P. First cyclotide from Hybanthus (Violaceae). DRAMP00884 SISCGESCVYIPCTVTALVGCTCKDKVCYLN 31 Cyclotide hyfl-A (Plant defensin) P84647 Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Protein level Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00885 GSPIQCAETCFIGKCYTEELGCTCTAFLCMKN 32 Cyclotide hyfl-B (Plant defensin) P84648 Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Protein level Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. "Function: Probably participates in a plant defense mechanism. PTM: This is is a cyclic peptide which may contain three disulfide bonds 6-22; 10-24; 15-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00886 GSPRQCAETCFIGKCYTEELGCTCTAFLCMKN 32 Cyclotide hyfl-C (Plant defensin) P84649 Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Protein level Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. "Function: Probably participates in a plant defense mechanism. PTM: This is is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00887 GSVPCGESCVYIPCFTGIAGCSCKSKVCYYN 31 Cyclotide hyfl-D (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00888 GEIPCGESCVYLPCFLPNCYCRNHVCYLN 29 Cyclotide hyfl-E (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00889 SISCGETCTTFNCWIPNCKCNHHDKVCYWN 30 Cyclotide hyfl-F (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00890 CAETCVVLPCFIVPGCSCKSSVCYFN 26 Cyclotide hyfl-G (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00891 CAETCIYIPCFTEAVGCKCKDKVCYKN 27 Cyclotide hyfl-H (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00892 GIPCGESCVFIPCISGVIGCSCKSKVCYRN 30 Cyclotide hyfl-I (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00893 GIACGESCAYFGCWIPGCSCRNKVCYFN 28 Cyclotide hyfl-J (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00894 GTPCGESCVYIPCFTAVVGCTCKDKVCYLN 30 Cyclotide hyfl-K (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00895 GTPCAESCVYLPCFTGVIGCTCKDKVCYLN 30 Cyclotide hyfl-L (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00896 GNIPCGESCIFFPCFNPGCSCKDNLCYYN 29 Cyclotide hyfl-M (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00897 CGETCVILPCISAALGCSCKDTVCYKN 27 Cyclotide hyfl-N (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00898 CGETCVIFPCISAAFGCSCKDTVCYKN 27 Cyclotide hyfl-O (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00899 CVWIPCISGIAGCSCKNKVCYLN 23 Cyclotide hyfl-P (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus floribundus (Greenviolet) Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Function: Probably participates in a plant defense mechanism. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00900 CGETCLFIPCIFSVVGCSCSSKVCYRN 27 Hymo A (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus monopetalus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00901 CGETCVTGTCYTPGCACDWPVCKRD 25 Hymo B (Plant defensin) No entry found Belongs to the cyclotide family Not found Hybanthus monopetalus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00902 CGETCIWGRCYSENIGCHCGFGICTLN 27 Hyst A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthusstellarioides Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00903 RGCYKICGETCLFIPCLTSVFGCSCKN 27 Hyve A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus vernonii Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00904 CGETCVVDTRCYTKKCSCAWPVCMRN 26 Hyca A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus calycinus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00905 CVWIPCISAAIGCSCKSKVCYRN 23 Hyde A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus debilissimus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00906 CGESCVYIPCTVTALLGCSCKDKVCYKN 28 Hyen A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus enneaspermus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. 7S55 Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00907 CGETCKVTKRCSGQGCSCLKGRSCYD 26 Hyen B (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus enneaspermus Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00908 CGETCVVLPCFIVPGCSCKSSVCYFN 26 Hyep A (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus epacroides Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00909 CGETCIYIPCFTEAVGCKCKDKVCYKN 27 Hyep B (Plant defensin) No entry found Belongs to the cyclotide family Not found Australian Hybanthus epacroides Not found Not found Bridge Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. Caution: The sequence is incomplete! No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16199617 Plant Cell. 2005 Nov;17(11):3176-3189. Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, Göransson U, Craik DJ. A continent of plant defense peptide diversity: cyclotides in Australian Hybanthus (Violaceae). DRAMP00910 GGTIFDCGESCFLGTCYTKGCSCGEWKLCYGTN 33 Tricyclon-A (Cyclotides; Plant defensin) P0C589 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Not found Protein level Beta strand (3 strands; 13 residues) Not found 1YP8 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has a weak hemolytic activity. PTM: Contains three disulfide bonds 7-21; 11-23; 16-29. Proteolytically processed in two steps to yield first two linear precursors, and then two cyclic peptides after removal of the N-terminal repeats (NTR) and short tails." Cytolysis [Ref:15893660] It has 2% hemolytic activity at 500 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys7 and Cys21, Cys11 and Cys23, Cys16 and Cys29. L No cytotoxicity information found Not found 15893660 Structure. 2005 May;13(5):691-701. Mulvenna JP, Sando L, Craik DJ. Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A. DRAMP00911 GGTIFDCGESCFLGTCYTKGCSCGEWKLCYGEN 33 Tricyclon-B (Plant defensin) P0C589 Belongs to the cyclotide family Not found Viola arvensis (European field pansy) (Field violet) Not found Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 7-21; 11-23; 16-29. Proteolytically processed in two steps to yield first two linear precursors, and then two cyclic peptides after removal of the N-terminal repeats (NTR) and short tails." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys7 and Cys21, Cys11 and Cys23, Cys16 and Cys29. L No cytotoxicity information found Not found 15893660 Structure. 2005 May;13(5):691-701. Mulvenna JP, Sando L, Craik DJ. Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A. DRAMP00912 GIPCAESCVWIPCTVTALLGCSCSNKVCYN 30 Root cyclotide 1 (Vhr1; Plant defensin) P83937 Belongs to the cyclotide family Not found Viola hederacea (Australian violet) Not found Protein level Combine helix and strand structure Not found 1VB8 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Tissue specificity: Expressed in roots. PTM: Contains three disulfide bonds 4-21; 8-23; 13-28. This is a cyclic peptide (cross-link at G1-N30)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21, Cys8 and Cys23,Cys13 and Cys28. L No cytotoxicity information found Not found 15295104 Plant Cell. 2004 Aug;16(8):2204-2216. Trabi M, Craik DJ. Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1. DRAMP00913 GLPVCGETCFGGTCNTPGCSCSYPICTRN 29 Cyclotide vibi-A (Plant defensin) P85239 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26. This is a cyclic peptide (cross-link between G1-N29)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26. L No cytotoxicity information found Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00914 GLPVCGETCFGGTCNTPGCTCSYPICTRN 29 Cyclotide vibi-B (Plant defensin) P85240 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26. This is a cyclic peptide (cross-link between G1-N29). Note: Sequence uncertainty at position 2 (L or I)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26. L No cytotoxicity information found Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00915 GLPVCGETCAFGSCYTPGCSCSWPVCTRN 29 Cyclotide vibi-C (Plant defensin) P85241 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26. This is a cyclic peptide (cross-link between G1-N29)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26. L No cytotoxicity information found Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00916 GLPVCGETCFGGRCNTPGCTCSYPICTRN 29 Cyclotide vibi-D (Plant defensin) P85242 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism. Has moderate levels of cytotoxic activity. PTM: Contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N29)." Human lymphoma cell line U-937 GTB (IC50>30 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L [Ref.18191970] Cytotoxicity: Human lymphoma cell line U-937 GTB (IC50>30 µM). Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00917 GIPCAESCVWIPCTVTALIGCGCSNKVCYN 30 Cyclotide vibi-E (Vbc1; Plant defensin) B1NRQ8, P85243 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity. PTM: Contains three disulfide bonds 4-21; 8-23; 13-28. This is a cyclic peptide (cross-link at G1-N3)." Human lymphoma cell line U-937 GTB (IC50=3.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21, Cys8 and Cys23,Cys13 and Cys28. L [Ref.18191970] Cytotoxicity: Human lymphoma cell line U-937 GTB (IC50=3.2 µM). Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00918 GTIPCGESCVFIPCLTSALGCSCKSKVCYKN 31 Cyclotide vibi-F (Plant defensin) P85244 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00919 GTFPCGESCVFIPCLTSAIGCSCKSKVCYKN 31 Cyclotide vibi-G (Plant defensin) P85245 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity. PTM: Contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." Human lymphoma cell line U-937 GTB (IC50=0.96 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L [Ref.18191970] Cytotoxicity: Human lymphoma cell line U-937 GTB (IC50=0.96 µM). Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00920 GLLPCAESCVYIPCLTTVIGCSCKSKVCYKN 31 Cyclotide vibi-H (Plant defensin) P85246 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity. PTM: Contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." Human lymphoma cell line U-937 GTB (IC50=1.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L [Ref.18191970] Cytotoxicity: Human lymphoma cell line U-937 GTB (IC50=1.6 µM). Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00921 GIPCGESCVWIPCLTSTVGCSCKSKVCYRN 30 Cyclotide vibi-I (Vbc2; Plant defensin) B1NRQ9 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism. PTM: Contains three disulfide bonds 4-20; 8-22; 13-27. This is a cyclic peptide (cross-link at G1-N30)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00922 GTFPCGESCVWIPCISKVIGCACKSKVCYKN 31 Cyclotide vibi-J (Vbc3; Plant defensin) B1NRR0 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00923 GIPCGESCVWIPCLTSAVGCPCKSKVCYRN 30 Cyclotide vibi-K (Vbc4; Plant defensin) B1NRR1 Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) Cytotoxic Protein level Bridge The cyclotides are head-to-tail macrocyclic and they have three disulfides arranged in a cystine knot, in which two disulfide bonds and their connecting backbone segments form an embedded ring that is penetrated by the third disulfide bond. Cyclotides exhibit a broad range of biological effects, including insecticidal, haemolytic, and cytotoxic effects. "Function: Probably participates in a plant defense mechanism and shows potent cytotoxic activity. PTM: Contains three disulfide bonds 4-20; 8-22; 13-27. This is a cyclic peptide (cross-link at G1-N31)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18191970 Phytochemistry. 2008 Feb;69(4):939-952. Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, Göransson U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. DRAMP00924 PGLGFY 6 Cyclopeptide E (Plant defensin) P85003 Not found Not found Annona cherimola (Custard apple) (Cherimoya) Anti-cancer, Cytotoxic Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity against human nasopharyngeal carcinoma. PTM: This is a cyclic peptide." Human nasopharyngeal carcinoma (IC50=17 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16040066 Phytochemistry. 2005 Oct;66(19):2376-2380. Wélé A, Zhang Y, Brouard JP, Pousset JL, Bodo B. Two cyclopeptides from the seeds of Annona cherimola. DRAMP00925 PGMGIYLPM 9 Cyclopeptide F (Plant defensin) P85002 Not found Not found Annona cherimola (Custard apple) (Cherimoya) Cytotoxic Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. Has cytotoxic activity. PTM: This is a cyclic peptide." Human nasopharyngeal carcinoma (IC50=60 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16040066 Phytochemistry. 2005 Oct;66(19):2376-2380. W©l© A, Zhang Y, Brouard JP, Pousset JL, Bodo B. Two cyclopeptides from the seeds of Annona cherimola. DRAMP00926 SAISCGETCFKFKCYTPRCSCSYPVCK 27 Violacin-A (Violacin-1; linearized uncyclotides; Plant defensin) Q2HY54 Not found Not found Viola odorata (Sweet violet) Antimicrobial Protein level Beta strand (4 strands; 9 residues) The three-dimensional solution structure of violacin A is determined and found to adopt the cystine knot fold of native cyclotides. (Ref.2) 2FQA resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has low hemolytic activity. Miscellaneous: The presence of a premature stop codon inhibits the translation of a key Asn residue that is thought to be required for cyclization. PTM: Contains three disulfide bonds 5-19; 9-21; 14-26." [Ref.16488428]show insecticidal, anti-HIV, antimicrobial, antineurotensive, cytotoxic and haemolytic activity [Ref:16488428]10% hemolytic activity at 1.0μM and 35% hemolytic activity at 1.5μM against human type A red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16872274##16488428 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 2006 Apr 14;357(5):1522-1535. Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Colgrave ML, Nguyencong P, Daly NL, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Discovery and characterization of a linear cyclotide from Viola odorata: implications for the processing of circular proteins. DRAMP00927 GSIPCAESCVYIPCFTGIAGCSCKNKVCYYN 31 Cyclotide vico-A (Plant defensin) P84635 Not found Not found Viola cotyledon (Violeta) Antimicrobial Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12782038 Anal Biochem. 2003 Jul 1;318(1):107-117. Göransson U, Broussalis AM, Claeson P. Expression of Viola cyclotides by liquid chromatography-mass spectrometry and tandem mass spectrometry sequencing of intercysteine loops after introduction of charges and cleavage sites by aminoethylation. DRAMP00928 GSIPCAESCVYIPCITGIAGCSCKNKVCYYN 31 Cyclotide vico-B (Plant defensin) P84636 Not found Not found Viola cotyledon (Violeta) Antimicrobial Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. PTM: Problely contains three disulfide bonds 5-21; 9-23; 14-28. This is a cyclic peptide (cross-link at G1-N31)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12782038 Anal Biochem. 2003 Jul 1;318(1):107-117. Göransson U, Broussalis AM, Claeson P. Expression of Viola cyclotides by liquid chromatography-mass spectrometry and tandem mass spectrometry sequencing of intercysteine loops after introduction of charges and cleavage sites by aminoethylation. DRAMP00932 SYFSAWAGPGCNNHNARYSKCGCSNIGHNVHGGYEFVYQGQTAAAYNTDNCKGVAQTRFSSSVNQACSNFGWKSVFIQC 79 Antimicrobial peptide 1 (PMAP1; Plant defensin) P83880 Not found Not found Pinus monticola (Western white pine) (Strobus monticola) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found "Tissue specificity: Detected at higher levels in needles and twigs from canker-resistant seedlings than in needles from canker-susceptible plants. During summer, detected on cankered, healthy and marginal bark. During winter, detected at lower levels in cankered bark and bark from the canker margin than in healthy bark (at protein level). Developmental stage: In summer, present at higher levels in older needles and twigs than in tissues from the current year. In winter, detected at high levels in both older and current-year needles and twigs. Induction: By wounding and by methyl jasmonate. PTM: Problely contains three disulfide bonds 11-67; 21-79; 23-51." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18943919##14759906 Phytopathology. 2006 Feb;96(2):164-170.##Tree Physiol. 1997 Oct;17(10):663-669. Ekramoddoullah AK, Liu JJ, Zamani A.##Davidson J, Ekramoddoullah AK. Cloning and Characterization of a Putative Antifungal Peptide Gene (Pm-AMP1) in Pinus monticola.##Analysis of bark proteins in blister rust-resistant and susceptible western white pine (Pinus monticola). DRAMP00934 RTCESQSHRFKGTCVRQSNCAAVCQTEGFHGGNCRGFRRRCFCTKHC 47 Vv-AMP1 (Vitis vinifera antimicrobial peptide 1; Plant defensin) No entry found Not found Not found Vitis vinifera (Berry) Antimicrobial, Antifungal Not found Not found Not found MOA: the inhibitory activity of Vv-AMP1 might be associated with altering the membrane permeability of the fungal membranes. Fungi: Fusarium oxysporum and Verticillium dahliae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18611251 BMC Plant Biol. 2008 Jul 8;8:75. de Beer A, Vivier MA. Vv-AMP1, a ripening induced peptide from Vitis vinifera shows strong antifungal activity. DRAMP00935 DVSFSLSGGGTASYEK 16 Ribosome-inactivating protein trichokirin (rRNA N-glycosidase; Plant defensin) P16093 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber) Cytotoxic Protein level Not found Not found "Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. PTM: Glycosylated." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3262509 Eur J Biochem. 1988 Oct 1;176(3):581-588. Casellas P, Dussossoy D, Falasca AI, Barbieri L, Guillemot JC, Ferrara P, Bolognesi A, Cenini P, Stirpe F. Trichokirin, a ribosome-inactivating protein from the seeds of Trichosanthes kirilowii Maximowicz. Purification, partial characterization and use for preparation of immunotoxins. DRAMP00936 DVSFRLSGATSKKKVYFISNLRKALPNEKKLYDIPLVRSSXSGSK 45 Ribosome-inactivating protein TAP-29 (rRNA N-glycosidase; Plant defensin) P23029 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber) Antiviral, Cytotoxic, Antimicrobial Protein level Not found Not found "Function: Capable of inhibiting HIV-1 infection and replication. It inactivates eukaryotic 60S ribosomal subunits. Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1713684 Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6570-4. Lee-Huang S, Huang PL, Kung HF, Li BQ, Huang PL, Huang P, Huang HI, Chen HC. TAP 29: an anti-human immunodeficiency virus protein from Trichosanthes kirilowii that is nontoxic to intact cells. DRAMP00937 KSCCRNTVARNCYNVCRIPGTPRPVCAATCDCKLITGTKCPPGYEK 46 Tu-AMP1 (Plant defensin) No entry found Belongs to the thionin family Not found Tulipa gesneriana L. Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Bacteria: Erwinia carotovora (IC50=11 µg/ml), Agrobacterium radiobacter (IC50=15 µg/ml), Agrobacterium rhizogenes (IC50=20 µg/ml);##Gram-positive bacteria: Clavibacter michiganensis (IC50=14 µg/ml), Curtobacterium flaccumfaciens (IC50=13 µg/ml).##Fungi: Fusarium oxysporum (IC50=2 µg/ml), Geotrichum candidum (IC50=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 15056889 Biosci Biotechnol Biochem. 2004 Mar;68(3):571-577. Fujimura M, Ideguchi M, Minami Y, Watanabe K, Tadera K. Purification, characterization, and sequencing of novel antimicrobial peptides, Tu-AMP 1 and Tu-AMP 2, from bulbs of tulip (Tulipa gesneriana L.). DRAMP00938 KSCCRNTTARNCYNVCRIPG 20 Tu-AMP2 (Plant defensin) No entry found Belongs to the thionin family Not found Tulipa gesneriana L. Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Erwinia carotovora (IC50=15 µg/ml), Agrobacterium radiobacter (IC50=17 µg/ml), Agrobacterium rhizogenes (IC50=20 µg/ml);##Gram-positive bacteria: Clavibacter michiganensis (IC50=17 µg/ml), Curtobacterium flaccumfaciens (IC50=15 µg/ml).##Fungi: Fusarium oxysporum (IC50=2 µg/ml), Geotrichum candidum (IC50=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15056889 Biosci Biotechnol Biochem. 2004 Mar;68(3):571-577. Fujimura M, Ideguchi M, Minami Y, Watanabe K, Tadera K. Purification, characterization, and sequencing of novel antimicrobial peptides, Tu-AMP 1 and Tu-AMP 2, from bulbs of tulip (Tulipa gesneriana L.). DRAMP00939 VDCGANPFKVACFNSCLLGPSTVFQCADFCACRLPAG 37 Type-5 thionin (Type V thionin; Plant defensin) Q05806 Belongs to the thionin family TTHV Triticum aestivum (Wheat) Cytotoxic Transcript level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40; 12-30; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1569564 J Mol Biol. 1992 Apr 20;224(4):1003-1009. Castagnaro A, Mara±a C, Carbonero P, Garc­a-Olmedo F. Extreme divergence of a novel wheat thionin generated by a mutational burst specifically affecting the mature protein domain of the precursor. DRAMP00940 TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN 46 Crambin (Plant defensin) P01542 Belongs to the thionin family THI2 Crambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica) Cytotoxic Protein level Combine helix and strand structure Not found 3NIR resolved by X-ray. "Function: The Function: of this hydrophobic plant seed protein is not known. Miscellaneous: Two isoforms exists, a major form PL (shown here) and a minor form SI. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6895315##21505232 Biochemistry. 1981 Sep 15;20(19):5437-5443.##Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):424-428. Teeter MM, Mazer JA, L'Italien JJ.##Schmidt A, Teeter M, Weckert E, Lamzin VS. Primary structure of the hydrophobic plant protein crambin.##Crystal structure of small protein crambin at 0.48Å resolution. DRAMP00941 KSCCRNTLARNCYNACRFTGGSQPTCGILCDCIHVTTTTCPSSHPS 46 Hellethionin-D (Plant defensin) P60057 Belongs to the thionin family Not found Helleborus purpurascens (Purple hellebore) Cytotoxic Protein level Combine helix and strand structure Not found 1NBL resolved by NMR. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains four disulfide bonds 3-40; 4-32; 12-30; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12600207 Biochemistry. 2003 Mar 4;42(8):2404-2411. Milbradt AG, Kerek F, Moroder L, Renner C. Structural characterization of hellethionins from Helleborus purpurascens. DRAMP00942 KSCCRTTLGRNCYNLCRSRGAQKLCSTVCRCKLTSGLSCPKGFPK 45 Alpha-2-purothionin (Plant defensin) P32032 Belongs to the thionin family THI1.2 Triticum aestivum (Wheat) Cytotoxic Transcript level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Problely contains four disulfide bonds 3-39; 5-31; 12-29; 16-25. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7824649 Plant Physiol. 1994 Nov;106(3):1221-1222. Castagnaro A, Mara±a C, Carbonero P, Garc­a-Olmedo F. cDNA cloning and nucleotide sequences of alpha 1 and alpha 2 thionins from hexaploid wheat endosperm. DRAMP00943 KSCCRSTLGRNCYNLCRARGAQKLCAGVCRCKISSGLSCPKGFPK 45 Alpha-1-purothionin (Plant defensin) P01544 Belongs to the thionin family THI1.1 Triticum aestivum (Wheat) Cytotoxic Protein level Combine helix and strand structure Not found 2PLH resolved by X-ray. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise Function: is not known. PTM: Contains four disulfide bonds 3-39; 4-31; 12-29; 16-25. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7824649##2235992 Plant Physiol. 1994 Nov;106(3):1221-1222.##Proteins. 1990;8(2):118-132. Castagnaro A, Mara±a C, Carbonero P, Garc­a-Olmedo F.##Teeter MM, Ma XQ, Rao U, Whitlow M. cDNA cloning and nucleotide sequences of alpha 1 and alpha 2 thionins from hexaploid wheat endosperm.##Crystal structure of a protein-toxin alpha 1-purothionin at 2.5A and a comparison with predicted models. DRAMP00944 KSCCKSTLGRNCYNLCRARGAQKLCANVCRCKLTSGLSCPKDFPK 45 Purothionin A-1 (Plant defensin) P01543 Belongs to the thionin family THI1.3 Triticum aestivum (Wheat) Cytotoxic Protein level Combine helix and strand structure Not found 1BHP resolved by X-ray. Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15299761 Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):914-924. Stec B, Rao U, Teeter MM. Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 2: structure of beta-purothionin at 1.7 A resolution. DRAMP00945 KSCCPTTTARNIYNTCRFGGGSRPVCAKLSGCKIISGTKCDSGWNH 46 Phoratoxin (Plant defensin) P01539 Belongs to the thionin family Not found Phoradendron tomentosum (California mistletoe) Cytotoxic Protein level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 4606908 Acta Pharm Suec. 1974 Sep;11(4):367-374. Mellstrand ST, Samuelsson G. Phoratoxin, a toxic protein from the mistletoe Pharoadendron tomentosum subsp. macrophyllum (Loranthaceae). The disulphide bonds. DRAMP00946 QKIPFKECYPACLVECKAGSKFPKYLKCPFTCTKECLQQPSPPSVSSNNIDESDYFCKLGCATYHCVSLSSIQNPNVERVSACVDSCSNKCTKKN 95 Thionin-like protein 2 (Plant defensin) A8MRP4 Belongs to the thionin family Not found Arabidopsis thaliana (Mouse-ear cress) Not found Homology Not found Not found Function: May be involved in plant defense. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11130712 Nature. 2000 Dec 14;408(6814):816-820. Theologis A, Ecker JR, Palm CJ, et al. Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana. DRAMP00947 KSCCPTTAARNQYNICRLPGTPRPVCAALSGCKIISGTGCPPGYRH 46 Denclatoxin-B (Plant defensin) P01541 Belongs to the thionin family Not found Dendrophthora clavata (Columbian mistletoe) Cytotoxic Protein level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Problely contains three disulfide bonds 3-40; 4-32; 16-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 906843 Acta Pharm Suec. 1977;14(3):245-254. Samuelsson G, Pettersson B. Toxic proteins from the mistletoe Dendrophtora clavata. II. The amino acid sequence of denclatoxin B. DRAMP00948 KSCCPSTTARNIYNTCRLTGTSRPTCASLSGCKIISGSTCBSGWBH 46 Ligatoxin-A (Plant defensin) P01540 Belongs to the thionin family Not found Phoradendron liga (Argentine mistletoe) Cytotoxic Protein level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7136736 Acta Pharm Suec. 1982;19(4):285-292. Thunberg E, Samuelsson G. Isolation and properties of ligatoxin A, a toxic protein from the mistletoe Phoradendron liga. DRAMP00949 KSCCPSTTARNIYNTCRLTGASRSVCASLSGCKIISGSTCDSGWNH 46 Ligatoxin-B (Plant defensin) P59358 Belongs to the thionin family Not found Phoradendron liga (Argentine mistletoe) Cytotoxic Protein level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40;4-32;16-26." Human lymphoma cell line U-937-GTB (IC50=1.8 µM);##primary multidrug-resistant renal adenocarcinoma cell line ACHN (IC50=3.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12049612 Biochem J. 2002 Sep 1;366(Pt 2):405-413. Li SS, Gullbo J, Lindholm P, Larsson R, Thunberg E, Samuelsson G, Bohlin L, Claeson P. Ligatoxin B, a new cytotoxic protein with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron liga. DRAMP00950 KSCCPBTTGRBIYBTCRFGGGSRZVCARISGCKIISASTCPSYPBK 46 Viscotoxin-1-PS (Vt1-PS; Plant defensin) P01537 Belongs to the thionin family THI2.4 Viscum album (European mistletoe) Cytotoxic Protein level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 4417993 Acta Pharm Suec. 1974 May;11(2):175-184. Samuelsson G, Jayawardene AL. Isolation and characterization of viscotoxin 1-Ps from Viscum album L. ssp. austriacum (Wiesb.) vollmann, growing on Pinus silvestris. DRAMP00951 KSCCPNTTGRNIYNACRLTGAPCPTCAKLSGCKIISGSTCPSDYPK 46 Viscotoxin A (Plants) Q9S9A2 Not found Not found Viscum album (European mistletoe) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8292787 Plant Mol Biol. 1993 Dec;23(6):1233-1242. Schrader-Fischer G, Apel K. cDNA-derived identification of novel thionin precursors in Viscum album that contain highly divergent thionin domains but conserved signal and acidic polypeptide domains. DRAMP00952 KSCCPNTTGRNIYNTCRLTGSSRETCAKLSGCKIISASTCPSNYPK 46 Viscotoxin A1 (Plant defensin) D0VWT3 Not found Not found Viscum album (European mistletoe) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Combine helix and strand structure Not found 3C8P resolved by X-ray. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18703848 Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):985-992. Pal A, Debreczeni JE, Sevvana M, Gruene T, Kahle B, Zeeck A, Sheldrick GM. Structures of viscotoxins A1 and B2 from European mistletoe solved using native data alone. DRAMP00953 KSCCPNTTGRNIYNTCRFGGGSREVCASLSGCKIISASTCPSYPDK 46 Viscotoxin-A2 (VtA2; Plant defensin) P32880, P01536 Belongs to the thionin family THI2.3 Viscum album (European mistletoe) Cytotoxic Protein level Combine helix and strand structure Not found 1JMN resolved by NMR. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 4607177##12733989 Acta Pharm Suec. 1974 Sep;11(4):381-386.##Biochem J. 2003 Aug 15;374(Pt 1):71-78. Olson T, Samuelsson G.##Coulon A, Mosbah A, Lopez A, Sautereau AM, Schaller G, Urech K, Roug© P, Darbon H. The disulphide bonds of viscotoxin A2 from the European mistletoe (Viscum album L. Loranthaceae).##Comparative membrane interaction study of viscotoxins A3, A2 and B from mistletoe (Viscum album) and connections with their structures. DRAMP00954 KSCCPNTTGRNIYNACRLTGAPRPTCAKLSGCKIISGSTCPSDYPK 46 Viscotoxin-A3 (Plant defensin) P01538 Belongs to the thionin family THI2.1 Viscum album (European mistletoe) Antimicrobial, Antifungal, Cytotoxic Protein level Combine helix and strand structure Not found 1OKH resolved by X-ray. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26. " Fungi: Fusarium solani, Sclerotinia sclerotiorum, Phytophtora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 1710983##4941626##10947973 Eur J Biochem. 1991 Jun 15;198(3):549-553.##Acta Chem Scand. 1971;25(6):2048-2054.##Biochem J. 2000 Sep 1;350 Pt 2:569-577. Schrader G, Apel K.##Samuelsson G, Pettersson B.##Romagnoli S, Ugolini R, Fogolari F, Schaller G, Urech K, Giannattasio M, Ragona L, Molinari H. Isolation and characterization of cDNAs encoding viscotoxins of mistletoe (Viscum album).##The disulfide bonds of viscotoxin A3 from the European mistletoe (Viscum album L., Loranthaceae).##NMR structural determination of viscotoxin A3 from Viscum album L. DRAMP00955 KSCCPNTTGRNIYNTCRLGGGSRERCASLSGCKIISASTCPSDYPK 46 Viscotoxin-B (VtB; Plant defensin) P08943, P01536, P84186 Belongs to the thionin family THI2.2 Viscum album (European mistletoe) Antimicrobial, Antifungal, Cytotoxic Protein level Combine helix and strand structure Not found 1JMP resolved by NMR.##2V9B resolved by X-ray. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise Function: is not known. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26." Fungi: Fusarium solani, Sclerotinia sclerotiorum, Phytophtora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1710983##12733989 Eur J Biochem. 1991 Jun 15;198(3):549-553.##Biochem J. 2003 Aug 15;374(Pt 1):71-78. Schrader G, Apel K.##Coulon A, Mosbah A, Lopez A, Sautereau AM, Schaller G, Urech K, Roug© P, Darbon H. Isolation and characterization of cDNAs encoding viscotoxins of mistletoe (Viscum album).##Comparative membrane interaction study of viscotoxins A3, A2 and B from mistletoe (Viscum album) and connections with their structures. DRAMP00956 KSCCPNTTGRNIYNTCRFAGGSRERCAKLSGCKIISASTCPSDYPK 46 Viscotoxin-C1 (VtC1; Plant defensin) P83554 Belongs to the thionin family Not found Viscum album (European mistletoe) Cytotoxic Protein level Combine helix and strand structure Not found 1ORL resolved by NMR.##3C8P resolved by X-ray. "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise Function: is not known. PTM: Contains three disulfide bonds 3-40; 4-32; 16-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9348108##14580196 Biol Chem. 1997 Sep;378(9):989-996.##Biochemistry. 2003 Nov 4;42(43):12503-10. Orr¹ S, Scaloni A, Giannattasio M, Urech K, Pucci P, Schaller G.##Romagnoli S, Fogolari F, Catalano M, Zetta L, Schaller G, Urech K, Giannattasio M, Ragona L, Molinari H. Amino acid sequence, S-S bridge arrangement and distribution in plant tissues of thionins from Viscum album.##NMR solution structure of viscotoxin C1 from Viscum album species Coloratum ohwi: toward a structure-Function: analysis of viscotoxins. DRAMP00957 KSCCRSTQARNIYNAPRFAGGSRPLCALGSGCKIVDDKKTPPND 44 Pp-AMP1 (P. pubescens AMP1; Plant defensin) No entry found Belongs to the thionin family Not found Phyllostachys pubescens (Japanese bamboo shoots) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Bridge Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Erwinia carotovora (IC50=22 µg/ml), Agrobacterium radiobacter (IC50=15 µg/ml), Agrobacterium rhizogenes (IC50=15 µg/ml);##Gram-positive bacteria: Clavibacter michiganensis (IC50=14 µg/ml), Curtobacterium flaccumfaciens (IC50=25 µg/ml).##Fungi: Fusarium oxysporum (IC50=2 µg/ml), Geotrichum candidum (IC50=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 15784998 Biosci Biotechnol Biochem. 2005 Mar;69(3):642-645. Fujimura M, Ideguchi M, Minami Y, Watanabe K, Tadera K. Amino acid sequence and antimicrobial activity of chitin-binding peptides, Pp-AMP 1 and Pp-AMP 2, from Japanese bamboo shoots (Phyllostachys pubescens). DRAMP00958 KSCCRSTTARNIYNGCRVPGTARPVCAKKSGCKIQEAKKCEPPYD 45 Pp-AMP2 (P. pubescens AMP2; Plant defensin) No entry found Belongs to the thionin family Not found Phyllostachys pubescens (Japanese bamboo shoots) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Bridge Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Erwinia carotovora (IC50=20 µg/ml), Agrobacterium radiobacter (IC50=13 µg/ml), Agrobacterium rhizogenes (IC50=15 µg/ml);##Gram-positive bacteria: Clavibacter michiganensis (IC50=18 µg/ml), Curtobacterium flaccumfaciens (IC50=20 µg/ml).##Fungi: Fusarium oxysporum (IC50=2 µg/ml), Geotrichum candidum (IC50=2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 15784998 Biosci Biotechnol Biochem. 2005 Mar;69(3):642-645. Fujimura M, Ideguchi M, Minami Y, Watanabe K, Tadera K. Amino acid sequence and antimicrobial activity of chitin-binding peptides, Pp-AMP 1 and Pp-AMP 2, from Japanese bamboo shoots (Phyllostachys pubescens). DRAMP00959 KICRRRSAGFKGPCMSNKNCAQVCQQEQWQQQNCDQPFRRCKCIRQC 47 Gamma1-purothionin (gamma1-P; thionin-like polypeptides; Plant defensin) No entry found Belongs to the thionin family Not found Triticum turgidum L cv Senatore Capelli (wheat endosperm) Not found Not found Beta strand Not found PTM: Contains four disulfide bonds. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2226781 FEBS Lett 1990; 270: 191-194. Colilla FJ, Rocher A, Mensez E. Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. DRAMP00960 KVCRQRSAQFKGPCVSDKNCAQVCLQEQWQQQNCDQPFRRCKCIRQC 47 Gamma2-purothionin (gamma2-P; thionin-like polypeptides; Plant defensin) No entry found Belongs to the thionin family Not found Triticum turgidum L cv Senatore Capelli (wheat endosperm) Not found Not found Not found Not found PTM: Contains four disulfide bonds. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2226781 FEBS Lett 1990; 270: 191-194. Colilla FJ, Rocher A, Mensez E. Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. DRAMP00961 KSCCRNTWARNCYNVCRLPGTISREICAKKCDCKIISGTTCPSDYPK 47 Thionin (Plant defensin) P07504 Belongs to the thionin family THI1 Pyrularia pubera (Buffalo nut) (Oil nut) Cytotoxic Protein level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Toxic dose: At concentrations of 0.04 mg/ml the protein causes visible disruption of cultured mouse B16 melanoma cells. PTM: Contains three disulfide bonds 3-41; 4-31; 16-27 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3985614 Arch Biochem Biophys. 1985 Apr;238(1):18-29. Vernon LP, Evett GE, Zeikus RD, Gray WR. A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence. DRAMP00962 RNCESLSHRFKGPCTRDSNC 20 Pseudothionin Solanum tuberosum 1 (Pth-St1; Plant defensin) No entry found Belongs to the thionin family Not found Solanum tuberosum (potato) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database Clavibacter michiganensis subspecies sepedonicus, Pseudomonas solanacearum and Fusarium solani. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8033886 Eur J Biochem. 1994 Jul 1;223(1):135-139. Moreno M, Segura A, Garc­a-Olmedo F. Pseudothionin-St1, a potato peptide active against potato pathogens. DRAMP00963 KSCCKNTTGRNCYNACRFAGGSRPVCATACGCKIISGPTCPRDYPK 46 Thionin BTH7 (Plant defensin) Q42838 Belongs to the thionin family Not found Hordeum vulgare (Barley) Cytotoxic Transcript level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains four disulfide bonds 3-40;4-32;12-30;16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Holtorf S, Schuetz C, Apel K, Bohlmann H. Specific and distinct expression patterns of two members of the thionin multigene family of barley in transgenic tobacco. DRAMP00964 KICCPRTIDRNIYNACRLTGASMTNCANLSGCKIVSGTTCPPGYTH 46 Thionin (Plant defensin) Q9SBK8 Belongs to the thionin family THI2 Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis) Cytotoxic Transcript level Not found Not found Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Lee S.Y, Cho M.J, Choi Y.O. Molecular cloning and characterization of flower specific thionin in Chinese cabbage. DRAMP00965 KSCCKNTTGRNCYNACHFAGGSRPVCATACGCKIISGPTCPRDYPK 46 Probable leaf thionin (Plant defensin) Q8H0Q5 Belongs to the thionin family Not found Hordeum vulgare (Barley) Cytotoxic Transcript level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Problely contains four disulfide bonds 3-40; 4-32; 12-30; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Kah B, Kogel K.H, Langen G. ORF of a leaf expressed barley thionin. DRAMP00966 KSCCKDTLARNCYNTCHFAGGSRPVCAGACRCKIISGPKCPSDYPK 46 Leaf-specific thionin DB4 (Hv-THDB4; Plant defensin) P08772 Belongs to the thionin family THI1.3 Hordeum vulgare (Barley) Cytotoxic Transcript level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Problely contains four disulfide bonds 3-40; 4-32; 12-30; 16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Mol. Gen. Genet. 207:446-454(1987) Bohlmann H, Apel K. Isolation and characterization of cDNAs coding for leaf-specific thionins closely related to the endosperm-specific hordothionin of barley (Hordeum vulgare L.). DRAMP18321 MAAFMKLIQFLATKGQKYVSLAWKRKGTILKWINAGQSFEWIYKQIKKLWA 51 Epidermicin NI01(Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Staphylococcus epidermidisstrain 224 Antimicrobial, Antibacterial, Anti-Gram+ Not found Epidermicin NI01 contains 51 residues with four tryptophan and nine lysine residues, and the sequence showed approximately 50% identity to peptides lacticin Z, lacticin Q, and aureocin A53. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22155816 Antimicrob Agents Chemother. 2012 Mar;56(3):1539-47. Sandiford S, Upton M. Identification, characterization, and recombinant expression of epidermicin NI01, a novel unmodified bacteriocin produced by Staphylococcus epidermidis that displays potent activity against Staphylococci. DRAMP01380 GLFTLIKCAYQLIAPTVACN 20 Odorranain-J1 (OdJ1; Frogs, amphibians, animals) A6MBN6 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Odorranain-J1 adopts 50.1% β-sheet and 13.7% turn structure in water solution. Function: Odorranain-J1 exhibites moderate antimicrobial activities against Gram-positive and Gram-negative bacteria and fungi. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=35.60 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=17.80 μg/ml), Bacillus subtilis (MIC=35.60 μg/ml).##Yeast: Candida albicans (MIC=8.90 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP00968 KSCCKDTLARNCYNTCRFAGGSRPVCAGACRCKIISGPKCPSDYPK 46 Leaf-specific thionin BTH6 (Plant defensin) P09618 Belongs to the thionin family Not found Hordeum vulgare (Barley) Antimicrobial, Antifungal Transcript level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains four disulfide bonds 3-40; 4-30; 12-26; 16-26." Fungi: Thievaliopsis paradoxa, Drechslera teres. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16453847##PubMed ID is not available EMBO J. 1988 Jun;7(6):1559-1565.##Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Bohlmann H, Clausen S, Behnke S, Giese H, Hiller C, Reimann-Philipp U, Schrader G, Barkholt V, Apel K.##Holtorf S, Schuetz C, Apel K, Bohlmann H. Leaf-specific thionins of barley-a novel class of cell wall proteins toxic to plant-pathogenic fungi and possibly involved in the defence mechanism of plants.##Specific and distinct expression patterns of two members of the thionin multigene family of barley in transgenic tobacco. DRAMP00969 KSCCRSTLGRNCYNLCRVRGAQKLCAGVCRCKLTSSGKCPTGFPK 45 Alpha-hordothionin (alpha-HT; Plant defensin) P01545 Belongs to the thionin family THI1.1 Hordeum vulgare (Barley) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3082629##2850969 Eur J Biochem. 1986 Apr 1;156(1):131-135.##Gene. 1988 Oct 30;70(2):271-281. Ponz F, Paz-Ares J, Hern¡ndez-Lucas C, Garc­a-Olmedo F, Carbonero P.##Rodr­guez-Palenzuela P, Pintor-Toro JA, Carbonero P, Garc­a-Olmedo F. Cloning and nucleotide sequence of a cDNA encoding the precursor of the barley toxin alpha-hordothionin.##Nucleotide sequence and endosperm-specific expression of the structural gene for the toxin alpha-hordothionin in barley (Hordeum vulgare L.). DRAMP00970 KSCCRSTLGRNCYNLCRVRGAQKLCANACRCKLTSGLKCPSSFPK 45 Beta-hordothionin (beta-HT; Plant defensin) P21742 Belongs to the thionin family THI1.2 Hordeum vulgare (Barley) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 1WUW resolved by X-ray. Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15848162 FEBS Lett. 2005 Apr 25;579(11):2301-2306. Johnson KA, Kim E, Teeter MM, Suh SW, Stec B. Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution. DRAMP00971 QKTCCPSQSTRKEFEDCISEGNLQILCSAESGCRDTYVGYCPSGFPY 47 Probable thionin-2.3 (Plant defensin) Q8VZK8, Q56XM5, Q6AWT2, Q9ZUL0 Belongs to the thionin family At2g15010 Arabidopsis thaliana (Mouse-ear cress) Cytotoxic Transcript level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Problely contains three disulfide bonds 5-41; 5-33; 17-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10617197##14593172 Nature. 1999 Dec 16;402(6763):761-768.##Science. 2003 Oct 31;302(5646):842-846. Lin X, Kaul S, Rounsley S, Shea TP, et al.##Yamada K, Lim J, Dale JM, Chen H, et al. Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.##Empirical analysis of transcriptional activity in the Arabidopsis genome. DRAMP00972 NICCPSIQARTFYNACLFAVGSPSSCIRNSSCLDISESTCPRGYTN 46 Probable thionin-2.4 (Plant defensin) Q9C8D6 Uncertain At1g66100 Arabidopsis thaliana (Mouse-ear cress) Cytotoxic Transcript level Not found Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains four disulfide bonds 3-40;4-32;16-26. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11130712##14593172 Nature. 2000 Dec 14;408(6814):816-820.##Science. 2003 Oct 31;302(5646):842-846. Theologis A, Ecker JR, Palm CJ, et al.##Yamada K, Lim J, Dale JM, et al. Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.##Empirical analysis of transcriptional activity in the Arabidopsis genome. DRAMP00973 KICCPSNQARNGYSVCRIRFSKGRCMQVSGCQNSDTCPRGWVN 43 Thionin-2.1 (Plant defensin) Q42596, Q8LCH6, Q9C7S9 Belongs to the thionin family THI2.1 Arabidopsis thaliana (Mouse-ear cress) Cytotoxic Transcript level Not found Not found "Function: Seems to function as a defense factor. Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Tissue specificity: Detected in rosette leaves and at a very high " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11130712##14593172##8552715 Nature. 2000 Dec 14;408(6814):816-820.##Science. 2003 Oct 31;302(5646):842-846.##Plant Physiol. 1995 Nov;109(3):813-820. Theologis A, Ecker JR, Palm CJ, et al.##Yamada K, Lim J, Dale JM, et al.##Epple P, Apel K, Bohlmann H. Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.##Empirical analysis of transcriptional activity in the Arabidopsis genome.##An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. DRAMP00974 KICCPTKDDRSVYFVCMLSVSSQFYCLLKSKCKNTSQTICPPGYTN 46 Thionin-2.2 (Plant defensin) Q42597, Q8LEF0, Q9FIW2 Belongs to the thionin family THI2.2 Arabidopsis thaliana (Mouse-ear cress) Cytotoxic Transcript level Bridge Not found "Function: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. PTM: Contains three disulfide bonds 3-40;4-32;16-26. Tissue specificity: Low basal expression in seedlings. Also detected in rosette leaves." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8552715##10048488 Plant Physiol. 1995 Nov;109(3):813-820.##DNA Res. 1998 Dec 31;5(6):379-391. Epple P, Apel K, Bohlmann H.##Asamizu E, Sato S, Kaneko T, Nakamura Y, Kotani H, Miyajima N, Tabata S. An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins.##Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones. DRAMP00975 RVCMKGSAGFKGLCMRDQNCAQVCLQEGWGGGNCDGVMRQCKCIRQC 47 SI alpha-2 (SIa2; Plant defensin) No entry found Not found Not found Sorghum bicolor (Seeds) Antimicrobial, Antifungal Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1995329 FEBS Lett. 1991 Feb 11;279(1):101-104. Bloch C Jr, Richardson M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins. DRAMP00976 VGECVRGRCPSGMCCSQFGYCGKGPKYCG 29 Antimicrobial peptide 1 (AC-AMP1; Plant defensin) P27275 Not found Not found Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found 1MMC "Function: Chitin-binding protein with a defensive Function: against numerous chitin containing fungal pathogens. It is also a potent inhibitor of Gram-positive bacteria. Miscellaneous: Its chitin-binding activity is strongly inhibited by divalent cations. PTM: Contains three disulfide bonds 4-15; 9-21; 14-28." Gram-positive bacteria: Bacillus megaterium (IC50=40 µg/ml), Sarcina lutea (IC50=250 µg/ml).##Fungi: Alternaria brassicola (IC50=7 µg/ml), Ascochyta pisi (IC50=8 µg/ml), Botrytis cinera (IC50=10 µg/ml), Colletotrichum lindemuthianum (IC50=8 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Trichoderma hamatum (IC50=7 µg/ml), Verticillium dahliae (IC50=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1567877##9176817 Biochemistry. 1992 May 5;31(17):4308-4314.##J Pept Res. 1997 Apr;49(4):336-340. Broekaert W.F, Marien W, Terras F.R.G, de Bolle M.F.C, Proost P, van Damme J, Dillen L, Claeys M, Rees S.B, Vanderleyden J, Cammue B.P.A.##el Bouyoussfi M, Laus G, Verheyden P, Wyns L, Tourwe D, Van Binst G. Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins.##Location of the three disulfide bonds in an antimicrobial peptide from Amaranthus caudatus using mass spectrometry. DRAMP00977 VGECVRGRCPSGMCCSQFGYCGKGPKYCGR 30 Antimicrobial peptide 2 (AC-AMP2; Plant defensin) P27275 Not found Not found Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Beta strand The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. 1MMC, 1ZNT, 1ZUV, 1ZWU resolved by NMR. "Function: Chitin-binding protein with a defensive Function: against numerous chitin containing fungal pathogens. It is also a potent inhibitor of Gram-positive bacteria. Miscellaneous: Its chitin-binding activity is strongly inhibited by divalent cations. PTM: Contains three disulfide bonds 4-15; 9-21; 14-28." Gram-positive bacteria: Bacillus megaterium (IC50=40 µg/ml), Sarcina lutea (IC50=250 µg/ml).##Fungi: Alternaria brassicola (IC50=7 µg/ml), Ascochyta pisi (IC50=8 µg/ml), Botrytis cinera (IC50=10 µg/ml), Colletotrichum lindemuthianum (IC50=8 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Trichoderma hamatum (IC50=7 µg/ml), Verticillium dahliae (IC50=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 1567877##8627629##9176817 Biochemistry. 1992 May 5;31(17):4308-4314.##J Mol Biol. 1996 May 3;258(2):322-333.##J Pept Res. 1997 Apr;49(4):336-340. Broekaert W.F, Marien W, Terras F.R.G, de Bolle M.F.C, Proost P, van Damme J, Dillen L, Claeys M, Rees S.B, Vanderleyden J, Cammue B.P.A.##Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P.##el Bouyoussfi M, Laus G, Verhey Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins.##H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. DRAMP00978 QTCASRCPRPCNAGLCCSIYGYCGSGNAYCGAGNCRCQCRG 41 Antifungal peptide 1 (EAFP1; Plant defensin) P83596 Belongs to the hevein-like family Not found Eucommia ulmoides (Hardy rubber tree) Antimicrobial, Antifungal Protein level Bridge Not found Function: Has antifungal activity. PTM: Contain five disulfide bonds 3-17; 7-37; 11-23; 16-30; 35-39, and Pyrrolidone carboxylic acid at position 1. Fungi: Phytophthora infestans, Ascochyta lycopersici (IC50=155 µg/ml), Verticillium dahliae, Gibberella zeae, Alternaria nicotianae, Fusarium moniliforme (IC50=56 µg/ml), Fusarium oxysporum (IC50=46 µg/ml) and Colletotrichum gossypii (IC50=35 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12067732 FEBS Lett. 2002 Jun 19;521(1-3):87-90. Huang R.-H, Xiang Y, Liu X.-Z, Zhang Y, Hu Z, Wang D.-C. Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv. DRAMP00979 QTCASRCPRPCNAGLCCSIYGYCGSGAAYCGAGNCRCQCRG 41 Antifungal peptide 2 (EAFP2; Plant defensin) P83597 Belongs to the hevein-like family Not found Eucommia ulmoides (Hardy rubber tree) Antimicrobial, Antifungal Protein level Combine helix and strand structure EAFP2 adopts a compact global fold composed of a 3(10) helix (Cys3-Arg6), an alpha-helix (Ala27-Cys31) and a three-stranded antiparallel beta-sheet (Cys16-Ser18, Cys23-Ser25, and Cys35-Cys37) and cross-linked by five disulfide bridges. The tertiary structure of EAFP2 shows a chitin-binding domain. 1P9G resolved by X-ray. "Function: Has antifungal activity. PTM: Contains five disulfide bonds 3-17; 7-37; 11-23; 16-30; 35-39, and Pyrrolidone carboxylic acid at position 1." Fungi: Phytophthora infestans, Ascochyta lycopersici (IC50=109 µg/ml), Verticillium dahliae, Gibberella zeae, Alternaria nicotianae, Fusarium moniliforme (IC50=18 µg/ml), Fusarium oxysporum (IC50=94 µg/ml) and Colletotrichum gossypii (IC50=56 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12067732##15363789##15147184 FEBS Lett. 2002 Jun 19;521(1-3):87-90.##J Struct Biol. 2004 Oct;148(1):86-97.##Biochemistry. 2004 May 25;43(20):6005-6012. Huang R.-H, Xiang Y, Liu X.-Z, Zhang Y, Hu Z, Wang D.-C.##Xiang Y, Huang RH, Liu XZ, Zhang Y, Wang DC.##Huang RH, Xiang Y, Tu GZ, Zhang Y, Wang DC. Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv.##Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution.##Solution structure of Eucommia antifungal peptide: a novel structural model distinct with a five-disulfide motif. DRAMP00980 AQRCGDQARGAKCPNCLCCGKYGFCGSGDAYCGAGSCQSQCRGC 44 Antimicrobial peptide 1a (WAMP-1a; Plant defensin) P85966 Belongs to the hevein-like family Not found Triticum kiharae (wheat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Not found 2LB7 resolved by NMR. PTM: Contains five disulfide bonds 4-19; 13-25; 16-44; 18-32; 37-41. Fungi: Bipolaris sorokiniana (IC50=5 µg/ml), Botrytis cinerea (IC50=20 µg/ml), Fusarium oxysporum (IC50=5 µg/ml), Fusarium solani (IC50=5 µg/ml), Fusarium verticillioides (IC50=30 µg/ml), Neurospora crassa (IC50=10 µg/ml);##Gram-positive bacterium: Clavibacter michiganensis (1.3cm inhibition for 2.5 µg/50µl);##Gram-negative bacteria: Erwinia carotovora (1.1cm for 2.5 µg/50µl), Pseudomonas syringae (0.9cm for 2.5 µg/50µl). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 19583772##16269343 FEBS J. 2009 Aug;276(15):4266-4275.##Peptides. 2005 Nov;26(11):2064-2073. Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA.##Egorov TA, Odintsova TI, Pukhalsky VA, Grishin EV. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif.##Diversity of wheat anti-microbial peptides. DRAMP00981 AQRCGDQARGAKCPNCLCCGKYGFCGSGDAYCGAGSCQSQCRGCR 45 Antimicrobial peptide 1b (WAMP-1b; Plant defensin) P85966 Belongs to the hevein-like family Not found Triticum kiharae (wheat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found 2LB7 PTM: Contains five disulfide bonds 4-19; 13-25; 16-44; 18-32; 37-41. Fungi: Bipolaris sorokiniana (IC50=5 µg/ml), Botrytis cinerea (IC50=20 µg/ml), Fusarium oxysporum (IC50=5 µg/ml), F. solani (IC50=5 µg/ml), F. verticillioides (IC50=30 µg/ml), Neurospora crassa (IC50=10 µg/ml);##Gram-positive bacterium: Clavibacter michiganensis (1.3cm inhibition for 2.5 µg/50µl);##Gram-negative bacteria: Erwinia carotovora (1.1cm for 2.5 µg/50µl), Pseudomonas syringae (0.9cm for 2.5 µg/50µl). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 19583772##16269343 FEBS J. 2009 Aug;276(15):4266-4275.##Peptides. 2005 Nov;26(11):2064-2073. Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA.##Egorov TA, Odintsova TI, Pukhalsky VA, Grishin EV. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif.##Diversity of wheat anti-microbial peptides. DRAMP00982 AQCGAQGGGATCPGGLCCSQWGWCGSTPKYCGAGCQSNCK 40 Fa-AMP1 (Fagopyrum antimicrobial peptide 1; hevein-type; Plant defensin) No entry found Belongs to the hevein-like family Not found Fagopyrum esculentum Moench (buckwheat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial avtivity against Gram-positive bacteria and Gram-negative bacteria, also has antifungal activity. Gram-positive bacteria: Clavibacter michiganensis (IC50=14 µg/ml), Curtobacterium accumfaciens (IC50=13 µg/ml);##Gram-negative bacteria: Erwinia carotovora (IC50=11 µg/ml), Agrobacterium radiobacter (IC50=24 µg/ml), Agrobacterium rhizogenes (IC50=20 µg/ml).##Fungi: Fusarium oxysporum (IC50=19 µg/ml), Geotrichum candidum (IC50=36 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12951494 Biosci Biotechnol Biochem. 2003 Aug;67(8):1636-1642. Fujimura M, Minami Y, Watanabe K, Tadera K. Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.). DRAMP00983 AQCGAQGGGATCPGGLCCSQWGWCGSTPKYCGAGCQSNCR 40 Fa-AMP2 (Fagopyrum antimicrobial peptide 2; hevein-type; Plant defensin) No entry found Belongs to the hevein-like family Not found Fagopyrum esculentum Moench (buckwheat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antibacterial avtivity against Gram-positive bacteria and Gram-negative bacteria, also has antifungal activity. Gram-positive bacteria: Clavibacter michiganensis (IC50=17 µg/ml), Curtobacterium accumfaciens (IC50=15 µg/ml);##Gram-negative bacteria: Erwinia carotovora (IC50=15 µg/ml), Agrobacterium radiobacter (IC50=17 µg/ml), Agrobacterium rhizogenes (IC50=24 µg/ml).##Fungi: Fusarium oxysporum (IC50=29 µg/ml), Geotrichum candidum (IC50=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12951494 Biosci Biotechnol Biochem. 2003 Aug;67(8):1636-1642. Fujimura M, Minami Y, Watanabe K, Tadera K. Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.). DRAMP00984 AGECVQGRCPSGMCCSQFGYCGRGPKYCGR 30 Antimicrobial peptide Ar-AMP (Ar-AMP; hevin-like peptides; Plant defensin) Q5I2B2 Belongs to the hevein-like family Not found Amaranthus retroflexus (Redroot amaranth) (Redroot pigweed) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found PTM: Contains three disulfide bonds 4-15; 9-21; 14-28. Fungi: Botrytis cinerea, Fusarium culmorum, Helminthosporium sativum and Alternaria consortiale.##Gram-positive bacterium: Bacillus subtilis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 16126239 Phytochemistry. 2005 Oct;66(20):2426-2431. Lipkin A, Anisimova V, Nikonorova A, Babakov A, Krause E, Bienert M, Grishin E, Egorov T. An antimicrobial peptide Ar-AMP from amaranth (Amaranthus retroflexus L.) seeds. DRAMP00985 QQCGRQASGRLCGNRLCCSQWGYCGSTASYCGAGCQSQCRS 41 Pn-AMP1 (PnAMP1; Plant defensin) P81591 Belongs to the hevein-like family Not found Ipomoea nil (Japanese morning glory) (Pharbitis nil) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Miscellaneous: Its antimicrobial activity is strongly inhibited by divalent cations. PTM: Contains four disulfide bonds 3-18; 12-24; 17-31; 35-39, and Pyrrolidone carboxylic acid at position 1." Gram-positive Bacterium: Bacillus subtilis (IC50=38 µg/ml).##Fungi (Medium A, Medium A+): Botrytis cinerea (IC50=16, 150 µg/ml), Colletotrichum langenarium (IC50=10, >200 µg/ml), Sclerotinia sclerotiorum (IC50=11, >200 µg/ml), Fusarium oxysporum (IC50=10, >200 µg/ml), Rhizoctonia solani (IC50=26, >200 µg/ml), Phytophthora capsici (IC50=5, 130 µg/ml), Phytophthora parasitica (IC50=3, 90 µg/ml), Saccharomyces cerevisiae (IC50=14, >200 µg/ml).##NOTE! Medium A+ = Medium A supplemented with 5 mM CaCl2. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 9507071 Biochim Biophys Acta. 1998 Jan 15;1382(1):80-90. Koo JC, Lee SY, Chun HJ, Cheong YH, Choi JS, Kawabata S, Miyagi M, Tsunasawa S, Ha KS, Bae DW, Han CD, Lee BL, Cho MJ. Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. DRAMP00986 QQCGRQASGRLCGNRLCCSQWGYCGSTASYCGAGCQSQCR 40 Pn-AMP2 (PnAMP2; Plant defensin) P81591 Belongs to the hevein-like family Not found Ipomoea nil (Japanese morning glory) (Pharbitis nil) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Miscellaneous: Its antimicrobial activity is strongly inhibited by divalent cations. PTM: Contains four disulfide bonds 3-18; 12-24; 17-31; 35-39, and Pyrrolidone carboxylic acid at position 1." Gram-positive bacterium: Bacillus subtilis (IC50=20 µg/ml).##Fungi (Medium A, Medium A+): Botrytis cinerea (IC50=2, 95 µg/ml), Colletotrichum langenarium (IC50=4, ND µg/ml), Sclerotinia sclerotiorum (IC50=3, >200 µg/ml), Fusarium oxysporum (IC50=2.5, >200 µg/ml), Rhizoctonia solani (IC50=75, >200 µg/ml), Phytophthora capsici (IC50=0.6, 150 µg/ml), Phytophthora parasitica (IC50=2, >200 µg/ml), Pythium spp. (IC50=2.5, ND µg/ml), Saccharomyces cerevisiae (IC50=8, >200 µg/ml).##NOTE! Medium A+ = Medium A supplemented with 5 mM CaCl2. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 9507071 Biochim Biophys Acta. 1998 Jan 15;1382(1):80-90. Koo JC, Lee SY, Chun HJ, Cheong YH, Choi JS, Kawabata S, Miyagi M, Tsunasawa S, Ha KS, Bae DW, Han CD, Lee BL, Cho MJ. Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. DRAMP00987 QQCGRQAGNRRCANNLCCSQYGYCGRTNEYCCTSQGCQSQCRRCG 45 Ee-CBPb (Hevein-like antimicrobial peptide; Plants) No entry found Belongs to the hevein-like family Not found Euonymus europaeus (European spindle tree) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found Not found Not found "Function: Ee-CBPb possesses a very strong antifungal activity. Besides fungi, Ee-CBP1 also inhibits the growth of Gram-positive bacteria but not that of Gram-negative bacteria and yeasts. PTM: Contains five disulfide bonds." Fungi: Alternaria brassicicola (IC50=3 µg/ml), Botrytis cinerea (IC50=1 µg/ml), Fusarium culmorum (IC50=3 µg/ml), Fusarium oxysporum f.sp.cubense (IC50=15 µg/ml), Fusarium oxysporum f.sp. Matthiolae (IC50=5 µg/ml), Mycosphaerella eumusae (IC50=6 µg/ml), Neurospora crassa (IC50=2 µg/ml), Phoma exigua (IC50=33 µg/ml), Phytophthora cryptogea (IC50=25 µg/ml), Pythium ultimum (IC50=33 µg/ml), Rhizoctonia solani (IC50=25 µg/ml).##Gram-positive bacteria: Bacillus megaterium (IC50=2 µg/ml), Sarcina lutea (IC50=7 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 15048569##12387889 Planta. 2004 Jun;219(2):221-232.##FEBS Lett. 2002 Oct 23;530(1-3):181-185. Van den Bergh KP, Roug© P, Proost P, Coosemans J, Krouglova T, Engelborghs Y, Peumans WJ, Van Damme EJ.##Van den Bergh KP, Proost P, Van Damme J, Coosemans J, Van Damme EJ, Peumans WJ. Synergistic antifungal activity of two chitin-binding proteins from spindle tree (Euonymus europaeus L.).##Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.). DRAMP00988 QQCGRQAGNRRCPNNLCCSQFGYCGRTNEYCCTGFGCQSNCRRCG 45 Ee-CBPl (Hevein-like antimicrobial peptide; Plants) No entry found Belongs to the hevein-like family Not found Euonymus europaeus (European spindle tree) Antimicrobial, Antifungal Not found Not found Not found "Function: Ee-CBP1 possesses a very strong antifungal activity. PTM: Contains Disulfide bond." Fungi: Alternaria brassicicola (IC50=0.6 µM), Botrytis cinerea (IC50=0.2 µM), Fusarium culmorum (IC50=0.6 µM), Fusarium oxysporum f. sp. cubense (IC50=3 µM), Fusarium oxysporum f. sp. matthiolae (IC50=1 µM), Mycosphaerella eumusae (IC50=1.2 µM), Neurospora crassa (IC50=0.4 µM), Phoma exigua (IC50=6.6 µM),Phytophthora cryptogea (IC50=5 µM), Pythium ultimum (IC50=6.6 µM), Rhizoctonia solani (IC50=5 µM), Trichoderma hamatum (IC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 15048569 Planta. 2004 Jun;219(2):221-232. Van den Bergh KP, Roug© P, Proost P, Coosemans J, Krouglova T, Engelborghs Y, Peumans WJ, Van Damme EJ. Synergistic antifungal activity of two chitin-binding proteins from spindle tree (Euonymus europaeus L.). DRAMP00989 EQCGRQAGGKLCPNNLCCSQWGWCGSTDEYCSPDHNCQSNCKD 43 Hevein (Hev b 6; Plants) P02877 Belongs to the hevein-like family HEV1 Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) Antimicrobial, Antifungal Protein level Combine helix and strand structure The first high-resolution solution-state structure of a member of the toxin-agglutinin folding motif with the WGA disulfide linkage is presented. 1HEV resolved by NMR.##1Q9B, 1WKX resolved by X-ray. "Function: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. Can inhibit fungal growth. PTM: Proteolytically processed to yield the two chains of the mature protein, and it Contains four disulfide bonds 3-18; 12-24; 17-31; 37-41. Allergenic properties: Causes an allergic reaction in human." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 2217194##8431421 Proc Natl Acad Sci U S A. 1990 Oct;87(19):7633-7637.##Biochemistry. 1993 Feb 16;32(6):1407-1422. Broekaert I, Lee HI, Kush A, Chua NH, Raikhel N.##Andersen NH, Cao B, Rodríguez-Romero A, Arreguin B. Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis).##Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif. DRAMP00990 KICERASGTWKGICIHSNDCNNQCVKWENAGSGSCHYQFPNYMCFCYFDC 50 Sm-AMP-D1 (Plant defensin) No entry found Not found Not found Stellaria media L (Common chickweed seeds) Antimicrobial, Antifungal Not found Not found Not found Function: Sm-AMP-D defensins displays strong antifungal activity against important plant pathogens being active at very low concentrations (IC50=1 M). Fungi: Fusarium oxysporum 16/10 (IC50=0.5 µM), Botrytis cinerea SGR-1 (IC50=0.35 µM), Bipolaris sorokiniana 6/10 (IC50=0.52 µM), Fusarium graminearum VKM F-1668 (IC50=0.52 µM), Fusarium avenaceum VKM F-2303 (IC50=1 µM), Phoma betae VKM F-2532 (IC50=0.52 µM), Pythium debaryanum VKMF-1505 (IC50=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21056078 Biochimie. 2011 Mar;93(3):450-456. Slavokhotova AA, Odintsova TI, Rogozhin EA, Musolyamov AK, Andreev YA, Grishin EV, Egorov TA. Isolation, molecular cloning and antimicrobial activity of novel defensins from common chickweed (Stellaria media L.) seeds. DRAMP00991 EQCGRQAGGKLCPNNLCCSQYGWCGSSDDYCSPSKNCQSNCKGGG 45 Pseudo-hevein (Minor hevein; hevein-like peptides; Plants) P80359 Not found Not found Hevea brasiliensis (Para rubber tree) Antimicrobial, Antifungal Protein level Bridge Not found "Function: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. Can inhibit fungal growth. PTM: Problely Contains four disulfide bonds 3-18; 12-24; 17-31; 37-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 7947977 Biochim Biophys Acta. 1994 Nov 16;1209(1):144-148. Soedjanaatmadja UM, Hofsteenge J, Jeronimus-Stratingh CM, Bruins AP, Beintema JJ. Demonstration by mass spectrometry that pseudo-hevein and hevein have ragged C-terminal sequences. DRAMP00992 KICERASGTWKGICIHSNDCNNQCVKWENAGSGSCHYQFPNYMCFCYFNC 50 Sm-AMP-D2 (Plant defensin) No entry found Not found Not found Stellaria media L (Common chickweed seeds) Antimicrobial, Antifungal Not found Not found Not found Function: Sm-AMP-D defensins displays strong antifungal activity against important plant pathogens being active at very low concentrations (IC50=1 M). Fungi: Fusarium oxysporum 16/10 (IC50=0.5 µM), Botrytis cinerea SGR-1 (IC50=0.35 µM), Bipolaris sorokiniana 6/10 (IC50=0.52 µM), Fusarium graminearum VKM F-1668 (IC50=0.52 µM), Fusarium avenaceum VKM F-2303 (IC50=1 µM), Phoma betae VKM F-2532 (IC50=0.52 µM), Pythium debaryanum VKMF-1505 (IC50=1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21056078 Biochimie. 2011 Mar;93(3):450-456. Slavokhotova AA, Odintsova TI, Rogozhin EA, Musolyamov AK, Andreev YA, Grishin EV, Egorov TA. Isolation, molecular cloning and antimicrobial activity of novel defensins from common chickweed (Stellaria media L.) seeds. DRAMP00993 QAGGQTCPGGICCSQWGYCGTTADYCSPNNNCQSNCWASG 40 WjAMP-1 (C-terminal domain of hevein; Plant defensin) No entry found Not found WjAMP-1 Wasabia japonica L. (Wasabi plant) (Wasabia japonica) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Not found Not found Not found Function: WjAMP-1 showed antimicrobial activity against both fungi and bacteria. Gram-negative bacteria: Escherichia coli (IC50=27.5 µg/ml), Pseudomonas cichorii (IC50=13.8 µg/ml), Pseudomonas glumae (IC50=20 µg/ml), Pseudomonas plantarii (IC50=22.5 µg/ml), Agrobacterium tumefaciens (IC50=12.5 µg/ml).##Fungi: Alternaria alternata (IC50=5.8 µg/ml), Botrytis cinerea (IC50=15 µg/ml), Fusarium solani (IC50=8.4 µg/ml), Magnaporte grisea (IC50=80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12668776 Plant Cell Physiol. 2003 Mar;44(3):296-303. Kiba A, Saitoh H, Nishihara M, Omiya K, Yamamura S. C-terminal domain of a hevein-like protein from Wasabia japonica has potent antimicrobial activity. DRAMP00994 QWGRRCCGWGPGRRYCVRWC 20 IB-AMP1 (IBAMP1; Basic peptide AMP1; Plants) O24006 Not found AMP Impatiens balsamina (Balsam) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Developmental stage: Highly expressed in dry mature seed and by the stages 2-5 of developing seed. The peptide IB-AMP1 is also detected at early stages of germination (24 hours and 48 hours postgermination). PTM: Contains two disulfide bonds C6-C16; C7-C2" Gram-positive bacteria: Bacillus subtilis (IC50=10 µg/ml), Micrococcus luteus (IC50=10 µg/ml), Staphylococcus aureus (IC50=30 µg/ml), Streptococcus faecalis (IC50=6 µg/ml).##Fungi: Alternaria longipes (IC50=3 µg/ml), Botrytis cinerea (IC50=12 µg/ml), Cladosporium sphaerospermum (IC50=1 µg/ml), Fusarium culmorum (IC50=1 µg/ml), Penicillium digitatum (IC50=3 µg/ml), Trichoderma viride (IC50=6 µg/ml), Verticillium alboatrum (IC50=3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9305910##9454588 J Biol Chem. 1997 Sep 26;272(39):24480-24487.##Biochemistry. 1998 Jan 27;37(4):983-990. Tailor RH, Acland DP, Attenborough S, Cammue BP, Evans IJ, Osborn RW, Ray JA, Rees SB, Broekaert WF.##Patel SU, Osborn R, Rees S, Thornton JM. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein.##Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1). DRAMP00995 QYGRRCCNWGPGRRYCKRWC 20 IB-AMP2 (IBAMP2; Basic peptide AMP2; Plants) O24006 Not found Not found Impatiens balsamina (Balsam) Antimicrobial, Antifungal Protein level Bridge Not found "Developmental stage: Highly expressed in dry mature seed and by the stages 2-5 of developing seed. PTM: Contains two disulfide bonds C6-C16; C7-C20 and Pyrrolidone carboxylic acid at position 1 (Probable)." Fungi: Alternaria longipes (IC50=12 µg/ml), Botrytis cinerea (IC50=25 µg/ml), Cladosporium sphaerospermum (IC50=6 µg/ml), Fusarium culmorum (IC50=6 µg/ml), Penicillium digitatum (IC50=6 µg/ml), Trichoderma viride (IC50=12 µg/ml), Verticillium alboatrum (IC50=12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9305910 J Biol Chem. 1997 Sep 26;272(39):24480-24487. Tailor RH, Acland DP, Attenborough S, Cammue BP, Evans IJ, Osborn RW, Ray JA, Rees SB, Broekaert WF. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein. DRAMP00996 QYRHRCCAWGPGRKYCKRWC 20 IB-AMP3 (IBAMP3; Basic peptide AMP3; Plants) O24006 Not found Not found Impatiens balsamina (Balsam) Antimicrobial, Antifungal Protein level Bridge Not found "Developmental stage: Highly expressed in dry mature seed and by the stages 2-5 of developing seed. PTM: Contains two disulfide bonds C6-C16; C7-C20 and Pyrrolidone carboxylic acid at position 1 (Probable)." Fungi: Alternaria longipes (IC50=6 µg/ml), Botrytis cinerea (IC50=6 µg/ml), Cladosporium sphaerospermum (IC50=3 µg/ml), Fusarium culmorum (IC50=6 µg/ml), Penicillium digitatum (IC50=3 µg/ml), Trichoderma viride (IC50=12 µg/ml), Verticillium alboatrum (IC50=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9305910 J Biol Chem. 1997 Sep 26;272(39):24480-24487. Tailor RH, Acland DP, Attenborough S, Cammue BP, Evans IJ, Osborn RW, Ray JA, Rees SB, Broekaert WF. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein. DRAMP00997 QWGRRCCGWGPGRRYCRRWC 20 IB-AMP4 (IBAMP4; Basic peptide AMP4; Plants) O24006 Not found Not found Impatiens balsamina (Balsam) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Developmental stage: Highly expressed in dry mature seed and by the stages 2-5 of developing seed. PTM: Contains two disulfide bonds C6-C16; C7-C20 and Pyrrolidone carboxylic acid at position 1 (Probable). Note: Peptide IB-AMP4 has a higher antifungal act Gram-positive bacteria: Bacillus subtilis (IC50=5 µg/ml), Micrococcus luteus (IC50=5 µg/ml), Staphylococcus aureus (IC50=20 µg/ml), Streptococcus faecalis (IC50=5 µg/ml);##Gram-negative bacteria: Xanthomonas campestris (IC50=6 µg/ml), Xanthomonas oryzae (IC50=15 µg/ml).##Fungi: Alternaria longipes (IC50=3 µg/ml), Botrytis cinerea (IC50=6 µg/ml), Cladosporium sphaerospermum (IC50=1 µg/ml), Fusarium culmorum (IC50=1 µg/ml), Penicillium digitatum (IC50=3 µg/ml), Trichoderma viride (IC50=6 µg/ml), Verticillium alboatrum (IC50=6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9305910##9454588 J Biol Chem. 1997 Sep 26;272(39):24480-24487.##Biochemistry. 1998 Jan 27;37(4):983-990. Tailor RH, Acland DP, Attenborough S, Cammue BP, Evans IJ, Osborn RW, Ray JA, Rees SB, Broekaert WF.##Patel SU, Osborn R, Rees S, Thornton JM. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein.##Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1). DRAMP00998 RSGRGECRRQCLRRHEGQPWETQECMRRCRRRG 33 Antimicrobial peptide MBP-1 (Maize Basic Peptide 1; Plant defensin) P28794 Not found Not found Zea mays (Maize) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Inhibitor of both bacterial and fungal growth in vitro. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Corynebacterium nebraskense ssp.##Fungi: Fusarium graminearum, Fusarium moniliforme, Aspergillus flavus, Alonina longipes, Sclerotinia sclerotiorum, Sclerotinia trifoliorum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1527010 J. Biol. Chem. 1992; 267:18814-18820 Duvick JP, Rood T, Rao AG, Marshak DR.1992 Purification and characterization of a novel antimicrobial peptide from maize (Zea mays L.) kernels. DRAMP00999 GFGCNGPWDEDDMQCHNHCKSIKGYKGGYCAKGGFVCKCY 40 Plectasin (fungal defensin) Q53I06 Not found DEF Pseudoplectania nigrella (Ebony cup) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Combine helix and strand structure Not found 1ZFU resolved by NMR. Function: Recombinant peptide is especially active against Streptococcus pneumoniae, including strains resistant to conventional antibiotics. Plectasin showes extremely low toxicity in mice, and cured them of experimental peritonitis and pneumonia caused by S. pneumoniae as efficaciously as vancomycin and penicillin. Gram-positive bacterium: Streptococcus pneumoniae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 16222292 Nature. 2005 Oct 13;437(7061):975-780. Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sönksen CP, Ludvigsen S, Ravent³s D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-J¸rgensen SG, S¸rensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. DRAMP01000 YQCGQGG 7 Ascalin (Plants) P84071 Not found Not found Allium cepa var. aggregatum (shallot) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found "Function: Has antifungal activity against Botrytis cinerea. Inhibits HIV-1 reverse transcriptase. Miscellaneous: Inhibits HIV-1 reverse transcriptase with an IC50 of 10 µM." Botrytis cinerea, HIV-1 reverse transcriptase (IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12126728 Peptides. 2002 Jun;23(6):1025-1029. Wang HX, Ng TB. Ascalin, a new anti-fungal peptide with human immunodeficiency virus type 1 reverse transcriptase-inhibiting activity from shallot bulbs. DRAMP01001 GVGYKVVVTTTAAADDDDVV 20 Arietin (Plants) P83988 Not found Not found Cicer arietinum (chickpea) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Inhibits cell-free translation in rabbit reticulocyte lysate system. Does not have mitogenic and anti-HIV-1 reverse transcriptase activities. Fungi: Botrytis cinerea, Fusarium oxysporum, Mycosphaerella arachidicola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12084511 Peptides. 2002 May;23(5):817-822. Ye XY, Ng TB, Rao PF. Cicerin and arietin, novel chickpea peptides with different antifungal potencies. DRAMP01002 RDWERREFERRQNELRREQEQRREELL 27 Alpha-benincasin (Plants) P83960 Not found Not found Benincasa hispida Antimicrobial, Antifungal Protein level Not found Not found "Function: Has weak antifungal activity toward C. comatus and P. piricola but not toward M. arachidicola. Inhibits cell-free translation in rabbit reticulocyte lysate system. Miscellaneous: IC50 of 20 pM in rabbit reticulocyte." Fungi: Coprinus comatus, Pseudocercospora piricola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12576080 Peptides. 2003 Jan;24(1):11-16. Ng TB, Parkash A, Tso WW. Purification and characterization of alpha- and beta-benincasins, arginine/glutamate-rich peptides with translation-inhibiting activity from wax gourd seeds. DRAMP01003 KTCENLADDY 10 Gymnin (Plants) P84200 Not found Not found Gymnocladus chinensis Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Exerts antifungal activity. Has weak mitogenic activity against murine splenocytes. Displays antiproliferative activity on a human hepatoma cell line and mouse leukemia cell lines. Inhibits human immunodeficiency virus-1 (HIV-1) reverse transcriptase. Fungi: Fusarium oxysporum (IC50=2 µM), Mycosphaerella arachidicola (IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499273 Peptides. 2003 Jul;24(7):963-968. Wong JH, Ng TB. Gymnin, a potent defensin-like antifungal peptide from the Yunnan bean (Gymnocladus chinensis Baill). DRAMP01005 VKSTGRADDDLAVKTKYLPP 20 Cicerarin (Plant defensin) P83986 Not found Not found Cicer arietinum (chickpea) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Has antifungal activity. Also inhibits HIV-1 reverse transcriptase. Fungi: Botrytis cinerea (IC50=20.6 µM), Mycosphaerella arachidicola (IC50=15.3 µM), Pseudocercospora piricola (IC50=8.2 µM).##Virus: HIV-1 RT (IC50=87.5 µM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12895650 Peptides. 2003 May;24(5):659-663. Chu KT, Liu KH, Ng TB. Cicerarin, a novel antifungal peptide from the green chickpea. DRAMP01006 ARCENFADSYRQPPISSSQT 20 Cicerin (Plant defensin) P83987 Not found Not found Cicer arietinum (chickpea) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Inhibits cell-free translation in rabbit reticulocyte lysate system. Fungi: Mycosphaerella arachidicola, Fusarium oxysporum, Botrytis cinerea (IC50=12 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12084511 Peptides. 2003 May;24(5):665-669. Cai YD, Liu XJ, Li YX, Xu XB, Chou KC. Cicerin and arietin, novel chickpea peptides with different antifungal potencies. DRAMP01007 MTCGQVQGNLAQCIGFLQKGGVVPPSCCTGVKNILNSSRTTADRRAVCSCLKAAAGAVRGINPNNAEALPGKCGVNIPYKISTSTNCNSIN 91 Non-specific lipid transfer peptide (LTP 1; nsLTP; Plants) P83434 Not found Not found Vigna radiata var. radiata (Mung bean) (Phaseolus aureus) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix (4 helices; 46 residues) The global fold of mung bean nsLTP1 is similar to those of the monocotyledonous nsLTP1 structures and consists of four alpha-helices stabilized by four disulfide bonds. 1SIY resolved by NMR. "Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. PTM: Contains four disulfide bonds 3-50; 13-27; 28-73; 48-87." Fungi: Fusarium solani, Fusarium oxysporum, Pythium aphanidermatum, Sclerotium rolfsii.##Gram-positive Bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 15350690##15823028 Peptides. 2004 Aug;25(8):1235-1242.##Biochemistry. 2005 Apr 19;44(15):5703-5712. Wang SY, Wu JH, Ng TB, Ye XY, Rao PF.##Lin KF, Liu YN, Hsu ST, Samuel D, Cheng CS, Bonvin AM, Lyu PC. A non-specific lipid transfer protein with antifungal and antibacterial activities from the mung bean.## Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean. DRAMP01008 SNDIYFNFQR 10 Antifungal lectin PVAP (Plant defensin) P84869 Not found Not found Phaseolus vulgaris (Kidney bean) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has hemagglutinating activity towards rabbit erythrocytes. Has antiproliferative activity towards L1210 tumor cell line with an IC50 of 3.6 µM. Miscellaneous: Antifungal, antiproliferative and hemagglutinating activity is abolished by incubatio" Fungi: Mycophaerella arachidicola (IC50=9.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16026901 Peptides. 2005 Dec;26(12):2397-2403. Xia L, Ng T.B. An antifungal protein from flageolet beans DRAMP01009 DDFLCAGGCL 10 Alliumin (Plants) P84796 Not found Not found Allium sativum (Garlic) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antifungal activity against M.arachidicola with an IC50 of 1.3 µM. Has antibacterial activity against the Gram-negative bacteria P. fluorescens. Has antiproliferative activity towards L1210 leukemia cells with an IC50 of 8.33 µM. Fungi: Mycosphaerella arachidicola (IC50=1.3 µM).##Gram-negative bacterium: Pseudomonas fluorescens. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15629528 Peptides. 2005 Feb;26(2):177-183. Xia L, Ng TB. Isolation of alliumin, a novel protein with antimicrobial and antiproliferative activities from multiple-cloved garlic bulbs. DRAMP01010 KTCENLADTFRGPCFATSNC 20 Lunatusin (Plants) No entry found Not found Not found Phaseolus lunatus L.(Chinese lima bean) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal Not found Not found Not found Function: It also inhibited proliferation in the breast cancer cell line MCF-7. Lunatusin reduced the activity of HIV-1 reverse transcriptase and it also inhibited translation in a cell-free rabbit reticulocyte lysate system. Its anti-fungal activity was Fungi: Fusarium oxysporum, Mycosphaerella arachidicola and Botrytis cinerea.##Gram-positive bacteria: Bacillus megaterium, Bacillus subtilis;##Gram-negative bacteria: Proteus vulgaris, Mycobacterium phlei. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16269344 Peptides. 2005 Nov;26(11):2086-2092. Wong JH, Ng TB. Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.). DRAMP01011 KTCENLADTFRGPCFATSNCDDHCKNKEHLLSGRCRDDFRCWCTRNC 47 White cloud bean defensin (Plant defensin) No entry found Not found Not found Phaseolus vulgaris cv. white cloud beans Antimicrobial, Antibacterial, Antifungal Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16687191 Peptides. 2006 Sep;27(9):2075-2081. Wong JH, Zhang XQ, Wang HX, Ng TB. A mitogenic defensin from white cloud beans (Phaseolus vulgaris). DRAMP01013 KTCENLADTYKGPCFTTGSCD 21 PvD1 (P. vulgaris defensin 1; Plants) F8QXP9 Not found Not found Phaseolus vulgaris (Seeds) Antimicrobial, Antifungal Predicted Bridge Not found Its activity involves membrane permeabilization, inhibition of medium acifification, and induction of ROS in fungi cells (Curr Microbiol. 2010 Dec 19. 62: 1209-1217). Fungi: Candida albicans, C. parapsilosis, Candida tropicalis, Candida guilliermondii, K. marxiannus, Saccharomyces cerevisiae, Fusarium oxysporum, F. solani, F. lateritium and R. solani. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18786582 Peptides. 2008 Dec;29(12):2090-2100. Games PD, Dos Santos IS, Mello EO, Diz MS, Carvalho AO, de Souza-Filho GA, Da Cunha M, Vasconcelos IM, Ferreira Bdos S, Gomes VM. Isolation, characterization and cloning of a cDNA encoding a new antifungal defensin from Phaseolus vulgaris L. seeds. DRAMP01014 RTCMIKKEGWGKCLIDTTCAHSCKNRGYIGGNCKGMTRTCYCLVNC 46 VrD1 (V.radiata defensin 1; Plants) No entry found Not found Not found Vigna radiata Antimicrobial, Antifungal Not found Combine helix and strand structure Not found 1TI5 resolved by NMR. Comment: No comments found on DRAMP database Fungi: Fusarium oxysporum, Pyricularia oryza, Rhizoctonia solani, Trichophyton rubrum, bruchid larva. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15080630 J Agric Food Chem 2004; 52: 2256-2261. Chen JJ et al Chen CS. Cloning and functional expression of a mungbean defensin VrD1 in Pichia pastoris. DRAMP01015 RTCMKKEGWGKCLIDTTCAHSCKNRGYIGGNCKGMTRTCYCLVNC 45 VaD1 (Plant defensin) No entry found Not found Not found Vigna angularis Kao Hsiung No.6 (Seeds) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found 1TI5 Comment: No comments found on DRAMP database Fungi: Fusarium oxysporum, Fusarium oxysporum f. sp. Pisi.##Gram-positive bacterium: Staphylococcus epidermidis;##Gram-negative bacterium: Salmonella typhimurium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15713009 J Agric Food Chem 2005; 53: 982-988. Chen G.-H. et al. Chen, C.-S. Cloning and characterization of a plant defensin VaD1 from Azuki Bean. DRAMP01019 KTCENLANTYRGPCFTTGSCDDHCKNKEHLRSGRCRDDFRCWCTRNC 47 VrD2 (Vigna radiata defensin 2; plant defensin) No entry found Not found Not found Vigna radiata Antimicrobial, Antibacterial, Antifungal Not found Combine helix and strand structure Not found 2GL1 resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Proteins 2007; 68: 530-540. Lin KF, Lee TR, Tsai PH, Hsu MP, Chen CS, Lyu PC. NMR solution structure of Vigna radiata Defensin 2 (VrD2). DRAMP01020 RVCMKGSQHHSFPCISDRLCSNECVKEEGGWTAGYCHLRYCRCQKAC 47 SIalpha1 (Plant defensin) No entry found Not found Not found Sorghum bicolor Antimicrobial, Antibacterial Not found Combine helix and strand structure Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9715910 Proteins. 1998 Aug 15;32(3):334-349. Bloch C Jr, Patel SU, Baud F, Zvelebil MJ, Carr MD, Sadler PJ, Thornton JM. 1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins. DRAMP01021 AQKCGEQGRGAKCPNCLCCGRYGFCGSTPDYCGVGCQSQCRGC 43 Antimicrobial peptide 1a (LAMP-1a; Plant defensin) P86521 Not found Not found Leymus arenarius (Lyme grass) (Elymus arenarius) Antimicrobial Protein level Bridge Not found PTM: Contains five disulfide bonds 4-19; 13-25; 16-43; 18-32; 36-40. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding PubMed ID is not available Submitted (APR-2010) to UniProtKB Odintsova TI. Unknown DRAMP01022 KGAPCAKKPCCGPLGHYKVDCSTIPDYPCCSKYGFCGSGPQYCG 44 Cy-AMP1 (Plant defensin) No entry found Not found Not found Cycas revoluta (cycad seeds) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Cy-AMP1 has antimicrobial activity against various plant-pathogenic fungi and bacteria. Gram-positive bacteria: Clavibacterium michiganensis (IC50=7.3 µg/ml), Curtobacterium flaccumfaciens (IC50=8.9 µg/ml);##Gram-negative bacteria: Agrobacterium radiobacter (IC50=8.3 µg/ml), Agrobacterium rhizogenes (IC50=8.5 µg/ml), Erwinia carobora (IC50=8.0 µg/ml).##Fungi: Fusarium oxysporum (IC50=6.0 µg/ml), Geotrichum candidum (IC50=7.4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 18778743 Peptides. 2008 Dec;29(12):2110-2117. Yokoyama S, Kato K, Koba A, Minami Y, Watanabe K, Yagi F. Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds. DRAMP01023 KGGPCAKKPCCGPLGHYKVDCSTIPDYPCCSKYGFCGSGPQYCG 44 Cy-AMP2 (Plant defensin) No entry found Not found Not found Cycas revoluta (cycad seeds) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Cy-AMP2 has antimicrobial activity against various plant-pathogenic fungi and bacteria. Gram-positive bacteria: Clavibacterium michiganensis (IC50=7.6 µg/ml), Curtobacterium flaccumfaciens (IC50=8.3 µg/ml);##Gram-negative bacteria: Agrobacterium radiobacter (IC50=7.8 µg/ml), Agrobacterium rhizogenes (IC50=8.2 µg/ml), Erwinia carobora (IC50=8.1 µg/ml).##Fungi: Fusarium oxysporum (IC50=7.1 µg/ml), Geotrichum candidum (IC50=7.0 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 18778743 Peptides. 2008 Dec;29(12):2110-2117. Yokoyama S, Kato K, Koba A, Minami Y, Watanabe K, Yagi F. Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds. DRAMP01024 AVTCNTVVSSLAPCVPFFAGSAAQPTAACCNGVRSLNSAARTTPDRRTACNCIKSSASSIGLNYNKAAKLPSRCTVNVTVPISPSVNCAT 90 Cy-AMP3 (Plant defensin) No entry found Not found Not found Cycas revoluta (cycad seeds) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Cy-AMP3 has weak antimicrobial activity against various plant-pathogenic fungi and bacteria. Gram-positive bacteria: Clavibacterium michiganensis (IC50=235 µg/ml), Curtobacterium flaccumfaciens (IC50=195 µg/ml);##Gram-negative bacteria: Agrobacterium radiobacter (IC50=260 µg/ml), Agrobacterium rhizogenes (IC50=235 µg/ml), Erwinia carobora (IC50=230 µg/ml).##Fungi: Fusarium oxysporum (IC50=250 µg/ml), Geotrichum candidum (IC50=200 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 18778743 Peptides. 2008 Dec;29(12):2110-2117. Yokoyama S, Kato K, Koba A, Minami Y, Watanabe K, Yagi F. Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds. DRAMP01025 ESEFDRQEYEECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQD 49 Vicilin-like Antimicrobial peptide 2a (MiAMP2a; Plant defensin) Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml).##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01026 DPQTDCQQCQRRCRQQESGPRQQQYCQRRCKEICEEEEEYN 41 Vicilin-like Antimicrobial peptide 2b (MiAMP2b; Plant defensin) Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2b has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01027 RQRDPQQQYEQCQKHCQRRETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEEDN 68 MiAMP2c (Gln- and Glu-rich; Plant defensin) No entry found Belongs to the vicilin-like family Not found Macadamia integrifolia (Macadamia nut) Antimicrobial, Antifungal Not found Rich Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01028 RQRDPQQQYEQCQERCQRHETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEED 67 Vicilin-like Antimicrobial peptide 2c-3 (MiAMP2c-3; Plant defensin) Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01029 RQRDPQQQYEQCQERCQRHETEPRHMQTCQQRCERRYEKEKRKQQKR 47 Vicilin-like Antimicrobial peptide 2c-2 (MiAMP2c-2; Plant defensin) Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01030 RQRDPQQQYEQCQERCQRHETEPRHMQTCQQRCERRYEKEKRKQQ 45 Vicilin-like Antimicrobial peptide 2c-1 (MiAMP2c-1; Plant defensin) Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01031 KRDPQQREYEDCRRRCEQQEPRQQYQCQRRCREQQ 35 Vicilin-like Antimicrobial peptide 2d (MiAMP2d; Plant defensin)fens Q9SPL4 Belongs to the vicilin-like family AMP2-2 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2d has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01032 DPQTECQQCQRRCRQQESDPRQQQYCQRRCKEICEEEEEYN 41 Vicilin-like Antimicrobial peptide 2b (MiAMP2b; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptides 2b has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01033 RQRDPQQQYEQCQKRCQRRETEPRHMQICQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEGD 67 Vicilin-like Antimicrobial peptide 2c-3 (MiAMP2c-3; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01034 RQRDPQQQYEQCQKRCQRRETEPRHMQICQQRCERRYEKEKRKQQKR 47 Vicilin-like Antimicrobial peptide 2c-2 (MiAMP2c-2; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01035 RQRDPQQQYEQCQKRCQRRETEPRHMQICQQRCERRYEKEKRKQQ 45 Vicilin-like Antimicrobial peptide 2c-1 (MiAMP2c-1; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01036 KRDPQQREYEDCRRHCEQQEPRLQYQCQRRCQEQQ 35 Vicilin-like Antimicrobial peptide 2d (MiAMP2d; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Antimicrobial peptides 2d has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01037 DPQTECQQCQRRCRQQESGPRQQQYCQRRCKEICEEEEEYN 41 Vicilin-like Antimicrobial peptide 2b (MiAMP2b; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2b has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01038 RQRDPQQQYEQCQKHCQRRETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEED 67 Vicilin-like Antimicrobial peptide 2c-3 (MiAMP2c-3; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01039 RQRDPQQQYEQCQKHCQRRETEPRHMQTCQQRCERRYEKEKRKQQKR 47 Vicilin-like Antimicrobial peptide 2c-2 (MiAMP2c-2; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01040 RQRDPQQQYEQCQKHCQRRETEPRHMQTCQQRCERRYEKEKRKQQ 45 Vicilin-like Antimicrobial peptide 2c-1 (MiAMP2c-1; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2c has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01041 KRDPQQREYEDCRRRCEQQEPRQQHQCQLRCREQQ 35 Vicilin-like Antimicrobial peptide 2d (MiAMP2d; Plant defensin) Q9SPL5 Belongs to the vicilin-like family AMP2-1 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antimicrobial peptides 2d has antibacterial and antifungal activity against a range of species (By similarity). Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml);##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml)##NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP01042 RHCESLSHRFKGPCTRDSNCASVCETERFSGGNCHGFRRRCFCTKPC 47 P322 (Plant defensin) No entry found Not found Not found Solanum tuberosum (potato tuber) Unknown Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Mol Biol 1988; 11:255-269. Stiekema WJ et al Louwerse JD. Molecular cloning and analysis of four potato tuber mRNAs. DRAMP01043 QICKAPSQTFPGLCFMDSSCRKYCIKEKFTGGHCSKLQRKCLCTKPC 47 TPP3 (Plant defensin) No entry found Not found Not found Lycopersicon esculentum Antimicrobial, Antifungal Not found Not found Not found 4UJ0 Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7647301 Plant Mol Biol 1995; 28:691-711. Milligan SB, Gasser CS. Nature and regulation of pistil-expressed genes in tomato. DRAMP01044 KTCENLVDTYRGPCFTTGSCDDHCKNKEHLLSGRCRDDVRCWCTRNC 47 Defensin-like protein (Clone PSAS10; Plant defensin) P18646 Not found Not found Vigna unguiculata (cowpea seeds) Antimicrobial, Antifungal Homology Bridge Not found This protein is required for germination. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2103443 Plant Mol Biol. 1990 Jul;15(1):59-64. Ishibashi N, Yamauchi D, Minamikawa T. Stored mRNA in cotyledons of Vigna unguiculata seeds: nucleotide sequence of cloned cDNA for a stored mRNA and induction of its synthesis by precocious germination. DRAMP01045 ITCGLVASKLAPCIGYLQGAPGPSAACCGGIKSLNSAAASPADRKTACTCLKSAATSMKGINYGKAASLPRQCGVSIPYAISPNTNCNAIH 91 IWF2 (Bv-LTP2; Plant defensin) No entry found Not found IWF1 Beta vulgaris (Sugar beet) Antimicrobial, Antifungal Not found Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Also has fungicide activity. Fungi: Cercospora beticola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 8790287 Plant Mol Biol. 1996 Jun;31(3):539-552. Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD. New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. DRAMP01046 GYGGHGGHGGHGGHGGHGGHGHGGGGHG 28 Shepherin I (fragement of shep-GRP; Plants) No entry found Not found GRP Capsella bursa-pastoris (shepherd's purse) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Not found Not found Circular dichroism (CD) spectra of shepherin I showes that shepherin I in 50% trifluoroethanol has 66.7% random coils, without any alpha-helices. "Function: These antimicrobial peptides exhibit antimicrobial activity against Gram-negative bacteria and fungi. Tissue specificity: Expressed in roots but not in leaves and stems." Gram-negative bacteria: Erwinia herbicola (IC50=62 µg/ml), Escherichia coli (IC50<2.5 µg/ml), Pseudomonas putida (IC50<2.5 µg/ml), Pseudomonas syringae (IC50<2.5 µg/ml), Salmonella typhimurium (IC50<2.5 µg/ml), Serratia sp. (IC50=8 µg/ml).##Fungi: Candida albicans (IC50=8 µg/ml), Cryptococcus neoformans (IC50<2.5 µg/ml), Saccharomyces cerevisiae (IC50<7 µg/ml), Alternaria alternata (IC50<7 µg/ml), Aspergillus flavus (IC50=65 µg/ml), Fusarium culmorum (IC50=72 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11117262 Plant Mol Biol. 2000 Sep;44(2):187-197. Park CJ, Park CB, Hong SS, Lee HS, Lee SY, Kim SC. Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris. DRAMP01047 GYHGGHGGHGGGYNGGGGHGGHGGGYNGGGHHGGGGHG 38 shepherin II (fragement of shep-GRP; Plants) No entry found Not found GRP Capsella bursa-pastoris (shepherd's purse) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Not found Not found Circular dichroism (CD) spectra of shepherin II showes that shepherin II in 50% trifluoroethanol has 75% random coils, without any alpha-helices. "Function: These antimicrobial peptides exhibit antimicrobial activity against Gram-negative bacteria and fungi. Tissue specificity: Expressed in roots but not in leaves and stems." Gram-negative bacteria: Erwinia herbicola (IC50=25 µg/ml), Escherichia coli (IC50<2.5 µg/ml), Pseudomonas putida (IC50<2.5 µg/ml), Pseudomonas syringae (IC50<2.5 µg/ml), Salmonella typhimurium (IC50=65 µg/ml), Serratia sp. (IC50<2.5 µg/ml).##Fungi: Candida albicans (IC50=5 µg/ml), Cryptococcus neoformans (IC50<2.5 µg/ml), Saccharomyces cerevisiae (IC50=3 µg/ml), Aspergillus flavus (IC50=60 µg/ml), Fusarium culmorum (IC50=68 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11117262 Plant Mol Biol. 2000 Sep;44(2):187-197. Park CJ, Park CB, Hong SS, Lee HS, Lee SY, Kim SC. Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris. DRAMP01048 HTPTPTPICKSRSHEYKGRCIQDMDCNAACVKESESYTGGFCNGRPPFKQCFCTKPCKRERAAATLRWPGL 71 Sd5 (sugarcane defensin 5; Plant defensin) No entry found Not found Not found Saccharum officinarum (Sugarcane) Antimicrobial, Antifungal Not found Combine helix and strand structure Based on circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy showed that the structures of these Sds were compatible with alpha/beta proteins, a feature expected for plant defensins. 2KSK resolved by NMR. Function: Sd5 is active against fungi, but not against bacteria. Fungi: Neurospora crassa and Fusarium solani (IC50=10-15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18618271 Plant Mol Biol. 2008 Nov;68(4-5):321-335. De-Paula VS, Razzera G, Medeiros L, Miyamoto CA, Almeida MS, Kurtenbach E, Almeida FC, Valente AP. Evolutionary relationship between defensins in the Poaceae family strengthened by the characterization of new sugarcane defensins. DRAMP01049 RHRHCFSQSHKFVGACLRESNCENVCKTEGFPSGECKWHGIVSKCHCKRIC 51 Sd3 (sugarcane defensin 3; Plant defensin) No entry found Not found Not found Saccharum officinarum (Sugarcane) Antimicrobial, Antifungal Not found Combine helix and strand structure Based on circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy showed that the structures of these Sds were compatible with alpha/beta proteins, a feature expected for plant defensins. Function: Sd3 is active against fungi, but not against bacteria. Fungi: Neurospora crassa and Aspergillus niger (IC50=1-3.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18618271 Plant Mol Biol. 2008 Nov;68(4-5):321-335. De-Paula VS, Razzera G, Medeiros L, Miyamoto CA, Almeida MS, Kurtenbach E, Almeida FC, Valente AP. Evolutionary relationship between defensins in the Poaceae family strengthened by the characterization of new sugarcane defensins. DRAMP01050 RYCLSQSHRFKGLCMSSSNCANVCQTENFPGGECKADGATRKCFCKKIC 49 Sd1 (sugarcane defensin 1; Plant defensin) B2CNV2 Not found PDEF Saccharum officinarum (Sugarcane) Antimicrobial, Antifungal Predicted Combine helix and strand structure Based on circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy showed that the structures of these Sds were compatible with alpha/beta proteins, a feature expected for plant defensins. Function: Sd1 is active against fungi, but not against bacteria. Fungi: Neurospora crassa, Aspergillus niger, Fusarium solani (IC50=1-2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18618271##PubMed ID is not available Plant Mol Biol. 2008 Nov;68(4-5):321-335.##Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. De-Paula VS, Razzera G, Medeiros L, Miyamoto CA, Almeida MS, Kurtenbach E, Almeida FC, Valente AP.##Padovan L, Segat L, Tossi A, Crovella S. Evolutionary relationship between defensins in the Poaceae family strengthened by the characterization of new sugarcane defensins.##Novel plant-defensin from sugarcane (Saccharum officinarum). DRAMP01051 KSTCKAESNTFPGLCITKPPCRKACLSEKFTDGKCSKILRRCICYKPC 48 NpThio1 (Plant defensin) No entry found Not found Not found Nicotiana excelsior Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Physiol 1997; 115:314. Yamada S, Komori T, Imaseki H. Unknown DRAMP01052 KDCKTESNTFPGICITKPPCRKACIKEKFTDGHCSKILRRCLCTKPC 47 NeThio2 (Plant defensin) No entry found Not found Not found Nicotiana excelsior Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Physiol 1997; 115:314. Yamada S, Komori T, Imaseki H. Unknown DRAMP01053 ATITFTNKCTRTVWPGG 17 Thaumatin-like protein (CdTLP; Plants) P84334 Not found Not found Cassia didymobotrya (Popcorn cassia) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity. Induction: By salicylic acid and by laminarin oligosaccharides. PTM: Contains one disulfide bond (By similarity)." Fungi: Candida albicans 586 (EC50=6.2 µM), Candida parapsilosis ATCC 22019 (EC50=2.2 µM), Candida krusei ATCC 14243 (EC50=2.5 µM), C. krusei 80 (EC50=5.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17056265 Plant Physiol Biochem. 2006 Oct;44(10):604-610. Vitali A, Pacini L, Bordi E, De Mori P, Pucillo L, Maras B, Botta B, Brancaccio A, Giardina B. Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture. DRAMP01054 QNICPRVNRIVTPCVAYGLGRAPIAPCCRALNDLRFVNTRNLRRAACRCLVGVVNRNPGLRRNPRFQNIPRDCRNTFVRPFWWRPRIQCGRINLTDKLIYL 105 Antimicrobial protein Ace-AMP1 (Ace-AMP1; Plant defensin) Q41258 Not found Not found Allium cepa (onion) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Bridge Not found "Function: Antifungal and antibacterial activity against the Gram-positive bacteria: B. megaterium and S. lutea. PTM: Contains four disulfide bonds 4-49; 14-26; 28-73; 47-89." Gram-positive bacteria: Bacillus megaterium, Sarcina Lutea.##Fungi (SMF-, SMF+): Alternaria brassicola (IC50=2.5, 1.5 µg/ml), Ascockyta pisi (IC50=1, 10 µg/ml), Botrytis cinerea (IC50=3, 7 µg/ml), Colletotrickum lindemutkianum (IC50=1.5, 1.5 µg/ml), Fusarium culmorum (IC50=6, 10 µg/ml), Fusarium oxysporum fsp. pisi (IC50=3.5, 4 µg/ml), Fusarium oxysporum fsp. lycopersici (IC50=3, 10 µg/ml),Nectria haematococca (IC50=3.5, 7 µg/ml),Phoma betae (IC50=1.5, 7 µg/ml), Pyrenopkora tritici-repentis (IC50=3, 3.5 µg/ml), Pyricularia oryzae (IC50=3, 7 µg/ml), Verticillium dahliae (IC50=0.25, 0.5 µg/ml).##[NOTE: SMF- = Synthetic growth Medium with low ionic strength; SMF+ = Synthetic growth Medium supplemented with with 1 mM CaCl2, 50 mM KC1] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7480341##9521681 Plant Physiol. 1995 Oct;109(2):445-455.##Biochemistry. 1998 Mar 17;37(11):3623-3637. Cammue BP, Thevissen K, Hendriks M, Eggermont K, Goderis IJ, Proost P, Van Damme J, Osborn RW, Guerbette F, Kader JC, et al.##Tassin S, Broekaert WF, Marion D, Acland DP, Ptak M, Vovelle F, Sodano P. A potent antimicrobial protein from onion seeds showing sequence homology to plant lipid transfer proteins.##Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins. DRAMP01055 AGCIKNGGRCNASAGPPYCCSSYCFQIAGQSYGVCKNR 38 P. americana AMP (Pa-AMP-1; PAFP-S; Cys-rich; Plant defensin) P81418, O82728 Belongs to the AMP family Not found Phytolacca americana (American pokeweed) (Phytolacca decandra) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Beta strand (3 strands; 13 residues) The global fold involves a cystine-knotted three-stranded antiparallel beta-sheet (residues 8-10, 23-27, 32-36), a flexible loop (residues 14-19), and four beta-reverse turns (residues 4-8, 11-14, 19-22, 28-32). This structure features all the characteristics of the knottin fold. It is the first structural model of an antifungal peptide that adopts a knottin-type structure. 1DKC resolved by NMR. "Function: Possesses antifungal activity. Tissue specificity: Seed specific. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds: 3-20; 10-24; 19-35. " Gram-positive bacteria: Bacillus megaterium (IC50=8 µg/ml), Staphyanococcus sp. (IC50=11 µg/ml).##Fungi: Alternaria panax, Fusarium sp., Rhizoctonia solani. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10759497##11551192 Plant Physiol. 2000 Apr;122(4):1015-1024.##Biochemistry. 2001 Sep 18;40(37):10973-10978. Liu Y, Luo J, Xu C, Ren F, Peng C, Wu G, Zhao J.##Gao GH, Liu W, Dai JX, Wang JF, Hu Z, Zhang Y, Wang DC. Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed.##Solution structure of PAFP-S: a new knottin-type antifungal peptide from the seeds of Phytolacca americana. DRAMP01056 ELCEKASQTWSGTCGKTKHCDDQCKSWEGAAHGACHVRDGKHMCFCYFNC 50 Ha-DEF1 (H. annuus defensin 1; Plants) No entry found Not found Not found Helianthus annuus (sunflower) Antimicrobial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Fungi: Saccharomyces cerevisiae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17375322 Planta. 2007 Aug;226(3):591-600. de Z©licourt A, Letousey P, Thoiron S, Campion C, Simoneau P, Elmorjani K, Marion D, Simier P, Delavault P. Ha-DEF1, a sunflower defensin, induces cell death in Orobanche parasitic plants. DRAMP01057 XXTKFDFFTLALQXPAXF 18 30 kDa antifungal protein (Plants) Q10722 Not found Not found Engelmannia peristenia (Engelmann's daisy) (Engelmannia pinnatifida) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity against the plant fungal pathogens. Does not have antifungal activity against the human pathogen C. albicans. Does not have ribonuclease activity. Tissue specificity: Leaves. Developmental stage: Expressed in young plants, no expression in mature plants. Miscellaneous: Resistant to heat and proteolysis. Biophysicochemical properties: Temperature dependence (Thermostable)." Fungi: Gaeumannomyces graminis, Phytophthora infestans, Phytophthora megasperma, Sclerotinia sclerotiorum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8670144 Biochem J. 1996 Jun 15;316 ( Pt 3):723-727. Huynh QK, Borgmeyer JR, Smith CE, Bell LD, Shah DM. Isolation and characterization of a 30 kDa protein with antifungal activity from leaves of Engelmannia pinnatifida. DRAMP01058 ATFDIQNKXTYTVWAAAWAPSYPGGXKQLD 30 Antifungal protein (Plants) P84061 Not found Not found Diospyros texana (Texas persimmon) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity against P. infestans. Tissue specificity: Expressed in the skin and the flesh but not the seed of the fruit. Developmental stage: Overripe fruit." Phytophthora infestans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8048935 Biochem Biophys Res Commun. 1994 Jul 29;202(2):666-672. Vu L, Huynh QK. Isolation and characterization of a 27-kDa antifungal protein from the fruits of Diospyros texana. DRAMP01059 VLSHNNESSYSDTSSCTSQ 19 Putative antimicrobial protein 1 (Plants) B3EWI5 Not found Not found Cenchritis muricatus (Beaded periwinkle) Antimicrobial Protein level Not found Not found Function: May have antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22367403 Curr Microbiol. 2012 May;64(5):501-505. López-Abarrategui C, Alba A, Lima LA, Maria-Neto S, Vasconcelos IM, Oliveira JT, Dias SC, Otero-Gonzalez AJ, Franco OL. Screening of antimicrobials from Caribbean sea animals and isolation of bactericidal proteins from the littoral mollusk Cenchritis muricatus. DRAMP01060 DLPECCSATELELDSGKQTS 20 Putative antimicrobial protein 2 (Plants) B3EWI6 Not found Not found Cenchritis muricatus (Beaded periwinkle) Antimicrobial Protein level Not found Not found Function: May have antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22367403 Curr Microbiol. 2012 May;64(5):501-505. López-Abarrategui C, Alba A, Lima LA, Maria-Neto S, Vasconcelos IM, Oliveira JT, Dias SC, Otero-Gonzalez AJ, Franco OL. Screening of antimicrobials from Caribbean sea animals and isolation of bactericidal proteins from the littoral mollusk Cenchritis muricatus. DRAMP01062 SESILIVHQQQSRSSGS 17 Putative antimicrobial protein 3 (Cm-p2; Plants) B3EWI8 Not found Not found Cenchritis muricatus (Beaded periwinkle) Antimicrobial, Antifungal Protein level Not found Not found Function: This peptide demonstrated the capacity to prevent the development of yeasts and filamentous fungi. Otherwise, Cm-p1 displayed no toxic effects against mammalian cells. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22210491 Biochimie. 2012 Apr;94(4):968-974. L³pez-Abarrategui C, Alba A, Silva ON, Reyes-Acosta O, Vasconcelos IM, Oliveira JT, Migliolo L, Costa MP, Costa CR, Silva MR, Garay HE, Dias SC, Franco OL, Otero-Gonz¡lez AJ. Functional characterization of a synthetic hydrophilic antifungal peptide derived from the marine snail Cenchritis muricatus. DRAMP01065 NSMERVEELRKKLQD 15 Chitin-binding protein HM30 (Plants) P83630 Belongs to the parathyroid hormone family Not found Hydrangea macrophylla (Bigleaf hydrangea) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity against phytopathogenic fungi. Has no chitinase or agglutination activities. Fungi: Alternria alternate, Alternaria cucumerina, Aspergillus niger, Collectotrichum gossypii, Fusarium oxysporum, F. oxysporum subsp melonis, Fusarium moniliforme, Thanatephorus cucumeris, Verticillium dahliae, Pyricularia oryzae Cav.. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 11812226 Protein Expr Purif. 2002 Feb;24(1):76-82. Yang Q, Gong ZZ. Purification and characterization of an ethylene-induced antifungal protein from leaves of Guilder rose (Hydrangea macrophylla). DRAMP01067 KQTENLADTY 10 Coccinin (Plant defensin) P84785 Belongs to the DEFL family Not found Phaseolus coccineus (Scarlet runner bean) (Phaseolus multiflorus) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Has strong antifungal activity. Inhibits the proliferation of leukemia cells in vitro. Inhibits human immunodeficiency virus-1 (HIV-1) reverse transcriptase (IC50=41 µM). Lacks mitogenic activity towards murine splenocytes. Fungi: Fusarium oxysporum (IC50=81±7 µM), Mycosphaerella arachidicola (IC50=75±5 µM), Physalospora piricola (IC50=89±4 µM), Rhizoctomia solani (IC50=134±2 µM), Botrytis cinerea (IC50=109±5 µM), Coprinus comatus (IC50=122±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15572193 Peptides. 2004 Dec;25(12):2063-2068. Ngai PH, Ng TB. Coccinin, an antifungal peptide with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from large scarlet runner beans. DRAMP01068 LNCGQVDSKMKPCLTYVQGGPGPSGECCNGVRDLHNQAQSSGDRQTVCNCLKGIARGIHNLNLNNAASIPSKCNVNVPYTISPDIDCSRIY 91 Non-specific lipid-transfer protein (Plant defensin) A8YPK3 Belongs to the plant LTP family ltp1 Hordeum vulgare (Barley) Antimicrobial Homology Not found Not found 1BE2##1JTB##1LIP##1MID##3GSH Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Niessen L. Behaviour of foam components in gushing beer. DRAMP01069 MADKGVGSRLSALFLLVLLVISIGMMQLEPAEGRTCKTPSGKFKGVCASRNNCKNVCQTEGFPSGSCDFHVANRKCYCSKPCP 83 Putative plant defensin SPI1B (Plants) Q8GTL2 Not found Not found Picea abies (Norway spruce) (Picea excelsa) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Fossdal CG. The putative gymnosperm plant defensin (SPI1) accumulates after seed germination and a related SPI1B cDNA is found in needles. DRAMP01070 AIPCGQVNSALASCVSYAKGSGASPPGACCSGVRRLAGLARSTADKQAACRCIKSAAGGLNPGKAASIPSKCGVSIPYSISASVDCSKIH 90 Non-specific lipid-transfer protein (Plants) Q1KMV1 Belongs to the plant LTP family Not found Triticum aestivum (Wheat) Antimicrobial, Antifungal Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 18257684 Mol Plant Microbe Interact. 2008 Mar;21(3):346-360. Sun JY, Gaudet DA, Lu ZX, Frick M, Puchalski B, Laroche A. Characterization and antifungal properties of wheat nonspecific lipid transfer proteins. DRAMP01071 AISCGQVASAIAPCISYARGQGSAPSAGCCSGVRSLNNAARTTADRRAACNCLKNAAAGVSGLNAGNAASIPSKCGVSIPYTISTSTDCSRVN 93 Non-specific lipid-transfer protein (Plants) Q2XX14 Belongs to the plant LTP family plt1 Zea mays subsp. parviglumis (Balsas teosinte) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16120802 Mol Biol Evol. 2005 Dec;22(12):2480-2490. Moeller DA, Tiffin P. Genetic diversity and the evolutionary history of plant immunity genes in two species of Zea. DRAMP01072 AISCGQVASAIAPCISYARGQGSGPSAGCCSGVKSLNNAARTTADRRAACNCLKNAAAGVSGLNAGNAASIPSKCGVSIPYTISTSTDCSRVN 93 Non-specific lipid-transfer protein (Plants) Q2XX25 Belongs to the plant LTP family plt1 Zea mays subsp. parviglumis (Balsas teosinte) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16120802 Mol Biol Evol. 2005 Dec;22(12):2480-2490. Moeller DA, Tiffin P. Genetic diversity and the evolutionary history of plant immunity genes in two species of Zea. DRAMP01073 AISCGQVNSALASCVSYAKGSGASPPGACCSGVRRLAGLARSTADKQAACRCIKSAAGGLNPGKAASIPSKCGVSIPYSISASVDCSKIH 90 Non-specific lipid-transfer protein (Plants) Q9FUK0 Belongs to the plant LTP family LTP1 Triticum aestivum (Wheat) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Seo Y.W, Jang C.S. Isolation and characterization of lipid transfer protein in wheat. DRAMP01074 AISCGQVNSALGPCISYARGSGANTSAACCSGVKRLAGSVRTSDDKKAACLCIKRAAGGLNPGKAADIPTKCRVTIPYKISSNVNCNNLH 90 Non-specific lipid-transfer protein (Plants) Q155V0 Belongs to the plant LTP family Not found Secale cereale (Rye) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16823370 Nat Biotechnol. 2006 Jul;24(7):852-855. Doxey AC, Yaish MW, Griffith M, McConkey BJ. Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. DRAMP01075 AISCGQVSSALSPCISYARGSGSSPPAACCSGVRSLAGAARSTADKQAACKCIKSAAGGLNAGKAAGIPSKCGVSIPYAISSSVDCSKIR 90 Non-specific lipid-transfer protein (Plants) Q1KMU9 Belongs to the plant LTP family LTP Triticum aestivum (Wheat) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 18257684 Mol Plant Microbe Interact. 2008 Mar;21(3):346-360. Sun JY, Gaudet DA, Lu ZX, Frick M, Puchalski B, Laroche A. Characterization and antifungal properties of wheat nonspecific lipid transfer proteins. DRAMP01076 AISCGQVSSALTPCVAYAKGSGTSPSGACCSGVRKLAGLARSTADKQATCRCLKSVAGGLNPNKAAGIPSKCGVSVPYTISASVDCSKIH 90 Non-specific lipid-transfer protein (Plants) Q9ATG4 Belongs to the plant LTP family LTP2 Triticum aestivum (Wheat) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Seo Y.W, Jang C.S, Bu S.Y, Kim J.B. Isolation and characterization of lipid transfer protein in wheat. DRAMP01077 AITCGQVNSAVGPCLTYARGGAGPSAACCSGVRSLKAAASSTADRRTACNCLKNAARGIKGLNAGNAASIPSKCGVSVPYTISASIDCSRVS 92 Non-specific lipid-transfer protein (Plants) Q2RBD2 Belongs to the plant LTP family Not found Oryza sativa subsp. japonica (Rice) Antimicrobial Transcript level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16188032 BMC Biol. 2005 Sep 27;3:20. Rice Chromosomes 11 and 12 Sequencing Consortia. The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications. DRAMP01078 AITCGQVSSAIAPCLSYARGTGSGPSASCCSGVRNLKSAASTAADRRAACNCLKNAARGVSGLNAGNAASIPSKCGVSIPYTISTSTDCSRVN 93 Non-specific lipid-transfer protein (Plants) O24583 Belongs to the plant LTP family Not found Zea mays (Maize) Antimicrobial Transcript level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 19936069 PLoS Genet. 2009 Nov;5(11):e1000740. Soderlund C, Descour A, Kudrna D, Bomhoff M, Boyd L, Currie J, Angelova A, Collura K, Wissotski M, Ashley E, Morrow D, Fernandes J, Walbot V, Yu Y. Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs. DRAMP01079 AITCGQVSSALSPCIPYARGNGANPSAACCSGVRRIAGAVQSTADKKTACNCIKRAAGGLNAGKAADIPSKCSVSIPYAINPSVDCSTIR 90 Non-specific lipid-transfer protein (Plants) Q155V1 Belongs to the plant LTP family Not found Secale cereale (Rye) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 16823370 Nat Biotechnol. 2006 Jul;24(7):852-855. Doxey AC, Yaish MW, Griffith M, McConkey BJ. Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. DRAMP01080 AITCGQVTHNVAPCFNYVKSGGAVPAACCKGVSNLNSMAKTTADRQQTCNCLKSAAGSIKGLNANLAAGLPGKCGVNVPYKISTSTNCNNVK 92 Non-specific lipid-transfer protein (Plants) Q4PLT5 Belongs to the plant LTP family LTP6 Fragaria ananassa (Strawberry) Antimicrobial Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Zuidmeer L, Salentijn EMJ. Cross-reactivity of a recombinant non-specific lipid transfer protein from strawberry. DRAMP01084 ILGAILPLVSGLLSNKL 17 Alyteserin-2b (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Function: Amtimicrobial peptide. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01086 ILGAILPLVSGLLSSKL 17 Alyteserin-2c (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Function: Amtimicrobial peptide. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01087 GLKDIFKAGLGSLVKNIAAHVAN 23 Alyteserin-1d (toads, amphibians, animals) No entry found Not found Not found Alytes obstetricans (European midwife toad) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Function: Amtimicrobial peptide. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19463738 Peptides. 2009 Jun;30(6):1069-1073. Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). DRAMP01092 QGRLGTQWAVGHLM 14 Alytesin (toads, amphibians, animals) P08944 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Alytes obstetricans (Common midwife toad) (Bufo obstetricans) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6141890 Comp Biochem Physiol C. 1984;77(1):99-108. Erspamer V, Erspamer GF, Mazzanti G, Endean R. Active peptides in the skins of one hundred amphibian species from Australia and Papua New Guinea. DRAMP01093 IIGPVLGLVGKPLESLLE 18 Bombinin GH-1L (bombinin H isomers; toads, amphibians, animals) No entry found Belongs to the bombinin family Not found Bombina orientalis (Oriental fire-bellied toad) Antimicrobial, Antibacterial Predicted Not found Not found "Function: Bombinins GH-1D showes only 2.5% hemolysis at 30 µM concentration. PTM: C-terminal amidation." GH-1L does not display any microbicidal activity against all the microorganisms tested. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11090921 Peptides. 2000 Nov;21(11):1673-1679. Mangoni ML, Grovale N, Giorgi A, Mignogna G, Simmaco M, Barra D. Structure-Function: relationships in bombinins H, antimicrobial peptides from Bombina skin secretions. DRAMP01095 GIGASILSAGKSALKGFAKGLAEHFAN 27 Bombinin-like peptide 2 (Contains: Bombinin H2; toads, amphibians, animals) P82286 Belongs to the bombinin family Not found Bombina variegata (Yellow-bellied toad) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Bombinin-like peptide 2 has antimicrobial activity, but no hemolytic activity. Preliminary evidence indicates that this peptide does not lyse and thus kill the bacteria by its antimicrobial activity. Bombinin H2 has antibacterial and hemolytic activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref:10333736]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10333736##223491 Biopolymers. 1998;47(6):435-450.##EMBO J. 1993 Dec;12(12):4829-4832. Simmaco M, Mignogna G, Barra D.##Mignogna G, Simmaco M, Kreil G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us?##Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. DRAMP01099 GIGAAILSAGKSIIKGLANGLAEHF 25 Bombinin-like peptide 4 (BLP-4; toads, amphibians, animals) P29005 Belongs to the bombinin family Not found Bombina orientalis (Oriental fire-bellied toad) Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix Not found "Function: Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. Tissue specificity: Expressed by the skin glands." [Ref.1744108]Gram-negative bacteria: Neisseria meningitidis, Neisseria gonorrhoeoe, Neisseria Iactamica, Neisseria cinerea. [Ref:1744108]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1744108 J Biol Chem. 1991 Dec 5;266(34):23103-23111. Gibson BW, Tang DZ, Mandrell R, Kelly M, Spindel ER. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. DRAMP01100 GIGGALLSAAKVGLKGLAKGLAEHFAN 27 Bombinin-like peptide 1 (Contains: Bombinin H; toads, amphibians, animals) P29006 Belongs to the bombinin family Not found Bombina variegata (Yellow-bellied toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antimicrobial activity, but low hemolytic activity. Preliminary evidence indicates that this peptide does not lyse and thus kill the bacteria by its antimicrobial activity. Bombinin H has antibacterial and hemolytic activity. Tissue specificity: Expressed by the skin glands." [Ref.1712299]Gram-positive bacteria: Staphylococcus species;##Gram-negative bacteria: Escherichia coli, Klebsiella pneumoniae, Enterobacter cloacae, Pseudomonas aeruginosa, Pseudomonas maltophilia, Alcaligenes denitrificans. [Ref:8223491]Has low hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1712299##8223491 Eur J Biochem. 1991 Jul 1;199(1):217-222.##EMBO J. 1993 Dec;12(12):4829-4832. Simmaco M, Barra D, Chiarini F, Noviello L, Melchiorri P, Kreil G, Richter K.##Mignogna G, Simmaco M, Kreil G, Barra D. A family of bombinin-related peptides from the skin of Bombina variegata.##Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. DRAMP01101 ILGPVLGLVGNALGGLIKNE 20 Maximin-Ht (Maximin-7; toads, amphibians, animals) P83086 Belongs to the bombinin family Not found Bombina maxima (Chinese large-webbed bell toad) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2001) to UniProtKB Chen TB, McClean S, Orr DF, Bjourson AJ, Rao PF, Shaw C. Isolation and structural characterisation of antimicrobial peptides from the venom of the Chinese large-webbed bell toad (Bombina maxima). DRAMP01102 ILGPVLSLVGNALGGLLKNE 20 Maximin-Hu (Maximin-8; toads, amphibians, animals) P83087 Belongs to the bombinin family Not found Bombina maxima (Chinese large-webbed bell toad) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11835991##PubMed ID is not available Peptides 2002; 23:427-435.##Submitted (JUL-2001) to UniProtKB. Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y.##Chen TB, McClean S, Orr DF, Bjourson AJ, Rao PF, Shaw C. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima.##Isolation and structural characterisation of antimicrobial peptides from the venom of the Chinese large-webbed bell toad (Bombina maxima). DRAMP01103 GSNKGFNFMVDMIQALSN 18 Maximin-S2 (chain of Maximins-S type B/C; toads, amphibians, animals) Q5GC92 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial Protein level Not found Not found Function: Maximin-S2 has an activity against mycoplasma but has no activity against common Gram-positive and Gram-negative bacteria nor fungi. Has no hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Asparagine amide at position 18. No MICs found in DRAMP database [Ref:15649437]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15649437 Biochem Biophys Res Commun. 2005 Feb 18;327(3):945-951. Wang T, Zhang J, Shen JH, Jin Y, Lee WH, Zhang Y. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima. DRAMP01104 GSNKGFNFMVDMINALSN 18 Maximin-S3 (chain of Maximins-S type B/C; toads, amphibians, animals) Q5GC92 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial Protein level Not found Not found Function: Maximin-S3 has an activity against mycoplasma but has no activity against common Gram-positive and Gram-negative bacteria nor fungi. Has no hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Asparagine amide at position 18. No MICs found in DRAMP database [Ref:15649437]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15649437 Biochem Biophys Res Commun. 2005 Feb 18;327(3):945-951. Wang T, Zhang J, Shen JH, Jin Y, Lee WH, Zhang Y. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima. DRAMP01106 GSNKGFNFMVDMIQALSK 18 Maximin-S5 (chain of Maximins-S type B/C; toads, amphibians, animals) Q5GC92 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial Protein level Not found Not found Function: Maximin-S3 has an activity against mycoplasma but has no activity against common Gram-positive and Gram-negative bacteria nor fungi. Has no hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Lysine amide at position 18. Mycoplasma [Ref:15649437]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15649437 Biochem Biophys Res Commun. 2005 Feb 18;327(3):945-951. Wang T, Zhang J, Shen JH, Jin Y, Lee WH, Zhang Y. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima. DRAMP01112 GIGGALLSAGKSALKGLAKGLAEHFAN 27 Maximin-11 (Maximin-6; toads, amphibians, animals) Q58T41, P83085 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: It has little hemolytic activity Yeast: Candida albicans. [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01113 GIGAKILGGVKTALKGALKELASTYVN 27 Maximin-7 (toads, amphibians, animals) Q58T58, Q58T74 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Function: It has little hemolytic activity. [Swiss_Prot Entry Q58T58]Yeast: Candida albicans [Ref:15770703]Little hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01114 GIGTKILGGLKTAVKGALKELASTYVN 27 Maximin-8 (toads, amphibians, animals) Q58T56 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Function: It has little hemolytic activity. [Ref.15770703]Yeast: Candida albicans [Ref:15770703]Little hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01115 GIGRKFLGGVKTTFRCGVKDFASKHLY 27 Maximin-9 (toads, amphibians, animals) Q58T55 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11835991 FEBS Lett. 2005 Aug 15;579(20):4443-4448 Wen-Hui Lee, Jie Zhang, Ying-Xia Zhang, Yang Jin, Ren Lai and Yun Zhang. Maximin 9, a novel free thiol containing antimicrobial peptide with antimycoplasma activity from frog Bombina maxima DRAMP01116 GIGGALLSAGKSALKGLAKGLAEHFAS 27 Maximin-10 (toads, amphibians, animals) Q58T45, Q58T39 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Maximin-10 shows antimicrobial activity against bacteria and against the fungus C. albicans. It has little hemolytic activity (By similarity). [Swiss_Prot Entry Q58T45]Yeast: Candida albicans [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01117 GIGTKIIGGLKTAVKGALKELASTYVN 27 Maximin-11 (toads, amphibians, animals) Q58T51 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01118 GIGGALLSAGKAALKGLAKGFAEHF 25 Maximin y type 2 (toads, amphibians, animals) Q58T94 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01119 GIGGALLSAGKSALKGLAKGFAEHF 25 Maximin-y (toads, amphibians, animals) Q58T91 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01120 ILGPVLSLVGSALGGLIKKI 20 Maximin-Hv (toads, amphibians, animals) Q58T91 , Q58T89 , Q58T94 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01121 ILGPVLGLVSNAIGGLIKKI 20 Maximin-Hw (toads, amphibians, animals) Q58T92 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01122 GIGGALLSAGKSALKGLAKGLVEHFAN 27 Maximin-z (toads, amphibians, animals) Q58T90 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01127 ILGPVLGLVSDTLDDVLGIL 20 Maximin-H5 (toads, amphibians, animals) Q8JHE1, Q58T54 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: A arginine mutant (i.e. 3D to 3R) was found to be HIV inhibitory (Wang G et al. 2010 Antimicrob. Agents Chemother. 54: 1343-1346). Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12127963 Biochem Biophys Res Commun 2002 Jul 26;295(4):796-799. Lai R, Liu H, Hui Lee W, Zhang Y. An anionic antimicrobial peptide from toad Bombina maxima. DRAMP01128 ILGPVIGTIGNVLGGLLKNL 20 Maximin-H6 (toads, amphibians, animals) Q58T72 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01129 ILGPVIKTIGGVIGGLLKNL 20 Maximin-H7 (toads, amphibians, animals) Q58T56 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01130 ILGPVLGLVSNALGGLLKNI 20 Maximin-H8 (toads, amphibians, animals) Q58T86, Q58T49 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01131 ILGPVLGLVSNALGGLIKKI 20 Maximin-H9 (toads, amphibians, animals) Q58T80, Q58T69 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01132 ILGPVLGLVSNALGGLLKNL 20 Maximin-H10 (toads, amphibians, animals) Q58T59 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Function: Shows strong hemolytic activity. [Swiss_Prot Entry Q58T59]Yeast: Candida albicans [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01133 ILGPVLGLVGSALGGLIKKI 20 Maximin-H11 (toads, amphibians, animals) Q58T95, Q58T65, Q58T64, Q58T48 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Function: Shows strong hemolytic activity. [Swiss_Prot Entry Q58T95]Yeast: Candida albicans [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01134 ILGPVIKTIGGVLGGLLKNL 20 Maximin-H13 (toads, amphibians, animals) Q58T58 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703 Eur J Immunol. 2005 Apr;35(4):1220-1229. Lee W.-H, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01135 LLGPVLGLVSNALGGLLKNI 20 Maximin-H12 (toads, amphibians, animals) Q58T87 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11835991##15770703 Peptides. 2002 Mar;23(3):427-435.##Eur J Immunol. 2005 Apr;35(4):1220-1229. Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y.##Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima.##Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. DRAMP01136 ILGPVLGLVGEPLGGLIKKI 20 Maximin-H14 (toads, amphibians, animals) Q58T46 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01137 ILGPVLGLVGNALGGLLKNL 20 Maximin-H15 (toads, amphibians, animals) Q58T43, Q58T39 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01138 ILGPVLSLVGNALGGLIKKI 20 Maximin-H16 (toads, amphibians, animals) Q58T93, Q58T40 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Shows strong hemolytic activity. [Swiss_Prot Entry Q58T93]Yeast: Candida albicans [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-1229.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01139 GIVDFAKKVVGGIRNALGI 19 Uperin-2.1 (toads, amphibians, animals) P82027 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Shows a medium antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Leuconostoc mesenteroides, Micrococcus luteus, Streptococcus uberis (medium antibacterial activity). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01140 GFVDLAKKVVGGIRNALGI 19 Uperin-2.2 (toads, amphibians, animals) P82028 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows a weak antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus, Leuconostoc mesenteroides, L. innocua, Micrococcus luteus, Staphylococcus aureus and Streptococcus uberis.##Gram-negative bacteria: Pasteurella haemolytica, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01141 GFFDLAKKVVGGIRNALGI 19 Uperin-2.3 (toads, amphibians, animals) P82029 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows a medium antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus, Leuconostoc mesenteroides, Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01142 GILDFAKTVVGGIRNALGI 19 Uperin-2.4 (toads, amphibians, animals) P82030 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows a weak antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus, Escherichia coli, Leuconostoc mesenteroides, L. innocua, Micrococcus luteus, Pasteurella haemolytica, Staphylococcus aureus and Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01143 GIVDFAKGVLGKIKNVLGI 19 Uperin-2.5 (toads, amphibians, animals) P82031 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows a medium antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Micrococcus luteus, Leuconostoc mesenteroides, Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01144 GILDIAKKLVGGIRNVLGI 19 Uperin-2.6 (toads, amphibians, animals) P82095 Not found Not found Uperoleia mjobergii (Australian toadlet) Unknown Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996;49:1325-1331. Bradford A.M, Bowie J.H, Tyler M.J, Wallace J.C. New antibiotic uperin peptides from the dorsal glands of the australian toadlet Uperoleia mjobergii. DRAMP01145 GIIDIAKKLVGGIRNVLGI 19 Uperin-2.7 (toads, amphibians, animals) P82039 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01146 GILDVAKTLVGKLRNVLGI 19 Uperin-2.8 (toads, amphibians, animals) P82040 Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus, Lactococcus lactis, Staphylococcus epidermidis, Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01147 GVLDAFRKIATVVKNVV 17 Uperin-3.1 (toads, amphibians, animals) P82032 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows a medium antibacterial activity. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Staphylococcus aureus, Leuconostoc mesenteroides. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01148 GVLDAFRKIATVVKNLV 17 Uperin-3.2 (toads, amphibians, animals) P82033 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01149 GVLDAFKKIATVVKNLV 17 Uperin-3.3 (toads, amphibians, animals) P82034 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01150 GVGDLIRKAVAAIKNIV 17 Uperin-3.4 (toads, amphibians, animals) P82041 Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01156 GVGDIFRKIVSTIKNVV 17 Uperin-3.7 (toads, amphibians, animals) P82044 Not found Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01157 GVGSFIHKVVSAIKNVA 17 Uperin-4.1 (toads, amphibians, animals) P82035 Not found Not found Uperoleia inundata (Floodplain toadlet) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows a medium antibacterial activity against L. mesenteriodes. PTM: Alanine amide at position 17." Gram-positive bacterium: Leuconostoc mesenteroides. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01158 FQFVNPSDIVFGS 13 Uperin-5.1 (toads, amphibians, animals) P82036 Not found Not found Uperoleia inundata (Floodplain toadlet) Unknown Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01159 GLAGAISSALDKLKQSQLIKNYAKKLGYPR 30 Uperin-6.1 (toads, amphibians, animals) P82037 Not found Not found Uperoleia inundata (Floodplain toadlet) Unknown Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01160 GLAGAISSVLDKLKQSQLIKNYAKKLGYPR 30 Uperin-6.2 (toads, amphibians, animals) P82038 Not found Not found Uperoleia inundata (Floodplain toadlet) Unknown Protein level Not found Not found "Function: Amphibian defense peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1996; 49:475-484. Bradford AM, Raftery MJ, Bowie JH, Tyler MJ, Wallace JC, Adams GW, Severini C. Novel uperin peptides from the dorsal glands of the australian floodplain toadlet Uperoleia inundata. DRAMP01161 GWFDVVKHIASAV 13 Uperin-7.1 (Frogs, amphibians, animals) P82050 Not found Not found Litoria ewingi (Brown tree frog) (Ewing's tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Antiviral Protein level Not found Not found "Function: Uperin 7.1 shows antibacterial activity against L. lactis. Uperin 7.1.1 is inactive. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Streptococcus uberis, Lactococcus lactis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Aust. J. Chem. 1997; 50:889-894. Steinborner ST, Bowie JH, Tyler MJ, Wallace JC. An unusual combination of peptides from the skin glands of Ewing's tree frog, Litoria ewingi. Sequence determination and antimicrobial activity. DRAMP01166 FLPMLAKLLSGFLGK 15 Preprotemporin-1SKd (Frogs, amphibians, animals) No entry found Not found Not found Rana sakuraii (Japanese brown frog) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP01168 RAEAVPPGFTPFRKP 15 Ranakinin-N (bradykinin-like peptide; Frogs, amphibians, animals) P86093 Belongs to the bradykinin family Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17994619 J Pept Sci. 2008 May;14(5):626-630. Liu X, You D, Chen L, Wang X, Zhang K, Lai R. A novel bradykinin-like peptide from skin secretions of the frog, Rana nigrovittata. DRAMP01169 ENREVPPGFTALIKTLRKCKII 22 Distinctin 1 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa distincta (Tree frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database Note: Distinctin chain 1 links to Distinctin chain 2 to form a heterodimeric peptide to exert antibacterial function. ##Gram-positive bacteria: Enterococcus faecalis (MIC=14.5 µM), Staphylococcus aureus (MIC=28.0 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=28.0 µM), Escherichia coli (MIC=14.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free "There is an intermolecular disulphide bridge between Distinctin chain 1 (Cys19) and Distinctin chain 2 (Cys22). There is an intermolecular disulphide bridge between Distinctin chain 1 (Cys19) and Distinctin chain 2 (Cys22)." L No cytotoxicity information found Not found 19189273 J Pept Sci. 2009 Apr;15(4):278-284. Vidovic V, Prongidi-Fix L, Bechinger B, Werten S. Production and isotope labeling of antimicrobial peptides in Escherichia coli by means of a novel fusion partner that enables high-yield insoluble expression and fast purification. DRAMP01171 GVVDILKGAGKDLLAHLVGKISEKV 25 Ocellatin-1 (Frogs, amphibians, animals) P83951 Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes and antibacterial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin dorsal glands." [Swiss_Prot Entry P83951]Gram-negative bacterium: Escherichia coli [Ref:15648972]Show hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15648972 Protein J. 2004 Nov;23(8):501-508. Nascimento AC, Zanotta LC, Kyaw CM, Schwartz EN, Schwartz CA, Sebben A, Sousa MV, Fontes W, Castro MS. Ocellatins: new antimicrobial peptides from the skin secretion of the South American frog Leptodactylus ocellatus (Anura: Leptodactylidae). DRAMP01172 GVLDIFKDAAKQILAHAAEKQI 22 Ocellatin-2 (Frogs, amphibians, animals) P83866 Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes and antibacterial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin dorsal glands." [Swiss_Prot Entry P83866]Gram-negative bacterium: Escherichia coli [Ref:15648972]Show hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15648972 Protein J. 2004 Nov;23(8):501-508. Nascimento AC, Zanotta LC, Kyaw CM, Schwartz EN, Schwartz CA, Sebben A, Sousa MV, Fontes W, Castro MS. Ocellatins: new antimicrobial peptides from the skin secretion of the South American frog Leptodactylus ocellatus (Anura: Leptodactylidae). DRAMP01173 GVLDILKNAAKNILAHAAEQI 21 Ocellatin-3 (Frogs, amphibians, animals) P83867 Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes and antibacterial activity against the Gram-negative bacterium E. coli. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." [Swiss_Prot Entry P83867]Gram-negative bacterium: Escherichia coli [Ref:15648972]Show hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15648972 Protein J. 2004 Nov;23(8):501-508. Nascimento AC, Zanotta LC, Kyaw CM, Schwartz EN, Schwartz CA, Sebben A, Sousa MV, Fontes W, Castro MS. Ocellatins: new antimicrobial peptides from the skin secretion of the South American frog Leptodactylus ocellatus (Anura: Leptodactylidae). DRAMP01175 AVLDILKDVGKGLLSHFMEKV 21 Ocellatin-5 (Frogs, amphibians, animals) P85443 Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic and antibacterial activities. Tissue specificity: Expressed by the skin dorsal glands." [Ref.19739090]Gram-postive bacterium: Staphylococcus aureus(100% inhibition at 64μg/mL);##Gram-negative bacterium: Escherichia coli(100% inhibition at 32μg/mL). [Ref:19739090]Show hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19739090## J Exp Zool A Ecol Genet Physiol. 2010 Jan 1;313(1):1-8.##Thesis (2007), University of Brasilia, Brazil Leite JM Jr, Silva LP, Silva-Leite RR, Ferrari AS, Noronha SE, Silva HR, Bloch C Jr, Leite JR.##Nascimento A.C.C. Leptodactylus ocellatus (Amphibia): mechanism of defense in the skin and molecular phylogenetic relationships.##Cytolytic peptides and proteases from the skin secretion of the frog Leptodactylus ocellatus). DRAMP01176 AVLDFIKAAGKGLVTNIMEKVG 22 Ocellatin-6 (Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19739090 J Exp Zool A Ecol Genet Physiol. 2010 Jan 1;313(1):1-8. Leite JM Jr, Silva LP, Silva-Leite RR, Ferrari AS, Noronha SE, Silva HR, Bloch C Jr, Leite JR. Leptodactylus ocellatus (Amphibia): mechanism of defense in the skin and molecular phylogenetic relationships. DRAMP01178 GVVDILKGAAKDLAGHLASKVMNKI 25 Ocellatin-K1 (Frogs, amphibians, animals) P86711 Not found Not found Leptodactylus knudseni (Knudsen's thin-toed frog) (Amazonian toad-frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Isoleucine amide at position 25. [Swiss_Prot Entry P86711]show antibacterial activity No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2010) to UniProtKB Cardozo-Filho J.L, Soares A.A, Bloch C. Jr, Silva L.P, Stabeli R.G, Calderon L.A. Identification of peptides from Amazonian Leptodactylus knudseni skin secretion by MALDI TOF/TOF. DRAMP01179 GVVDILKGAGKDLLAHALSKLSEKV 25 Ocellatin-V1 (Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus validus Garman (Caribbean frog) Antimicrobial, Antibacterial Not found Not found Not found Function: The very low antimicrobial potency (MIC>200 µM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18501993 Peptides. 2008 Aug;29(8):1287-1292. King JD, Leprince J, Vaudry H, Coquet L, Jouenne T, Conlon JM. Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae). DRAMP01180 GVLDILKGAGKDLLAHALSKISEKV 25 Ocellatin-V2 (Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus validus Garman (Caribbean frog) Antimicrobial, Antibacterial Not found Not found Not found Function: The very low antimicrobial potency (MIC>200 µM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18501993 Peptides. 2008 Aug;29(8):1287-1292. King JD, Leprince J, Vaudry H, Coquet L, Jouenne T, Conlon JM. Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae). DRAMP01181 GVLDILTGAGKDLLAHALSKLSEKV 25 Ocellatin-V3 (Frogs, amphibians, animals) No entry found Not found Not found Leptodactylus validus Garman (Caribbean frog) Antimicrobial, Antibacterial Not found Not found Not found Function: The very low antimicrobial potency (MIC>200 µM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18501993 Peptides. 2008 Aug;29(8):1287-1292. King JD, Leprince J, Vaudry H, Coquet L, Jouenne T, Conlon JM. Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae). DRAMP01183 GVLDILKGAAKDLAGHVATKVINKI 25 Syphaxin (SPX; Frogs, amphibians, animals) P85279 Not found Not found Leptodactylus syphax (Burgundy thin-toed frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has hemolytic and antibacterial activity. PTM: Isoleucine amide at position 25. Tissue specificity: Expressed by the skin dorsal glands. [Swiss_Prot Entry P85279]show antibacterial activity [Ref:17628627]Show hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17628627 Toxicon. 2007 Sep 15;50(4):572-580. Dourado F.S, Leite J.R.S.A, Silva L.P, Melo J.A.T, Bloch C. Jr, Schwartz E.F. Antimicrobial peptide from the skin secretion of the frog Leptodactylus syphax. DRAMP01186 IGVIKLSLCEEERNADEEKRRDDPDEMDVEVEKR 34 Chensinin-1CEb (Frogs, amphibians, animals) No entry found Not found Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Function: Has moderate antimicrobial activity against microorganisms. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21303203 Zoolog Sci. 2011 Feb;28(2):112-117. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01187 FTLKKSQLLLFFLGTINFSLCEEERNAEEERRDYPEEKDVEVEKR 45 Chensinin-3CE (Frogs, amphibians, animals) No entry found Not found Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Function: Has moderate antimicrobial activity against microorganisms. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21303203 Zoolog Sci. 2011 Feb;28(2):112-117. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01193 FLPKLFAGIISKNF 14 Andersonin-Y2 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi. No MICs found in DRAMP database [Ref:22029824]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01196 KEKLKLKCKAPKCYNDKLACT 21 Andersonin-G1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi and has no hemolytic activity under the test conditions. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>200 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC>200 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>200 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC>200 µg/ml). [Ref:22029824]Non-hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01197 ENMFNIKSSVESDSFWG 17 Andersonin-N1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi and has no hemolytic activity under the test conditions. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>200 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC>200 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>200 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC>200 µg/ml). [Ref:22029824]Non-hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01198 EMLKKKKEVKMERKT 15 Andersonin-Q1 (Frogs, amphibians, animals) No entry found Not found Not found Odorrana andersonii (Golden crossband frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Weakly active against bacteria and fungi and has no hemolytic activity under the test conditions. [Ref.22029824]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>200 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC>200 µg/ml);##Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC>200 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC>200 µg/ml). [Ref:22029824]Non-hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01205 GLFDIIKNIVSTL 13 Dahlein-1.1 (Frogs, amphibians, animals) P84273 Not found Not found Litoria dahlii (Dahl's aquatic frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Weak wide spectrum antimicrobial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11555873 Rapid Commun Mass Spectrom. 2001;15(18):1726-1734. Wegener KL, Brinkworth CS, Bowie JH, Wallace JC, Tyler MJ. Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry. DRAMP01206 GLFDIIKNIFSGL 13 Dahlein-1.2 (Frogs, amphibians, animals) P84263 Not found Not found Litoria dahlii (Dahl's aquatic frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Weak wide spectrum antimicrobial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11555873 Rapid Commun Mass Spectrom. 2001;15(18):1726-1734. Wegener KL, Brinkworth CS, Bowie JH, Wallace JC, Tyler MJ. Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry. DRAMP01207 CYSAAKYPGFQEFINRKYKSSRF 23 Galensin (Frogs, amphibians, animals) Q90W78 Not found Not found Kassina senegalensis (Senegal running frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against the Gram-positive bacteria: M. luteus and the Gram-negative bacteria E. coli. Tissue specificity: Expressed by the skin dorsal glands." Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Reid C.N, Bjourson A.J, Shaw C. Galensin, a novel homodimeric antimicrobial peptide from the defensive skin secretion of Kassina senegalensis: isolation, structural characterisation and cloning of precursor cDNA. DRAMP01210 MFTLKKTLLLLFFLGTINLSLCKEERDADEERRDDPDKRDVEVEKRFLSGILKLAFKIPSVLCAVLKNC 69 Pleurain-D1 antimicrobial peptide (Frogs, amphibians, animals) B5L1C2 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-583. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP01211 MFTLKKTLLLLFFLGTINLSLCKEERDADEERRDDPDKRDVEVEKRFLSGILKLASKIPSVLCAVLKNC 69 Pleurain-D2 antimicrobial peptide (Frogs, amphibians, animals) B5L1D6 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-583. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP01212 SIITMTREAKLPQLWKQIACRLYNTC 26 Pleurain-A3 (Pleurain A3; Frogs, amphibians, animals) A8B5P7 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Has little hemolytic activity on red blood cells. Tissue specificity: Expressed by the skin dorsal glands." [Swiss_Prot Entry A8B5P7]has activity against Gram-positive and -negative bacteria, and fungi [Ref:17764786]Little hemolytic activity on red blood cells even with peptide concentration up to 200 μg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17764786 Peptides. 2007 Oct;28(10):2069-2074. Wang X, Song Y, Li J, Liu H, Xu X, Lai R, Zhang K. A new family of antimicrobial peptides from skin secretions of Rana pleuraden. DRAMP01213 SIITTTKEAKLPQLWKQIACRLYNTC 26 Pleurain-A4 (Pleurain A4; Frogs, amphibians, animals) A8B5Q0 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Has little hemolytic activity on red blood cells. Tissue specificity: Expressed by the skin dorsal glands." [Swiss_Prot Entry A8B5Q0]has activity against Gram-positive and -negative bacteria, and fungi [Ref:17764786]Little hemolytic activity on red blood cells even with peptide concentration up to 200 μg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17764786 Peptides. 2007 Oct;28(10):2069-2074. Wang X, Song Y, Li J, Liu H, Xu X, Lai R, Zhang K. A new family of antimicrobial peptides from skin secretions of Rana pleuraden. DRAMP01215 FFGAIAAALPHVISAIKNAL 20 Kassinatuerin-2Mb (Frogs, amphibians, animals) No entry found Not found Not found Kassina maculata (African hyperoliid frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Alpha helix Secondary structure prediction analysis revealed that virtually the entire structure of each kassinatuerin-2 related peptide is composed of alpha-helix, the helix was not amphipathic like many other amphibian skin antimicrobial peptides, in which there is a hydrophobic face and a positively charged faces the latter presumably interacting with the negatively charged glycocalyx of cell membranes. Function: Has relatively potent growth inhibitory activity against the Gram-positive bacterium, S. aureus, but were ineffective against the Gram-negative bacterium, E. coli and were relatively ineffective against the pathogenic yeast, C. albicans. Has hemolytic activity as demonstrated using horse erythrocytes. [Ref.19427345]Gram-positive bacterium: Staphylococcus aureus [Ref:19427345]18% hemolytic activity at 16 μM, 45–50% hemolytic activity at 120 μM against horse erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19427345 Peptides. 2009 Aug;30(8):1428-1433. Wang L, Zhou M, McGrath S, Chen T, Gorman SP, Walker B, Shaw C. A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata. DRAMP01216 FVGAIAAALPHVISAIKNAL 20 Kassinatuerin-2Mc (Frogs, amphibians, animals) No entry found Not found Not found Kassina maculata (African hyperoliid frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Alpha helix Secondary structure prediction analysis revealed that virtually the entire structure of each kassinatuerin-2 related peptide is composed of alpha-helix, the helix was not amphipathic like many other amphibian skin antimicrobial peptides, in which there is a hydrophobic face and a positively charged faces the latter presumably interacting with the negatively charged glycocalyx of cell membranes. Function: Has relatively potent growth inhibitory activity against the Gram-positive bacterium, S. aureus, but were ineffective against the Gram-negative bacterium, E. coli and were relatively ineffective against the pathogenic yeast, C. albicans. Has hemolytic activity as demonstrated using horse erythrocytes. [Ref.19427345]Gram-positive bacterium: Staphylococcus aureus [Ref:19427345]18% hemolytic activity at 16 μM, 45–50% hemolytic activity at 120 μM against horse erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19427345 Peptides. 2009 Aug;30(8):1428-1433. Wang L, Zhou M, McGrath S, Chen T, Gorman SP, Walker B, Shaw C. A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata. DRAMP01217 IIGAIAAALPHVINAIKNTF 20 Kassinatuerin-2Md (Frogs, amphibians, animals) No entry found Not found Not found Kassina maculata (African hyperoliid frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Alpha helix Secondary structure prediction analysis revealed that virtually the entire structure of each kassinatuerin-2 related peptide is composed of alpha-helix, the helix was not amphipathic like many other amphibian skin antimicrobial peptides, in which there is a hydrophobic face and a positively charged faces the latter presumably interacting with the negatively charged glycocalyx of cell membranes. Function: Has relatively potent growth inhibitory activity against the Gram-positive bacterium, S. aureus, but were ineffective against the Gram-negative bacterium, E. coli and were relatively ineffective against the pathogenic yeast, C. albicans. Has hemolytic activity as demonstrated using horse erythrocytes. [Ref.19427345]Gram-positive bacterium: Staphylococcus aureus [Ref:19427345]18% hemolytic activity at 16 μM, 45–50% hemolytic activity at 120 μM against horse erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19427345 Peptides. 2009 Aug;30(8):1428-1433. Wang L, Zhou M, McGrath S, Chen T, Gorman SP, Walker B, Shaw C. A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata. DRAMP18320 SASIVKTTIKASKKLCRGFTLTCGCHFTGKK 31 Epilancin 15X(Bacteriocin) P86047 Belongs to the lantibiotics family (Class I bacteriocin) Not found Staphylococcus epidermidis 15X154 Antimicrobial, Antibacterial, Anti-Gram+ Non helix or strand structure The peptide was found to highly resemble the previously identified epilancin K7 with 68% sequence identity, three nearly identical lanthionine rings and a modified amino acid at the N-terminus. The C-terminal B and C rings of epilancin 15X are structurally similar to the D and E rings of nisin A that are believed to be involved in pore formation. 1W9N resolved by NMR The compound contains an unusual N-terminal D-lactate group that could be essential for biological activity. This study demonstrates that this moiety confers stability against proteolytic degradation by aminopeptidases. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15792796##21802007 FEBS Lett. 2005 Mar 28;579(9):1917-22.##Chem Biol. 2011 Jul 29;18(7):857-67. Ekkelenkamp MB, Hanssen M, Danny Hsu ST, de Jong A, Milatovic D, Verhoef J, van Nuland NA.##Vel Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis.##Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate. DRAMP01223 GFMDTAKQVAKNVAVTLIDKLRCKVTGGC 29 Palustrin-2AJ2 (PL2AJ12; Frogs, amphibians, animals) G3F828 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Displays broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria. Has low hemolytic activity, low cytotoxicity and low antioxidant activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 23-29 and Cleavage on pair of basic residues." [Swiss_Prot Entry G3F828]broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria [Ref:21816202]Show slight hemolytic activity against human and rabbit erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21816202 Biochimie. 2012 Feb;94(2):328-334. Chen Z, Yang X, Liu Z, Zeng L, Lee W, Zhang Y. Two novel families of antimicrobial peptides from skin secretions of the Chinese torrent frog, Amolops jingdongensis. DRAMP01225 GIFPKIIGKGIVNGIKSLAKGVGMKVFKAGLNNIGNTGCNNRDEC 45 Palustrin-3AR (Frogs, amphibians, animals) No entry found Not found Not found Rana areolata (North American crawfish frog) Antimicrobial, Antibacterial, Antiviral Not found Not found Not found This peptide could inhibit HIV infection at a concentration that is also toxic to T cells (J Virol 2005; 79:11598-11606). No MICs found in DRAMP database [Ref:12429503] HC50=200 µM against human erythrocytes Cyclic Free Cyclization (Cys39 and Cys45) Disulfide bond between Cys39 and Cys45. L No cytotoxicity information found Not found 12429503 Biochim Biophys Acta. 2002 Nov 19;1601(1):55-63. Ali MF, Lips KR, Knoop FC, Fritzsch B, Miller C, Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. DRAMP01226 ALFSILRGLKKLGKMGQAFVNCEIYKKC 28 Palustrin-1a (Frogs, amphibians, animals) P84274 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01230 GFLSTVKNLATNVAGTVLDTIRCKVTGGCRP 31 Palustrin-2a (Frogs, amphibians, animals) P84278 Not found Not found Rana palustris (Pickerel frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Tissue specificity: Expressed by the skin glands. Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Basir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01236 GLWDSIKNFGKTIALNVMDKIKCKIGGGCPP 31 Palustrin-2CE (Frogs, amphibians, animals) No entry found Not found Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21303203 Zoolog Sci. 2011 Feb;28(2):112-117. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01239 GLWNTIKEAGKKFAINVLDKIRCGIAGGCKT 31 Palustrin-2CG1 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Aug 19. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01240 MFTMKKSPLVLFFLGIVSLSLCQEERSADDEEGEVIEEEVKRGFWDTIKQAGKKFFLNVLDKIRCKVAGGCRT 73 Palustrin-OG1 antimicrobial peptide (Frogs, amphibians, animals) A6MBT7 Not found Not found Odorrana grahami (Yunnanfu frog) Unknown Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01241 IGTISLSLCEQERDADEDEGETLEE 25 Palustrin-RA2 antimicrobial peptide (Frogs, amphibians, animals) D2K8I5 Not found Not found Rana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases Yang X, Liang X, Zhang Y, Lee WH. The highest antimicrobial peptide diversity, skin antimicrobial peptide peptidomics of amphibian, Rana andersonii. DRAMP01242 MFTLKKTLFLVFFLGMVSLSLCEQERHAHEETSNDPTEEENAAGNEESGEEGDMEKRFLLFPLMCKIQGKC 71 Japonicin-1Npa (Frogs, amphibians, animals) D0ES73 Not found Not found Nanorana parkeri Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20153801 Biochimie. 2010 May;92(5):475-481. Lu Z, Zhai L, Wang H, Che Q, Wang D, Feng F, Zhao Z, Yu H. Novel families of antimicrobial peptides with multiple functions from skin of Xizang plateau frog, Nanorana parkeri. DRAMP01243 MFTLKKSLFLVFFLGMVSLALCRHERHAHEESSNDPTEEENAAGNEESGEEGDMEKRFVLPLVMCKILRKC 71 Japonicin-1Npb (Frogs, amphibians, animals) D0ES74 Not found Not found Nanorana parkeri Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20153801 Biochimie. 2010 May;92(5):475-481. Lu Z, Zhai L, Wang H, Che Q, Wang D, Feng F, Zhao Z, Yu H. Novel families of antimicrobial peptides with multiple functions from skin of Xizang plateau frog, Nanorana parkeri. DRAMP01247 MFTLKKPLLLLFFLGTINLSLCQDETNAEEERRDEEVAKMEEIKRGLLSGILGAGKHIVCGLTGCAKA 68 OGG1 antimicrobial peptide (Frogs, amphibians, animals) B5L181 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP01256 SAVGRHSRRFGLRKHRKH 18 Dybowskin-2CDYb (Frogs, amphibians, animals) B5A9T0 Not found Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antimicrobial active against Gram-negative bacteria and Gram-negative bacteria. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01262 RPPGFSPFR 9 Bradykinin (Frogs, amphibians, animals) P86627 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet May target bradykinin receptors (BDKRB) 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01263 RPPGFSPF 8 Des-Arg-bradykinin (Frogs, amphibians, animals) P86628 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01264 RPPGFTPFR 9 [Thr6]-bradykinin (Frogs, amphibians, animals) P86629 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01265 RPPGFTPF 8 Des-Arg-[Thr6]-bradykinin (Frogs, amphibians, animals) P86630 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01266 RPPGFSPFRIY 11 Phyllokinin (Frogs, amphibians, animals) P86631 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01267 RPPGFTPFRIY 11 [Thr6]-Phyllokinin (Frogs, amphibians, animals) P86632 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle, Amphibian defense peptide. Tissue specificity: Expressed by the skin glands. Note: Sequence uncertainty at position 10 (I or L)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01268 QEYRGWMDF 9 [Arg4]-Phyllocaerulein (Frogs, amphibians, animals) P86625 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: Pyrrolidone carboxylic acid at Q1 and Phenylalanine amide at F9." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01269 YAFGYPS 7 Dermorphin (Frogs, amphibians, animals) P86633 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: D-amino acid (D-alanine) at A2 and Amidation (Serine amide) at S7. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01270 YMFHLMD 7 [D-Met2]-deltorphin (Frogs, amphibians, animals) P86634 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: D-amino acid (D-methionine) at M2 and Amidation (Aspartic acid 1-amide) at D7. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP18404 INWLKLGKMVIDAL 14 Polybia-MPII (mastoparan; insects, arthropods, invertebrates, animals) No entry found Not found Not found venom, the social wasp, Pseudopolybia vespiceps testacea Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Fuction: It demonstrated a potent ability to suppress endotoxin lipopolysaccharide (LPS)-mediated induction of the pro-inflammatory cytokine TNF-a in human peripheral blood mononuclear cells by 94%. It also completely protected mice against an invasive S. aureus infection when given I.P. to mice at 8 mg/kg 4 hr prior to initiation of the infection. Surface immobilization led to enhanced antimicrobial activity against P. aeruginosa. Gram-positive bacteria: S. aureus(MIC 2.3 ug/ml);##Gram-negative bacteria: P. aeruginosa (MIC 9 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28108242 Int J Antimicrob Agents. 2017 Feb;49(2):167-175. 2017 Silva JC, Neto LM, Neves RC, Gon?alves JC, Trentini MM, Mucury-Filho R, Smidt KS, Fensterseifer IC, Silva ON, Lima LD, Clissa PB, Vilela N, Guilhelmelli F, Silva LP, Rangel M, Kipnis A, Silva-Pereira I, Franco OL, Junqueira-Kipnis AP, Bocca AL, Mortari MR. Evaluation of the antimicrobial activity of the mastoparan Polybia-MPII isolated from venom of the social wasp Pseudopolybia vespiceps testacea (Vespidae, Hymenoptera) DRAMP18403 VKGSWSKKFEVIA 13 Tridecaptin A1 (TriA1; lipopeptides; nonribosomally synthesized peptide antibiotic) No entry found Not found Not found Paenibacillus terrae; old: Bacillus circulans NRRL B-30644 Antimicrobial, Antibacterial Nonhelixbeta Not found 2N5Y There are three D-type 2,4-diaminobutyrate (Dab), represented by K's here. In addition, residue V1, S4, W5, and I12 are also D-amino acids. Active against Gram+ B. subtilis JH642 (MIC 50 uM), S. aureus ATCC 25923 (100 uM), Gram- food pathogens C. jejuni NCTC 11168 (MIC 100 uM), E. coli DH5alpha (MIC 50 uM), and Salmonella enterica serovar Typhimurium (25 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24382692 Chembiochem. 2014 Jan 24;15(2):243-9. Lohans CT1, van Belkum MJ, Cochrane SA, Huang Z, Sit CS, McMullen LM, Vederas JC. Biochemical, structural, and genetic characterization of tridecaptin A?, an antagonist of Campylobacter jejuni. DRAMP18402 GKGSWSKKIEVIA 13 Tridecaptin B1 (TriB1; lipopeptides; nonribosomally synthesized peptide antibiotic, Gram-positive No entry found Not found Not found Paenibacillus polymyxa NRRL B-30507 Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Comment: No comments found on DRAMP database Active against multidrug resistant Gram-negative bacteria. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25959079 Org Biomol Chem. 2015 Jun 7;13(21):6073-81. doi: 10.1039/c5ob00780a. Cochrane SA, Lohans CT, van Belkum MJ, Bels MA, Vederas JC. Studies on tridecaptin B(1), a lipopeptide with activity against multidrug resistant Gram-negative bacteria DRAMP18401 ILSAIWSGIKGLL 13 Uy17 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Urodacus yaschenkoi Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against M. luteus (MIC 15 uM), S. aureus (30 uM), and L. monocytogenes (MIC 15 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28067810 Toxins (Basel). 2017 Jan 6;9, 22. doi: 10.3390/toxins9010022. Luna-Ramirez K, Tonk M, Rahnamaeian M, Vilcinskas A. Bioactivity of Natural and Engineered Antimicrobial Peptides from Venom of the Scorpions Urodacus yaschenkoi and U. manicatus DRAMP01275 FLSLIPHIVSGVASIAKHFG 20 Phylloseptin-s1 (Frogs, amphibians, animals) F7UI84 Not found preproPLS-S1 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Abbassi F, Galanth C, Piesse C, Nicolas P, Amiche M, Ladram A. Phylloseptins from phyllomedusa sauvagei. DRAMP01276 FLSLIPHIVSGVASLAKHFG 20 Phylloseptin-s2 (Frogs, amphibians, animals) F7UI85 Not found preproPLS-S2 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Abbassi F, Galanth C, Piesse C, Nicolas P, Amiche M, Ladram A. Phylloseptins from phyllomedusa sauvagei. DRAMP01277 FLSLIPHIVSGVASLAIHFG 20 Phylloseptin-s3 (Frogs, amphibians, animals) F7UI86 Not found preproPLS-S3 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Abbassi F, Galanth C, Piesse C, Nicolas P, Amiche M, Ladram A. Phylloseptins from phyllomedusa sauvagei. DRAMP18319 ITSHSLCTPGCAKTGSFNSFCC 22 BsaA2(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Staphylococcus aureus strain 26 Antimicrobial, Antibacterial, Anti-Gram+ Bridge Tandem MS analysis identified two sequence tags (Dhb-PGCAK/Q-Dhb-G and I/L-Dhb-Dha-H [due to the use of CID, Dha/Dhb represents either a dehydrated amino acid or a site of thioether bridge cleavage]) that matched the deduced amino acid sequence of BsaA2.Thioether bonds between residues 3 and 7, 8-11, 16-21, and 19-22. This bacteriocin is identical to staphylococcin Au-26 initially reported in 1992. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20023032 J Bacteriol. 2010 Feb;192(4):1131-42. Daly KM, Upton M, Sandiford SK, Draper LA, Wescombe PA, Jack RW, O'Connor PM, Rossney A, G?tz F, Hill C, Cotter PD, Ross RP, Tagg JR. Production of the Bsa lantibiotic by community-acquired Staphylococcus aureus strains. DRAMP01279 FLISIPYSASIGGTATLTGTA 21 Phylloseptin Bu-1 (Frogs, amphibians, animals) P86282 Not found Not found Phyllomedusa burmeisteri (Brazilian common walking leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. Tissue specificity: Expressed by the skin glands. PTM: Alanine amide at A21." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2009) to UniProtKB Conceicao K, Klitzke C.F, Brito R.C, Andrade D.F, Junca F.A, Biondi I, Lopes-Ferreira M. Identification of peptides from Phyllomedusa burmesteri skin secretomics by nano LC MS/MS. DRAMP01280 FLLSLPHLASGLASLVLSK 19 Phylloseptin Bu-2 (Frogs, amphibians, animals) P86283 Not found Not found Phyllomedusa burmeisteri (Brazilian common walking leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. Tissue specificity: Expressed by the skin glands. PTM: Lysine amide at L19." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2009) to UniProtKB Conceicao K, Klitzke C.F, Brito R.C, Andrade D.F, Junca F.A, Biondi I, Lopes-Ferreira M. Identification of peptides from Phyllomedusa burmesteri skin secretomics by nano LC MS/MS. DRAMP01281 FLSLIPHAINAISAIANHF 19 Phylloseptin-J1 (PLS-J1; PS-J1; Frogs, amphibians, animals) P86614 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01282 FLSLIPHAINAISAIADHF 19 Phylloseptin-J2 (PLS-J2; PS-J2; Frogs, amphibians, animals) P86615 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01283 FLSLIPHAINAISAIANHL 19 Phylloseptin-J3 (PLS-J3; PS-J3; Frogs, amphibians, animals) P86616 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1979) (Anura, Hylidae, Phyllomedusinae). DRAMP01284 FLSLIPHAINAISAIAHHL 19 Phylloseptin-J4 (PLS-J4; PS-J4; Frogs, amphibians, animals) P86617 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1980) (Anura, Hylidae, Phyllomedusinae). DRAMP01285 FLSLIPHAISAISAIAHHL 19 Phylloseptin-J5 (PLS-J5; PS-J5; Frogs, amphibians, animals) P86618 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1980) (Anura, Hylidae, Phyllomedusinae). DRAMP01286 FLSLIPHAISAISAIANHL 19 Phylloseptin-J6 (PLS-J6; PS-J6; Frogs, amphibians, animals) P86619 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1980) (Anura, Hylidae, Phyllomedusinae). DRAMP01287 FLSLIPHAISAISAIADHL 19 Phylloseptin-J7 (PLS-J7; PS-J7; Frogs, amphibians, animals) P86620 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1980) (Anura, Hylidae, Phyllomedusinae). DRAMP01289 FLSLIPKIAGGIASLVKNL 19 Phylloseptin-1 (PStar 01; Frogs, amphibians, animals) P84929 Not found Not found Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01290 FLSLIPHIATGIAALAKHL 19 Phylloseptin-2 (PStar 02; Frogs, amphibians, animals) P84930 Not found Not found Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01291 FFSMIPKIATGIASLVKNL 19 Phylloseptin-3 (PStar 03; Frogs, amphibians, animals) P84931 Not found Not found Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01292 FLSLIPHAINAVSTLVHHSG 20 Phylloseptin-4 (PS-4; Frogs, amphibians, animals) P84569 Not found psn4 Phyllomedusa oreades (Orange-legged leaf frog) (Monkey frog) Antiprotozoal Protein level Not found Not found "Function: Has antiprotozoal activity against Trypanosoma cruzi. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Trypanosoma cruzi (IC50=5.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752569 Peptides. 2005 Apr;26(4):565-573. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. DRAMP01293 FLSLIPHAINAVSAIAKHS 19 Phylloseptin-5 (PS-5; Frogs, amphibians, animals) P84570 Not found psn5 Phyllomedusa oreades (Orange-legged leaf frog) (Monkey frog) Antiprotozoal Protein level Not found Not found "Function: Has antiprotozoal activity against Trypanosoma cruzi. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Trypanosoma cruzi (IC50=4.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752569 Peptides. 2005 Apr;26(4):565-573. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. DRAMP01294 FPPWL 5 Tryptophyllin-5.1 (Frogs, amphibians, animals) P84573 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defense peptide. May have antimicriobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Nat. Chem. Biol. 0:0-0(2007) Silva LP, Brand GD, Bloch C Jr. High-throughput imaging co-localization of peptides and proteins. DRAMP01295 NLVSALIEGRKYLKNVLKKLNRLKEKNKAKNSKENN 36 Distinctin-like peptide (Frogs, amphibians, animals) Q17UZ0 Belongs to the frog skin active peptide family ppdis-H1 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Thesis (2006), University of Ulster Coleraine, United Kingdom Thompson AH. A genomic/proteomic approach to isolating and identifying bioactive peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP18400 FLSTIWNGIKGLL 13 Uy192 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Urodacus yaschenkoi Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against M. luteus (MIC 15 uM), E. coli (15 uM), S. aureus (15 uM), L. grayi (15 uM), L. fleischmannii (MIC 4 uM), and L. monocytogenes (MIC 4 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28067810 Toxins (Basel). 2017 Jan 6;9, 22. doi: 10.3390/toxins9010022. Luna-Ramirez K, Tonk M, Rahnamaeian M, Vilcinskas A. Bioactivity of Natural and Engineered Antimicrobial Peptides from Venom of the Scorpions Urodacus yaschenkoi and U. manicatus DRAMP18399 FPFLLSLIPSAISAIKRL 18 Uy234 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Urodacus yaschenkoi Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against M. luteus (MIC 2 uM), L. grayi (MIC 4 uM), and L. monocytogenes (MIC 8 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28067810 Toxins (Basel). 2017 Jan 6;9, 22. doi: 10.3390/toxins9010022. Luna-Ramirez K, Tonk M, Rahnamaeian M, Vilcinskas A. Bioactivity of Natural and Engineered Antimicrobial Peptides from Venom of the Scorpions Urodacus yaschenkoi and U. manicatus DRAMP01298 FRPALIVRTKGK 12 Hyposin-J1 (HPS-J1; Frogs, amphibians, animals) P86613 Not found Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. PTM: Lysine amide at K12." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01299 FRPALIVRTKGTRL 14 Hyposin-HA4 (Hyposin-4; Frogs, amphibians, animals) P84957 Not found Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP01300 LRPAVIVRTKGK 12 Hyposin-HA3 (Hyposin-3; Frogs, amphibians, animals) P84956 Not found Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP01304 SLIPHAINAVSAIAKHF 17 Phylloseptin-6 (PS-6; Frogs, amphibians, animals) P84571 Not found psn6 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752569 Peptides. 2005 Apr;26(4):565-573. Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. DRAMP01307 FLSLIPTAINAVSALAKHF 19 Phylloseptin-8 (PS-8; Frogs, amphibians, animals) P85883 Not found psn-8 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01308 FLSLIPHAINAVSALAKHF 19 Phylloseptin-8 (PS-8; Frogs, amphibians, animals) P85447 Not found Not found Phyllomedusa tomopterna (Tiger-striped leaf frog) (Pithecopus tomopternus) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (FEB-2008) to UniProtKB de sa Mandel S.M, Mundim N.C.C.R, Freitas T, Silva L.P, Bloch C. Jr. Dermaseptins and phylloseptins of Phyllomedusa (Hylidae) secretion. DRAMP18318 ITSFIGCTPGCGKTGSFNSFCC 22 BacCH91(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) bacCH91 Staphylococcus aureus CH-91 Antimicrobial, Antibacterial, Anti-Gram+ Not found Similar to Gallidermin and epidermin. The fourth residue was phenylalanine in BacCH91 but lysine in both epidermin and gallidermin, which explains the more hydrophobic character of BacCH91. The bacteriocin was not affected by any of the staphylococcal peptidases tested, particularly StpC. BacCH91 was unaffected by trypsin and proteinase K. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23196985 Appl Microbiol Biotechnol. 2013 Aug;97(16):7229-39. Wladyka B, Wielebska K, Wloka M, Bochenska O, Dubin G, Dubin A, Mak P. Isolation, biochemical characterization, and cloning of a bacteriocin from the poultry-associated Staphylococcus aureus strain CH-91. DRAMP01310 FLGLLPSIVSGAVSLVKKL 19 Phylloseptin-9 (PS-9; Frogs, amphibians, animals) Q0VZ38, P84905 Not found psn-9 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16713656 Peptides. 2006 Sep;27(9):2129-2136. Chen T, Zhou M, Gagliardo R, Walker B, Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. DRAMP01311 FLSLLPSLVSGAVSLVKKL 19 Phylloseptin-10 (PS-10; Frogs, amphibians, animals) Q0VZ39, P84906 Not found psn-10 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16713656 Peptides. 2006 Sep;27(9):2129-2136. Chen T, Zhou M, Gagliardo R, Walker B, Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. DRAMP01312 FLSLLPSLVSGAVSLVKIL 19 Phylloseptin-11 (PS-11; Frogs, amphibians, animals) Q0VZ40 Not found psn-11 Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16713656 Peptides. 2006 Sep;27(9):2129-2136. Chen T, Zhou M, Gagliardo R, Walker B, Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. DRAMP01313 FLSLIPHAINAVSALVHHF 19 Phylloseptin-12 (PS-12; Frogs, amphibians, animals) P84904 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2006) to UniProtKB Silva L.P, Brand G.D, Bloch C. Jr. High-throughput co-localization of peptides and proteins by imaging mass spectrometry. DRAMP01315 FLSLIPHAINAVGVHAKHF 19 Phylloseptin 13 (PS-13; Frogs, amphibians, animals) P84938 Not found psn13 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01316 FLSLIPAAISAVSALADHF 19 Phylloseptin 14 (PS-14; Frogs, amphibians, animals) P84939 Not found psn14 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01317 LLSLVPHAINAVSAIAKHF 19 Phylloseptin 15 (PS-15; Frogs, amphibians, animals) Q0VKG9, P84940 Not found psn15 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17553595 Peptides. 2007 Jul;28(7):1331-1343. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01318 LRPAVIVRTKAL 12 Antimicrobial peptide 1 (Frogs, amphibians, animals) P84524 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium M. luteus. Tissue specificity: Expressed by the venom gland." Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2005) to UniProtKB. Thompson A.H. Antimicrobial peptides derived from the venom of the South American tree frog, Phyllomedusa hypochondrialis. DRAMP01321 MFTLKKSLLLLFFLGTINLSLCEQERNAEEERRDDLGERQAEVEKRFFPIVGKLLSG 57 Amolopin-n1 antimicrobial peptide (Frogs, amphibians, animals) C5H0E2 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01322 FTMKKSLLLLFFLGTINLSLCEQERNAEEERRDDLGERQAEVEKR 45 Amolopin-n2 antimicrobial peptide (Frogs, amphibians, animals) C5H3Z4 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Transcript level Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide from Amolops loloensis. DRAMP01323 MFTMKKSLLLLFFLGTIHLSLCEQERNAEEERRDDLGERQAEVEKRFLPIAGKLLSGLSGLLGK 64 Amolopin-2e antimicrobial peptide (Frogs, amphibians, animals) C5H0D6 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01324 MFTLKKSLLLLFFLGTINLSLCEQERNAEEERRDEPDERNAEVEKRFFPIVGKLLFGLSGLLGK 64 Amolopin-2f antimicrobial peptide (Frogs, amphibians, animals) C5H0D7 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01325 MFTLKKSLLLLFFLGTINLSLCEQERNAEEERRDEPDERNAEVEKRFFPIVGKLLSGLSGLLGK 64 Amolopin-2g antimicrobial peptide (Frogs, amphibians, animals) C5H0D8 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01326 MFTLKKSLLLLFFLGTINLSLCEQERNAEEERRDDLGERQAEVEKRFFPIVGKLLFGLFGLLGK 64 Amolopin-2h antimicrobial peptide (Frogs, amphibians, animals) C5H0D9 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01327 MFPLKKSLLLLFFLATINLSLCEQERNAEEERRDEPDERNAEVEKRFFPIVGKLLSGLLGK 61 Amolopin-2i antimicrobial peptide (Frogs, amphibians, animals) C5H0E0 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01328 MFTLKKSLLLLFFLATINLSFCEQERNAEEERRDEPDERNAEVEKRFFPIVGKLLFGLLGK 61 Amolopin-2k antimicrobial peptide (Frogs, amphibians, animals) C5H0E1 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01329 MFTMKKSLLLLFFLGAISLSLCEQERDADEEETEGGAKVETVKRASVPPGFTPFRVAPEIV 61 Amolopin-5a antimicrobial peptide (Frogs, amphibians, animals) C5H0C9 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01330 MFTMKKSLLLLFFLGMISLSLCKQERDANEERRDDPDENEENGGEAKVEEIKRAARPPLGCKAAFC 66 Amolopin-6a antimicrobial peptide (Frogs, amphibians, animals) C5H0D0 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01331 MFTMKKSLLLLFFLGMISLSLCKQERDANEERRDDPDENEENGGEAKVEEIKRAARPPLRCKAAFC 66 Amolopin-6b antimicrobial peptide (Frogs, amphibians, animals) C5H0D1 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01332 MFTMKKSLLLLFFLGAISLSLCEQERDADEEDGGEVTEEEVKRAAFRGCWTKNYSPKPCLGKR 63 Amolopin-7a antimicrobial peptide (Frogs, amphibians, animals) C5H0D2 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01333 MFTMKKSLLLLFFLGMISLSLCKQERDANEERRDDPDENEENGGEAKVEEIQRGARPPLRCKAALC 66 Amolopin-8a antimicrobial peptide (Frogs, amphibians, animals) C5H0D3 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01334 MFTLKKSMLLLFFLGTISLSLCEEERNADEDDGEKEVKRGIFALIKTAAKFVGKNLLKQAGKAGLEHLACKANNQC 76 Amolopin-9a antimicrobial peptide (Frogs, amphibians, animals) C5H0D4 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01335 MFTMKKSLLLLFFLGTISLSLCEEERSADEDDGEKGVKRGIFSLIKTAAKFVGKNLLKQAGKAGVEHLACKANNQC 76 Amolopin-9b antimicrobial peptide (Frogs, amphibians, animals) C5H0D5 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19843479 Comp Biochem Physiol B Biochem Mol Biol. 2010 Jan;155(1):72-76. Wang M, Wang Y, Wang A, Song Y, Ma D, Yang H, Ma Y, Lai R. Five novel antimicrobial peptides from skin secretions of the frog, Amolops loloensis. DRAMP01336 NILSSIVNGINRALSFFG 18 Amolopin-p1 C5H0C7 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: defense response to bacterium. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01337 NVLSSVANGINRALSFFG 18 Amolopin-p2 C5H0C8 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. Wang A, Lai R. cDNA Cloning of a Novel Antimicrobial Peptide From the Skin of Amolops loloensis. DRAMP01338 FLPMLAGLAANFLPKLFCKITKKC 24 Amolopin-1a (Frogs, amphibians, animals) A0SN41, A0SN38, A0SN39 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus, Bacillus dysenteriae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01340 FLPPSPWKETFRTT 14 Amolopin-3a (Frogs, amphibians, animals) A6XFB5 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. Lai R, Liang J. No title found DRAMP01342 FLPIVGKLLSGLL 13 Amolopin-2b (Frogs, amphibians, animals) A0SN47, A0SN48 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus, Bacillus dysenteriae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01343 FLPMLAGLAANLLPKLFCKITKKC 24 Amolopin-1c (Frogs, amphibians, animals) A0SN43 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus, Bacillus dysenteriae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01344 LLPIVGKLLSGLL 13 Amolopin-2c (Frogs, amphibians, animals) A0SN50 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus, Bacillus dysenteriae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17000029 Peptides 2006; 27: 3085-3091. Lu Y et al Lai R2006 Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis DRAMP01345 FLPMLAGLAANFLPELFCKITKKC 24 Amolopin-1d (Frogs, amphibians, animals) A0SN44 Not found Not found Amolops loloensis (Rufous-spotted torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Has antibacterial against Gram-positive and Gram-negative bacteria. Also has antifungal activity against C. albicans. Gram-positive bacteria: Staphylococcus aureus, Bacillus dysenteriae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17000029 Peptides. 2006 Dec;27(12):3085-3091. Lu Y, Li J, Yu H, Xu X, Liang J, Tian Y, Ma D, Lin G, Huang G, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. DRAMP01348 RVCSAIPLPICH 12 Tigerinin-RC1 (Frogs, amphibians, animals) C7ENH5 Not found Not found Fejervarya cancrivora (crab-eating frog) Not found Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. Lu Y, Song Y, Wang L, Yang H, Zhang K, Lai R. Purification, characterization and cloning of two novel tigerinin-like peptides from skin secretions of Fejervarya cancrivora. DRAMP01349 RVCMAIPLPLCH 12 Tigerinin-RC2 (Frogs, amphibians, animals) C7ENH6 Not found Not found Fejervarya cancrivora (crab-eating frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. Lu Y, Song Y, Wang L, Yang H, Zhang K, Lai R. Purification, characterization and cloning of two novel tigerinin-like peptides from skin secretions of Fejervarya cancrivora. DRAMP01388 GFSPNLPGKGLRIS 14 Odorranain-R1 (OdR1; Frogs, amphibians, animals) A6MBR8 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antifungal Transcript level Not found Not found Function: Odorranain-R1 appears to be narrowly antifungal with low potency against Candida albicans. [Ref.17272268] Yeast: Candida albicans (MIC=50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01363 GFLDKLKKGASDFANALVNSIKGT 24 Frenatin-4 (Frogs, amphibians, animals) P82023 Not found Not found Litoria infrafrenata (Giant tree frog) (White-lipped tree frog) Antimicrobial Protein level Not found Not found "Function: Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." Wide spectrum antimicrobial peptide. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9225251 J Pept Sci. 1996 Mar-Apr;2(2):117-124. Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata. DRAMP01365 GLFGVLAKVASHVVPAIAEHFQA 23 Maculatin-1.2 (Frogs, amphibians, animals) P82067 Not found Not found Litoria genimaculata (Green-eyed tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows antibacterial activity against S. aureus and S. uberis. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." Gram-positive bacteria: Staphylococcus aureus, Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9620615 J Pept Sci. 1998 Apr;4(2):111-115. Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC. The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1. DRAMP01366 GLLGLLGSVVSHVVPAIVGHF 21 Maculatin-1.3 (frog, amphibia, animals) No entry found Not found Not found Litoria eucnemis (Australian anurans) Antimicrobial, Antibacterial, Antiviral Not found Not found Not found Function: Has antiviral activity. The peptide is HIV inhibitory (EC50=4 µM). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15203252 Peptides. 2004; 25: 1035-1054. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01369 GLLQTIKEKLESLESLAKGIVSGIQA 26 Maculatin-3.1 (Frogs, amphibians, animals) P82069 Not found Not found Litoria genimaculata (brown-spotted treefrog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Shows antibacterial activity against S. uberis. Tissue specificity: Expressed by the skin dorsal glands. PTM: C-terminal amidation." Gram-positive bacterium: Streptococcus uberis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9620615 J Pept Sci. 1998 Apr;4(2):111-115. Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC. The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1. DRAMP01379 GFFTLIKAANKLINKTVNKEAGKGGLEIMA 30 Odorranain-I1 (OdI1; Frogs, amphibians, animals) No entry found Not found Not found Rana grahami (Yunnanfu frog) (Huia grahami) Antimicrobial Homology Not found Not found Function: Found no antimicrobial activity against the tested microbes and also has no hemolytic activity against red cell. [Ref.17272268]Not detectable activity [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01382 VEVQVRDKGKGIYGLSPLRQPAP 23 Odorranain-L1 (OdL1; Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Function: Found no antimicrobial activity against the tested microbes and also has no hemolytic activity against red cell. [Ref.17272268]Not detectable activity [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01385 AVPLIYNRPGIYVTKRPKGK 20 Odorranain-O1 (OdO1; Frogs, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Function: Found no antimicrobial activity against the tested microbes and also has no hemolytic activity against red cell. [Ref.17272268]Not detectable activity [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01404 GLFTFIKCAYKLRAPAVAC 19 Odorranain-J2 antimicrobial peptide (Frogs, amphibians, animals) A6MBN7 Not found Not found Odorrana grahami (Yunnanfu frog ) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01405 GVLGTVKNLLIGAGKSAAQSVLKTLSCKLFNDC 33 Odorranain-C6 antimicrobial peptide (Frogs, amphibians, animals) A6MBF3, A6MBK2 Not found Not found Odorrana grahami (Yunnanfu frog ) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01406 AVPLIYNRPGIYAPKRPKGK 20 Antimicrobial peptide odorranain-O3 (Frogs, amphibians, animals) C3RTI0 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Ma Y, Lai R, Wu J, Li J. Antimicrobial peptide from skin of Odorrana grahami. DRAMP01407 MFTLKKSLFVLFFLGIVSLSVCEHNRDADEEDGGEAIGGEVRRAALKGCWTKSIPPKPCSGKR 63 Antimicrobial peptide odorranain B4 (Frogs, amphibians, animals) D0PRC0 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Ma Y, Li J. No title found on DRAMP DRAMP01408 MFTLKKSLLVLFFLGIVSLSVCEHNRDADEEDGGEVTGEEVKRAALKGCWTNSIPPKPCSGKR 63 Antimicrobial peptide odorranain B5 (Frogs, amphibians, animals) D0PRC1 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Ma Y, Li J. No title found on DRAMP DRAMP18317 MGAVIKVGAKVIGWGAASGAGLYGLEKILKK 31 Aureocin A70 (AurD)(Bacteriocin) Q93GF8 Belongs to the class II bacteriocin aurD Staphylococcus aureus A70 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Aureocin A70 is a multipeptide bacteriocin composed of four related peptides that are small (30-31 amino acid residues), strongly cationic (pI of 9.85 to 10.04) and highly hydrophobic. These peptides also have a high content of small amino acid residues like glycine (23 Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11531330 J Mol Biol. 2001 Aug 31;311(5):939-49. Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. DRAMP01425 GLLSGVLGVGKKVDCGLSGLC 21 Nigrocin-OG21 (frog, amphibians, animals) No entry found Not found Not found Odorrana grahami (Yunnanfu frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Showes an effect on HIV when applied in combination with OdK1. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01444 GLLDSIKGMAISAGKGALQNLLKVASCKLDKTC 33 Nigrocin-1 (Frogs, amphibians, animals) P0C008 Not found Not found Pelophylax nigromaculatus (Black-spotted frog) (Rana nigromaculata) (frog skin active peptide) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Has weak hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Contains one disulfide bond 27-33. (By similarity)" [Ref.11682065]Gram-positive bacterium: Micrococcus luteus(MIC=2.5μg/ml);##Gram-negative bacteria: Shigella dysenteriae(MIC=10μg/ml), Klebsiella pneumoniae(MIC=10μg/ml), Pseudomonas aeruginosa(MIC=75μg/ml), Salmonella typhimurium(MIC=22.5μg/ml), Proteus mirabilis(MIC>200μg/ml), Serratia marcescens(MIC>200μg/ml);##Yeast: Candida albicans(MIC=100μg/ml). [Ref:11682065]1.1% hemolytic activity at 100μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11682065 FEBS Lett. 2001 Oct 19;507(1):95-100. Park S, Park SH, Ahn HC, Kim S, Kim SS, Lee BJ, Lee BJ. Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata. DRAMP01445 GLLSKVLGVGKKVLCGVSGLC 21 Nigrocin-2 (Nigrocin-2LVa; Frogs, amphibians, animals) P0C009 Not found Not found Rana nigromaculata (Black-spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Thanks to its single linear amphipathic alpha-helix, may integrate into membrane phospholipids, leading to lysis of the membrane. Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Has weak hemolytic activity. Tissue specificity: Expressed by the skin dorsal glands. PTM: Contains one disulfide bond 15-21. (By similarity)" [Ref.11682065]Gram-positive bacterium: Micrococcus luteus(MIC=2.5μg/ml);##Gram-negative bacteria: Shigella dysenteriae(MIC=10μg/ml), Klebsiella pneumoniae(MIC=10μg/ml), Pseudomonas aeruginosa(MIC=100μg/ml), Salmonella typhimurium(MIC=22.5μg/ml), Proteus mirabilis(MIC>200μg/ml), Serratia marcescens(MIC>200μg/ml);##Yeast: Candida albicans(MIC=150μg/ml). [Ref:11682065] It has 0.9% hemolytic activity at 100μg/ml against human red blood cells Cyclic Free Cyclization (Cys15 and Cys21) Disulfide bond between Cys15 and Cys21. L No cytotoxicity information found Cell membrane 11682065 FEBS Lett. 2001 Oct 19;507(1):95-100. Park S, Park SH, Ahn HC, Kim S, Kim SS, Lee BJ, Lee BJ. Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata. DRAMP01446 VIEPKCYKYEGKKCPPDINPVCGTDKRTYYNECALCVFIRQSTKKADKAIKIKKWGKC 58 Proteinase inhibitor PSKP-1 (Frogs, amphibians, animals) P83578 Not found Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Shows hemagglutinating activity, inhibits prolyl endopeptidase. May have a role in mucosal defense against microbes by interacting directly with their membranes. Gram-negative bacterium: Escherichia coli (EC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15153102 Eur J Biochem. 2004 Jun;271(11):2117-2126. Gebhard L.G, Carrizo F.U, Stern A.L, Burgardt N.I, Faivovich J, Lavilla E, Ermacora M.R. A Kazal prolyl endopeptidase inhibitor isolated from the skin of Phyllomedusa sauvagii. DRAMP01448 SLFSIFKTAAKFVGKNLLKQAGKAGLETLACKAKNEC 37 Esculentin-2-CG1 (Frogs, amphibians, animals) No entry found Not found Not found Not found Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP01449 IKDAAKLIGKTVAKEAGKTGLELMACKITNQC 32 Esculentin-2-OG3 antimicrobial peptide (Frogs, amphibians, animals) A6MAX1 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01450 GLFTLIKGAAKLIGRTVAKEAGKTGLELMACKITNQC 37 Esculentin-2-OG5 antimicrobial peptide (Frogs, amphibians, animals) A6MAX6 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01451 FTLKKSLLVLFFLGTISLSLCQEERAADEEDNGEVEE 37 Esculentin-2-OG11 antimicrobial peptide (Frogs, amphibians, animals) B5L1A6 Not found Not found Rana grahami (Yunnanfu frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP18316 MGALIKTGAKIIGSGAAGGLGTYIGHKILGK 31 Aureocin A70 (AurC)(Bacteriocin) Q93GF7 Belongs to the class II bacteriocin aurC Staphylococcus aureus A70 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Aureocin A70 is a multipeptide bacteriocin composed of four related peptides that are small (30-31 amino acid residues), strongly cationic (pI of 9.85 to 10.04) and highly hydrophobic. These peptides also have a high content of small amino acid residues like glycine (23 Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11531330 J Mol Biol. 2001 Aug 31;311(5):939-49. Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. DRAMP18315 MGAVAKFLGKAALGGAAGGATYAGLKKIFG 30 Aureocin A70 (AurB)(Bacteriocin) Q93GF6 Belongs to the class II bacteriocin aurB Staphylococcus aureus A70 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Aureocin A70 is a multipeptide bacteriocin composed of four related peptides that are small (30-31 amino acid residues), strongly cationic (pI of 9.85 to 10.04) and highly hydrophobic. These peptides also have a high content of small amino acid residues like glycine (23 Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11531330 J Mol Biol. 2001 Aug 31;311(5):939-49. Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. DRAMP01460 GLFSILKGVGKIAIKGLGKNLGKMGLDLVSCKISKEC 37 Esculentin-2Vb (2VEb; Frogs, amphibians, animals) Q1JS89 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana versabilis (Chinese bamboo leaf odorous frog) (Rana versabilis) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide (By similarity). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16621152 Peptides. 2006 Jul;27(7):1738-1744. Chen T, Zhou M, Rao P, Walker B, Shaw C. The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides. DRAMP01463 GLFSKFNKKKIKSGLIKIIKTAGKEAGLEALRTGIDVIGCKIKGEC 46 Esculentin-1SEa (Frogs, amphibians, animals) P85059 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sevosa (Dusky gopher frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one dislfide bond 40-46." Gram-negative bacterium: Escherichia coli K12;##Gram-positive bacterium: Micrococcus luteus NCT C2665. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16386333 Peptides. 2006 Jun;27(6):1313-1319. Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. DRAMP01464 GLFSKFNKKKIKSGLFKIIKTAGKEAGLEALRTGIDVIGCKIKGEC 46 Esculentin-1SEb (Frogs, amphibians, animals) P85054 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sevosa (Dusky gopher frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one dislfide bond 40-46." Gram-negative bacterium: Escherichia coli K12;##Gram-positive bacterium: Micrococcus luteus NCT C2665. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16386333 Peptides. 2006 Jun;27(6):1313-1319. Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. DRAMP01465 GIFSKLAGKKLKNLLISGLKSVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1R (Frogs, amphibians, animals) P86018 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (Laughing frog) (Marsh frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 40-46." [Swiss_Prot Entry P86018]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref:18855342]Low hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01466 GILSLVKVAKLAGKTFAKEGGKFGLEFIACKVTNQC 36 Esculentin-2R (Frogs, amphibians, animals) P86016 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (Laughing frog) (Marsh frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 30-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01467 GIFSLVKGVAKLAGKTLAKEGGKFGLELAMCKIAKQC 37 Esculentin-2Rb (Frogs, amphibians, animals) P86021 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (Laughing frog) (Marsh frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01468 GILSLVKGAAKLLGKGLAKEGGKVGLEFIACKVTNQC 37 Esculentin-2Ra (Frogs, amphibians, animals) P86017 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (Laughing frog) (Marsh frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP18314 MGKLAIKAGKIIGGGIASALGWAAGEKAVGK 31 Aureocin A70 (AurA)(Bacteriocin) Q93GF5 Belongs to the class II bacteriocin aurA Staphylococcus aureus A70 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Aureocin A70 is a multipeptide bacteriocin composed of four related peptides that are small (30-31 amino acid residues), strongly cationic (pI of 9.85 to 10.04) and highly hydrophobic. These peptides also have a high content of small amino acid residues like glycine (23 Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11531330 J Mol Biol. 2001 Aug 31;311(5):939-49. Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. DRAMP01481 NIFSLLSLGAKVLGKTLLKSAGKAGAEQLACKATNQC 37 Esculentin-2Wa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (North American New World frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP18313 TPALAVVTTVLPAAAVTTAKSV 22 Sclerosin(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Pseudomonas sp. strain DF41 Antimicrobial, Antibacterial Not found Warning: this peptide contains non-natural amino acids although they are represented using the closest standard 20 amino acids. Specifically, T1, T8, T17, and T18 are dehydrated into Dhb. P12 is 3,4-dehydrated (Dhp). In total, five residues are dehydrated. Residue K20 is Dab (2,4-diaminobutyric acid). Finally, the acyl chain CH(3)-(CH(2))(6)-CH(OH)-CH(2)-CO is attached to the N-terminus. Thus, the entire sequence is CH(3)-(CH(2))(6)-CH Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22838838 Can J Microbiol. 2012 Aug;58(8):1027-34. Berry CL, Brassinga AK, Donald LJ, Fernando WG, Loewen PC, de Kievit TR. Chemical and biological characterization of sclerosin, an antifungal lipopeptide. DRAMP01488 GIFSKLAGKKIKNLISGLKNIGKEVGMDVVRTGIDIAGCKIKGEC 45 Esculentin-1C (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Unknown Antimicrobial, Antibacterial Not found Alpha helix Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15232222 Mol Cells. 2004 Jun 30;17(3):469-476. Won HS, Kim SS, Jung SJ, Son WS, Lee B, Lee BJ. Structure-activity relationships of antimicrobial peptides from the skin of Rana esculenta inhabiting in Korea. DRAMP01489 GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1A (Frogs, amphibians, animals) P40843 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European Edible frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 2N6M##5XDJ "Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 40-46." [Swiss_Prot Entry P40843]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref:8163497]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01492 GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKIAKQC 37 Esculentin-IIb (Frogs, amphibians, animals) P40846 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European Edible frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species. [Swiss_Prot Entry P40846]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref:8163497]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01498 GLFSKFAGKGIKNFLNKGVKHIGKE 25 Esculentin-1-OA6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01500 KISGKAIKNLFIKGAKNVGKEVGMDVVRTGIDVVGCKIKGEC 42 Esculentin-1-OR2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana andersonii (Chinese odorous frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01512 QVFTLIKGATQLIRKTLGEQ 20 Esculentin-2-OR6 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana rotodora (Chinese odorous frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22029824 J Proteome Res. 2012 Jan 1;11(1):306-319. Yang X, Lee WH, Zhang Y. Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs. DRAMP01514 GIFSKFGRKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC 46 Esculentin-1 (Frogs, amphibians, animals) P84840 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antimicrobial peptide (By similarity). Stimulates insulin secretion by BRIN-BD11 cells in vitro. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref.8163497] MHC>100 µM against human red blood cell. Cyclic Free Cyclization (Cys40 and Cys46) Disulfide bond between Cys40 and Cys46. L No cytotoxicity information found Not found 16394170 J Endocrinol. 2006 Jan;188(1):1-9. Marenah L, Flatt PR, Orr DF, Shaw C, Abdel-Wahab YH. Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity. DRAMP18312 MTDANVDARRARAPHGISGAIAGVVAGCAATIEIGCVEGAIAGIGPSGIASMIAALWTCRSKYRRFSSGSGYVMLLSWSAEFVFGYFIGCRCGFLLSQK 99 Propionicin PLG-1(Bacteriocin) I2HA02 Not found plg-1 Propionibacterium thoeniiP127 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Propionicin PLG-1 is active against a variety of microorganisms such as propionibacteria, as well as many other gram-positive and gram-negative bacteria and even fungi.Propionicin PLG-1 is stable after long-term storage in a dry or frozen state and rapidly kills sensitive cells upon exposure in culture medium or skim milk. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11010864 Appl Environ Microbiol. 2000 Oct;66(10):4230-6. Faye T, Langsrud T, Nes IF, Holo H. Biochemical and genetic characterization of propionicin T1, a new bacteriocin from Propionibacterium thoenii. DRAMP01744 FLPLIGKVLSGIL 13 Temporin-G (Frogs, amphibians, animals) P79875 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP01743 FLPLIGKVLSGIL 13 Temporin-F (Frogs, amphibians, animals) P56921 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic Protein level Not found Not found "Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP01742 VLPIIGNLLNSLL 13 Temporin-E (Frogs, amphibians, animals) P56920 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP01519 GVFSFLKTGAKLLGSTLLKMAGKAGAEHLACKATNQC 37 Esculentin-2PRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (North American oregon spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria and against the fungus C. albicans. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Ranapretiosa: implications for species resistance to chytridiomycosis. DRAMP01522 GILDSFKQFAKGVGKDLIKGAAQGVLSTMSCKLAKTC 37 Rugosin-C (Frogs, amphibians, animals) P80956 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 31-37." Gram-positive bacterium: Staphylococcus aureus 209P. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7612013 Biochem. Biophys. Res. Commun. 1995; 212: 249-254. Suzuki S, Ohe Y, Kagegawa T, Tatemoto K. Isolation and characterization of novel antimicrobial peptides, rugosins A, B and C, from the skin of the frog, Rana rugosa. DRAMP01523 KGAAKGLLEVASCKLSKSC 19 Rugosin A-like peptide (Frogs, amphibians, animals) P84912 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana saharica (Sahara frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Stimulates insulin secretion by BRIN-BD11 cells in vitro. Has antibacterial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16269346 Peptides. 2005 Nov;26(11):2117-2123. Marenah L, Flatt P.R, Orr D.F, Shaw C, Abdel-Wahab Y.H.A. Isolation and structural characterization of novel Rugosin A-like insulinotropic peptide from the skin secretions of Rana saharica frog. DRAMP01527 FTMKKSLFLILFLGAIPLSMC 21 Nigroain-L antimicrobial peptide (Frogs, amphibians, animals) C0ILB3 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01528 FTMKKSLLFIFFLGTISLSLC 21 Nigroain-H antimicrobial peptide (Frogs, amphibians, animals) C0ILB0 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01529 FTMKKSLLLIFFLGTISLSLC 21 Nigroain-H antimicrobial peptide (Frogs, amphibians, animals) C0ILA9 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01530 FTMKKSPLLLFFLGTISLSLC 21 Nigroain-E antimicrobial peptide (Frogs, amphibians, animals) C0ILA0, C0ILA2 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01531 FTMKKSLLLIFFLGTISLSLCEQER 25 Nigroain-D antimicrobial peptide (Frogs, amphibians, animals) C0IL92, C0IL99, C0IL98 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01532 FTMKKSLFLLFFLGTISLSLC 21 Nigroain-B antimicrobial peptide (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Predicted Not found Not found Function: Amphibian defensive peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01534 CVISAGWDHKVRCKLTGNC 19 Nigroain-B2 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Bridge Not found PTM: Contains one disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01535 CKIALPYHMRCRVLGRC 17 Nigroain-B3 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Bridge Not found PTM: Contains one disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01536 CVISAGWNHKIR 12 Nigroain-B4 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Bridge Not found PTM: Contains one disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01537 MFTMKKSLLLLFFLGVISLSLCKQKRHADEEGNEVSGGEAKVEEVKRFKTWKRPPFQTSCSGIIKE 66 Nigroain-C antimicrobial peptide (Frogs, amphibians, animals) C0IL83 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Genomics. 2010,95:66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01538 FKTWKRPPFQTSCSGIIKE 19 Nigroain-C1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01540 CVHWQTNPARTSCIGP 16 Nigroain-D1 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Not found Not found PTM: Contains one disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01541 CVHWQTNPARTSRIGP 16 Nigroain-D2 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Not found Not found PTM: Contains one disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01544 GCTQWINNIHGRICVRN 17 Nigroain-E2 (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01545 SFLSKFKDIALDVPRMRARVY 21 Nigroain-I (Frogs, amphibians, animals) No entry found Not found Not found Rana nigrovittata (Black-striped frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovitt. DRAMP01548 MEIKYLLTVFLVLLIVSDHCQAFLFSLIPSAISGLISAFKGRRKRDLNGQIDHFKNFRKRDAELEELLSKLPIY 74 Caerin-1 A9NJH7 Not found Not found Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. Zhu S, Gao B. Scorpion venom gland caerin-like antibacterial peptide gene: inducible expression and RNA editing. DRAMP01551 GLLGVLGSVAKHVLPHVVPVIAEHL 25 Caerin-1.2 (Frogs, amphibians, animals) P56227 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Australian frog) Antimicrobial, Antibacterial,Antiviral Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation." [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 22 µM." Not found 26026377##PubMed ID is not available Peptides. 2015 Sep;71:296-303. ##J. Chem. Res. 1993; 138: 910-936. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01554 GLLSSLSSVA 10 Caerin-1.4.1 (Chain of Caerin-1.4) P62545, P56229, P62544 Belongs to the frog skin active peptide (FSAP) family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available J. Chem. Res. 1993,138:910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01556 GLFSVLGAVAKHVLPHVVPVIAEKL 25 Caerin-1.6 (Frogs, amphibians, animals) P62546, P56231, P81249, P62547 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria xanthomera (Orange-thighed frog) (Litoria chloris) Antimicrobial, Antibacterial,Antiviral Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin dorsal glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility By similarity. PTM: C-terminal amidation." [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L "[Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 10 µM." Cell membrane 26026377##9230483##9204574##9516047 Peptides. 2015 Sep;71:296-303. ##J Pept Sci. 1997 May-Jun;3(3):181-185.##Rapid Commun Mass Spectrom. 1997;11(9):997-1000.##J Pept Res. 1998 Feb;51(2):121-126. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Steinborner ST, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ, Ramsay SL.##Steinborner ST, Waugh RJ, Bowie JH, Tyler MJ.##Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera.##New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera. Part 2. Sequence determination using mass spectrometry and associated techniques.##New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. DRAMP01557 GLFKVLGSVAKHLLPHVAPVIAEKL 25 Caerin-1.7 (Frogs, amphibians, animals) P62548, P62549, P56232, P81250 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria xanthomera (Orange-thighed frog) (Litoria chloris) Antimicrobial, Antibacterial,Antiviral Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin dorsal glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility By similarity. PTM: C-terminal amidation." [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation Free L [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 12.5 µM. Cell membrane 26026377##9230483##9204574##9516047 Peptides. 2015 Sep;71:296-303. ##J Pept Sci. 1997 May-Jun;3(3):181-185.##Rapid Commun Mass Spectrom. 1997;11(9):997-1000.##J Pept Res. 1998 Feb;51(2):121-126. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Steinborner ST, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ, Ramsay SL.##Steinborner ST, Waugh RJ, Bowie JH, Tyler MJ.##Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera.##New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera. Part 2. Sequence determination using mass spectrometry and associated techniques.##New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. DRAMP01558 FKVLGSVAKHLLPHVAPVIAEK 22 Caerin-1.7.1 (Chain of Caerin-1.7) P62549, P56232, P81250 Belongs to the frog skin active peptide (FSAP) family (Caerin subfamily) Not found Litoria chloris (Blue-thighed frog) Not found Protein level Not found Not found PTM: Caerin-1.7.1 does not have any antibacterial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9516047 J Pept Res. 1998 Feb;51(2):121-126. Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ. New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. DRAMP01559 GLFKVLGSVAKHLLPHVVPVIAEKL 25 Caerin-1.8 (Frogs, amphibians, animals) P81251 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria chloris (Blue-thighed frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Alpha helix Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin dorsal glands. Domain: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity). PTM: C-terminal amidation." Litoria chloris No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9516047 J Pept Res. 1998 Feb;51(2):121-126. Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ. New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. DRAMP01561 MEIKYLLTVFLVLLIVSDHCQAFLFSLIPSAISGLISAFKGKRRRDLNAQIDQFKNFRKRDAELEELLSKLPIY 74 Caerin-2 (Venom antimicrobial peptide-10) A9NJH6 Not found Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available##Pubmed ID is not available Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.##Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. Zhu S, Gao B.##Zhu S, Gao B. Scorpion venom gland caerin-like antibacterial peptide gene: inducible expression and RNA editing.##Genomic organization of the MeVAMP-10, a venom antimicrobial peptide from Mesobuthus eupeus. DRAMP01564 ALGGLLADVVKSKEQPA 17 Caerin-2.2.1 (Chain of Caerin-2.2) P62570, P62571, P56234 Belongs to the frog skin active peptide (FSAP) family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) (Litoria gilleni) Antimicrobial Protein level Not found Not found Function: Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Pubmed ID is not available J. Chem. Res. 1993,138:910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01565 GLVSSIGKALGGLLADVVKTKEQPA 25 Caerin-2.4 (Frogs, amphibians, animals) P56236 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Chem. Res. 1993; 138: 910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01566 GLVASIGRALGGLLADVVKSKEQPA 25 Caerin-2.5 (Frogs, amphibians, animals) P56237 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gilleni (Centralian tree frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Chem. Res. 1993; 138: 910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01569 GLWQKIKDKASELVSGIVEGVK 22 Caerin-3.1 (Frogs, amphibians, animals) P62562, P56238, P62563, P86505 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria gilleni (Centralian tree frog) (Litoria splendida) (Litoria rothii) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." Gram-positive bacterium: Micrococcus luteus (MIC<0.4 µg/ml). (Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##15203252##16124032##195396 J. Chem. Res. 1993; 138: 910-936.##Peptides. 2004 Jun;25(6):1035-1054.##Rapid Commun Mass Spectrom. 2005;19(18):2716-2724.##Toxicon. 2009 Nov;54(6):828-835. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.##Brinkworth CS, Bowie JH, Bilusich D, Tyler MJ.##Sherman PJ, Jackway RJ, Nicholson E, Musgrave IF, Boontheung P, Bowie JH. Peptides from Australian frogs. The structures of the caerins from Litoria caerula.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.##The rothein peptides from the skin secretion of Roth's tree frog Litoria rothii. Sequence determination using positive and negative ion electrospray mass spectrometry.##Activities of seasonably variable caerulein and rothein skin peptides from the tree frogs Litoria splendida and Litoria rothii. DRAMP01571 GLWEKIKEKANELVSGIVEGVK 22 Caerin-3.3 (Frogs, amphibians, animals) P56240 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Chem. Res. 1993; 138: 910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01572 GLWEKIREKANELVSGIVEGVK 22 Caerin-3.4 (Frogs, amphibians, animals) P56241 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Chem. Res. 1993; 138: 910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01575 GLWQKIKSAAGDLASGIVEAIKS 23 Caerin-4.2 (Frogs, amphibians, animals) P56243 Belongs to the frog skin active peptide family (Caerin subfamily) Not found Litoria caerulea (Green tree frog); also L.caerulea/L.splendida hybrid Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Tissue specificity: Expressed by the skin parotoid and/or rostral glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Chem. Res. 1993; 138: 910-936. Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ. Peptides from Australian frogs. The structures of the caerins from Litoria caerula. DRAMP01579 GLFGILGSVAKHVLPHVVPVIAEHS 25 Caerin 1.12 (Frogs, amphibians, animals) Q800R8 Not found Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01580 GLLSVLGSLKLIVPHVVPLIAEHL 24 Caerin 1.13 (Frogs, amphibians, animals) Q800R7 Not found Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01581 SVLGKSVAKHLPHVVPVIAEKT 22 Caerin 1.14 (Frogs, amphibians, animals) Q800R6 Not found Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01582 GLFGLAKGSVAKPHVVPVISQLV 23 Caerin 1.15 (Frogs, amphibians, animals) Q800R5 Not found Not found Litoria caerulea (Green tree frog) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP18310 ITVCISVC 8 Patellamide A(Bacteriocin) No entry found Belongs to the class I bacteriocin patE Prochloron didemni Unknown Not found Not found Before both peptides, there is a 5-aa conserved region consisting of the consensus G(LV)E(AP)S. The sequence AYDGE terminates the patellamide A sequence and directly precedes the stop codon. Between the two patellamides, the 8-aa sequence AYDGVEPS seems to encode for both a start and stop cyclization sequence, with the consensus stop sequence being AYDG(EV). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15883371 Proc Natl Acad Sci U S A. 2005 May 17;102(20):7315-20. Schmidt EW, Nelson JT, Rasko DA, Sudek S, Eisen JA, Haygood MG, Ravel J. Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. DRAMP18311 VTACITFC 8 Patellamide C(Bacteriocin) No entry found Belongs to the class I bacteriocin patE Prochloron didemni Unknown Not found Not found Before both peptides, there is a 5-aa conserved region consisting of the consensus G(LV)E(AP)S. The sequence AYDGE terminates the patellamide A sequence and directly precedes the stop codon. Between the two patellamides, the 8-aa sequence AYDGVEPS seems to encode for both a start and stop cyclization sequence, with the consensus stop sequence being AYDG(EV). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15883371 Proc Natl Acad Sci U S A. 2005 May 17;102(20):7315-20. Schmidt EW, Nelson JT, Rasko DA, Sudek S, Eisen JA, Haygood MG, Ravel J. Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. DRAMP01592 FDVIKKVASVIGGL 14 Citropin-1.1.1 (Frogs, amphibians, animals) P81835, P81836, P81837 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bacteriostatic action for Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01593 DVIKKVASVIGGL 13 Citropin-1.1.2 (Frogs, amphibians, animals) P81835, P81836, P81837 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bacteriostatic action for Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01595 FDIIKKVASVVG 12 Citropin-1.2.1 (Frogs, amphibians, animals) P81840, P81841, P81842, P81843 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bacteriostatic action for Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01596 DIIKKVASVVG 11 Citropin-1.2.2 (Frogs, amphibians, animals) No entry found Not found Not found Litoria citropa (Blue Mountains tree-frog) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1 . DRAMP01597 GLFDIIKKVAS 11 Citropin-1.2.3 (Frogs, amphibians, animals) P81840 Not found Not found Litoria citropa (Australian blue mountains tree frog) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01598 GLFDIIKKVASVVGLASP 18 Citropin-1.2.4 (Frogs, amphibians, animals) P81844 Not found Not found Litoria citropa (Australian blue mountains tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01599 GLFDIIKKVASVVGLASQ 18 Citropin-1.2.5 (Frogs, amphibians, animals) P81845 Not found Not found Litoria citropa (Australian blue mountains tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01604 GLFDVIKKVASVIGLASQ 18 Citropin-1.1.4 (Frogs, amphibians, animals) P81839 Not found Not found Litoria citropa (Australian blue mountains tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01605 DLFQVIKEKLKELTGGVIEGIQGV 24 Citropin-3.1.2 (Frogs, amphibians, animals) P81851, P81852, P81853 Not found Not found Litoria citropa (Australian blue mountains tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the dorsal and submental skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10504394 Eur J Biochem. 1999 Oct;265(2):627-637. Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BC, Wallace JC, Tyler MJ. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. DRAMP01609 GLFDIVKKVVGALGSL 16 Aurein-2.2 (Frogs, amphibians, animals) P82389 Not found Not found Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Alpha helix Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin dorsal glands." Gram-positive bacteria: Bacillus cereus (MIC=100 μg/ml), Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=12 μg/ml), Micrococcus luteus (MIC=25 μg/ml), , Staphylococcus epidermidis (MIC=25 μg/ml), Streptococcus uberis (MIC=100 μg/ml), Staphylococcus aureus (MIC=25 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01610 GLFDIVKKVVGAIGSL 16 Aurein-2.3 (Frogs, amphibians, animals) P82390 Not found Not found Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Alpha helix Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin dorsal glands." [Ref.10951191]Gram-positive bacteria: Bacillus cereus (MIC=100 μg/ml), Leuconostoc lactis (MIC=25 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=25 μg/ml), Staphylococcus aureus (MIC=100 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01611 GLFDIVKKVVGTLAGL 16 Aurein-2.4 (Frogs, amphibians, animals) P82391 Not found Not found Litoria aurea (Green; also golden bell frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Protein level Not found Not found "Function: The aurein antibiotics show more activity towards gram-positive than gram-negative pathogens. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Tissue specificity: Expressed by the skin dorsal glands." [Ref.10951191]Gram-positive bacteria: Bacillus cereus (MIC=25 μg/ml), Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=25 μg/ml), Staphylococcus epidermidis (MIC=25 μg/ml), Streptococcus uberis (MIC=25 μg/ml), Staphylococcus aureus (MIC=25 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10951191##15203252 Eur J Biochem. 2000 Sep;267(17):5330-5341.##Peptides. 2004 Jun;25(6):1035-1054. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.##Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.##Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP01615 GLFDIVKKIAGHIA 14 Aurein-3.1.1 (Frogs, amphibians, animals) P69021 Not found Not found Litoria aurea (Green and golden bell frog) Antimicrobial, Antibacterial, Anti-cancer Protein level Not found Not found "Function: Has antimicrobial activity against L.lactis, L.innocua, M.luteus, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10951191 Eur J Biochem. 2000 Sep;267(17):5330-5341. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the australian bell frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. DRAMP01616 FDIVKKIAGHIAGSI 15 Aurein-3.1.2 (Frogs, amphibians, animals) P69021 Not found Not found Litoria aurea (Green and golden bell frog) Antimicrobial, Antibacterial, Anti-cancer Protein level Not found Not found "Function: Has antimicrobial activity against L.lactis, L.innocua, M.luteus, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10951191 Eur J Biochem. 2000 Sep;267(17):5330-5341. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the australian bell frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. DRAMP01619 FDIVKKIAGHIVSSI 15 Aurein-3.3.1 (Frogs, amphibians, animals) P82396 Not found Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-cancer Protein level Not found Not found "Function: Antimicrobial activity against L.lactis, M.luteus, P.multocida, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10951191 Eur J Biochem. 2000 Sep;267(17):5330-5341. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the australian bell frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. DRAMP18309 WAIVLL 6 Baceridin(Bacteriocin) No entry found Not found Not found plant-associated Bacillus strain Antimicrobial, Antibacterial, Anti-Gram+ Not found A circular peptide where residues 2, 3, and 5 are D-amino acids. Baceridin was tested for antimicrobial and cytotoxic activity and displayed moderate cytotoxicity (1 Gram-positive(weakly) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24692199 Chembiochem. 2014 May 5;15(7):1021-9. Niggemann J, Bozko P, Bruns N, Wodtke A, Gieseler MT, Thomas K, Jahns C, Nimtz M, Reupke I, Br Baceridin, a cyclic hexapeptide from an epiphytic bacillus strain, inhibits the proteasome. DRAMP01624 ILGPILGLVSNAGGLL 16 Bombinin-H6 (bombinin H isomers; Frogs, amphibians, animals) No entry found Belongs to the bombinin family Not found Not found Antimicrobial, Antibacterial Not found Not found Not found "Function: H6 shows the greatest activity, causing 60% hemolysis at a very low peptide concentration (4 µM). PTM: C-terminal amidation." H6 does not display any microbicidal activity against all the microorganisms tested. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11090921 Peptides. 2000 Nov;21(11):1673-1679. Mangoni ML, Grovale N, Giorgi A, Mignogna G, Simmaco M, Barra D. Structure-Function: relationships in bombinins H, antimicrobial peptides from Bombina skin secretions. DRAMP18308 MGISSPALPQNTADLFQLDLEIGVEQSLASPAITSVSWCTPGCTSEGGGSGCSHCC 56 Planosporicin(Bacteriocin) R4ZCJ5 Belongs to the lantibiotics family (Class I bacteriocin) pspA Planomonospora alba Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database broad-spectrum No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17469849 Biochemistry. 2007 May 22;46(20):5884-95. Castiglione F, Cavaletti L, Losi D, Lazzarini A, Carrano L, Feroggio M, Ciciliato I, Corti E, Candiani G, Marinelli F, Selva E. A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp. DRAMP01629 GWMSKIASGIGTFLSGVQQG 20 Phylloxin-S1 (Frogs, amphibians, animals) No entry found Belongs to the Phyllomedusinae subfamily Not found Phyllomedusa sauvagii (Waxy Monkey Leaf Frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18644413 Peptides. 2008 Nov;29(11):2074-2082. Amiche M, Ladram A, Nicolas P. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. DRAMP01630 AVWKDFLKNIGKAAGKAVLNSVTDMVNE 28 Dermaseptin-LI1 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa hypochondrialis (Orange legged leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18644413 Peptides. 2008 Nov;29(11):2074-2082. Amiche M, Ladram A, Nicolas P. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. DRAMP01631 GLWKSLLKNVGKAAGKAALNAVTDMVNQ 28 Dermaseptin-S7 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14599725 Regul Pept. 2003 Nov 15;116(1-3):139-146. Chen T, Tang L, Shaw C. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. DRAMP01632 ALWKTMLKKLGTVALHAGKAALGAAADTISQ 31 Dermaseptin-S8 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Alpha helix Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14599725 Regul Pept. 2003 Nov 15;116(1-3):139-146. Chen T, Tang L, Shaw C. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. DRAMP01633 DEEKRENEDEENQEDDEQSEMRRGLRSKIWLWVLLMIWQESNKFKKM 47 Dermaseptin S9 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa sauvagii (Painted-belly leaf frog) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP01634 EEEKREGENEKEQEDDNQSEEKRGLVSDLLSTVTGLLGNLGGGGLKKI 48 Preprodermaseptin S10 (Frogs, amphibians, animals) Q1EN14 Not found drsS10 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found Function: Defense response to bacterium No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. Amiche M., Lequin O., Vanhoye D., Bruston F., Ladram A., Convert O., Nicolas P. A new structural motif of alpha-helical antimicrobial peptides with a nonamphipathic hydrophobic core and cationic termini. DRAMP01635 EEEKRENEDEEEQEDDEQSEEKRALWKTLLKGAGKVFGHVAKQFLGSQGQPES 53 Preprodermaseptin S11 (Frogs, amphibians, animals) Q1EN13 Not found drsS11 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found Function: Defense response to bacterium No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. Amiche M., Lequin O., Vanhoye D., Bruston F., Ladram A., Convert O., Nicolas P. A new structural motif of alpha-helical antimicrobial peptides with a nonamphipathic hydrophobic core and cationic termini. DRAMP01636 EEEKRENEDEENQEDDEQSEMRRGLWSKIKEAAKTAGKMAMGFVNDMVGEQ 51 Preprodermaseptin S12 (Frogs, amphibians, animals) Q1EN12 Not found drsS12 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found Function: Defense response to bacterium No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. Amiche M., Lequin O., Vanhoye D., Bruston F., Ladram A., Convert O., Nicolas P. A new structural motif of alpha-helical antimicrobial peptides with a nonamphipathic hydrophobic core and cationic termini. DRAMP01637 DEEKRENEDEENQEDDEQSEMRRGLRSKIKEAAKTAGKMALGFVNDMAGEQ 51 Dermaseptin S13 (Frogs, amphibians, animals) Q1EN11 Not found drsS13 Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial Homology Not found Not found Function: Defense response to bacterium No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. Amiche M., Lequin O., Vanhoye D., Bruston F., Ladram A., Convert O., Nicolas P. A new structural motif of alpha-helical antimicrobial peptides with a nonamphipathic hydrophobic core and cationic termini. DRAMP01640 GLWKSLLKNVGVAAGKAALNAVTDMVNQ 28 Dermaseptin-2 (DShypo02; Frogs, amphibians, animals) P84597 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16844081 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia). DRAMP01641 ALWKDVLKKIGTVALHAGKAAFGAAADTISQGGS 34 Dermaseptin-3 (DShypo03; Frogs, amphibians, animals) P84598 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found Function: May have antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16844081 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia). DRAMP01642 GLWSTIKQKGKEAAIAAAKAAGKAVLNAASEAL 33 Dermaseptin-4 (DShypo04; Frogs, amphibians, animals) P84599 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found Function: May have antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16844081 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia). DRAMP01644 GLWSTIKQKGKEAAIAAAKAAGQAVLNSASEAL 33 Dermaseptin-6 (DShypo06; Frogs, amphibians, animals) P84601 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16844081 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia). DRAMP01645 GLWSTIKQKGKEAAIAAAKAAGQAALNAASEAL 33 Dermaseptin-7 (DShypo07; Frogs, amphibians, animals) P84880 Not found Not found Phyllomedusa hypochondrialis (Orange-legged leaf frog) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16844081 Biochem Biophys Res Commun. 2006 Sep 1;347(3):739-746. Brand GD, Leite JR, de Sá Mandel SM, Mesquita DA, Silva LP, Prates MV, Barbosa EA, Vinecky F, Martins GR, Galasso JH, Kuckelhaus SA, Sampaio RN, Furtado JR Jr, Andrade AC, Bloch C Jr. Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia). DRAMP01652 GLWNKIKEAASKAAGKAALGFVNEMV 26 Dermaseptin-B5 (Dermaseptin BV; Frogs, amphibians, animals) P81487 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial Protein level Alpha helix Not found "Function: Possesses a potent antimicrobial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation (Potential)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9614066 J Biol Chem. 1998 Jun 12;273(24):14690-7. Charpentier S, Amiche M, Mester J, Vouille V, Le Caer JP, Nicolas P, Delfour A. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. DRAMP01653 ALWKDILKNAGKAALNEINQLVNQ 24 Dermaseptin-B6 (Dermaseptin BVI; Frogs, amphibians, animals) P81490, Q98TQ1 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Possesses a potent antimicrobial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9614066 J Biol Chem. 1998 Jun 12;273(24):14690-7. Charpentier S, Amiche M, Mester J, Vouille V, Le Caer JP, Nicolas P, Delfour A. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. DRAMP01654 GLWSKIKEAGKAVLTAAGKAALGAVSDAV 29 Dermaseptin-B8 (Frogs, amphibians, animals) No entry found Not found Not found Phyllomedusa bicolor (Two-colored leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9305726 FEBS Lett. 1997 Sep 1;414(1):27-32. Vouille V, Amiche M, Nicolas P. Structure of genes for dermaseptins B, antimicrobial peptides from frog skin. Exon 1-encoded prepropeptide is conserved in genes for peptides of highly different structures and activities. DRAMP01655 GLWSNIKTAGKEAAKAALKAAGKAALGAVTDAV 33 Dermaseptin DRG1 (Dermaseptin-1; Dermaseptin-B7, DRS-B7; Frogs, amphibians, animals) Q90ZK3 Belongs to the frog skin active peptide family (Dermaseptin subfamily) DRG1 Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (Potential). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Amiche M. Unknown DRAMP01656 RGLWSKIKEAGKAALTAAGKAALGAVSDAV 30 Dermaseptin DRG2 (Dermaseptin-2; Frogs, amphibians, animals) Q90ZK5 Belongs to the frog skin active peptide family (Dermaseptin subfamily) DRG2 Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (Potential). Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Amiche M. Unknown DRAMP01658 GLWKNMLSGIGKLAGQAALGAVKTLV 26 Dermaseptin-J1 (DRS-J1; Frogs, amphibians, animals) P86635 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01659 GLWKNMLSGIGKLAGEAALGAVKTLV 26 Dermaseptin-J2 (DRS-J2; Frogs, amphibians, animals) P86636 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01660 ALWKNMLSGIGKLAGQAALGAVKTLV 26 Dermaseptin-J3 (DRS-J3; Frogs, amphibians, animals) P86637 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01661 ALWKDMLSGIGKLAGQAALGAVKTLV 26 Dermaseptin-J4 (DRS-J4; Frogs, amphibians, animals) P86638 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01662 GLWSKIKEAGKAAVKAAGKAALGAVANSV 29 Dermaseptin-J5 (DRS-J5; Frogs, amphibians, animals) P86683 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01663 GLWSKIKEAGKAAVKAAGKAALGAVADSV 29 Dermaseptin-J6 (DRS-J6; Frogs, amphibians, animals) P86684 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP18307 APVPFSCTRGCLTHLV 16 LMW peptide (Bacteriocin) No entry found Not found Not found Pediococcus pentosaceus IE-3 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Unlike pediocin-like bacteriocins, the low molecular weight peptide (LMW) showed resistance to different proteases. Moreover, peptide treated with reducing agent like dithiothreitol (DTT) exhibited increased activity against both Gram-positive and Gram-negative test strains in comparison to native peptide. However, peptide treated with oxidizing agent such as hydrogen peroxide (H2O2) did not show any antimicrobial activity. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25158757 BMC Microbiol. 2014 Aug 27;14:226. Singh PK, Sharma S, Kumari A, Korpole S. A non-pediocin low molecular weight antimicrobial peptide produced by Pediococcus pentosaceus strain IE-3 shows increased activity under reducing environment. DRAMP01665 GLWKSLLKNVGKAAGKAALNAVTDMVNQA 29 Dermaseptin-J8 (DRS-J8; Frogs, amphibians, animals) P86640 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01666 GLWKSLLKNVGKAAGKAALNAVTDMVNQS 29 Dermaseptin-J9 (DRS-J9; Frogs, amphibians, animals) P86641 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01667 ALWKSLLKGAGQLVGGVVQHFMGSQGQPES 30 Dermaseptin-J10 (DRS-J10; Frogs, amphibians, animals) P86642 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01669 ALWFTMLKKLGTMALHAGKAALGAAANTISQGTQ 34 Dermaseptin-2 (DS II; Dermaseptin-S2, DS2; Frogs, amphibians, animals) P80278 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiprotozoal Protein level Alpha helix Not found "Function: Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Expressed by the skin glands." Aspergillus fumigatus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8306981 Eur J Biochem. 1994 Jan 15;219(1-2):145-154. Mor A, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. DRAMP01670 ALWKNMLKGIGKLAGKAALGAVKKLVGAES 30 Dermaseptin-3 (DS III; Dermaseptin-S3, DS3; Frogs, amphibians, animals) P80279 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal, Antiprotozoal Protein level Alpha helix Not found "Function: Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. Binds to healthy erythrocytes (this binding is receptor independent), but has no significant hemolytic activity. Does not bind to P. falciparum infected erythrocytes, but accumulates within the parasite. Kills the parasite, but has no hemolytic activity on the host cell. Tissue specificity: Expressed by the skin glands." [Ref.9395500]Fungi: Aspergillus fumigatus;##Protozoa: Malarial parasite strain H (IC50=0.8 µg/ml), Malarial parasite strain NF54 (IC50=0.26 µg/ml). [Ref:8306981]No significant hemolytic activity against rabbit red blood cells;##[Ref:9395500]Non-hemolytic activity against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binds to healthy erythrocytes (this binding is receptor independent). 8306981##9395500 Eur J Biochem. 1994 Jan 15;219(1-2):145-155.##J Biol Chem. 1997 Dec 12;272(50):31609-31616. Mor A, Nicolas P.##Ghosh JK, Shaool D, Guillaud P, Cicéron L, Mazier D, Kustanovich I, Shai Y, Mor A. Isolation and structure of novel defensive peptides from frog skin.##Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis. DRAMP01671 ALWMTLLKKVLKAAAKALNAVLVGANA 27 Dermaseptin-4 (DS IV; Dermaseptin-S4, DS4; Frogs, amphibians, animals) P80280 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Combine strand and Turn structure Not found "Function: Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1. Probably acts by disturbing membrane functions with its amphipathic structure. Has strong hemolytic activity. Does not bind to P. falciparum infected erythrocytes, but accumulates within the parasite. Tissue specificity: Expressed by the skin glands. Pharmaceutical use: Derivatives of this peptide may be used as therapeutic agents to treat bacterial infections and malaria, and to prevent infection by herpes simplex virus type 1 and HIV-1." [Swiss_Prot Entry P80280]Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1 [Ref:11850249]IC50=20 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet healthy erythrocytes (this binding is receptor independent). 8306981##11850249##9395500 Eur J Biochem. 1994 Jan 15;219(1-2):145-154.##Antimicrob Agents Chemother. 2002 Mar;46(3):689-694.##J Biol Chem. 1997 Dec 12;272(50):31609-31616. Mor A, Nicolas P.##Navon-Venezia S, Feder R, Gaidukov L, Carmeli Y, Mor A.##Ghosh JK, Shaool D, Guillaud P, Cicéron L, Mazier D, Kustanovich I, Shai Y, Mor A. Isolation and structure of novel defensive peptides from frog skin.##Antibacterial properties of dermaseptin S4 derivatives with in vivo activity.##Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis. DRAMP01672 GLWSKIKTAGKSVAKAAAKAAVKAVTNAV 29 Dermaseptin-5 (DS V; Dermaseptin-S5, DS5; Frogs, amphibians, animals) P80281 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "MOA: Probably acts by disturbing membrane functions with its amphipathic structure. Binds to healthy erythrocytes (this binding is receptor independent), and has strong hemolytic activity. Does not bind to P.falciparum infected erythrocytes, but accumulates within the parasite. Pharmaceutical use: Derivatives of this peptide may be used as therapeutic agents to treat bacterial infections and malaria, and to prevent infection by herpes simplex virus type 1 and HIV-1." [Swiss_Prot Entry P80281]Possesses a potent antimicrobial activity against bacteria, fungi and protozoa [Ref:8306981]Show strong hemolytic activity against rabbit healthy erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8306981 Eur J Biochem. 1994 Jan 15;219(1-2):145-154. Mor A, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. DRAMP01673 GLWSKIKETGKEAAKAAGKAALNKIAEAV 29 Dermaseptin-1 (DStar 01; Frogs, amphibians, animals) P84921 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, the Gram-negative bacteria E. coli and P. aeruginosa, and the yeasts C. albicans and P. brasiliensis. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Swiss_Prot Entry P84921]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa.;##Fungi: Candida albicans and Paracoccidioides brasiliensis. [Ref:PubMed ID is not available]40% hemolytic activity at 128 µg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP18306 KYYGNGVTXGKHSXXVDXG 19 Pediocin ACCEL(Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Pediococcus pentosaceus ACCEL Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found It was inactivated by various proteases and stable at pH 2.0-6.0 and <100 Celsius degree. More than 80% activity was left even after 15 min of heating at 121 Celsius degree and pH 2.0-4.0. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14995112 J Agric Food Chem. 2004 Mar 10;52(5):1146-51. Wu CW, Yin LJ, Jiang ST. Purification and characterization of bacteriocin from Pediococcus pentosaceus ACCEL. DRAMP01675 GLFKTLIKGAGKMLGHVAKQFLGSQGQPES 30 Dermaseptin-3 (DStar 03; Frogs, amphibians, animals) P84923 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, the Gram-negative bacteria E. coli and P. aeruginosa, and the yeasts C. albicans and P. brasiliensis. Has hemolytic activity. Tissue specificity: Expressed by the skin glands." [Swiss_Prot Entry P84923]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa;##Fungi: Candida albicans and Paracoccidioides brasiliensis. [Ref:PubMed ID is not available]100% hemolytic activity at 128 µg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01676 ALWKDILKNAGKAALNEINQIVQ 23 Dermaseptin-4 (DStar 04; Frogs, amphibians, animals) P84924 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, the Gram-negative bacteria E. coli and P. aeruginosa. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Swiss_Prot Entry P84924]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa. [Ref:PubMed ID is not available]5% hemolytic activity at 128 µg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01677 GLWSKIKEAAKTAGKAAMGFVNEMV 25 Dermaseptin-5 (DStar 05; Frogs, amphibians, animals) P84925 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, the Gram-negative bacteria E. coli and P. aeruginosa, and the yeasts C. albicans and P. brasiliensis. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Swiss_Prot Entry P84925]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa;##Fungi: Candida albicans and Paracoccidioides brasiliensis. [Ref:PubMed ID is not available]15% hemolytic activity at 128 µg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01678 ALWKNMLKGIGKLAGQAALGAVKTLVGA 28 Dermaseptin-6 (DStar 06; Frogs, amphibians, animals) P84926 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, and the Gram-negative bacteria E. coli and P. aeruginosa. Has hemolytic activity. Tissue specificity: Expressed by the skin glands." [Swiss_Prot Entry P84926]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa. [Ref:PubMed ID is not available]Show hemolytic activity at 612 µM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01679 ALWKDVLKKIGTVALHAGKAALGAVADTISQ 31 Dermaseptin-7 (DStar 07; Frogs, amphibians, animals) P84927 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antimicrobial peptide, active against the Gram-positive bacterium S. aureus, and the Gram-negative bacteria E. coli and P. aeruginosa. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Swiss_Prot Entry P84927]Gram-positive bacteria: Staphylococcus aureus, Enterococcus faecalis;##Gram-neagtive bacterium: Pseudomonas aeruginosa. [Ref:PubMed ID is not available]Show hemolytic activity at 286 µM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01680 SLRGFLKGVGTALAGVGKVVADQFDKLLQAGQ 32 Dermaseptin-8 (DStar 08; Frogs, amphibians, animals) P84928 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tarsius (Brownbelly leaf frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium S. aureus, and the Gram-negative bacteriun E. coli. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." [Swiss_Prot Entry P84928]Gram-positive bacteria: Staphylococcus aureus;##Gram-neagtive bacterium: Escherichia coli. [Ref:PubMed ID is not available]Show hemolytic activity at 432 µM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2006) to UniProtKB. Prates M.V, Jardim D.P, Silva L.P, Gordo M, Leite J.R.S.A, Figueredo R.C.R, Amaral A.C, Felipe M.S.S, Bloch C. Jr. Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia). DRAMP01681 GLWSKIKTAGKEAAKAAAKAAGKAALNAVSEAI 33 Dermaseptin-S6 (DS6; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14599726 Regul Pept. 2003 Nov 15;116(1-3):147-154. Chen T, O'Rourke M, Orr DF, Coulter DJ, Hirst DG, Rao P, Shaw C. Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima. DRAMP01682 GLRSKIWLWVLLMIWQESNKFKKM 24 Dermaseptin-S9 (DS9; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (South American hylid frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16401077 Biochemistry. 2006 Jan 17;45(2):468-480. Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P, Amiche M. Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. DRAMP01683 ALWKTLLKGAGKVFGHVAKQFLGSQGQPES 30 Dermaseptin-S11 (DS11; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16401077 Biochemistry. 2006 Jan 17;45(2):468-480. Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P, Amiche M. Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. DRAMP01684 GLWSKIKEAAKTAGKMAMGFVNDMV 25 Dermaseptin-S12 (DS12; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16401077 Biochemistry. 2006 Jan 17;45(2):468-480. Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P, Amiche M. Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. DRAMP01685 GLRSKIKEAAKTAGKMALGFVNDMA 25 Dermaseptin-S13 (DS13; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16401077 Biochemistry. 2006 Jan 17;45(2):468-480. Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P, Amiche M. Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. DRAMP01686 SLGSFMKGVGKGLATVGKIVADQFGKLLEA 30 Dermaseptin AA-1-1 (Frogs, amphibians, animals) O93221 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01687 SLWSKIKEMAATAGKAALNAVTGMVNQ 27 Dermaseptin AA-3-1 (Frogs, amphibians, animals) O93223 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01688 GMFTNMLKGIGKLAGQAALGAVKTLA 26 Dermaseptin AA-3-3 (Frogs, amphibians, animals) O93224 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01689 GMWGSLLKGVATVVKHVLPHALSSQQS 27 Dermaseptin AA-3-4 (Frogs, amphibians, animals) O93225 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01690 GMWSTIRNVGKSAAKAANLPAKAALGAISEAV 32 Dermaseptin AA-3-6 (Frogs, amphibians, animals) O93226 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01691 GLVSGLLNTAGGLLGDLLGSLGSLSG 26 Dermaseptin AA-2-5 (Frogs, amphibians, animals) O93222 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis annae (Blue-sided leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01692 ALWKTLLKKVGKVAGKAVLNAVTNMANQNEQ 31 Dermaseptin PD-2-2 (Frogs, amphibians, animals) O93452 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Pachymedusa dacnicolor (Giant mexican leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01693 GMWSKIKNAGKAAAKASKKAAGKAALGAVSEAL 33 Dermaseptin PD-3-3 (DRS-DA3; Frogs, amphibians, animals) O93453 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Pachymedusa dacnicolor (Giant mexican leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP18305 KVTKSVKSIPVKI 13 Paenibacterin (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Paenibacillus thiaminolyticus OSY-SE Antimicrobial, Antibacterial Not found A C15 fatty acid chain is attahced to the N-terminus of the peptide (XXL). The carboxyl-terminal Ile is connected to Thr by ester linkage (XXJ). In addition, the first and fourth K's are ornithine (represented with K). Comment: No comments found on DRAMP database Broad-spectrum No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22367082 Appl Environ Microbiol. 2012 May;78(9):3156-65. Guo Y, Huang E, Yuan C, Zhang L, Yousef AE. Isolation of a Paenibacillus sp. strain and structural elucidation of its broad-spectrum lipopeptide antibiotic. DRAMP01695 GVVTDLLNTAGGLLGNLVGSLSG 23 Dermaseptin PD-3-6 (Plasticin-DA1; Frogs, amphibians, animals) O93454 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Pachymedusa dacnicolor (Giant mexican leaf frog) Antimicrobial, Antibacterial Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01696 LLGDLLGQTSKLVNDLTDTVGSIV 24 Dermaseptin PD-3-7 (Frogs, amphibians, animals) O93455 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Pachymedusa dacnicolor (Giant mexican leaf frog) Antimicrobial, Antibacterial Protein level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP01697 GMWSKIKNAGKAAKAAAKAAGKAALGAVSEAM 32 Dermaseptin-DA4 (DRS-DA4; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Pachymedusa dacnicolor (Mexican frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found It shows selective activity against gram-negative bacteria and not toxic to fresh rat erythrocytes. DRS-DA4 is a potent chemoattractant for human leukocytes and is devoid of hemolytic activity. [Ref.FEBS J. 2009 Nov;276(22):6773-6786.]Gram-negative bacteria:Escherichia coli ML35p(MIC=5 µM), Escherichia coli 363 ATCC 11775(MIC=5 µM), Peudomonas aeruginosa ATCC 27853(MIC=40 µM). [Ref. FEBS J. 2009 Nov;276(22):6773-6786.]Show no hemolytic activity against rat blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available FEBS J. 2009 Nov;276(22):6773-6786. Auvynet C, Joanne P, Bourdais J, Nicolas P, Lacombe C, Rosenstein Y. Dermaseptin DA4, although closely related to dermaseptin B2, presents chemotactic and Gram-negative selective bactericidal activities. DRAMP01699 GLWSKIKDVAAAAGKAALGAVNEALGEQ 28 Dermaseptin-H2 (Dermaseptin-like peptide 2, DMS2; Frogs, amphibians, animals) P84937 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial, Antibacterial Protein level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Thesis (2006), University of Ulster Coleraine, United Kingdom. Thompson A.H. A genomic/proteomic approach to isolating and identifying bioactive peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP01700 GLWSTIKNVAAAAGKAALGAL 21 Dermaseptin-H3 (Dermaseptin-like peptide 3, DMS3; Frogs, amphibians, animals) Q17UY8 Belongs to the frog skin active peptide family (Dermaseptin subfamily) dpp-H3 Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Staphylococcus aureus, Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17553595 Peptides. 2007 Jul;28(7):1331-43. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. DRAMP18304 VLSIVACSSGCGSGKTAASCVETCGNRCFTNVGSLC 36 Paenicidin A (Bacteriocin) K7TS19 Belongs to the lantibiotics family (Class I bacteriocin) paeA Paenibacillus polymyxa NRRL B-30509 Antimicrobial, Antibacterial, Anti-Gram+ Not found There are three lanthionines (between residues 3-7; 8-11; 19-24) and three methyllanthionines rings (between residues 16-20; 23-28; 30-36). Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23167271 J Am Chem Soc. 2012 Dec 5;134(48):19540-3. Lohans CT, Huang Z, van Belkum MJ, Giroud M, Sit CS, Steels EM, Zheng J, Whittal RM, McMullen LM, Vederas JC. Structural characterization of the highly cyclized lantibiotic paenicidin A via a partial desulfurization/reduction strategy. DRAMP01704 SVLSTITDMAKAAGRAALNAITGLVNQ 27 Dermaseptin-C3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Unknown Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18644413 Peptides. 2008 Nov;29(11):2074-2082. Amiche M, Ladram A, Nicolas P. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. DRAMP01705 DLWNSIKDMAAAAGRAALNAVTGMVNQ 27 Dermaseptin-like peptide (SmDLP; Frogs, amphibians, animals) P83914 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Schistosoma mansoni (Blood fluke) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Has hemolytic activity on human and duck erythrocytes. [Swiss_Prot Entry P83914]Gram-positive bacterium: Micrococcus luteus;##Yeast: Candida albicans. [Ref:6539015]Show hemolytic activity on human and duck erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6539015 J Parasitol. 2005 Dec;91(6):1340-1351. Quinn GA, Heymans R, Rondaj F, Shaw C, de Jong-Brink M. Schistosoma mansoni dermaseptin-like peptide: structural and functional characterization. DRAMP01706 GLLSGILNTAGGLLGNLIGSLSNGES 26 Dermaseptin-like DRP-AC-1 (Frogs, amphibians, animals) Q800S2 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01707 GLLSGILNSAGGLLGNLIGSLSNGES 26 Dermaseptin-like DRP-AC-2 (Frogs, amphibians, animals) Q800S1 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01708 SVLSTITDMAKAAGRAALNAITGLVNQGEQ 30 Dermaseptin-like DRP-AC-3 (Frogs, amphibians, animals) Q800S0 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP01709 ALWKDLLKNVGIAAGKAVLNKVTDMVNQ 28 Dermaseptin-1 (DStomo01; Frogs, amphibians, animals) P85523 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa tomopterna (Tiger-striped leaf frog，Pithecopus tomopternus) Antimicrobial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2008) to UniProtKB. de Sa Mandel S.M, Mundim N.C.C.R, Silva L.P, Prates M.V, Bloch C. Jr. Dermaseptins and phylloseptins of Phyllomedusa (Hylidae) secretion. DRAMP01710 ALWKTMLKKLGTVALHAGKAALGAAADTISQGA 33 Dermaseptin DS VIII-like peptide (Frogs, amphibians, animals) P86280 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa burmeisteri (Brazilian common walking leaf frog) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2009) to UniProtKB Conceicao K, Klitzke C.F, Brito R.C, Andrade D.F, Junca F.A, Biondi I, Lopes-Ferreira M. Identification of peptides from Phyllomedusa burmesteri skin secretomics by nano LC MS/MS. DRAMP01711 ALWKNMLKGIGKLAGKAALGAVK 23 Dermaseptin III-like peptide (Frogs, amphibians, animals) P86281 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phyllomedusa burmeisteri (Brazilian common walking leaf frog) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found MOA: Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2009) to UniProtKB. Conceicao K, Klitzke C.F, Brito R.C, Andrade D.F, Junca F.A, Biondi I, Lopes-Ferreira M. Identification of peptides from Phyllomedusa burmesteri skin secretomics by nano LC MS/MS. DRAMP18303 VLSIVACSSGCGSGKTAASCVETCGNRCFTNVGSLC 36 Paenicidin A (Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) paeA Paenibacillus polymyxa NRRL B-30509 Antimicrobial, Antibacterial, Anti-Gram+ Not found There are three lanthionines (between residues 3-7; 8-11; 19-24) and three methyllanthionines rings (between residues 16-20; 23-28; 30-36). Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23167271##24382692 J Am Chem Soc. 2012 Dec 5;134(48):19540-3.##Chembiochem. 2014 Jan 24;15(2):243-9. Lohans CT, Huang Z, van Belkum MJ, Giroud M, Sit CS, Steels EM, Zheng J, Whittal RM, McMullen LM, Vederas JC.##Lohans CT, van Belkum MJ, Cochrane SA, Huang Z, Sit CS, McMullen LM, Vederas JC. Structural characterization of the highly cyclized lantibiotic paenicidin A via a partial desulfurization/reduction strategy.##Biochemical, structural, and genetic characterization of tridecaptin A?, an antagonist of Campylobacter jejuni. DRAMP01713 VHLEEILLLLFFLGTISLSLCEEERDADEEENEVSGYAANVNVKRCGYKHGRANCGRG 58 OGA1 antimicrobial peptide (Frogs, amphibians, animals) B5L172 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Antiviral Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP01714 MFTMKKSLLLLFFLGTINLSFCQEETNAEEERRDEEVAKMEEIKRGLLSGPRCGEESTMWT 61 OGF2 antimicrobial peptide (Frogs, amphibians, animals) B5L190 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP01715 MFTLKKPLLLLFFLGTINLSLCQDETNAEEERRDEEVVKMEEIKRGLLSGILGAGKHIVCGLTGCAKA 68 OGG1 antimicrobial peptide (Frogs, amphibians, animals) B5L183 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP01716 MFTLKKSLLLLFFLGTINLSLCQDVTNAEEERRDEEVAKMEEIKRGLLRPPRCGEAYSMWT 61 OGF1 antimicrobial peptide (Frogs, amphibians, animals) B5L180 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP01717 SLGSFLKGVGTTLASVGKVVSDQFGKLLQAGQ 32 Dermatoxin (Frogs, amphibians, animals) Q9PT75, P81566 Belongs to the frog skin active peptide family (Dermaseptin subfamily) DRT Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Possesses a potent antimicrobial activity against Gram-positive bacteria and less active against Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. Tissue specificity: Highest expression in skin and to a lesser extent in brain and intestine. Miscellaneous: The sequence shown corresponds to the dermatoxin isolated from frog skin. A variant of it is present in frog brain." Gram-positive bacteria: Bacillus megaterium, Corynebacterium glutamicumm, Staphylococcus aureus (++);##Gram-negative bacteria: mollicutes Acholeplasma laidlawii, Spiroplasma melliferum (++); Burkholderia cepacia, Pseudomonas aeruginosa, Salmonella typhimurium and S. meliloti (+). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10880984 Eur J Biochem. 2000 Jul;267(14):4583-4592. Amiche M, Seon AA, Wroblewski H, Nicolas P. Isolation of dermatoxin from frog skin, an antibacterial peptide encoded by a novel member of the dermaseptin genes family. DRAMP01718 SLGGFLKGVGKALAGVGKVVADQFGNLLQAGQ 32 Dermatoxin-J1 (DRT-J1; Frogs, amphibians, animals) P86621 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01719 SLGGFLKGVGKALAGVGKMVADQFGNLLQAGQ 32 Dermatoxin-J2 (DRT-J2; Frogs, amphibians, animals) P86622 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01720 SLGGFLKGVGKVLAGVGKVVADQFGNLLEAGQ 32 Dermatoxin-J3 (DRT-J3; Frogs, amphibians, animals) P86623 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP01722 FLAGLIGGLAKML 13 Temporin-LTe antimicrobial peptide (Frogs, amphibians, animals) G5CKS1 Not found Not found Hylarana latouchii (broad-folded frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22426384 Biochimie. 2012 Jun;94(6):1317-1326. Wang H, Yu Z, Hu Y, Yu H, Ran R, Xia J, Wang D, Yang S, Yang X, Liu J. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii. DRAMP01723 FLPILGKLLSGFL 13 Temporin-TOa (Frogs, amphibians, animals) D5MTH4 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides. 2010,0:0-0. Tazato S, Conlon JM, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides and bradykinin from the skin and brain of Oki Tago's brown frog, Rana tagoi okiensis. DRAMP01724 FLPILGKLLSGLL 13 Temporin-TOb (Frogs, amphibians, animals) D5MTH5 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides. 2010,0:0-0. Tazato S, Conlon JM, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides and bradykinin from the skin and brain of Oki Tago's brown frog, Rana tagoi okiensis. DRAMP01725 FLPFVGNLLKGLL 13 Temporin-CG1 antimicrobial peptide (Frogs, amphibians, animals) E1AWD7 Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01726 FFPIVGKLLSGLF 13 Temporin-CG2 antimicrobial peptide (Frogs, amphibians, animals) E1AWD8 Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01727 FLPIVGKLLSGLF 13 Temporin-CG3 antimicrobial peptide (Frogs, amphibians, animals) E1AWE0 Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01728 FLPILGNLLNGLL 13 Temporin-CG4 antimicrobial peptide (Frogs, amphibians, animals) E1AWE1 Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01729 FLPFVGNLLNGLL 13 Temporin-CG5 antimicrobial peptide (Frogs, amphibians, animals) E1B232 Not found Not found Amolops chunganensis (Chungan torrent frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP02857 ILPWKWPWWPWRR 13 Indolicidin (Cathelicidin-4; mammals, animals) P33046, A3KN14 Belongs to the cathelicidin family CATHL4 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level No secondary structure The backbone structure in DPC, well defined between residues 3 and 11, is extended, with two half-turns at residues Lys-5 and Trp-8. The backbone structure in SDS, well defined between residues 5 and 11, is also extended, but lackes the bend in the C-terminal half. Indolicidin in complexes with DPC has a central hydrophobic core composed of proline and tryptophan, which is bracketed by positively charged regions near the peptide termini 1G8C, 1G89 resolved by NMR. "Function: Potent microbicidal activity; active against Staphylococcus aureus, Escherichia coli and Candida albicans. Tissue specificity: Large granules of neutrophils. PTM: Contains two disulfide bonds and C-terminal amidation." [Ref.12074933] Gram-positive bacterium: Staphylococcus aureus (MIC=0.003%);##Gram-negative bacterium: Escherichia coli (MIC=0.007%);##Fungus: Candida albicans (MIC=0.015%) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1537821##11123901##12074933 J Biol Chem. 1992 Mar 5;267(7):4292-4295.##Biochemistry. 2000 Dec 26;39(51):15765-74.##Life Sci. 2002 Jul 5;71(7):747-50. Selsted ME, Novotny MJ, Morris WL, Tang YQ, Smith W, Cullor JS.##Rozek A, Friedrich CL, Hancock RE.##Kowalska K, Carr DB, Lipkowski AW. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils.##Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.##Direct antimicrobial properties of substance P. DRAMP01741 LLPIVGNLLNSLL 13 Temporin-D (Frogs, amphibians, animals) P56919 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix Not found Relative to Temporins A, B, and H, temporin D showed the greatest hemolytic activity. Thus, although it lacks antibacterial activity, this peptide may also plays a role in host defense by showing toxicity to eukaryotes) (Eur. J Biochem 2000; 267: 1447-1454). [Ref.9022710]Gram-positive bacterium: Bacillus megaterium [Ref.10691983]55% hemolysis at 10 μM, 90% hemolysis at 20 μM, 95% hemolysis at 40μM, 100% hemolysis at 60 μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710##10691983 Eur J Biochem. 1996 Dec 15;242(3):788-792.##Eur J Biochem. 2000 Mar;267(5):1447-54. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D.##Mangoni ML, Rinaldi AC, Di Giulio A, Mignogna G, Bozzi A, Barra D, Simmaco M. Temporins, antimicrobial peptides from the European red frog Rana temporaria.##Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. DRAMP02819 GLLKRIKTLL 10 Anoplin (Insects, arthropods, invertebrates, animals) P0C005 Not found Not found Anoplius samariensis (Solitary wasp) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix The peptide adopts a random coil structure in water and tends to fold into an 2MJQ,2MJR,2MJS,2MJT [Ref.29614317]Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi.##[Ref.25316570]Function: Exhibits potent activity in stimulating degranulation from rat peritoneal mast cells but not from RBL-2H3 cells. Exhibits broad-spectrum antimicrobial activity against both Gram-negative bacteriapositive and Gram-negative bacterianegative bacteria. Has no hemolytic activity towards human erythrocytes. [Ref.29614317]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=26 μg/mL);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=13 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=19.5 μg/mL).##[Ref.25316570]Gram-positive bacteria : Staphylococcus aureus (MIC=64 μg/ml), bacillus subtilis (MIC=32 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC=64 μg/ml), Peudomonas eruginosa (MIC=32 μg/ml).##[Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=200 μg/ml), Bacillus subtilis DELTA (MIC=300 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=200 μg/ml), Pseudomonas aeruginosa PAO (MIC=100 μg/ml), Zymomonas mobilis 10988 (MIC=40 μg/ml);##Fungi : Candida parapsilosis (MIC=15 μg/ml) [Ref.25316570] 1% hemolysis at 12.5 μg/ml , 2% hemolysis at 25 μg/ml , 1% hemolysis at 50 μg/ml , 1.5% hemolysis at 100 μg/ml , 1.5% hemolysis at 200 μg/ml against mice red blood cells.##[Ref.27862650]3% hemolysis at 100μg/ml , 6% hemolysis at 200μg/ml , 10% hemolysis at 300μg/ml , 12% hemolysis at 500μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29614317##25316570#27862650 Peptides. 2018 Jun;104:7-14.##J Pept Sci. 2014 Dec;20(12):945-51. doi: 10.1002/psc.2705.##J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG.##Yang Wang, Jianbo Chen, Xin Zheng, Xiaoli Yang, Panpan Ma,Ying Cai,Bangzhi Zhangb,and Yuan Chen##Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin.##Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity##Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP04395 AMVGT 5 EP3 (Earthworm,animals) No entry found Belongs to the antibacterial vermipeptides family (AVPF) Not found Eisenia foetida (Common brandling worm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. [Ref.European Journal of Soil Biology, 2007, 43 S127-S134] Gram-negative bacteria: Pseudomonas pyocyanea (IC=12.58 μg/ml), Acinetobacter baumanii (IC=12.58 μg/ml), Klebsiella terrigena (IC=12.58 μg/ml);## Gram-positive bacteria: Enterococcus gallinarum (IC=12.58 μg/ml), Enterococcus faecalis (IC=25.68 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available European Journal of Soil Biology, 2007, 43:S127-S134 C Wang, Z Suna, X Zhang, G Xu## Ito Y, Yoshikawa A, Hotani T, Fukuda S, Sugimura K, Imoto T. A novel antimicrobial vermipeptide family from earthworm Eisenia fetida. DRAMP04394 AMVSS 5 EP2 (Earthworm,animals) No entry found Belongs to the antibacterial vermipeptides family (AVPF) Not found Eisenia foetida (Common brandling worm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative and Gram-positive bacteria. [Ref.European Journal of Soil Biology, 2007, 43 S127-S134] Gram-negative bacteria: Pseudomonas pyocyanea (IC=11.4 μg/ml), Acinetobacter baumanii (IC=11.4 μg/ml), Klebsiella terrigena (IC=11.4 μg/ml);##Gram-positive bacteria: Enterococcus gallinarum (IC=11.4 μg/ml), Enterococcus faecalis (IC=22.8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available European Journal of Soil Biology, 2007, 43:S127-S134. C Wang, Z Suna, X Zhang, G Xu## Ito Y, Yoshikawa A, Hotani T, Fukuda S, Sugimura K, Imoto T. A novel antimicrobial vermipeptide family from earthworm Eisenia fetida. DRAMP02396 ACSAG 5 OEP3121 (EP5-1;earthworm,animals) P84182 Not found Not found Eisenia foetida (Common brandling worm) (Common dung-worm) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Not found Not found Function: Displays antimicrobial activity. The effects of EP5 on HeLa cells lead to the cancer cell's apoptosis and break down. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15253156##PubMed ID is not available Acta Biochim Biophys Sin (Shanghai). 2004 Apr;36(4):297-302.##European Journal of Soil Biology, 2007, 43:S127-S134. Liu YQ, Sun ZJ, Wang C, Li SJ, Liu YZ.##C Wang, Z Suna, X Zhang, G Xu. Purification of a novel antibacterial short peptide in earthworm Eisenia foetida.##A novel antimicrobial vermipeptide family from earthworm Eisenia fetida. DRAMP01747 ILPIIGKILSTIF 13 Temporin-1CEe (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Temporin-1CEe showed higher antimicrobial activity against Gram-positive bacteria: than Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21303203 Zoolog Sci. 2011 Feb;28(2):112-117. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis. DRAMP02242 GLMDVFKGAAKNLLASALDKIRCKVTKC 28 Ranatuerin-2PRa (frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC=13μM);## Gram-positive bacterium: Staphylococcus aureus(MIC>100μM);## Yeast: Candida albicans(MIC=100μM) [Ref.15003829] HC50=150μM against human erythrocytes Cyclic Free Cyclization (Cys23 and Cys28) Disulfide bond between Cys23 and Cys28. L No cytotoxicity information found Not found 15003829 Regul Pept. 2004 May 15;118(3):135-141. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP01749 FLPIVGRLISGLL 13 Temporin-1ARa (Temporin 1ARa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana areolata (crawfish frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12429503 Biochim Biophys Acta 2002; 1601: 55-63. Ali M et al Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata DRAMP01756 MFTLKKSLLLLFFLGTNISLSLCEEERDADQEERRDDPEERDVEVEKRFLFPIASMLGKVLGK 65 Temporin-2-RA2 peptide (Frogs, amphibians, animals) E3SZL6 Not found Not found Odorrana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Yang X, Liang X, Zhang Y, Lee WH. The highest antimicrobial peptides diversity, skin antimicrobial peptides peptidomics of Amphibian, Rana andersonii. DRAMP01757 MFTLKKPLLLLFFLGTINLSLCEEEERDIDQEERRDDPEERDVEVEKRFLFPLAKASFLGKVLGK 65 Temporin-1-RA1 peptide (Frogs, amphibians, animals) E3SZL5 Not found Not found Odorrana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Yang X, Liang X, Zhang Y, Lee WH. The highest antimicrobial peptides diversity, skin antimicrobial peptides peptidomics of Amphibian, Rana andersonii. DRAMP01758 FLSAITSILGKFF 13 Temporin-1SPa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp. Biochem. Physiol. C 2004; 139: 31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog Rana septentrionalis. DRAMP01760 FLPIIGQLLSGLL 13 Temporin-1AUa (Temporin 1AUa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana aurora (Northern red-legged frog) Antimicrobial, Antibacterial Not found Not found Not found Function: It lacks basic residues and only showed weak activity against bacteria or very weak effect on erythrocytes. Therefore, other functions other than antimicrobial should be sought. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15325526 Dev Comp Immunol 2005; 29: 83-90. Conlon JM et al Jouenne T. host-defense peptides isolated from the skin secretions of the Northern red-legged frog Rana aurora aurora. DRAMP01761 FLPILGNLLSGLL 13 Temporin-PRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (Oregon spotted frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Emanahmed, Coquet L, Jouenne T, Jérômeleprince, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Ranapretiosa: implications for species resistance to chytridiomycosis. DRAMP01762 FLPIITNLLGKLL 13 Temporin-PRb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (Oregon spotted frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Emanahmed, Coquet L, Jouenne T, Jérômeleprince, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Ranapretiosa: implications for species resistance to chytridiomycosis. DRAMP01763 NFLDTLINLAKKFI 14 Temporin-PRc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (Oregon spotted frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Emanahmed, Coquet L, Jouenne T, Jérômeleprince, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Ranapretiosa: implications for species resistance to chytridiomycosis. DRAMP01767 FLPALAGIAGLLGKIFGK 18 Temporin-She (Frogs, amphibians, animals) D5GRW4 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-She Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Biol. Chem. 0:0-0(2010). Abbassi F, Lequin O, Piesse C, Goasdoue N, Foulon T, Nicolas P, Ladram A. A. Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide. DRAMP01770 AVDLAKIANIANKVLSSLFGK 21 Temporin-1SKc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sakuraii (Japanese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17174009 Peptides. 2007 Mar;28(3):505-514. Suzuki H, Iwamuro S, Ohnuma A, Coquet L, Leprince J, Jouenne T, Vaudry H, Taylor CK, Abel PW, Conlon JM. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii. DRAMP01772 FLPLIGKILGTILGK 15 Temporin-1Ob (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147973 Peptides. 2007 Mar;28(3):524-532. Ohnuma A, Conlon JM, Yamaguchi K, Kawasaki H, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Japanese mountain brown frog Rana ornativentris: evidence for polymorphism among preprotemporin mRNAs. DRAMP01774 FLPLLASLFSGLF 13 Temporin-1Od (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17147973 Peptides. 2007 Mar;28(3):524-532. Ohnuma A, Conlon JM, Yamaguchi K, Kawasaki H, Coquet L, Leprince J, Jouenne T, Vaudry H, Iwamuro S. Antimicrobial peptides from the skin of the Japanese mountain brown frog Rana ornativentris: evidence for polymorphism among preprotemporin mRNAs. DRAMP01778 FLPAALAGIGGILGKLFGK 19 Temporin-1Sd (Frogs, amphibians, animals) D4YWD0 Belongs to the frog skin active peptide family (Brevinin subfamily) preproTemp-1Sd Pelophylax saharicus (Sahara frog) (Rana saharica) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Biol. Chem. 2010;0:0-0. Abbassi F, Lequin O, Piesse C, Goasdoue N, Foulon T, Nicolas P, Ladram A. A. Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide. DRAMP18302 SCNCVCGFCCSCSPSA 16 GE2270A(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Nonomuraea Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Elongation Factor Tu (EF-Tu) PubMed ID is not available BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. 1997 JAN 13;230(2):320-326. Mohrle VG,Tieleman LN,Kraal B. Elongation Factor Tu1 of the Antibiotic GE2270A Producer Planobispora rosea Has an Unexpected Resistance Profile against EF-Tu Targeted Antibiotics. DRAMP01786 FLPIVGRLISGIL 13 Temporin-CPb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (New World frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP01792 SIFPAIVSFLSKFL 14 Temporin 1HKa (Temporin-1HKa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana heckscheri Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17005262 Regul Pept 2007; 138: 87-93. Conlon JM et al Moler PE. Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group. DRAMP01793 FLPFLKSILGKIL 13 Temporin-1OLa (Temporin 1OLa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana okaloosae (Florida bog frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17005262 Regul Pept 2007; 138: 87-93. Conlon JM et al Moler PE. Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group. DRAMP01794 FLPFFASLLGKLL 13 Temporin-1OLb (Temporin 1OLb; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana okaloosae (Florida bog frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17005262 Regul Pept 2007; 138: 87-93. Conlon JM et al Moler PE. Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group. DRAMP01795 SILPTIVSFLSKVF 14 Temporin-1Ga (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01796 SILPTIVSFLSKFL 14 Temporin-1Gb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01797 SILPTIVSFLTKFL 14 Temporin-1Gc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01798 FILPLIASFLSKFL 14 Temporin-1Gd (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP01799 ILPILGNLLNGLL 13 Temporin-1PRa (Temporin 1PRa; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: It shows only very weak antimicrobial and hemolytic activity. [Ref.15003829]Gram-positive bacteria: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacteria:Escherichia coli (MIC>100 µM);##Fungi:Candida albicans (MIC>100 µM) [Ref:15003829]HC50>300 μM against washed human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15003829 Regul. Pept 2004; 118: 135-141. Conlon JM et al Pal T. A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP01800 ILPILGNLLNSLL 13 Temporin-1PRb (Temporin 1PRb; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15003829 Regul. Pept 2004; 118: 135-141. Conlon JM et al Pal T. A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP01801 FIGPIISALASLFG 14 Temporin-1DYa (Frogs, amphibians, animals) P0C5X6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Active against the Gram-positive bacteria: S. aureus and Gram-negative bacteria E.coli. Tissue specificity: Expressed by the skin glands. PTM: Glycine amide at position 14. Gram-positive bacterium: Staphylococcus aureus (MIC>60 µM);##Gram-negative bacterium: Escherichia coli (MIC>60 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP01802 FFGSVLKLIPKIL 13 Temporin-PTa (Frogs, amphibians, animals) P0C8U2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Has antibacterial activity against the Gram-positive bacteria: S. aureus ATCC 25923 and the Gram-negative bacteria E.coli ATCC 25726. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. Gram-positive bacterium: Staphylococcus aureus ATCC 25923;##Gram-negative bacterium: Escherichia coli ATCC 25726 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01803 VLPLVGNLLNDLL 13 Temporin-CDYa (Frogs, amphibians, animals) B3VZU3 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Antimicrobial activity againist Gram-negative bacteria and Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01804 ILPILAPLIGGLL 13 Temporin-CDYb (Brevinin-1CDYb; Frogs, amphibians, animals) B3VZU4 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Has low activity against the Gram-positive bacteria: S. aureus and Gram-negative bacteria E.coli. Has weak hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. [Swiss_Prot Entry B3VZU4]Gram-positive bacterium: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacterium: Escherichia coli (MIC>100 µM). [Ref:19539775]HC50=180 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01805 FIGPLISALASLFKG 15 Temporin-CDYd (Frogs, amphibians, animals) B3VZU5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Antimicrobial activity againist Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01806 FIGPIISALASLFGG 15 Temporin-CDYe (Frogs, amphibians, animals) B3VZU6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Antimicrobial activity againist Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP01810 FLPIIAKVLSGLL 13 Temporin-1BYa (Frogs, amphibians, animals) P84116 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Antibacterial activity against the Gram-positive bacteria: S. aureus. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-3 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP01813 FLPVIAGLLSKLF 13 Temporin 1Ec (Temporin-1Ec; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta Unknown Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides 2003; 24: 955-961. Ali MF et al Conlon JM. Characterization of novel antimicrobial peptides fromthe skins of frogs of the Rana esculenta complex. DRAMP18352 ATYYGNGVYCNKQECWVDWNKASKEIGKIIVNGWVQHGPWAPR 43 Durancin GL (bacteriocin) No entry found Belongs to the class IIa bacteriocin. Not found Enterococcus durans Antimicrobial, Antibacterial Not found Not found Fuction: Plasmid-encoded bacteriocin is active against the indicator strain E. durans 41D-S1, L. monocytogenes strains, including nisin-resistant L. monocytogenes NR30. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22493306 Microbiology. 2012 Jun;158(Pt 6):1523-32. Du L, Somkuti GA, Renye JA Jr. Molecular analysis of the bacteriocin-encoding plasmid pDGL1 from Enterococcus durans and genetic characterization of the durancin GL locus. DRAMP18301 SCTTCECSCSCSS 13 nocathiacin I(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Nocardia sp. ATCC202099 Antimicrobial, Antibacterial Not found NOC-I shares the overall similarity in structure to the naturally occurring but un-glycosylated analogue, nosiheptide (NOS). NOC-I is further functionalized by the methoxylation of a dehydrothreonine in the macrocyclic core,N-hydroxylation ofthe indole moiety, rigid constraining of these two systems viaan etherbondinadditiontotwoesterlinkages,andappendingofa rare sugar moiety, 2,4,6-tri-deoxy-3-methyl-4-N,N-dimethylaminoL-hexose. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20473441 Mol Biosyst. 2010 Jul;6(7):1180-5. Ding Y, Yu Y, Pan H, Guo H, Li Y, Liu W. Moving posttranslational modifications forward to biosynthesize the glycosylated thiopeptide nocathiacin I in Nocardia sp. ATCC202099. DRAMP01387 GLLSGILGAGKHIVCGLSGPCQSLNRKSSDVEYHLAKC 38 Odorranain-P2a (OdP2a; Frogs, amphibians, animals) A6MBR1 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Odorranain-P2a exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Has no hemolytic activity against red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=6.25 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.12 μg/ml), Bacillus subtilis (MIC=12.5 μg/ml).##Yeast: Candida albicans (MIC=3.12 μg/ml). [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04210 GIGKHVGKALKGLKGLLKGLGES 24 Adepantin-1 (Automatically Designed Peptide antibacterial 1; synthetic) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Helix Not found Function: Antibacterial activity against Gram negative bacteria. Has hemolytic activity. [Ref.19947578] Gram-negative bacteria: Escherichia coli ATCC (MIC=2-4 μM), Pseudomonas aeruginosa (MIC=16 μM). [Ref.19947578] HC50>800 μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membranes 19947578 J Chem Inf Model. 2009 Dec;49(12):2873-82 Juretić D, Vukicević D, Ilić N, Antcheva N, Tossi A. Computational design of highly selective antimicrobial peptides. DRAMP01824 ILPLVGNLLNDLL 13 Temporin-1Ja (Frogs, amphibians, animals) P83307 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana japonica (Japanese reddish frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against the Gram-negative bacteria E. coli and the Gram-positive bacteria: S. aureus. Tissue specificity: Expressed by the skin glands. PTM: Leucine amide at position 13. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11835990 Peptides. 2002 Mar;23(3):419-425. Isaacson T, Soto A, Iwamuro S, Knoop FC, Conlon JM. Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. DRAMP01825 HFLGTLVNLAKKIL 14 Temporin-1DRa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana aurora draytonii (California red-legged frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16307827 Peptides. 2006 Jun;27(6):1305-1312. Conlon JM, Al-Ghafari N, Coquet L, Leprince J, Jouenne T, Vaudry H, Davidson C. Evidence from peptidomic analysis of skin secretions that the red-legged frogs, Rana aurora draytonii and Rana aurora aurora, are distinct species. DRAMP01826 RIGVLLARLPKLFSLFKLMGKKV 23 RV-23 (Frogs, amphibians, animals) No entry found Not found Not found Rana aurora draytonii (California red-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix Not found [Ref.27271216]Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=12.5 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli (MIC=6.25 μM), Pseudomonas aeruginosa (MIC=6.25 μM), Klebsiella pneumoniae (MIC=6.25 μM) [Ref.27271216] 60% hemolysis at 20 μM , 90% hemolysis at 40 μM , 100% hemolysis at 60 μM , 100% hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16307827##27271216 Peptides. 2006 Jun;27(6):1305-1312.##Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Conlon JM, Al-Ghafari N, Coquet L, Leprince J, Jouenne T, Vaudry H, Davidson C.##Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Evidence from peptidomic analysis of skin secretions that the red-legged frogs, Rana aurora draytonii and Rana aurora aurora, are distinct species.##Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP01740 LLPILGNLLNGLL 13 Temporin-C (Frogs, amphibians, animals) P56918 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. PTM: Leucine amide at position 13. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP01126 ILGPVISKIGGVLGGLLKNL 20 Maximin-H4 (Toads, amphibians, animals) P83084, Q58T61, Q58T60 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Shows strong hemolytic activity. [Ref.11835991] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=12 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=6 μg/ml), Bacillus pyocyaneus CMCCB 1010 (MIC=12 μg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=6 μg/ml). [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01125 ILGPVLGLVGNALGGLIKKI 20 Maximin-H3 (Toads, amphibians, animals) P83083, Q58T42, Q58T44, Q58T45, Q58T52, Q58T55, Q58T62, Q58T68, Q58T70 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Shows strong hemolytic activity. [Ref.11835991] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=20 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=10 μg/ml), Bacillus pyocyaneus CMCCB 1010 (MIC=20 μg/ml);##Fungi: Candida albicans ATCC 2002 (MIC=5 μg/ml). [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP18299 WNDTGKDADGAEY 13 Taromycin A (Bacteriocin) No entry found Belongs to the lipopeptides family Not found marine actinomycete Saccharomonospora sp. CNQ-490 Antimicrobial, Antibacterial, Anti-Gram+ Not found Taromycin A differs from Daptomycin only in serveal places: 1) residue T11 is an D-Ala; 2) W is chlorinated at position 6; 3) Kny is also chlorinated at position 4; and 4) it carried an octa-2,4-dienoyl lipid side chain. Warning: the sequence is a close mimic of the natural counterpart. For example, kynurenine-13 (Kyn) is represented by Y here. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24449899 Proc Natl Acad Sci U S A. 2014 Feb 4;111(5):1957-62. Yamanaka K, Reynolds KA, Kersten RD, Ryan KS, Gonzalez DJ, Nizet V, Dorrestein PC, Moore BS. Direct cloning and refactoring of a silent lipopeptide biosynthetic gene cluster yields the antibiotic taromycin A. DRAMP18298 CCSCSCSTCTCTCTCASSAATKM 23 Listeriolysin S(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Listeria monocytogenes F2365 Unknown Not found Not found Comment: A haemolytic and cytotoxic factor, designated Listeriolysin S, which contributes to virulence of the pathogen. This haemolysin is only induced under oxidative stress conditions and contributes to murine virulence and in survival in polymorphonuclear neutrophils. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18787690 PLoS Pathog. 2008 Sep 12;4(9):e1000144. Cotter PD, Draper LA, Lawton EM, Daly KM, Groeger DS, Casey PG, Ross RP, Hill C. Listeriolysin S, a novel peptide haemolysin associated with a subset of lineage I Listeria monocytogenes. DRAMP01835 GFRDVLKGAAKEFVKTVAGHIAN 23 Ascaphin-1M (Frogs, amphibians, animals) No entry found Not found Not found A. montanus (North America inland frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18983817 Biochim Biophys Acta. 2009 Aug;1788(8):1556-1563. Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from the skins of North American frogs. DRAMP01836 GFREVLKGAAKAFVKTVAGHIANI 24 Ascaphin-3M (Frogs, amphibians, animals) No entry found Not found Not found A. montanus (North America inland frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18983817 Biochim Biophys Acta. 2009 Aug;1788(8):1556-1563. Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from the skins of North American frogs. DRAMP01837 GFKDWIKGAAKKLIKTVASNIANQ 24 Ascaphin-4M (Frogs, amphibians, animals) No entry found Not found Not found A. montanus (North America inland frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18983817 Biochim Biophys Acta. 2009 Aug;1788(8):1556-1563. Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from the skins of North American frogs. DRAMP01838 GIKDWIKGAAKTLIKTVASHIANQ 24 Ascaphin-5M (Frogs, amphibians, animals) No entry found Not found Not found A. montanus (North America inland frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18983817 Biochim Biophys Acta. 2009 Aug;1788(8):1556-1563. Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from the skins of North American frogs. DRAMP01839 GFKDWIKSAAKKLIKTVASNIANQ 24 Ascaphin-7M (Frogs, amphibians, animals) No entry found Not found Not found A. montanus (North America inland frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18983817 Biochim Biophys Acta. 2009 Aug;1788(8):1556-1563. Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from the skins of North American frogs. DRAMP01841 GFRDVLKGAAKQFVKTVAGHIANI 24 Ascaphin-2 (Frogs, amphibians, animals) P0CJ26 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. [Ref.15207717]Gram-negative bacterium: Escherichia coli [Ref.15207717]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01843 GFKDWIKGAAKKLIKTVAANIANQ 24 Ascaphin-4 (Frogs, amphibians, animals) P0CJ28 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. [Ref.15207717]Gram-negative bacterium: Escherichia coli [Ref.15207717]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01845 GFKDWIKGAAKKLIKTVASSIANE 24 Ascaphin-6 (Frogs, amphibians, animals) P0CJ30 Belongs to the ascaphin family Not found Ascaphus truei (Coastal tailed frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. Caution: May represent an artifactually modified form of ascaphin-7 arising from hydrolysis during the purification procedure." [Ref.15207717]Gram-negative bacterium: Escherichia coli [Ref.15207717]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15207717 Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175. Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP01848 GFKKLLKGAAKALVKTVLF 19 [D4k]ascaphin-8 No entry found Not found Not found Ascaphus truei (Coastal tailed frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22374306 Peptides. 2012 Apr;34(2):275-282. Popovic S, Urbán E, Lukic M, Conlon JM. Peptides with antimicrobial and anti-inflammatory activities that have therapeutic potential for treatment of acne vulgaris. DRAMP01850 RGFMDTAKNVAKNMAVTLLDNLKCKITKAC 30 Odorranain-F-RA1 antimicrobial peptide (Frogs, amphibians, animals) D2K8I2, D2K8E4 Not found Not found Rana andersonii (Golden crossband frog) Not found Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ database Yang X, Liang X, Zhang Y, Lee W.-H. The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP18297 ISVCITVC 8 Patellamide D(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Lissoclinum patella Unknown Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2724305 J Med Chem. 1989 Jun;32(6):1349-54. Degnan BM, Hawkins CJ, Lavin MF, McCaffrey EJ, Parry DL, van den Brenk AL, Watters DJ. New cyclic peptides with cytotoxic activity from the ascidian Lissoclinum patella. DRAMP18296 WXAVFXNMAKYMFKSQSKXVVIGFLVAS 28 Leucocin H beta(Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Leuconostoc MF215B Antimicrobial, Antibacterial, Anti-Gram+ Not found No sequence homology to other known bacteriocins could be demonstrated. It also appeared that the two peptides themselves shared little or no sequence homology. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10387116 Curr Microbiol. 1999 Jul;39(1):43-8. Blom H, Katla T, Holck A, Sletten K, Axelsson L, Holo H. Characterization, production, and purification of leucocin H, a two-peptide bacteriocin from Leuconostoc MF215B. DRAMP01853 FLPLIAGLAANFLPKLFCKITKKC 24 Brevinin-1-RAB2 antimicrobial peptide (Frogs, amphibians, animals) D2K8D2, D2K8G7 Not found Not found Rana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. Yang X, Liang X, Zhang Y, Lee W.-H. The highest antimicrobial peptide diversity, skin antimicrobialpeptides peptidomics of Amphibian, Rana andersonii. DRAMP01854 GFLDTLKNMALNAAKGAGGSVLKALFCKLFKTC 33 Brevinin-2-RA21 antimicrobial peptide (Frogs, amphibians, animals) D2K8J5 Not found Not found Rana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ database Yang X, Liang X, Zhang Y, Lee W.-H. The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP01855 GLLDTFKNLALNAAKSAGVSVLNSLSCKLFKTC 33 Brevinin-2E-OG4 antimicrobial peptide (Frogs, amphibians, animals) A6MAT9, A6MAU0 Not found Not found Odorrana grahami (Yunnanfu frog ) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP18295 WXIGVTGAALGTGKGVKNVI 20 Leucocin H alpha(Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Leuconostoc MF215B Antimicrobial, Antibacterial, Anti-Gram+ Not found No sequence homology to other known bacteriocins could be demonstrated. It also appeared that the two peptides themselves shared little or no sequence homology. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10387116 Curr Microbiol. 1999 Jul;39(1):43-8. Blom H, Katla T, Holck A, Sletten K, Axelsson L, Holo H. Characterization, production, and purification of leucocin H, a two-peptide bacteriocin from Leuconostoc MF215B. DRAMP01857 GLLDTLKNMAINAAKDAGVSVLNTLSCKLSKTC 33 Brevinin-2-RA20 antimicrobial peptide (Frogs, amphibians, animals) D2K8J4 Not found Not found Rana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ database Not found The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP01858 GLLDTLKNMAINAAKGAGVSVLNALSCKLSKTC 33 Brevinin-2-RA6 antimicrobial peptide (Frogs, amphibians, animals) D2K8C6, D2K8D4, D2K8D8 Not found Not found Odorrana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Not found The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP01859 GLLDTLKNMATNAAKGAGVSVLKALSCKLFKTC 33 Brevinin-2-RA22 antimicrobial peptide (Frogs, amphibians, animals) D2K8J6 Not found Not found Odorrana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ database Not found The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP01860 MFTFKKSMLLLFFLGTINLSLCEQERNADEEERRDDEDKRDVEVEKRFLGSLLGLVGKIVPTLICKISKKC 71 Brevinin-1RTa antimicrobial peptide (Frogs, amphibians, animals) D1MIZ4 Not found Not found Amolops ricketti (Chinese sucker frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. ntification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP01861 MFTSKKSLLVLFFLGTISLSFCEEERNADEDDGEMTEEVKRGILDTLKEFGKTAAKGIAQSLLSTASCKLAKTC 74 Brevinin-2RTb antimicrobial peptide (Frogs, amphibians, animals) D1MIZ8 Not found Not found Amolops ricketti (Chinese sucker frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. ntification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP01862 MFTSKKSMLLLFFLGTINLSLCEQERNADEEERRDDEDKRDVEVEKRFLGSLLGLVGKVVPTLFCKISKKC 71 Brevinin-1RTb antimicrobial peptide (Frogs, amphibians, animals) D1MIZ6 Not found Not found Amolops ricketti (Chinese sucker frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. ntification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP01863 MFTTKKSLLVLFFLGTISLSFCEEERNADEDDGEMTEEEKRGLMSTLKDFGKTAAKEIAQSLLSTASCKLAKTC 74 Brevinin-2RTa antimicrobial peptide (Frogs, amphibians, animals) D1MIZ7 Not found Not found Amolops ricketti (Chinese sucker frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. ntification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP01864 SFLTSFKDMAIKVAKDAGVNILNTISCKIFKTC 33 Brevinin-2-RA13 antimicrobial peptide (Frogs, amphibians, animals) D2K8C8 Not found Not found Rana andersonii (golden crossband frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ database Not found The highest antimicrobial peptide diversity, skin antimicrobialpeptide peptidomics of amphibian, Rana andersonii. DRAMP01865 MFTMKKSLLLLFFLGTISLSLCEQERDAEEEEGSENGAEDIKLNRVVKCSYRLGSPDSRCN 61 Odorranain-A-RA1 antimicrobial peptide (Frogs, amphibians, animals) D2K8C3 Not found Not found Odorrana andersonii (golden crossband frog) Antibiotic Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Yang X, Liang X, Zhang Y, Lee WH. The highest antimicrobial peptides diversity, skin antimicrobial peptides peptidomics of Amphibian, Rana andersonii. DRAMP01866 MFTLKKSLLLLFFLGTINLSLCEQERDADEEERRDDDEMDVEVEKRFLPLFLPKIICAITKKC 63 Mantzorumin-D1 antimicrobial peptide (Frogs, amphibians, animals) E1B245 Not found Not found Amolops mantzorum Antibiotic Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops mantzorum. DRAMP01867 MFTLKKSMLLLFFLGTINLSLCEQERDAEEERRDDEDKRDVEVEKRFVLGVVTKLLPSLFCMITKKC 67 Hainanensisin-A4 antimicrobial peptide (Frogs, amphibians, animals) E7EKF2 Not found Not found Amolops hainanensis (Hainan sucker frog) Antibiotic Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops hainanensis. DRAMP01868 MFTFKKSMLLLFFLGTINLSLCEQERNADEEERRDDPDETNVEVEKRFLPLLAGVVANFLPQIICKIARKC 71 Brevinin-1E-RTa antimicrobial peptide (Frogs, amphibians, animals) D1MIZ4 Not found Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibiotic Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP01871 FLPIIASVAAKLIPSIVCRITKKC 24 Brevinin-1SPc (Frogs, amphibians, animals) No entry found Not found Not found Rana septentrionalis (mink frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: Has inhibitory activity towards reference strains of bacteria and an opportunistic yeast pathogen. Also has hemolytic activity against human erythrocytes. No MICs found in DRAMP database [Ref.15556063]HC50=3 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15556063 Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):31-38. Bevier CR, Sonnevend A, Kolodziejek J, Nowotny N, Nielsen PF, Conlon JM. Purification and characterization of antimicrobial peptides from the skin secretions of the mink frog (Rana septentrionalis). DRAMP01874 VIPFVASVAAEMMPHVYCAASRKC 24 Brevinin-1Eba (Frogs, amphibians, animals) No entry found Not found Transcript level Rana esculenta Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-61. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01882 MFTLKKTLLLIFVLGTISLSLCEQERGADEDEGEAVEEIKRGLLDSVKEGLKKVAGQLLDTLKCKISGCTPA 72 Pleurain-M1 antimicrobial peptide (Frogs, amphibians, animals) B5L1L3 Not found Not found Rana pleuraden (Yunnan pond frog) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-583. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP01883 MRMSIKCFAVIFVAFAFFLGQISRAEACIPDGGRCHESDPGPGCCSGFCYRERNWKDGDCRKRP 64 Salivary gland antimicrobial peptide 1 Q3LTD6 Not found Not found Bradysia hygida Antimicrobial Predicted Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases da Silva JAC, Zanarotti GM, Gallina AP, de Almeida JC. The innate immune system of larvae and pupae of Bradysia hygida (Diptera, Sciaridae) is provided with an additional external preventive mechanism of defense, which is regulated in development. DRAMP01884 MFTMKKSLLLLFFLGMISLSLCQDERGADEDDGGEMTEEEKRGAFGNFLKGVAKKAGLKILSIAQCKLSGTC 72 Nigroain-F antimicrobial peptide (Frogs, amphibians, animals) C0ILA3 Not found Not found Rana nigrovittata (Black-striped frog) (Hylarana nigrovittata) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Genomics. 2010,95:66-71. Ma Y., Liu C., Liu X., Wu J., Yang H., Wang Y., Li J., Yu H., Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP01894 FFPIVAGVAGQVLKKIFCTISKKC 24 Brevinin 1Pg (Frogs, amphibians, animals) A9CBI5 Not found Not found Rana pipiens (Northern leopard frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17938991 J Mol Evol. 2007 Nov;65(5):605-615. Tennessen JA, Blouin MS. Selection for antimicrobial peptide diversity in frogs leads to gene duplication and low allelic variation. DRAMP01895 FTSKKSMLLFFFLGTISLSLCQ 22 Brevinin-2CE (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana chensinensis (Chinese brown frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21303203 Zoolog Sci. 2011 Feb;28(2):112-117. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis. DRAMP01901 GILDKLKEFGISAARGVAQSLLNTASCKLAKTC 33 Brevinin-2CG1 (Frogs, amphibians, animals) No entry found Not found Not found Amolops chunganensis Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Not found Not found Not found Function: Primarily active against Gram-positive bacteria. Also highly active against Gram-negative P. faecalis X29 and S. rubidaea. Gram-negative bacteria: P. faecalis X29, S. rubidaea. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22951323 Peptides. 2012 Nov;38(1):41-53. Yang X, Xia J, Yu Z, Hu Y, Li F, Meng H, Yang S, Liu J, Wang H. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis. DRAMP01902 GLLDTFKNMALNAAKSAGVSVLNSLSCKLSKTC 33 Brevinin-2E-OG7 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01903 FLPLLAGLAANFLPKLFCKITKKC 24 Brevinin-1E-OG1 (brevinin-1E-OG3; Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01904 GLLDTFKNLALNAPKSAGVSVLNSLSCKLSKTC 33 Brevinin-2E-OG2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01905 FLPLLAGLAANFLPKLFCKITRKC 24 Brevinin-1E-OG5 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01906 FLPFLAGLAANFLPKLFCKITRKC 24 Brevinin-1E-OG4 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP01907 FFPLIAGLAANFLPQILCKIARKC 24 Antimicrobial peptide brevinin-1E-OG7 (Frogs, amphibians, animals) C3RTH8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Yunnanfu frog) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Ma Y, Lai R, Wu J, Li J. Antimicrobial peptide from skin of Odorrana grahami. DRAMP01908 GILDTLKNLAKTAGKGILKSLVNTASCKLSGQC 33 Brevinin 2Ta (Frogs, amphibians, animals) P82268 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial Transcript level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 27-33. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. Simmaco M, Miele R, Mangoni M.L, Barra D. A cDNA clone encoding brevinin 2Ta from Rana temporaria. DRAMP01915 GVLGTVKNLLIGAGKSAAQSVLKTLSCKLSNDC 33 Brevinin-2GRb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grahami (Asian frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database [Ref.16621155] LC50=180 μM against human erythrocytes. Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 16621155##17272268 Peptides. 2006 Sep;27(9):2111-2117.##Mol Cell Proteomics. 2007 May;6(5):882-894. Conlon JM, Al-Ghaferi N, Abraham B, Jiansheng H, Cosette P, Leprince J, Jouenne T, Vaudry H.##Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami.##Anti-infection peptidomics of amphibian skin. DRAMP01916 GVIIDTLKGAAKTVAAELLRKAHCKLTNSC 30 Brevinin-2GU (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana guntheri (Asian frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19332309 J Biosci Bioeng. 2009 Apr;107(4):460-463. Zhou QF, Li MY, Li CW. Cloning and expression of a novel insulin-releasing peptide, brevinin-2GU from Escherichia coli. DRAMP01917 FFPNVASVPGQVLKKIFCAISKKC 24 Brevinin-1PLa (Frogs, amphibians, animals) B6CPR5 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (Pickerel frog) Antimicrobial, Antifungal Protein level Not found Not found Inhibit the growth of Batrachochytrium dendrobatidis (Bd) (MIC=50 µM), a fungus that might have played a role in killing many frogs. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18799711##11087945 Mol Biol Evol. 2008 Dec;25(12):2669-2680.##Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. Tennessen JA, Blouin MS.##Basir YJ, Knoop FC, Dulka J, Conlon JM. Balancing selection at a frog antimicrobial peptide locus: fluctuating immune effector alleles? ##Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP01923 FFPAIFRLVAKVVPSIICSVTKKC 24 Brevinin-1R (Frogs, amphibians, animals) P86027 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342##18855342 Mass Spectrom. 2007;4:79-88.##Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Artemenko K.A, Samgina T.Y, Lebedev A.T, Doyle J.R, Llewellyn L.E, Bilusich D, Bowie J.H.##Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Host-defence peptides from the skin secretion of the European marsh frog Rana ridibunda.##De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01924 FLPAIFRMAAKVVPTIICSITKKC 24 Brevinin-1Ea (Frogs, amphibians, animals) P40835 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. [Swiss_Prot Entry P40835]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50=0.5 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01925 VIPFVASVAAEMQHVYCAASRKC 23 Brevinin-1Eb (Frogs, amphibians, animals) P40836 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (European frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. [Swiss_Prot Entry P40836]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50=0.5 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01926 FLPLLAGLAANFFPKIFCKITRKC 24 Brevinin-1Ec (Frogs, amphibians, animals) P86150 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana ridibunda (Laughing frog) (Marsh frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. [Swiss_Prot Entry P86150]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.18855342]show hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01927 GILDTLKNLAISAAKGAAQGLVNKASCKLSGQC 33 Brevinin-2Ea (Frogs, amphibians, animals) P40837 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40837]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01928 GILDTLKNLAKTAGKGALQGLVKMASCKLSGQC 33 Brevinin-2Eb (Frogs, amphibians, animals) P40838 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40838]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01929 GILLDKLKNFAKTAGKGVLQSLLNTASCKLSGQC 34 Brevinin-2Ec (Frogs, amphibians, animals) P40839, P84842 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) (Rana saharica (Sahara frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40839]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497##16394170 J Biol Chem. 1994 Apr 22;269(16):11956-11961.##J Endocrinol. 2006 Jan;188(1):1-9. Simmaco M, Mignogna G, Barra D, Bossa F.##Marenah L, Flatt PR, Orr DF, Shaw C, Abdel-Wahab YH. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.##Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity. DRAMP01930 VIPFVASVAAEMMHHVYCAASKRC 24 Brevinin-1Ed (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Korea) Antimicrobial, Antibacterial, Anti-Gram+ Not found Alpha helix Not found This is a narrow spectrum AMP from the frog. Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15232222 Mol Cells. 2004 Jun 30;17(3):469-476. Won HS, Kim SS, Jung SJ, Son WS, Lee B, Lee BJ. Structure-activity relationships of antimicrobial peptides from the skin of Rana esculenta inhabiting in Korea. DRAMP01931 GILDSLKNLAKNAGQILLNKASCKLSGQC 29 Brevinin-2Ed (Frogs, amphibians, animals) P40840 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40840]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01932 GIFDKLKNFAKGVAQSLLNKASCKLSGQC 29 Brevinin-2Ee (Frogs, amphibians, animals) P40841 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity [Swiss_Prot Entry P40841]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.8163497]LC50>100 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8163497 J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP01936 GLWNTKLEAGLLFAMGKLDLKRCLKAGGC 29 Brevinin-2Ek (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta complex Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found "Function: Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli (By similarity). Sequence similarity: This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14499272 Peptides. 2003 Jul;24(7):955-961. Ali MF, Knoop FC, Vaudry H, Conlon JM. Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex. DRAMP01945 FLPLVRGAAKLIPSVVCAISKRC 23 Brevinin-1SE (Frogs, amphibians, animals) P85056 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sevosa (Dusky gopher frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Gram-negative bacterium: Escherichia coli K12;##Gram-positive bacterium: Micrococcus luteus NCT C2665. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16386333 Peptides. 2006 Jun;27(6):1313-1319. Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. DRAMP01946 GLFNVFKGLKTAGKHVAGSLLNQLKCKVSGGC 32 Brevinin-20a (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana Ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11892844 J Pept Res. 2001 Nov;58(5):349-356. Kim JB et al Conlon JM. Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris. DRAMP01947 GIFNVFKGALKTAGKHVAGSLLNQLKCKVSGEC 33 Brevinin-20b (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana Ornativentris (Japanese mountain brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11892844 J Pept Res. 2001 Nov;58(5):349-356. Kim JB et al Conlon JM. Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris. DRAMP18293 KGGSGVIHTISHEVIYNSWNFVFTCCS 27 Bacteriocin J46 (Bacteriocin) P71449 Belongs to the lantibiotics family (Class I bacteriocin) lcp J Lactococcus lactis J46 Unknown Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8588891 Lett Appl Microbiol. 1996 Jan;22(1):76-9. Huot E, Barrena-Gonzalez C, Petitdemange H. Comparative effectiveness of nisin and bacteriocin J46 at different pH values. DRAMP18294 ALQFIQNTASGALYYNTKTHKYQYQQTSGA 30 lactococcin Z(Bacteriocin) No entry found Belongs to the class IId bacteriocin lczA Lactococcus lactis QU 7 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Lactococcin Z showed homology to lactococcins A, B and M. Comment: No comments found on DRAMP database Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26093857 Probiotics Antimicrob Proteins. 2015 Sep;7(3):222-31. Ishibashi N, Seto H, Koga S, Zendo T, Sonomoto K. Identification of Lactococcus-Specific Bacteriocins Produced by Lactococcal Isolates, and the Discovery of a Novel Bacteriocin, Lactococcin Z. DRAMP01952 FMGGLIKAATKALPAAFCAITKKC 24 Brevinin-1PTb (Frogs, amphibians, animals) P0C8T2 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24." Gram-positive bacterium: Staphylococcus aureus ATCC 25923;##Gram-negative bacterium: Escherichia coli ATCC 25726. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01954 GLLDTLKNMAINAAKGAGQSVLNTLSCKLSKTC 33 Brevinin-2HSb (Frogs, amphibians, animals) P0C8T0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana hosii (Hose's rock frog) (Rana hosii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923;##Gram-negative bacterium: Escherichia coli ATCC 25726. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01958 GFLDSFKNAMIGVAKSAGKTALNTLACKIDKTC 33 Brevinin-2PTd (Frogs, amphibians, animals) P0C8T6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana picturata (Malaysian fire frog) (Hylarana picturata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 27-33." Gram-positive bacterium: Staphylococcus aureus ATCC 25923;##Gram-negative bacterium: Escherichia coli ATCC 25726. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys27 and Cys33) Disulfide bond between Cys27 and Cys33. L No cytotoxicity information found Not found 18621071 Toxicon. 2008 Sep 1;52(3):465-473. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, King JD. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). DRAMP01960 FLPILASLAAKFGPKLFCLVTKKC 24 Brevinin-1BYa (Frogs, amphibians, animals) P84111 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has hemolytic activity. [Ref.14531844]Gram-positive bacterium: Staphylococcus aureus(MIC=2 µM);##Gram-negative bacterium: Escherichia coli(MIC=17 µM);##Yeast: Candida albicans(MIC=3 µM) [Ref.14531844]HC50=4 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP01961 FLPILASLAAKLGPKLFCLVTKKC 24 Brevinin-1BYb (Frogs, amphibians, animals) P84112 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has hemolytic activity. [Ref.14531844]Gram-positive bacterium: Staphylococcus aureus(MIC=4 µM);##Gram-negative bacterium: Escherichia coli(MIC=16 µM);##Yeast: Candida albicans(MIC=16 µM). [Ref.14531844]HC50=4 µM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP01962 FLPILASLAATLGPKLLCLITKKC 24 Brevinin-1BYc (Frogs, amphibians, animals) P84113 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans (weak activity). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-3 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP01964 FLPIIAGVAAKVLPKIFCAISKKC 24 Brevinin-1BLb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates blairi (leopard frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01966 FLPVIAGVAANFLPKLFCAISKKC 24 Brevinin-1Ya (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates yavapaiensis (North America leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.19254736] Gram-positive bacteria : Staphylococcus aureus(MIC=3 μM);##Gram-negative bacteria : Escherichia coli(MIC=50 μM);##Fungi : Candida albicans(MIC=12 μM) [Ref.19254736] LC50=18 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01967 FLPIIAGAAAKVVQKIFCAISKKC 24 Brevinin-1Yb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates yavapaiensis (North America leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.19254736] Gram-positive bacteria : Staphylococcus aureus(MIC=3 μM);##Gram-negative bacteria : Escherichia coli(MIC=25 μM);##Fungi : Candida albicans(MIC=3 μM) [Ref.19254736] LC50=16 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19254736 Toxicon. 2009 Jun;53(7-8):699-705. doi: 10.1016/j.toxicon.2009.02.018. Conlon JM, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis. DRAMP01972 FLPLLPSALPSFLCLVFKKC 20 Brevinin-1ZHc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01973 FLPLLLSALPSFSCLVFKKC 20 Brevinin-1ZHd (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana zhenhaiensis (Chinese brown frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular Cloning and Functional Characterization of Novel Antimicrobial Peptides from the Skin of Brown Frog, Rana zhenhaiensis. DRAMP01975 VIPFVASVAAEMMQHVYCAASRRC 24 Brevinin-1Ra (Frogs, amphibians, animals) P86028 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 18-24." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342##18280749 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525.##J Am Soc Mass Spectrom. 2008 Apr;19(4):479-487. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT.##Samgina TY, Artemenko KA, Gorshkov VA, Poljakov NB, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda.##Oxidation versus carboxamidomethylation of S-S bond in ranid frog peptides: pro and contra for de novo MALDI-MS sequencing. DRAMP01976 GIMDTLKNLAKTAGKGALQSLLNHASCKLSGQC 33 Brevinin-2Eg (Frogs, amphibians, animals) P86154 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity. [Swiss_Prot Entry P86154]Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species [Ref.18855342]show hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP18292 FKKKKRNIGTFVFFAIALFCTVMFAYLLLTNQYVPIDYNVPRYA 44 LsbA(Bacteriocin) O68888 Belongs to the class IId bacteriocin lsbA Lactococcus lactis Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive(narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12801935 J Biol Chem. 2003 Sep 5;278(36):34291-8. Gajic O, Buist G, Kojic M, Topisirovic L, Kuipers OP, Kok J. Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. DRAMP01978 KLKNFAIGVAQSLLNKASCKLSGQC 25 Brevinin-2R (Frogs, amphibians, animals) P85095 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial, Antibacterial, Anti-cancer Protein level Not found Not found Function: Cytotoxicity towards malignant cells, including Jurkat (T-cell leukemia), BJAB (B-cell lymphoma), HT29/219, SW742 (colon carcinomas), L929 (fibrosarcoma), MCF-7 (breast adenocarcinoma), A549 (lung carcinoma), acts via the activation of the lysosomal-mitochondrial death pathway and autophagy-like cell death. Does not show significant hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 19-25. [Swiss_Prot Entry P85095]Cytotoxic to cancer cells, acts via the activation of the lysosomal-mitochondrial death pathway and autophagy-like cell death [Ref.18494941]2.5% hemolytic activity at 200 μg/ml against sheep erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18494941 Cell Mol Med. 2008 Jun;12(3):1005-1022. Ghavami S, Asoodeh A, Klonisch T, Halayko AJ, Kadkhoda K, Kroczak TJ, Gibson SB, Booy EP, Naderi-Manesh H, Los M. Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway. DRAMP01979 GILDSLKNFAKDAAGILLKKASCKLSGQC 29 Brevinin-2Ra (Frogs, amphibians, animals) P86022 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. (By similarity) Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 23-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01980 GLMSTLKGAATNAAVTLLNKLQCKLTGTC 29 Brevinin-2Rb (Frogs, amphibians, animals) P86023 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. (By similarity) Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 23-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01981 GLMSTLKGAATNVAVTLLNKLQCKLTGTC 29 Brevinin-2Rc (Frogs, amphibians, animals) P86024 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. (By similarity) Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 23-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP01982 GILDSLKNLAKNAAQILLNKASCKLSGQC 29 Brevinin-2Rd (Frogs, amphibians, animals) P86025 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. (By similarity) Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 23-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP18291 LAMVKYYGNGVSCNWRKHSCKKGLSVDWVYFGLLHNLGALRWYQHR 46 Garviecin LG34(Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Lactococcus garvieae LG34 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Garviecin LG34 showed resistance to heat and low pH, and was sensitive to proteolytic enzymes but not to lipase and amylase. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Food Control. 2015 Apr;50:896-900. Gao YR,Li DP,Liu S,Zhang LY. Garviecin LG34, a novel bacteriocin produced by Lactococcus garvieae isolated from traditional Chinese fermented cucumber. DRAMP01984 FLPLIASVAANLAPKIICKITKTC 24 Brevinin-1HS2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Huia schmackeri (Chinese piebald odorous frog) Antimicrobial Not found Not found Not found "Function: Antimicrobial peptide homologs. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18423796 Peptides. 2008 Aug;29(8):1456-1460. Quan Z, Zhou M, Chen W, Chen T, Walker B, Shaw C. Novel brevinins from Chinese piebald odorous frog (Huia schmackeri) skin deduced from cloned biosynthetic precursors. DRAMP01985 GLWDTIKQAGKKIFLSVLDKIRCKVAGGC 29 Brevinin-2HS1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Huia schmackeri (Chinese piebald odorous frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found "Function: Antimicrobial peptide homologs. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18423796 Peptides. 2008 Aug;29(8):1456-1460. Quan Z, Zhou M, Chen W, Chen T, Walker B, Shaw C. Novel brevinins from Chinese piebald odorous frog (Huia schmackeri) skin deduced from cloned biosynthetic precursors. DRAMP01987 SILGTVKDLLIGAGKSAALSVLKGLSCKLSKDC 33 Brevinin-2HS3 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Huia schmackeri (Chinese piebald odorous frog) Antimicrobial Not found Not found Not found "Function: Antimicrobial peptide homologs. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18423796 Peptides. 2008 Aug;29(8):1456-1460. Quan Z, Zhou M, Chen W, Chen T, Walker B, Shaw C. Novel brevinins from Chinese piebald odorous frog (Huia schmackeri) skin deduced from cloned biosynthetic precursors. DRAMP01988 FFGTALKIAANVLPTAICKILKKC 24 Brevinin-1LTa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (Chinese frog fauna) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Tissue specificity: Expressed by the skin glands. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 19022312 Peptides. 2009 Feb;30(2):273-282. Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). DRAMP01989 FFGTALKIAANILPTAICKILKKC 24 Brevinin-1LTb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (Chinese frog fauna) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found "This peptide differs from Brevinin-1LTa by only one residue (I vs. V). This conservative change allows to predict that this peptide has all the activities of Brevinin-1LTa. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 19022312 Peptides. 2009 Feb;30(2):273-282. Wang H, Lu Y, Zhang X, Hu Y, Yu H, Liu J, Sun J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). DRAMP01991 FFGSVLKVAAKVLPAALCQIFKKC 24 Brevinin-1LT2 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Hylarana latouchii (Chinese broad-folded frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19340924 Biochimie. 2009 Apr;91(4):540-547. Wang H, Yan X, Yu H, Hu Y, Yu Z, Zheng H, Chen Z, Zhang Z, Liu J. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae). DRAMP01992 FLPLVRVAAKLIPSVVCAISKRC 23 Brevinin-1CPa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (North American frog) Antimicrobial, Antibacterial Not found Not found Not found Function: Antimicrobial peptides. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP01993 FLPVLARLAVKFLPSIVCAATKKC 24 Brevinin-1Wa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates capito (the New World frog) Antimicrobial Not found Not found Not found Function: Antimicrobial peptides. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19635516 Peptides. 2009 Oct;30(10):1775-1781. Conlon JM, Meetani MA, Coquet L, Jouenne T, Leprince J, Vaudry H, Kolodziejek J, Nowotny N, King JD. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae). DRAMP18289 KRKKHRCRVYNNGMPTGMYRWC 22 Bactofencin A (Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Lactobacillus salivarius DPC6502 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24169573 MBio. 2013 Oct 29;4(6):e00498-13. O'Shea EF, O'Connor PM, O'Sullivan O, Cotter PD, Ross RP, Hill C. Bactofencin A, a new type of cationic bacteriocin with unusual immunity. DRAMP18290 IGGALGNALNGLGTWANMMNGGGFVNQWQVYANKGKINQYRPY 43 Garvicin A (Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Lactococcus garvieae 21881 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive(certain) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23666326 Appl Environ Microbiol. 2013 Jul;79(14):4336-46. Maldonado-Barrag Garvicin A, a novel class IId bacteriocin from Lactococcus garvieae that inhibits septum formation in L. garvieae strains. DRAMP18287 MSYEKLNNEELSKILGGNGINWGAVAGSCASGAVIGAAFGNPLTGCVANSAFSFSWQAFKNRPRPKKIA 69 Blp1b(Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus salivarius BGHO1 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22739096 Int J Antimicrob Agents. 2012 Aug;40(2):127-34. Busarcevic M, Dalgalarrondo M. Purification and genetic characterisation of the novel bacteriocin LS2 produced by the human oral strain Lactobacillus salivarius BGHO1. DRAMP18288 KRGPNCVGNFLGGLFAGAAAGVPLGPAGIVGGANLGMVGGALTCL 45 Sln1 (Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus salivarius DPC6005 Antimicrobial, Antibacterial Not found Not found Shown is the sequence for chain a, which is identical at the amino acid level to the chain a of ABP-118. The peptide sequence for chain b is also similar to chain b of ABP-118 with only two changes: T43 to Ala and Arg46 to His. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17416691 Appl Environ Microbiol. 2007 Jun;73(11):3719-23. Barrett E, Hayes M, O'Connor P, Gardiner G, Fitzgerald GF, Stanton C, Ross RP, Hill C. Salivaricin P, one of a family of two-component antilisterial bacteriocins produced by intestinal isolates of Lactobacillus salivarius. DRAMP18286 ECELAKVDGGYTPKNCAMAVGGGMLSGAIRGGMSGTVFGVGTGNLAGAFAGAHIGLVAGGLACIGGYLGSH 71 Blp1a(Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus salivarius BGHO1 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22739096 Int J Antimicrob Agents. 2012 Aug;40(2):127-34. Busarcevic M, Dalgalarrondo M. Purification and genetic characterisation of the novel bacteriocin LS2 produced by the human oral strain Lactobacillus salivarius BGHO1. DRAMP02002 FLPALIGIAAKALPSLLCKITKKC 24 Brevinin-1P (Frogs, amphibians, animals) Q2UXW0 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana fukienensis (Fukien gold-striped pond frog) (Rana plancyi fukienensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antimicrobial peptide.(By similarity). It shows hemolytic activity against host erythrocytes. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139929 Peptides. 2006 Jan;27(1):42-48. Chen T, Li L, Zhou M, Rao P, Walker B, Shaw C. Amphibian skin peptides and their corresponding cDNAs from single lyophilized secretion samples: identification of novel brevinins from three species of Chinese frogs. DRAMP02003 FFPAILRVAAKVGPAVLCAITKKC 24 Brevinin-1S (Frogs, amphibians, animals) Q2UXV9 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana schmackeri (Schmacker's frog) (Huia schmackeri) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antimicrobial peptide.(By similarity) Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 18-24." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139929 Peptides. 2006 Jan;27(1):42-48. Chen T, Li L, Zhou M, Rao P, Walker B, Shaw C. Amphibian skin peptides and their corresponding cDNAs from single lyophilized secretion samples: identification of novel brevinins from three species of Chinese frogs. DRAMP18285 TNWKKIGKCYAGTLGSAVLGFGAMGPVGYWAGAGVGYASFC 41 Bacteriocin LS2 (Bacteriocin) I0B594 Belongs to the class IId bacteriocin bacls2 Lactobacillus salivarius BGHO1 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Note that the strain Lactobacillus salivarius BGHO1 exhibits a wide antimicrobial spectrum against S. flexneri, S. sonnei, S. dysenteriae, S. boydii, Y. enterocolitica, S. enteritidis, L. innocua, S. aureus, E. faecalis, M. flavus, S. pneumoniae and S. mutans. However, this broad spectrum could result from synergistic effect of its bacteriocins and the lactic acid which, in addition to the general antimicrobial effects exhibited by lowering the pH, can permeabilise the outer membrane of Gram-negative bacteria and make them more vulnerable to the effects of bacteriocins. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22739096 Int J Antimicrob Agents. 2012 Aug;40(2):127-34. Busarcevic M, Dalgalarrondo M. Purification and genetic characterisation of the novel bacteriocin LS2 produced by the human oral strain Lactobacillus salivarius BGHO1. DRAMP18284 IYWIADQFGIHLATGTARKLLDAMASGASLGTAFAAILGVTLPAWALAAAGALGATAA 58 Reutericin 6 (Bacteriocin) No entry found Belongs to the class IIc bacteriocin Not found Lactobacillus reuteri LA6 Antimicrobial, Antibacterial, Anti-Gram+ Alpha helix Not found L.reuteri LA6 has the structural gene for gassericin A with no variations among those primers. These results indicate that a bacteriocin of the same structure has been produced by different lactobacilli species isolated from the same infant. Gram-positive(certain) No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found PubMed ID is not available Letters in Applied Microbiology. 1991 Dec;13(6):281 T. Toba, S.K. Samant, E. Yoshioka and T. Itoh Reutericin 6, a new bacteriocin produced by Lactobacillus reuteri LA 6. DRAMP18283 KTKQQFLIKAQTQLFKVFGYTL 22 Plantaricin ZJ5 (Bacteriocin) T1WIT7 Belongs to the class IId bacteriocin Not found Lactobacillus plantarum ZJ5 Antimicrobial, Antibacterial Not found Not found Comment: 37% similar to Warnericin RK.The peptide activity was lost by treatment with pepsin and proteinase K (62%) but not affected by lipase or alpha-amylase. broad-spectrum No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25147943 PLoS One. 2014 Aug 22;9(8):e105549. Song DF, Zhu MY, Gu Q. Purification and characterization of Plantaricin ZJ5, a new bacteriocin produced by Lactobacillus plantarum ZJ5. DRAMP02011 GILDTLKHLAKTAGKGALQSLLNHASCKLSGQC 33 Brevinin-2Tb (Frogs, amphibians, animals) P82269 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antimicrobial peptide.(By similarity) Tissue specificity: Expressed by the skin glands. PTM: Problely contains one disulfide bond 27-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02012 VNPIILGVLPKFVCLITKKC 20 Brevinin-1T (Brevinin-2T; Frogs, amphibians, animals) P82232 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against representative Gram-negative and Gram-positive bacteria: and exhibits a very high hemolytic activity. [Swiss_Prot Entry P82232]Antibacterial activity against representative Gram-negative and Gram-positive bacteria [Ref.10333736]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02013 FITLLLRKFICSITKKC 17 Brevinin-1Ta (Frogs, amphibians, animals) P82233 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against representative Gram-negative and Gram-positive bacteria: and exhibits no hemolytic activity. [Swiss_Prot Entry P82233]Antibacterial activity against representative Gram-negative and Gram-positive bacteria [Ref.10333736]Non-hemolytic Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02014 GLWETIKNFGKKFTLNILHKLKCKIGGGC 29 Brevinin-2Tc (Frogs, amphibians, animals) P82234 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibacterial activity against representative Gram-negative and Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02015 GLWETIKNFGKKFTLNILHNLKCKIGGGC 29 Brevinin-2Td (Frogs, amphibians, animals) P82235 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibacterial activity against representative Gram-negative and Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10333736 Biopolymers. 1998;47(6):435-450. Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP02016 FLSLALAALPKFLCLVFKKC 20 Brevinin-1DYa (Frogs, amphibians, animals) P0C5W6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial peptide. Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 14-20. [Swiss_Prot Entry P0C5W6]Gram-positive bacterium: Staphylococcus aureus (low activity);##Gram-negative bacterium: Escherichia coli (MIC<15 µM). [Ref.17688900]LC50<5 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP02017 GLLSAVKGVLKGAGKNVAGSLMDKLKCKLFGGC 33 Brevinin-2DYa (Frogs, amphibians, animals) P0C5X1 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 27-33." Gram-negative bacterium: Escherichia coli (MIC<15 µM);##Gram-positive bacterium: Staphylococcus aureus (MIC<15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP02018 FLSLALAALPKLFCLIFKKC 20 Brevinin-1DYb (Brevinin-1CDYb; Frogs, amphibians, animals) P0C5W7 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has low activity against the Gram-positive bacteria: S. aureus and the Gram-negative bacteria E. coli. Has hemolytic activity. Has a strong hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 14-20." [Swiss_Prot Entry P0C5W7]Gram-positive bacterium: Staphylococcus aureus (low activity);##Gram-negative bacterium: Escherichia coli (MIC<15 µM). [Ref.17688900]LC50<6 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775##17688900 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178.##Toxicon. 2007 Nov;50(6):746-756. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH.##Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii.##Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP02020 FLPLLLAGLPKLLCLFFKKC 20 Brevinin-1DYc (Frogs, amphibians, animals) P0C5W8 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antimicrobial peptide. Has low activity against the Gram-positive bacteria: S. aureus and the Gram-negative bacteria E.coli (MIC<15 µM). Has hemolytic activity. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 14-20." [Swiss_Prot Entry P0C5W8]Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli (MIC<15 µM). [Ref.17688900]LC50<7 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17688900 Toxicon. 2007 Nov;50(6):746-756. Conlon JM, Kolodziejek J, Nowotny N, Leprince J, Vaudry H, Coquet L, Jouenne T, Iwamuro S. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. DRAMP18282 QWGGG 5 Plantaricin ZJ008 (Bacteriocin) No entry found Not found Not found Lactobacillus plantarum ZJ008 Antimicrobial, Antibacterial Not found The sequence showed no homology with known bacteriocins. Warning: only the N-terminal amino acid sequence has been elucidated for this 20-residue bacteriocin. This bacteriocin was highly thermostable (121 Celsius degree, 30 min) and exhibited narrow pH stability (pH 4.0 broad-spectrum No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 25038669 Food Chem. 2014 Dec 15;165:216-23. Zhu X, Zhao Y, Sun Y, Gu Q. Purification and characterisation of plantaricin ZJ008, a novel bacteriocin against Staphylococcus spp. from Lactobacillus plantarum ZJ008. DRAMP02027 GLFSVVTGVLKAVGKNVAGSLLEQLKCKISGGC 33 Brevinin-2CDYb (Frogs, amphibians, animals) P86042 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 27-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP18281 GRADYNFGYGLGRGTRKFFNGIGRWVRKTF 30 Plantaricin KL-1Y (Bacteriocin) No entry found Belongs to the class IIb bacteriocin Not found Lactobacillus plantarum KL-1 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found It showed synergistic effects with KL-1X and KL-1Z, two additional peptides whose sequences have not been established. Gram-positive, Gram-negative (broad-spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25862353 World J Microbiol Biotechnol. 2015 Jun;31(6):983-94. Rumjuankiat K, Perez RH, Pilasombut K, Keawsompong S, Zendo T, Sonomoto K, Nitisinprasert S. Purification and characterization of a novel plantaricin, KL-1Y, from Lactobacillus plantarum KL-1. DRAMP02029 FLPLLLAGLPKLLCFLFKKC 20 Brevinin-1CDYd (Frogs, amphibians, animals) B3VZU1 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial activity againist Gram-negative bacteria and Gram-positive bacteria. Tissue specificity: Expressed by the skin glands. PTM: contains one disulfide bond 14-20." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19539775 Comp Biochem Physiol B Biochem Mol Biol. 2009 Oct;154(2):174-178. Jin LL, Li Q, Song SS, Feng K, Zhang DB, Wang QY, Chen YH. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii. DRAMP18280 VFHAYSARGNYYGNCPANWPSCRNNYKSAGGK 32 Plantaricin 163 (Bacteriocin) No entry found Not found Not found Lactobacillus plantarum 163 Antimicrobial, Antibacterial Not found Not found Plantaricin 163 was highly thermostable (20 min, 121 degrees C), active in the presence of acidic pH (3-5), sensitive to protease, and exhibited broad-spectrum antimicrobial activity against LAB and other tested Gram-positive and Gram-negative bacteria. broad-spectrum No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24228753 J Agric Food Chem. 2013 Nov 27;61(47):11676-82. Hu M, Zhao H, Zhang C, Yu J, Lu Z. Purification and characterization of plantaricin 163, a novel bacteriocin produced by Lactobacillus plantarum 163 isolated from traditional Chinese fermented vegetables. DRAMP02079 FLPLLAASFACTVTKKC 17 Brevinin-1AVa (Frogs, amphibians, animals) P86159 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana arvalis (Moor frog) Antimicrobial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18280749##19308951 J Am Soc Mass Spectrom. 2008 Apr;19(4):479-487.##Rapid Commun Mass Spectrom. 2009 May;23(9):1241-1248. Samgina TY, Artemenko KA, Gorshkov VA, Poljakov NB, Lebedev AT.##Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Oxidation versus carboxamidomethylation of S-S bond in ranid frog peptides: pro and contra for de novo MALDI-MS sequencing.##Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region. DRAMP02080 FVPLLVSKLVCVVTKKC 17 Brevinin-1AVb (Frogs, amphibians, animals) P86160 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana arvalis (Moor frog) Antimicrobial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18280749##19308951 J Am Soc Mass Spectrom. 2008 Apr;19(4):479-487.##Rapid Commun Mass Spectrom. 2009 May;23(9):1241-1248. Samgina TY, Artemenko KA, Gorshkov VA, Poljakov NB, Lebedev AT.##Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Oxidation versus carboxamidomethylation of S-S bond in ranid frog peptides: pro and contra for de novo MALDI-MS sequencing.##Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region. DRAMP18279 AYSLQMGATAIKQVKKLFKKWGW 23 Plantaricin A(Bacteriocin) P80214 Belongs to the class IIb bacteriocin plnA Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) Antimicrobial, Antibacterial, Anti-Gram+ Alpha helix Active plantaricin A is composed of an alpha chain and a beta chain. The sequence of alpha chain and beta chain, however, are essential identical with the only difference being one additional Ala at the N-terminus of chain b. The 3D structure of chain a in DPC micelles has been determined by NMR spectroscopy (J Biol Chem. 2005 Jun 17;280(24):22945-50). The helical region (residues 12-21) are good for membrane targeting as well as the ph 1YTR resolved by NMR Active plantaricin A is composed of an alpha chain and a beta chain. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8245827 J Gen Microbiol. 1993 Sep;139(9):1973-8. Nissen-Meyer J, Larsen AG, Sletten K, Daeschel M, Nes IF. Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides. DRAMP18278 YSYFGGSNGYSWRDKRGHWHYTVTKGGFETVIGIIGDGWGSAGAPGPGQH 50 BacSJ(Bacteriocin) No entry found Belongs to the class II bacteriocin Not found Lactobacillus paracasei subsp. paracasei BGSJ2-8 Unknown Not found BLAST protein sequence homology search revealed that BacSJ showed a very high homology with acidocin M from L. acidophilus TK8912. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available ARCHIVES OF BIOLOGICAL SCIENCES. 2010;62(2):231-243. Kojic M,Lozo J,Jovcic B,Strahinic I,Fira D,Topisirovic L. A SUCCESSFUL USE OF A NEW SHUTTLE CLONING VECTOR PA13 FOR THE CLONING OF THE BACTERIOCINS BACSJ and ACIDOCIN 8912 DRAMP18277 DIDITGCSACKYAAGQVCTIGCSAAGGFICGLLGITIPVAGLSCLGFVEIVCTVADEYSGCGDAVAKEACNRAGLC 76 Halocin C8 (Bacteriocin) P83716 Not found proC8 Halobacterium sp. (strain AS7092) Antimicrobial, Antibacterial disulphide bridges HalC8 contains 10 cysteines that could form disulphide bridges, leading to a little decrease in molecular weight. quite stable, can be desalted, boiled, frozen, subjected to organic solvents, and stored in culture supernatant at 4 No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell wall 12811620##15978083 Extremophiles. 2003 Oct;7(5):401-7.##Mol Microbiol. 2005 Jul;57(2):537-49. Li Y, Xiang H, Liu J, Zhou M, Tan H.##Sun C, Li Y, Mei S, Lu Q, Zhou L, Xiang H. Purification and biological characterization of halocin C8, a novel peptide antibiotic from Halobacterium strain AS7092.##A single gene directs both production and immunity of halocin C8 in a haloarchaeal strain AS7092. DRAMP02087 FLPVLAGLTPSIVPKLVCLLTKKC 24 Brevinin-1PRb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (North oregon spotted frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found The MIC of Ranatuerin-2PRe is >50 µM. No MICs found in DRAMP database [Ref.21295070] LC50=80μM against human erythrocytes. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: implications for species resistance to chytridiomycosis. DRAMP02088 FFPMLAGVAARVVPKVICLITKKC 24 Brevinin-1PRc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (North oregon spotted frog) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 21295070 Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Mechkarska M, Ahmed E, Coquet L, Jouenne T, Leprince J, Vaudry H, Hayes MP, Padgett-Flohr G. Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: implications for species resistance to chytridiomycosis. DRAMP02089 FLPMLAGLAASMVPKLVCLITKKC 24 Brevinin-1La (Brevinin-1PRd; Frogs, amphibians, animals) P82825 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Brevinin-1PRd isolated from the Oregon spotted frog shares the same sequence with this entry. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP01124 ILGPVLSMVGSALGGLIKKI 20 Maximin-H2 (Toads, amphibians, animals) P83082 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi.Shows strong hemolytic activity. [Ref.11835991] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=20 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=2 μg/ml), Bacillus pyocyaneus CMCCB 1010 (MIC=4 μg/ml);##Fungi: Candida albicans ATCC 2002 (MIC=2 μg/ml). [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01123 ILGPVISTIGGVLGGLLKNL 20 Maximin-H1 (Toads, amphibians, animals) P83080, P83081, Q58T74, Q58T41 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Shows strong hemolytic activity. [Ref.11835991] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=9 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=4.5 μg/ml), Bacillus pyocyaneus CMCCB 1010 (MIC=9 μg/ml).##Yeast: Candida albicans ATCC 2002 (MIC=4.5 μg/ml). [Ref:11835991]90–100% hemolytic activity at 50 μg/ml against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01111 SIGAKILGGVKTFFKGALKELASTYLQ 27 Maximin-5 (Toads, amphibians, animals) P83084, Q58T60, Q58T61 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral, Anti-cancer Protein level Not found Maximins are linear cationic peptides and easy to form membrane pore and they may induce a detergent-type disruption of sperm membrane like in the case of magainins. "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has little hemolytic activity. No amidation at the C-terminus. Tissue specificity: Expressed by the skin glands." [Ref.11835991] Gram-negative bacterium: Klebsiella pneumoniae (MIC=3.6 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.6 μg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=7.2 μg/ml), Bacillus megatherium (MIC=12 μg/ml), Bacillus dysenteriae (MIC=12 μg/ml).##Fungi: Candida albicans ATCC 2002 (MIC=1.2 μg/ml), Aspergillus flavus IFFI 4015 (MIC=12 μg/ml), Penicillium uticale IFFI 2001 (MIC=12 μg/ml);##Virus: HIV-1 (IC50=34.4 μg/ml, EC50=39.8 μg/ml);##Cancer cell lines: C8166 (IC50=34.4 μg/ml). [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01110 GIGGVLLSAGKAALKGLAKVLAEKYAN 27 Maximin-4 (Toads, amphibians, animals) P83083, Q58T42, Q58T44, Q58T52, Q58T62, Q58T77, Q58T79 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral, Anti-cancer Protein level Not found Maximins are linear cationic peptides and easy to form membrane pore and they may induce a detergent-type disruption of sperm membrane like in the case of magainins. 2MHW resolved by NMR Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has little hemolytic activity. Possess a significant cytotoxicity against tumor cell lines. Possess a significant anti-HIV activity. High spermicidal activity. [Ref.11835991] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2.7 µg/ml), Klebsiella pneumoniae (MIC=15 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=2.7 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=2.7 µg/ml), Bacillus megatherium (MIC=1.5 µg/ml), Bacillus dysenteriae (MIC=2.7 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=15 µg/ml);##Virus: HIV-1 (IC50=24.2 µg/ml, EC50=21.9 µg/ml);##Cancer cell lines: C8166 (IC50=24.2 µg/ml), Molt-4 (IC50=35.4 µg/ml). [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP01109 GIGGKILSGLKTALKGAAKELASTYLH 27 Maximin-3 (Toads, amphibians, animals) P83082, Q58T40, Q58T43, Q58T46, Q58T48, Q58T64, Q58T65, Q58T68, Q58T69 Belongs to the bombinin family Not found Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral, Anti-cancer Protein level Not found Maximins are linear cationic peptides and easy to form membrane pore and they may induce a detergent-type disruption of sperm membrane like in the case of magainins. 6HZ2 "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Has little hemolytic activity. Possess a significant cytotoxicity against tumor cell lines. Possess a significant anti-HIV activity. High spermicidal activity. No amidation at the C-terminus. Toxic dose: LD50 is 4.3 mg/kg by intraperitoneal injection into mice. Tissue specificity: Expressed by the skin glands." [Ref.11835991] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.9 µg/ml), Klebsiella pneumoniae (MIC=3.1 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.1 µg/ml), Bacillus pyocyaneus CMCCB 10104 (MIC=1.5 µg/ml), Bacillus megatherium (MIC=0.9 µg/ml), Bacillus dysenteriae (MIC=0.9 µg/ml);##Yeast: Candida albicans ATCC 2002 (MIC=15 µg/ml);##Virus: HIV-1 (IC50=11.4 µg/ml, EC50=1.5 µg/ml);##Cancer cell lines: C8166 (IC50=11.4 µg/ml), Molt-4 (IC50=25.2 µg/ml), BIU-87 (IC50=28 µg/ml), T24 (IC50=18 µg/ml). [Ref:11835991]Little hemolytic activity at 50 μg/ml against red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 15770703##11835991 Eur J Immunol. 2005 Apr;35(4):1220-9.##Peptides. 2002 Mar;23(3):427-435. Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W.##Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification.##Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP02100 FLPIIASVAAKVFPKIFCAISKKC 24 Brevinin-1Pe (Frogs, amphibians, animals) P82845 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02103 FLGSLLGLVGKIVPTLICKISKKC 24 Brevinin-1RTc (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Amolops ricketti (Chinese sucker frog) Antimicrobial, Antibacterial Not found Not found Not found "Function: Brevinin-2RTc has antibacterial activity. PTM: Contains one disulfide bond 27-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet [Ref.22100518]Not found 22100518 Peptides. 2012 Jan;33(1):27-34. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). DRAMP18353 ENDHRMPYELNRPNNLSKGGAKCGAAIA 28 Durancin L28-1A (bacteriocin) No entry found Belongs to the class IIa bacteriocin. Not found Enterococcus durans L28-1 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against Gram+ bacteria: L. sakei ssp. sakei JCM 1157T, L. sanfranciscensis JCM 5668, L. coryniformis ssp.coryniformis JCM 1164, L. plantarum NRIC 1067, L. animalis JCM 5670, L. pentosus JCM 1558, L. gasseri JCM 5344 , L. helveticus JCM 1554, L. lactis JCM 6123, L. lactis ssp. lactis C101910, L. lactis ssp. lactis IFO 12007 , E. faecium MR006 , E. durans MY411, C. divergens JCM 5816, W. paramesenteroides NRIC 1542, W. kandleri JCM 5817, W. halotolerans JCM 1114, and W. minor JCM 1168T. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15892738 Lett Appl Microbiol. 2005;40(6):430-5 Yanagida F, Chen Y, Onda T, Shinohara T. Durancin L28-1A, a new bacteriocin from Enterococcus durans L28-1, isolated from soil. DRAMP18276 LQSNININTAAAVILIFNQVQVGALCAPTPVSGGGPPP 38 HalR1(Bacteriocin) No entry found Not found Not found Halobacterium salinarum GN101 Archaeolytic Not found HalR1 is 63% identical and 71% similar to HalS8. Unlike HalH6, HalR1 does not appear to be archaeolytic, since it causes no change in the optical density or cell morphology of stationary phase Hbt. salinarum, nor can it form zones of inhibition on fully grown lawns. HalR1 has a dose-dependent, archaeostatic effect on growing Hbt. salinarum. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11938468 J Ind Microbiol Biotechnol. 2002 Jan;28(1):23-31. O'Connor EM, Shand RF. Halocins and sulfolobicins: the emerging story of archaeal protein and peptide antibiotics. DRAMP02107 MFTLKKSLLLLFFLGTINLSLCEQERDADEEERRDDPDERDVEVEKRFLPLLAGLAANFLPKLFCKITRKG 71 Brevinin-1E-OG2 antimicrobial peptide (Frogs, amphibians, animals) A6MAR9 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP18354 ITSFSLCTPGCAKTGSFNSYCC 22 Hyicin 3682 (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Staphylococcus hyicus 3682 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28285660 Microbiol Res. 2017 May;198:36-46. Carlin Fagundes P, Nascimento de Sousa Santos I, Silva Francisco M, Mattos Albano R, de Freire Bastos MD. Genetic and biochemical characterization of hyicin 3682, the first bacteriocin reported for Staphylococcus hyicus. DRAMP18273 KYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWKS 43 Enterocin CRL35 (Bacteriocin) No entry found Belongs to the class IIa bacteriocin munA Enterococcus mundtii CRL35 Antibacterial, Antiviral, Anti-Gram+, Antimicrobial Bridge Not found Both biological activities, antibacterial and antiviral, were destroyed after incubation of the enterocin with protease IV or by raising the pH. Gram-positive, virus(certain) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 10493605##11040432 Int J Antimicrob Agents. 1999 Aug;12(4):293-9.##FEMS Microbiol Lett. 2000 Nov 1;192(1):79-83. Wachsman MB, Far Antiviral activity of enterocin CRL35 against herpesviruses.##Effect of enterocin CRL35 on Listeria monocytogenes cell membrane. DRAMP18272 MAKEFGIPAAVAGTVINVVVAGGWVTTIVSILTAVGSGGLSLLAAAGRESIKAYLKKEIKKKGKRAVIAW 70 Enterocin AS-48RJ (Bacteriocin) No entry found Belongs to the class IIc bacteriocin Not found Enterococcus faecium RJ16 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found 1E68 resolved by NMR This is a natural variant of AS-48, where residue 20 is a Glu (Val in As-48RJ). It has the same activity spectrum as AS-48 . Gram-positive, Gram-negative (broad-spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16094865 Syst Appl Microbiol. 2005 Jul;28(5):383-97. Abriouel H, Lucas R, Ben Omar N, Valdivia E, Maqueda M, Mart Enterocin AS-48RJ: a variant of enterocin AS-48 chromosomally encoded by Enterococcus faecium RJ16 isolated from food. DRAMP02115 AWLDKLKSLGKVVGKVAIGVAQHYLNPQQ 29 Raniseptin-2 (Rsp-2; Frogs, amphibians, animals) P86185 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02116 AWLDKLKSIGKVVGKVAIGVAKNLLNPQ 28 Raniseptin-3 (Rsp-3; Frogs, amphibians, animals) P86038 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02117 AWLDKLKSLGKVVGKVGLGVVQNYLNPRQ 29 Raniseptin-4 (Rsp-4; Frogs, amphibians, animals) P86186 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02118 AWLDKLKNLGKVVGKVALGVVQNYLNPRQ 29 Raniseptin-5 (Rsp-5; Frogs, amphibians, animals) P86187 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02119 ALLDKLKSLGKVVGKVALGVVQNYLNPRQ 29 Raniseptin-6 (Rsp-6; Frogs, amphibians, animals) P86039 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02120 ALLDKLKSLGKVVGKVALGVAQHYLNPQQ 29 Raniseptin-7 (Rsp-7; Frogs, amphibians, animals) P86040 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Protein level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02121 ALLDKLKSLGKVVGKVAIGVAQHYLNPQQ 29 Raniseptin-8 (Rsp-8; Frogs, amphibians, animals) P86188 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02122 ALLDKLKSLGKVVGKVAIGVAQHYLNPQ 28 Raniseptin-9 (Rsp-9; Frogs, amphibians, animals) P86189 Belongs to the frog skin active peptide family (Dermaseptin subfamily) Not found Hypsiboas raniceps (Chaco tree frog) (Hyla roeschmanni) Unknown Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18976634 Biochem Biophys Res Commun. 2008 Dec 26;377(4):1057-1061. Magalhães BS, Melo JA, Leite JR, Silva LP, Prates MV, Vinecky F, Barbosa EA, Verly RM, Mehta A, Nicoli JR, Bemquerer MP, Andrade AC, Bloch C Jr. Post-secretory events alter the peptide content of the skin secretion of Hypsiboas raniceps. DRAMP02123 FIGAILPAIAGLVHGLINR 19 Hylin-b1 (Hy-b1; Frogs, amphibians, animals) P84002 Not found Not found Hyla biobeba (Brazilian tree frog) Antimicrobial Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes. May have antimicrobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref.15638808]Show hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15638808 Protein Pept Lett. 2005 Jan;12(1):89-93. Castro MS, Matsushita RH, Sebben A, Sousa MV, Fontes W. Hylins: bombinins H structurally related peptides from the skin secretion of the Brazilian tree-frog Hyla biobeba. DRAMP02124 FIGAILPAIAGLVGGLINR 19 Hylin-b2 (Hy-b2; Frogs, amphibians, animals) P84003 Not found Not found Hyla biobeba (Brazilian tree frog) Antimicrobial Protein level Not found Not found "Function: Has hemolytic activity against human erythrocytes. May have antimicrobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref.15638808]Show hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15638808 Protein Pept Lett. 2005 Jan;12(1):89-93. Castro MS, Matsushita RH, Sebben A, Sousa MV, Fontes W. Hylins: bombinins H structurally related peptides from the skin secretion of the Brazilian tree-frog Hyla biobeba. DRAMP02132 GLASTLGSFLGKFAKGGAQAFLQPK 25 Antimicrobial peptide 3 (XT-3; Levitide-like peptide; Frogs, amphibians, animals) P84383 Belongs to the gastrin/cholecystokinin family (Magainin subfamily) Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli, when in combination with XT1 and XT6. Gram-positive bacteria: Staphylococcus aureus;##Gram-negative bacteria: E.coli (Combination with XT1 and XT6). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02134 GMATKAGTALGKVAKAVIGAAL 22 Antimicrobial peptide 5 (XT-5; PGLa-like peptide; Frogs, amphibians, animals) P84385 Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacterium S. aureus, Gram-negative bacterium E.coli and yeast C. albicans. Has strong hemolytic activity against human red blood cells. Tissue specificity: Skin." [Ref.11738090]Gram-positive bacteria: Staphylococcus aureus (MIC>100 µM);##Gram-negative bacteria: Escherichia coli (MIC>100 µM);##Fungi: Candida albicans (MIC>100 µM) [Ref.11738090]HC50>150 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11738090 Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP02137 GLLKPLLKIAAKVGSNLL 18 [G4K]XT-7 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22374306 Peptides. 2012 Apr;34(2):275-282. Popovic S, Urbán E, Lukic M, Conlon JM. Peptides with antimicrobial and anti-inflammatory activities that have therapeutic potential for treatment of acne vulgaris. DRAMP02138 GWGDTFGKVLKNFAKVAGVKAAK 23 XTG1 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP02139 GWGDTFLKTMAKIAKVGPKLLHS 23 XTG2 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP02140 GFWSSALEGLKKFAKGGLEALTNPK 25 XPF-SP1 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP02141 GLASTIGSLLGKFAKGGAQAFLQPK 25 XPF-SP2 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP02143 GFLGPLLKLGLKGAAKLLPQLLPSRQQ 27 CPF-SP2 (Frogs, amphibians, animals) No entry found Not found Not found Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP02144 MPVAVGPYGQSQPSCFDRVKMGFMMGFAVGMAAGALFGTFSCLRFGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC 79 Reactive oxygen species modulator 1 (ROS modulator 1; Frogs, amphibians, animals) A4QNF3 Belongs to the MGR2 family romo1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity against a variety of bacteria. Acts by inducing bacterial membrane breakage (By similarity). Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation. Domain: Contains a transmembrane helix domian." S. aureus, Pseudomonas aeruginosa and M. tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Unknown NIH - Xenopus Gene Collection (XGC) project DRAMP02145 FVPIWM 6 Electrin-1 (Frogs, amphibians, animals) P82096 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02146 FVHPM 5 Electrin-3 (Frogs, amphibians, animals) P82099 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02147 FITVH 5 Electrin-4 (Frogs, amphibians, animals) P82100 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02148 IYEPEIA 7 Electrin-5 (Frogs, amphibians, animals) P82101 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02149 NEEEKVKWEPDVP 13 Electrin-2.1 (Frogs, amphibians, animals) P82097 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02150 NEEEKVKWQPDVP 13 Electrin-2.2 (Frogs, amphibians, animals) P82098 Not found Not found Litoria rubella (Desert tree frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Aust. J. Chem. 1999;52:639-645. Wabnitz PA, Bowie JH, Tyler MJ, Wallace JC. Peptides from the skin glands of the Australian buzzing tree frog Litori electrica. Comparison with the skin peptides from Litoria rubella. DRAMP02151 MASLKKFLFLVLFLGMVSLSICDKEKREGENEEEEEEHEEESEEKRGLFSFLPKVIGVIGPLIHPPS 67 Preprofallaxidin-4 (Frogs, amphibians, animals) B5LUQ5 Belongs to the frog skin active peptide family Dermas Not found Litoria fallax (Eastern dwarf tree frog) Unknown Transcript level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18803332 Rapid Commun Mass Spectrom. 2008 Oct;22(20):3207-3216. Jackway RJ, Bowie JH, Bilusich D, Musgrave IF, Surinya-Johnson KH, Tyler MJ, Eichinger PC. The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins. DRAMP02152 MASLKKSLFLVLFLGFVSLSICEEEKREDKEDEGENEEAEENHEERSEEKRFLPLLASLVGGLLGKRS 68 Preprofallaxidin-5 (Frogs, amphibians, animals) B5LUQ6 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Litoria fallax (Eastern dwarf tree frog) Unknown Transcript level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18803332 Rapid Commun Mass Spectrom. 2008 Oct;22(20):3207-3216. Jackway RJ, Bowie JH, Bilusich D, Musgrave IF, Surinya-Johnson KH, Tyler MJ, Eichinger PC. The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins. DRAMP02153 FLPAIAGILSQLF 13 Hemolytic protein A1 (Frogs, amphibians, animals) P32415 Not found Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Shows hemolytic activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref.11738090]5% hemolytic activity at 1 nmol/ml, 20% hemolytic activity at 1.5nmol/ml, 30% hemolytic activity at 2nmol/ml, 60% hemolytic activity at 2.5nmol/ml, 88% hemolytic activity at 3nmol/ml, 95% hemolytic activity at 3.5nmol/ml against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2317508 Biochim Biophys Acta. 1990 Mar 26;1033(3):318-323. Simmaco M, De Biase D, Severini C, Aita M, Erspamer GF, Barra D, Bossa F. Purification and characterization of bioactive peptides from skin extracts of Rana esculenta. DRAMP02154 FLPLIAGLLGKLF 13 Hemolytic protein B9 (Frogs, amphibians, animals) P32416 Not found Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Unknown Protein level Not found Not found "Function: Shows hemolytic activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database [Ref.11738090]4% hemolytic activity at 1 nmol/ml, 5% hemolytic activity at 1.5nmol/ml, 17% hemolytic activity at 2nmol/ml, 20% hemolytic activity at 2.5nmol/ml, 35% hemolytic activity at 3nmol/ml, 90% hemolytic activity at 3.5nmol/ml against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2317508 Biochim Biophys Acta. 1990 Mar 26;1033(3):318-323. Simmaco M, De Biase D, Severini C, Aita M, Erspamer GF, Barra D, Bossa F. Purification and characterization of bioactive peptides from skin extracts of Rana esculenta. DRAMP02155 MSAVPFTRVLLISGFLAHLLLSTFVTLTVCKEVTEESDDLSKRNVLQRQLWAVGSLMGKKSLENTNRRSDEDMEISALFRGSPLKVKRSD 90 [Leu8]-phyllolitorin (Frogs, amphibians, animals) P08948 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7997236 Mol Endocrinol. 1994 Aug;8(8):943-951. Nagalla SR, Barry BJ, Spindel ER. Cloning of complementary DNAs encoding the amphibian bombesin-like peptides Phe8 and Leu8 phyllolitorin from Phyllomedusa sauvagei: potential role of U to C RNA editing in generating neuropeptide diversity. DRAMP02156 QQWAVGHFM 9 Litorin (Frogs, amphibians, animals) P08945 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Litoria aurea (Green; also golden bell frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1140241 Experientia. 1975 May 15;31(5):510-511. Anastasi A, Erspamer V, Endean R. Aminoacid composition and sequence of litorin, a bombesin-like nonapeptide from the skin of the Australian leptodactylid frog Litoria aurea. DRAMP02157 MSAVPFTRVLLISGFLAHLLLSTFVTLTVCKEVTEESDDLSKRNVLQRQLWAVGSFMGKKSLENTNRRSDEDMEISALFRGSPLKVKRSD 90 [Phe8]-phyllolitorin (Frogs, amphibians, animals) P08947 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7997236##3868775 Mol Endocrinol. 1994 Aug;8(8):943-951.##Peptides. 1985;6 Suppl 3:7-12. Nagalla SR, Barry BJ, Spindel ER.##Erspamer V, Melchiorri P, Falconieri Erspamer G, Montecucchi PC, de Castiglione R. Cloning of complementary DNAs encoding the amphibian bombesin-like peptides Phe8 and Leu8 phyllolitorin from Phyllomedusa sauvagei: potential role of U to C RNA editing in generating neuropeptide diversity.##Phyllomedusa skin: a huge factory and store-house of a variety of active peptides. DRAMP02158 QLWATGHFM 9 Rhodei-litorin (Frogs, amphibians, animals) P08946 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Phyllomedusa rohdei (Rohde's leaf frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3838283 FEBS Lett. 1985 Mar 11;182(1):53-56. Barra D, Falconieri Erspamer G, Simmaco M, Bossa F, Melchiorri P, Erspamer V. Rohdei-litorin: a new peptide from the skin of Phyllomedusa rohdei. DRAMP02159 FVGAALKVLANVLPPVISWIKQ 22 Melittin-related peptide (Frogs, amphibians, animals) P86158 Not found Not found Rana arvalis (Moor frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19308951 Rapid Commun Mass Spectrom. 2009 May;23(9):1241-1248. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region. DRAMP02160 SEEEKRQPWLPFG 13 Peroniin-1.1b (Frogs, amphibians, animals) P86495 Belongs to the frog skin active peptide family (Peroniin subfamily) Not found Litoria peronii (Emerald spotted tree frog) (Hyla peronii) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19642086 Rapid Commun Mass Spectrom. 2009 Sep;23(17):2628-2636. Bilusich D, Jackway RJ, Musgrave IF, Tyler MJ, Bowie JH. The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides. DRAMP02161 DAQEKRQPWIPFV 13 Peroniin-1.2a (Frogs, amphibians, animals) P86490 Belongs to the frog skin active peptide family (Peroniin subfamily) Not found Litoria peronii (Emerald spotted tree frog) (Hyla peronii) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19642086 Rapid Commun Mass Spectrom. 2009 Sep;23(17):2628-2636. Bilusich D, Jackway RJ, Musgrave IF, Tyler MJ, Bowie JH. The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides. DRAMP02162 DAQEKRQPWLPFV 13 Peroniin-1.3a (Frogs, amphibians, animals) P86493 Belongs to the frog skin active peptide family (Peroniin subfamily) Not found Litoria peronii (Emerald spotted tree frog) (Hyla peronii) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19642086 Rapid Commun Mass Spectrom. 2009 Sep;23(17):2628-2636. Bilusich D, Jackway RJ, Musgrave IF, Tyler MJ, Bowie JH. The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides. DRAMP02163 QPWLPFR 7 Peroniin-1.5 (Frogs, amphibians, animals) P86482 Belongs to the frog skin active peptide family (Peroniin subfamily) Not found Litoria peronii (Emerald spotted tree frog) (Hyla peronii) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19642086 Rapid Commun Mass Spectrom. 2009 Sep;23(17):2628-2636. Bilusich D, Jackway RJ, Musgrave IF, Tyler MJ, Bowie JH. The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides. DRAMP02164 QVPQWAVGHFM 11 Ranatensin (Frogs, amphibians, animals) P08950 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Rana pipiens (Northern leopard frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2458345 J Biol Chem. 1988 Sep 15;263(26):13317-23. Krane IM, Naylor SL, Helin-Davis D, Chin WW, Spindel ER. Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin. DRAMP02165 QTPQWATGHFM 11 Ranatensin-C (Frogs, amphibians, animals) P08951 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Rana pipiens (Northern leopard frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6141890 Comp Biochem Physiol C. 1984;77(1):99-108. Erspamer V, Erspamer GF, Mazzanti G, Endean R. Active peptides in the skins of one hundred amphibian species from Australia and Papua New Guinea. DRAMP02166 SNTALRRYNQWATGHFM 17 Ranatensin-R (Frogs, amphibians, animals) P08952 Belongs to the bombesin/neuromedin-B/ranatensin family Not found Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 445685 Chem Pharm Bull (Tokyo). 1979 Feb;27(2):492-498. Yasuhara T, Ishikawa O, Nakajima T. The studies on the active peptide in the skin of Rana rugosa. II. The structure of ranatensin-R, the new ranatensin analogue, and granuliberin-R, the new mast cell degranulating peptide. DRAMP02167 FPPWF 5 Tryptophyllin-T2-1 (Pha-T2-1; Tryptophyllin-11; Frogs, amphibians, animals) P84952 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02168 FPPWE 5 Tryptophyllin-T2-2 (Pha-T2-2; Tryptophyllin-3; Frogs, amphibians, animals) P84943 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP18397 FFSALLSGIKSLF 13 Um4 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Urodacus manicatus Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against M. luteus (MIC 8 uM), E. coli (8 uM), S. aureus (15 uM), L. grayi (15 uM), L. fleischmannii (MIC 4 uM), and L. monocytogenes (MIC 8 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28067810 Toxins (Basel). 2017 Jan 6;9, 22. doi: 10.3390/toxins9010022. Luna-Ramirez K, Tonk M, Rahnamaeian M, Vilcinskas A. Bioactivity of Natural and Engineered Antimicrobial Peptides from Venom of the Scorpions Urodacus yaschenkoi and U. manicatus DRAMP02170 FPPWM 5 Tryptophyllin-T2-4 (Pha-T2-4; Tryptophyllin-8; Frogs, amphibians, animals) P84948 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02171 LPPWIG 6 Tryptophyllin-T2-5 (Pha-T2-5; Tryptophyllin-1; Frogs, amphibians, animals) P84941 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02172 KPPWRL 6 Tryptophyllin-T2-6 (Pha-T2-6; Tryptophyllin-6; Frogs, amphibians, animals) P84946 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02173 KPWERL 6 Tryptophyllin-T2-7 (Pha-T2-7; Tryptophyllin-7; Frogs, amphibians, animals) P84947 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02174 KPWERE 6 Tryptophyllin-T2-8 (Pha-T2-8; Tryptophyllin-12; Frogs, amphibians, animals) P84953 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02175 VPPIGWF 7 Tryptophyllin-T2-9 (Pha-T2-9; Tryptophyllin-4; Frogs, amphibians, animals) P84944 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusahypochondrialis azurea) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02176 QDKPFWSPPIYPV 13 Tryptophyllin-T3-1 (Pj-T3-1; Frogs, amphibians, animals) P86610 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1. Note: Sequence uncertainty at position 3 (K or Q) and 10 (I or L)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP02177 QDKPFWSPPIYPH 13 Tryptophyllin-T3-2 (Pj-T3-2; Frogs, amphibians, animals) P86611 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1. Note: Sequence uncertainty at position 3 (K or Q) and 10 (I or L)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP02178 QDKPFWDPPIYPV 13 Tryptophyllin-T3-3 (Pj-T3-3; Frogs, amphibians, animals) P86612 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phasmahyla jandaia (Jandaia leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1. Note: Sequence uncertainty at position 3 (K or Q) and 10 (I or L)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20932854 Toxicon. 2011 Jan;57(1):35-52. Rates B, Silva LP, Ireno IC, Leite FS, Borges MH, Bloch C Jr, De Lima ME, Pimenta AM. Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae). DRAMP02179 QDKPFWPPPIYIM 13 Tryptophyllin-T3-1 (Pha-T3-1; Tryptophyllin-9; Frogs, amphibians, animals) P84949 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02180 QDKPFWPPPIYPM 13 Tryptophyllin-T3-2 (Pha-T3-2; Tryptophyllin-10; Frogs, amphibians, animals) P84950 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-3613. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP02181 GPIPWQR 7 Tryptophyllin-1 (Frogs, amphibians, animals) P84831 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Ascaphus truei (Coastal tailed frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15922344 Gen Comp Endocrinol. 2005 Sep 1;143(2):193-199. Conlon JM, Jouenne T, Cosette P, Cosquer D, Vaudry H, Taylor CK, Abel PW. Bradykinin-related peptides and tryptophyllins in the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP02182 GPIPWQRRI 9 Tryptophyllin-2 (Frogs, amphibians, animals) P84834 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Ascaphus truei (Coastal tailed frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15922344 Gen Comp Endocrinol. 2005 Sep 1;143(2):193-199. Conlon JM, Jouenne T, Cosette P, Cosquer D, Vaudry H, Taylor CK, Abel PW. Bradykinin-related peptides and tryptophyllins in the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP02183 DPWDWV 6 Tryptophyllin-3 (Frogs, amphibians, animals) P84833 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Ascaphus truei (Coastal tailed frog) Unknown Protein level Not found Not found "Fuunction: Putative defense peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15922344 Gen Comp Endocrinol. 2005 Sep 1;143(2):193-199. Conlon JM, Jouenne T, Cosette P, Cosquer D, Vaudry H, Taylor CK, Abel PW. Bradykinin-related peptides and tryptophyllins in the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP02184 EPRTPWDWV 9 Tryptophyllin-4 (Frogs, amphibians, animals) P84822 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Ascaphus truei (Coastal tailed frog) Antimicrobial Protein level Not found Not found "Fuunction: Putative defense peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15922344 Gen Comp Endocrinol. 2005 Sep 1;143(2):193-199. Conlon JM, Jouenne T, Cosette P, Cosquer D, Vaudry H, Taylor CK, Abel PW. Bradykinin-related peptides and tryptophyllins in the skin secretions of the most primitive extant frog, Ascaphus truei. DRAMP02185 QEKPYWPPPIYPM 13 Tryptophyllin-13 (Frogs, amphibians, animals) P04096 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa rohdei (Rohde's leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. PTM: Pyrrolidone carboxylic acid at Q1." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Pept. Protein Res. 1986;27:175-182. Montecucchi PC, Gozzini L, Erspamer V. Primary structure determination of a tryptophan-containing tridecapeptide from Phyllomedusa rohdei. DRAMP02186 FPPWVL 6 Tryptophyllin-14 (Frogs, amphibians, animals) P85877 Belongs to the frog skin active peptide family (Tryptophillin subfamily) Not found Phyllomedusa centralis (Mato Grosso leaf frog) Antimicrobial Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15922344 Submitted (JUN-2008) to UniProtKB Silva LP, Bonatto CC, Bloch C Jr. Not found DRAMP02187 GLLDVVKGAAKNLLASALDKLKCKVTGC 28 Ranatuerin-2AVa (Frogs, amphibians, animals) P86161 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana arvalis (Moor frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity against the Gram-positive bacterium L. lactis. PTM: Contains one disulfide bond 23-28." Gram-positive bacterium: L. lactis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19308951 Rapid Commun Mass Spectrom. 2009 May;23(9):1241-1248. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region. DRAMP02188 GLMDMVKGAAKNLFASALDTLKCKITGC 28 Ranatuerin-2AVb (Frogs, amphibians, animals) P86162 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana arvalis (Moor frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity (By similarity). PTM: Contains one disulfide bond 23-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19308951 Rapid Commun Mass Spectrom. 2009 May;23(9):1241-1248. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region. DRAMP02189 GIMDTVKNAAKDLAGQLLDKLKCKITAC 28 Ranatuerin-2PLg (Frogs, amphibians, animals) D3UA80 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana palustris (Pickerel frog) Antimicrobial Homology Not found Not found "Function: Antimicrobial peptide (By similarity). PTM: Contains one disulfide bond (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02190 GIMDTVKGVAKTVAASLLDKLKCKITGC 28 Ranatuerin-2Vb (ranat2Vb; 2VEb; Frogs, amphibians, animals) Q1JS90 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Odorrana versabilis (Chinese bamboo leaf odorous frog) (Rana versabilis) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide (By similarity). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 23-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16621152 Peptides. 2006 Jul;27(7):1738-1744. Chen T, Zhou M, Rao P, Walker B, Shaw C. The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides. DRAMP18271 LTANLGISSYAAKKVIDIINTGSAVATIIALVTAVVGGGLITAGIVATAKSLIKKYGAKYAAAW 64 NKR-5-3B(Bacteriocin) No entry found Belongs to the class IIc bacteriocin Not found Enterococcus faecium NKR-5-3 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found 2MP8 APD analysis reveals that the sequence of NKR-5-3B most resembles (62.1% similarity) bacterial Amylocyclicin. Structurally, it is highly similar to carnocyclin A,. In addition, the charge distribution of enterocin NKR-5-3B, carnocyclin A and enterocin AS-48 are also highly conserved. Gram-positive (broad) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26174911 Biochemistry. 2015 Aug 11;54(31):4863-76. Himeno K, Rosengren KJ, Inoue T, Perez RH, Colgrave ML, Lee HS, Chan LY, Henriques ST, Fujita K, Ishibashi N, Zendo T, Wilaipun P, Nakayama J, Leelawatcharamas V, Jikuya H, Craik DJ, Sonomoto K. Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium. DRAMP02192 DDGIEMTEEEVKRGILDLVTHVAKNLAAQLLDKLKCKMTGC 41 Ranatuerin-2PTa (Frogs, amphibians, animals) D3UA81 Not found Not found Rana pretiosa Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02193 AFFTTVKNLVTNVAGTVIDKMKCKLTGEC 29 Ranatuerin-2PTb (Frogs, amphibians, animals) D3UA86 Not found Not found Rana pretiosa Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02194 DDGVEITEEEVKRGLMDTVKNVAKNLAGHMLDKLKCKITGSC 42 Ranatuerin-2BLa (Frogs, amphibians, animals) D3UA78 Not found Not found Rana blairi Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02195 SFLTTVKKLVTNVAALAGTVIDTIKCKITGGCRT 34 Ranatuerin-2BLc (Frogs, amphibians, animals) D3UA84 Not found Not found Rana blairi Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02196 DDGVEITEEEVKRGLMDTVKNAAKNLAGQMLDKLKCKITGSC 42 Ranatuerin-2BLb (Frogs, amphibians, animals) D3UA79 Not found Not found Rana blairi Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20179920 Immunogenetics. 2010 May;62(5):333-343. Tennessen JA, Blouin MS. A revised leopard frog phylogeny allows a more detailed examination of adaptive evolution at ranatuerin-2 antimicrobial peptide loci. DRAMP02197 MFTMKKSLLLFFFLGTISLSLCEEERGADEDDGVELTEEEVKRGLLSSFKGVAKGVAKDLAGKLLEKLKCKITGC 75 Ranatuerin-2SRa (Frogs, amphibians, animals) J9RZ39 Not found Not found Rana sierrae (Nevada yellow-legged frog) Antimicrobial Homology Not found Not found Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dis. Aquat. Organ. 2013,0:0-0. Robertson LS, Fellers GM, Marranca JM, Kleeman PM. Non-lethal collection of skin secretions for expression analysis and identification of antimicrobial peptide transcripts from six North American frog species. DRAMP02198 MFTLKKSLLLFFFLGTISLSLCEEERGADEDDDVEMTEEEVKRGIMDSVKGVAKNLAAKLLEKLKCKITGC 71 Ranatuerin-2SRb (Frogs, amphibians, animals) J9RWR2 Not found Not found Rana sierrae (Nevada yellow-legged frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dis. Aquat. Organ. 2013,0:0-0. Robertson LS, Fellers GM, Marranca JM, Kleeman PM. Non-lethal collection of skin secretions for expression analysis and identification of antimicrobial peptide transcripts from six North American frog species. DRAMP02199 MFTLKKSMLLLFFLGTISFSLCEEERGADKDDGGEITEEVKRGFLDVIKDTAQNLFATVLDKIKCKVTKC 70 Ranatuerin-2TGa (Frogs, amphibians, animals) D5MTI4 Not found Not found Rana tagoi (Tago frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides 0:0-0(2010 Tazato S, Conlon JM, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides andbradykinin from the skin and brain of Oki Tago's brown frog, Ranatagoi okiensis. DRAMP02200 MFTVKKSLLLLFFLGTITLSLCEQERGADEDNGGEMTEEEVKRGLFLDTLKGAAKDVAGKLLEGLKCKITGCKP 74 Ranatuerin-2RC antimicrobial peptide (Frogs, amphibians, animals) C5IAZ1 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ database Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptidefrom Rana catesbeiana. DRAMP02201 MFTLKKSLLLLFFLGTINLSLCEEERDAGDDQGEVVKQEVKRAFFTTFKNLVTNVAGTVIDKMKCKLTGEC 71 Ranatuerin-2BYa (Frogs, amphibians, animals) J9RRZ4 Not found Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dis. Aquat. Organ. 2013,0:0-0. Robertson LS, Fellers GM, Marranca JM, Kleeman PM. Non-lethal collection of skin secretions for expression analysis and identification of antimicrobial peptide transcripts from six North American frog species. DRAMP02202 MFTLKKSLLLFFFLGTISLSLCEEERGADEDDGVELTEEEVKRGILSTFKGLAKGVAKDLAGKLLDKFKCKITGC 75 Ranatuerin-2BYb (Frogs, amphibians, animals) J9RWR8 Not found Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dis. Aquat. Organ. 2013,0:0-0. Robertson LS, Fellers GM, Marranca JM, Kleeman PM. Non-lethal collection of skin secretions for expression analysis and identification of antimicrobial peptide transcripts from six North American frog species. DRAMP02203 MFTMKKSLLLLFFLGTINLSLCEEERDADQEERRDDPGERDVQVEKRFLPIAPMLGKYLGK 61 Ranatuerin-5Ca antimicrobial peptide (Frogs, amphibians, animals) C5IAZ8 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ database Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptidefrom Rana catesbeiana. DRAMP02204 MFTLKKSLLLLFFLGTINLSLCEEERDADQEERRDDPGERDVQVEKRFLPIASMLGKYLGK 61 Ranatuerin-5Cb antimicrobial peptide (Frogs, amphibians, animals) C5IB02 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ database Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptidefrom Rana catesbeiana. DRAMP02205 MFTLKKSMLLLFFLGTISLSLCQDEGADEDHGGEMTTEEKRGLMDIFKVAVNKLLAAGMNKPRCKAAHC 69 Ranatuerin-2YJ (Frogs, amphibians, animals) G1ERV9 Not found Not found Rana dybowskii (Dybovsky's frog) (Korean brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22702542 Can J Microbiol. 2012 Jul;58(7):848-855. Yang SJ, Xiao XH, Xu YG, Li DD, Chai LH, Zhang JY. Induction of antimicrobial peptides from Rana dybowskii under Rana grylio virus stress, and bioactivity analysis. DRAMP02206 RGADEDDGVEITEEEVKRGLMDTVKNAAKNLAGQLLDRLKCKITGC 46 Ranatuerin 2CHa (Frogs, amphibians, animals) A9CBH4 Not found Not found Rana chiricahuensis Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database [Ref.21262304] LC50=135 µM against human erythrocytes Cyclic Free Cyclization (Cys41 and Cys46) Disulfide bond between Cys41 and Cys46. L No cytotoxicity information found Not found 17938991 J Mol Evol. 2007 Nov;65(5):605-615. Tennessen JA, Blouin MS. Selection for antimicrobial peptide diversity in frogs leads to gene duplication and low allelic variation. DRAMP02207 DDDQVEVQQEVKRGFLSTVKNLATNVAGTVIDTLKCKVTGGCRT 44 Ranatuerin 2CHb (Frogs, amphibians, animals) A9CBH6 Not found Ranatuerin2b Rana chiricahuensis Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database [Ref.21262304] LC50=120 µM against human erythrocytes Cyclic Free Free Disulfide bond between Cys36 and Cys42. L No cytotoxicity information found Not found 17938991 J Mol Evol. 2007 Nov;65(5):605-615. Tennessen JA, Blouin MS. Selection for antimicrobial peptide diversity in frogs leads to gene duplication and low allelic variation. DRAMP02208 MFPLKKSLLLLFFFGTIPLSFCEQERGADEEEGNGEKEIKRSMFSVLKDLGKVGLGFVACKVNKQC 66 Ranatuerin-1Ca antimicrobial peptide (Frogs, amphibians, animals) C5IAZ2 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ database Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptidefrom Rana catesbeiana. DRAMP02209 MFTLKKSLLLLFFLGTITLSLCEQERGADEEEGNGEKEIKRSMFSVLKNLGKVGLGFVACKVNKQC 66 Ranatuerin-1Cb antimicrobial peptide (Frogs, amphibians, animals) C5IAZ4, C5IAZ5, C5IAZ3 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ database Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptidefrom Rana catesbeiana. DRAMP02210 MFTSKKSMLLLFFLGTISLSLCEEERDEDEVIEEEVKRGLLSVFKGVLKGVGKNVAGSLLDQLKCKISGGC 71 Ranatuerin-2AMa protein (Frogs, amphibians, animals) A0AAR9 Not found ranatuerin-2AMa Rana amurensis (Korean brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16790295 Peptides. 2006 Nov;27(11):2688-2694. Zhou M, Liu Y, Chen T, Fang X, Walker B, Shaw C. Components of the peptidome and transcriptome persist in lin wa pi: the dried skin of the Heilongjiang brown frog (Rana amurensis) as used in traditional Chinese medicine. DRAMP02211 MFTSKKSMLLLFFLGTISLSLCQEERDADEDEVIEEEVKRGLFSVVKGVLKGVGKNVAGSLLDQLKCKISGGC 73 Ranatuerin-2AMb protein (Frogs, amphibians, animals) A0AAS0 Not found ranatuerin-2AMb Rana amurensis (Korean brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16790295 Peptides. 2006 Nov;27(11):2688-2694. Zhou M, Liu Y, Chen T, Fang X, Walker B, Shaw C. Components of the peptidome and transcriptome persist in lin wa pi: the dried skin of the Heilongjiang brown frog (Rana amurensis) as used in traditional Chinese medicine. DRAMP02212 MFTLKKSLLLFFFLGTISLSLCEQERGADEDDGVEMTEEEVKRGLADYWRTAFRANFANLGPGIRCKSARC 71 Antimicrobial peptide ranatuerin-2ZHa (Frogs, amphibians, animals) J9R283 Not found Not found Rana zhenhaiensis Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22943778 Zoolog Sci. 2012 Sep;29(9):553-558. Xu B, Che H, Kang L, Zheng S, Mu S, Wan F. Molecular cloning and functional characterization of novel antimicrobial peptides from the skin of brown frog, Rana zhenhaiensis. DRAMP02213 MFTLKKSMLLLFFLGTISLSLCQEERGADEDDGGEMTEEVKRGLLNVIKDTAQNLFAAALDKLKCKVTKCN 71 Ranatuerin-2TOa (Frogs, amphibians, animals) D5MTH6 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides 2010,0:0-0. Tazato S, Conlon J.M, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides andbradykinin from the skin and brain of Oki Tago's brown frog, Ranatagoi okiensis. DRAMP02214 MFTLKKSMLLLFFLGTISLSLCQEERGADEDDGGEMTEEVKRGLLNVIKDTAQNLFAAALEKLKCKVTKCN 71 Ranatuerin-2TOb (Frogs, amphibians, animals) D5MTH7 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides 2010,0:0-0. Tazato S, Conlon J.M, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides andbradykinin from the skin and brain of Oki Tago's brown frog, Ranatagoi okiensis. DRAMP02215 MFTLKKSMLLLFFLGTISLSLCQEERGADEDDGGEMTEEVKRGLLNVIRDTAQNLFAAALEKLKCKVTKCN 71 Ranatuerin-2TOc (Frogs, amphibians, animals) D5MTH8 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides 2010,0:0-0. Tazato S, Conlon J.M, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides andbradykinin from the skin and brain of Oki Tago's brown frog, Ranatagoi okiensis. DRAMP02216 MFTLKKSMLLLFFLGTISLSLCQEERGADEDDGGEMTEEVKRGLLNVIKDTAQNLFTAALEKLKCKVTKCN 71 Ranatuerin-2TOd (Frogs, amphibians, animals) D5MTH9 Not found Not found Rana tagoi okiensis (Oki brown frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Peptides 2010,0:0-0. Tazato S, Conlon J.M, Iwamuro S. Cloning and expression of genes enocoding antimicrobial peptides andbradykinin from the skin and brain of Oki Tago's brown frog, Ranatagoi okiensis. DRAMP02217 AAKLLLNPKFRCKAAFC 17 Ranatuerin-2Ra (Frogs, amphibians, animals) P86020 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide (By similarity). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 12-17." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP02218 AVNIPFKVKFRCKAAFC 17 Ranatuerin-2R (Frogs, amphibians, animals) P86019 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Pelophylax ridibundus (Marsh frog) (Rana ridibunda) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide (By similarity). Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 12-17." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18855342 Rapid Commun Mass Spectrom. 2008 Nov;22(22):3517-3525. Samgina TY, Artemenko KA, Gorshkov VA, Ogourtsov SV, Zubarev RA, Lebedev AT. De novo sequencing of peptides secreted by the skin glands of the Caucasian Green Frog Rana ridibunda. DRAMP02226 GLMDTVKNAAKNLAGQLLDTIKCKMTGC 28 Ranatuerin-2ARa (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana areolata (North American crawfish frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database [Ref:12429503] HC50=100 µM against human erythrocytes Cyclic Free Cyclization (Cys23 and Cys28) Disulfide bond between Cys23 and Cys28. L No cytotoxicity information found Not found PubMed ID is not available Biochim Biophys Acta. 2002 Nov 19;1601(1):55-63. Ali MF, Lips KR, Knoop FC, Fritzsch B, Miller C, Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. DRAMP02227 GFLSTVKNLATNVAGTVIDTIKCKVTGGC 29 Ranatuerin-2Pa (Frogs, amphibians, animals) Q8QFQ3 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12413397 Biochem J. 2003 Apr 1;371(Pt 1):125-130. Chen T, Farragher S, Bjourson AJ, Orr DF, Rao P, Shaw C. Granular gland transcriptomes in stimulated amphibian skin secretions. DRAMP02232 FLPIASLLGKYL 12 Ranatuerin-5 (Frogs, amphibians, animals) P82820 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Function: Antimicrobial peptide (By similarity). Tissue specificity: Expressed by the skin glands." Gram-positive bacterium: Staphylococcus aureus (MIC>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784389 Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-592. Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. DRAMP02240 GMFSVLKNLGKVGLGFVACKINKQC 25 Ranatuerin-1Gb (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana grylio (North American pig frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10828493 Regul Pept. 2000 Jun 30;90(1-3):53-60. Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Abel PW, Conlon JM. Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. DRAMP02086 FLPVLTGLTPSIVPKLVCLLTKKC 24 Brevinin-1PRa (frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pretiosa (North oregon spotted frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC>100μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=13μM);## Yeast: Candida albicans(MIC=100μM).[Ref.21295070] Gram-negative bacterium: Escherichia coli(MIC>100μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=50μM);## Yeast: Candida albicans(MIC=100μM). [Ref.15003829] HC50=7μM against human erythrocytes.##[Ref.21295070] LC50= 150μM against human erythrocytes. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 15003829##21295070 Regul Pept. 2004 May 15;118(3):135-141.## Dev Comp Immunol. 2011 Jun;35(6):644-649. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica.## Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: implications for species resistance to chytridiomycosis. DRAMP02243 GLLSGLKKVGKHVAKNVAVSLMDSLKCKISGDC 33 Ranatuerin-1T (Brevinin-2T; Frogs, amphibians, animals) P82740, P82236 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10422869##10333736 Peptides. 1999;20(2):159-163.##Biopolymers. 1998;47(6):435-450. Goraya J, Knoop FC, Conlon JM.##Simmaco M, Mignogna G, Barra D. Ranatuerin 1T: an antimicrobial peptide isolated from the skin of the frog, Rana temporaria.##Antimicrobial peptides from amphibian skin: what do they tell us? DRAMP01384 DEKGPKWKR 9 Odorranain-N1 (OdN1; Frogs, amphibians, animals) A6MBP9 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antifungal Transcript level Not found Not found Function: Odorranain-N1 appears to be narrowly antifungal with low potency against Candida albicans. [Ref.17272268] Yeast: Candida albicans (MIC=35.20 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP18270 KINWGSVGGSCVGGAVIGGALGGLGGAGGGCLTGAIGSIWDQW 43 Enterocin NKR-5-3Z(Bacteriocin) I4DXG1 Belongs to the class IIb bacteriocin enkZ Enterococcus faecium NKR-5-3 Antimicrobial, Antibacterial, Anti-Gram+ Not found Ent53A and Ent53Z, components of a class IIb bacteriocin, show synergistic antimicrobial activity. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25149515 Appl Environ Microbiol. 2014 Nov;80(21):6647-55. Ishibashi N, Himeno K, Masuda Y, Perez RH, Iwatani S, Zendo T, Wilaipun P, Leelawatcharamas V, Nakayama J, Sonomoto K. Gene cluster responsible for secretion of and immunity to multiple bacteriocins, the NKR-5-3 enterocins. DRAMP18269 YSSKDCLKDIGKGIGAGTVAGAAGGGLAAGLGAIPGAFVGAHFGVIGGSAACIGGLLGN 59 Enterocin NKR-5-3A(Bacteriocin) I4DXG0 Belongs to the class IIb bacteriocin enkA Enterococcus faecium NKR-5-3 Antimicrobial, Antibacterial, Anti-Gram+ Not found Ent53A and Ent53Z, components of a class IIb bacteriocin, show synergistic antimicrobial activity. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25149515 Appl Environ Microbiol. 2014 Nov;80(21):6647-55. Ishibashi N, Himeno K, Masuda Y, Perez RH, Iwatani S, Zendo T, Wilaipun P, Leelawatcharamas V, Nakayama J, Sonomoto K. Gene cluster responsible for secretion of and immunity to multiple bacteriocins, the NKR-5-3 enterocins. DRAMP02249 AIMDTIKDTAKTVAVGLLNKLKCKITGC 28 Ranatuerin-2SEB (Frogs, amphibians, animals) P85058 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sevosa (dusky gopher frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli K12;##Gram-positive bacterium: Micrococcus luteus NCT C2665. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16386333 Peptides. 2006 Jun;27(6):1313-1319. Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. DRAMP02250 GIMDTIKDTAKTVAVGLLNKLKCKITGC 28 Ranatuerin-2SEC (Frogs, amphibians, animals) P85053 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana sevosa (dusky gopher frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli K12;##Gram-positive bacterium: Micrococcus luteus NCT C2665. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16386333 Peptides. 2006 Jun;27(6):1313-1319. Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. DRAMP02253 GIMDSVKGLAKNLAGKLLDSLKCKITGC 28 Ranatuerin-IIbYb (Ranatuerin-2bYa; Frogs, amphibians, animals) P84115 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-2 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP02258 GILSTFKGLAKGVAKDLAGNLLDKFKCKITGC 32 Ranatuerin-IIbYa (Ranatuerin-2bYa; Frogs, amphibians, animals) P84114 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana boylii (Foothill yellow-legged frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Show weak hemolytic activity. [Ref.14531844]Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus [Ref.14531844]HC50=120 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14531844 J Pept Res. 2003 Nov;62(5):207-213. Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pál T, Rollins-Smith LA. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. DRAMP02259 GIGKYLHSAKKFGKAWVGEIMNS 23 Magainin 2 analogue (F5Y, F16W-MG2) P11006 Belongs to the gastrin/cholecystokinin family (Magainin subfamily) Not found Xenopus laevis (African clawed frog) Unknown Protein level Alpha helix (1 helices; 12 residues) The peptide assumed α-helices in the lipid environment, as characterized by double minima around 208 and 222 nm. The [θ]222 value, a measure of helicity, of I (−17,900 deg cm2 dmol−1) was ca. 20% smaller than that of F16W-MG2 (−23,200 deg cm2 dmol−1). 1DUM resolved by NMR Membrane Permeabilization: The peptide-induced membrane permeabilization was examined on the basis of the efflux of the fluorescent dye calcein from egg PG LUVs. The mutant I (F5Y, F16W-MG2) showed a slightly weaker but comparable leakage activity compared with F16W-MG2. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11180056 Biopolymers. 2001 Apr 5;58(4):437-446. Hara T, Kodama H, Kondo M, Wakamatsu K, Takeda A, Tachi T, Matsuzaki K. Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue. DRAMP02260 GMASKAGTIAGKIAKTAIKLAL 22 PGLa-B1 No entry found Not found Not found Xenopus borealis Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22036891 Gen Comp Endocrinol. 2012 May 1;176(3):513-518. Conlon JM, Mechkarska M, King JD. Host-defense peptides in skin secretions of African clawed frogs (Xenopodinae, Pipidae). DRAMP02261 GMASKAGSIVGKIAKIALGAL 21 PGLa-B2 No entry found Not found Not found Xenopus borealis Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22036891 Gen Comp Endocrinol. 2012 May 1;176(3):513-518. Conlon JM, Mechkarska M, King JD. Host-defense peptides in skin secretions of African clawed frogs (Xenopodinae, Pipidae). DRAMP02262 GLGSLLGKAFKIGLKTVGKMMGGAPREQ 28 CPF-B1 No entry found Not found Not found Xenopus borealis Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20656059 Comp Biochem Physiol C Toxicol Pharmacol. 2010 Nov;152(4):467-472. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Antimicrobial peptides with therapeutic potential from skin secretions of the Marsabit clawed frog Xenopus borealis. DRAMP02263 GMASKAGSVLGKVAKVALKAAL 22 PGLa-AM1 No entry found Not found Not found Xenopus amieti Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22326566 Int J Antimicrob Agents. 2012 Apr;39(4):317-320. Conlon JM, Sonnevend A, Pál T, Vila-Farrés X. Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group. DRAMP02264 GIWKTIKSMGKVFAGKILQNL 21 [D4K]B2RP No entry found Not found Not found Lithobates septentrionalis Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22326566 Int J Antimicrob Agents. 2012 Apr;39(4):317-320. Conlon JM, Sonnevend A, Pál T, Vila-Farrés X. Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group. DRAMP02265 MPVAVGPYGQSQPNCFDRVKMGFMMGFAVGMAAGALFGTFSCLRFGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC 79 Reactive oxygen species modulator 1 (ROS modulator 1; Frogs, amphibians, animals) Q4V7T9 Belongs to the MGR2 family romo1 Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity against a variety of bacteria. Acts by inducing bacterial membrane breakage (By similarity). Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation. Domain: Contains a transmembrane helix domian." S. aureus, Pseudomonas aeruginosa and M. tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Unknown NIH - Xenopus Gene Collection (XGC) project DRAMP02266 KPSSDADEDNDEVERYVRGWASKIGQTLGKIAKVGLQGLMQPKREAMLRSAEAQGMIGTLTSKRIKQG 68 Prolevitide (Frogs, amphibians, animals) P13684 Belongs to the gastrin/cholecystokinin family Not found Xenopus laevis (African clawed frog) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2830279 J Biol Chem. 1988 Mar 5;263(7):3279-3283. Poulter L, Terry AS, Williams DH, Giovannini MG, Moore CH, Gibson BW. Levitide, a neurohormone-like peptide from the skin of Xenopus laevis. Peptide and peptide precursor cDNA sequences. DRAMP02267 LKCVNLQANGIKMTQECAKEDTKCLTLRSLKKTLKFCASGRTCTTMKIMSLPGEQITCCEGNMCNA 66 Antimicrobial amphipathic helix-forming peptide (Frogs, amphibians, animals) No entry found Not found Not found Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8203742 Anal Biochem. 1994 Feb 15;217(1):84-90. James S, Gibbs BF, Toney K, Bennett HP. Purification of antimicrobial peptides from an extract of the skin of Xenopus laevis using heparin-affinity HPLC: characterization by ion-spray mass spectrometry. DRAMP02270 GIGKFLHSAGKFGKAFVGEIMKS 23 Magainin-1 (Magainin I; chain of Magainins; Frogs, amphibians, animals) P11006 Belongs to the magainin family magainins Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents. Tissue specificity: Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3299384 Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-5453. Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. DRAMP02284 GLNTLKKVFQGLHEAIKLINNHVQ 24 Pseudin-1 (Pseudin 1; Frogs, amphibians, animals) P83188 Not found Not found Pseudis paradoxa (Paradoxical frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Possesses antifungal activity against C. albicans and is also active against E. coli and S. aureus. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689009 Biochem Biophys Res Commun. 2001 Nov 9;288(4):1001-1005. Olson L 3rd, Soto AM, Knoop FC, Conlon JM. Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. DRAMP02285 GLNALKKVFQGIHEAIKLINNHVQ 24 Pseudin-2 (Pseudin 2; Frogs, amphibians, animals) P83189 Not found Not found Pseudis paradoxa (Paradoxical frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Possesses antifungal activity against C. albicans and is also active against E. coli and S. aureus. Has low hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the skin glands." [Ref.11689009]Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus;##Yeast: Candida albicans [Ref.11689009]50% hemolysis of human erythrocytes is >300 μM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689009 Biochem Biophys Res Commun. 2001 Nov 9;288(4):1001-1005. Olson L 4rd, Soto AM, Knoop FC, Conlon JM. Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. DRAMP02286 GINTLKKVIQGLHEVIKLVSNHE 23 Pseudin-3 (Pseudin 3; Frogs, amphibians, animals) P83190 Not found Not found Pseudis paradoxa (Paradoxical frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Possesses antifungal activity against C. albicans and is also active against E. coli and S. aureus. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689009 Biochem Biophys Res Commun. 2001 Nov 9;288(4):1001-1005. Olson L 5rd, Soto AM, Knoop FC, Conlon JM. Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. DRAMP02287 GINTLKKVIQGLHEVIKLVSNHA 23 Pseudin-4 (Pseudin 4; Frogs, amphibians, animals) P83191 Not found Not found Pseudis paradoxa (Paradoxical frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: Possesses antifungal activity against C. albicans and is also active against E. coli and S. aureus. Tissue specificity: Expressed by the skin glands." Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689009 Biochem Biophys Res Commun. 2001 Nov 9;288(4):1001-1005. Olson L 6rd, Soto AM, Knoop FC, Conlon JM. Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. DRAMP02297 FPMKKSLLLIFFLGTINLSFCEEERNAEEEKRDGDDEMDVEVQKR 45 Gaegurin-6-RN antimicrobial peptide (Frogs, amphibians, animals) C0ILG5, C0ILJ5 Not found Not found Rana nigrovittata (black-striped frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database Comment: No comments found on DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02298 FTMKKSLLLIFFLGTINLSLCEEERNAEEEKRDGDDEMDVEVQKR 45 Gaegurin-6-RN antimicrobial peptide (Frogs, amphibians, animals) C0ILJ3, C0ILH9, C0ILH1, C0ILG3, C0ILJ4 Not found Not found Rana nigrovittata (black-striped frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database Comment: No comments found on DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02299 FTMKKSLLLLFFLGTINLSLCEKERNAEEEKRDGDDETDVEVQK 44 Gaegurin-6-RN antimicrobial peptide (Frogs, amphibians, animals) C0ILJ2 Not found Not found Rana nigrovittata (black-striped frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database Comment: No comments found on DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19778602 Genomics. 2010 Jan;95(1):66-71. Ma Y, Liu C, Liu X, Wu J, Yang H, Wang Y, Li J, Yu H, Lai R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. DRAMP02301 MKIIVVLAVLMLVSAQVCLVSAAEMGHSSDNELSSRDLVKRFFLPPCAHKGTCGKRSIESSEGANGGE 68 Riparin-1.5 amide (Frogs, amphibians, animals) A6MWT0 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Unknown Transcript level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys47 and Cys53. L No cytotoxicity information found Not found 18601958 Regul Pept. 2008 Nov 29;151(1-3):80-87. Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02302 FPLPCAYKGTYC 12 Riparin-1.3 (Frogs, amphibians, animals) P86126 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 5-12." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys5 and Cys12) Disulfide bond between Cys5 and Cys12. L No cytotoxicity information found Not found 16470724##18601958 Rapid Commun Mass Spectrom. 2006;20(5):797-803.##Regul Pept. 2008 Nov 29;151(1-3):80-87. Maselli VM, Bilusich D, Bowie JH, Tyler MJ.##Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry.##Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02303 MKIIVVLAVLMLVSAQVCLVSAAEMGHSSDNELSSRDLVKRFFLPPCAYKGTCNH 55 Riparin-1.4 (Frogs, amphibians, animals) A6MWS7 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 6-12." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys47 and Cys53. L No cytotoxicity information found Not found 16470724 Rapid Commun Mass Spectrom. 2006;20(5):797-803. Maselli VM, Bilusich D, Bowie JH, Tyler MJ. Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry. DRAMP02304 MKIIVFLAVLMLVSAQVCLVSAAEMEHSSDNELSSRDLVKRFFLPPCAHKGTCNH 55 Riparin-1.5 acid (Frogs, amphibians, animals) A6MWS9 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Unknown Protein level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands. PTM: Contains one disulfide bond 6-12." Comment: No comments found on DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys47 and Cys53. L No cytotoxicity information found Not found 16470724 Rapid Commun Mass Spectrom. 2006;20(5):797-803. Maselli VM, Bilusich D, Bowie JH, Tyler MJ. Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry. DRAMP02305 MKIIVFLAVLMLVSAQVCLVSAAEMEHSSDNELSSRDLVKRFPLPSCVYTRTCGKRDIESSEGANGGE 68 Riparin-1.6 (Frogs, amphibians, animals) A6MWS8 Not found Not found Crinia riparia (Streambank froglet) (Flinders Ranges froglet) Unknown Transcript level Not found Not found "Function: Amphibian defensive peptide. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys47 and Cys53. L No cytotoxicity information found Not found 18601958 Regul Pept. 2008 Nov 29;151(1-3):80-87. Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02309 IIGHLIKTALGFLGL 15 Signiferin-2.2 (Frogs, amphibians, animals) P86132 Not found Not found Crinia signifera (Common eastern froglet) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity against a wide spectrum of Gram-positive bacteria. Lacks antibacterial activity against the Gram-negative bacteria E. cloacae and E. coli. Tissue specificity: Expressed by the skin glands. PTM: C-terminal amidation." Gram-negative bacteria: Enterobacter cloacae ATCC 13047 (MIC≤100 µM), Escherichia coli ATCC3 5218 (MIC≤100 µM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15317042##16470724##18601958 Rapid Commun Mass Spectrom. 2004;18(18):2155-2161.##Rapid Commun Mass Spectrom. 2006;20(5):797-803.##Regul Pept. 2008 Nov 29;151(1-3):80-87. Maselli VM, Brinkworth CS, Bowie JH, Tyler MJ.##Maselli VM, Bilusich D, Bowie JH, Tyler MJ.##Jackway RJ, Pukala TL, Maselli VM, Musgrave IF, Bowie JH, Liu Y, Surinya-Johnson KH, Donnellan SC, Doyle JR, Llewellyn LE, Tyler MJ. Host-defence skin peptides of the Australian Common Froglet Crinia signifera: sequence determination using positive and negative ion electrospray mass spectra.##Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry.##Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends. DRAMP02310 AANFGPSVFTPEVHETWQKFLNVVVAALGKQYH 33 HbbetaP-1 (fish, chordates, animals) No entry found Not found Not found Ictalurus punctatus (Catfish) Antimicrobial, Antibacterial, Antiparasitic Not found Not found Not found Function: Showes moderate activity against Gram-negative bacteria, Aeromonas hydrophila and Vibrio alginolyticus, but no activity against Gram-positive bacteria such as S. aureus, Streptococcus faecalis S. iniae. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18538841 Dev Comp Immunol. 2008;32(11):1301-1312. Ullal AJ, Litaker RW, Noga EJ. Antimicrobial peptides derived from hemoglobin are expressed in epithelium of channel catfish (Ictalurus punctatus, Rafinesque). DRAMP02311 SGPVPSGCLRCICVVESGXRMPNPV 25 Lysozyme (1,4-beta-N-acetylmuramidase; starfish, chordates, animals) P37715 Belongs to the glycosyl hydrolase 22 family Not found Asterias rubens (Common European starfish) (Asterias vulgaris) Antimicrobial Protein level Not found Not found Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1149747 Eur J Biochem. 1975 May;54(1):19-23. Jolles J, Jolles P. The losozyme from Asterias rubens. DRAMP02313 QIHLSLCGLCCNCCHNIGCGFCCKF 25 Hepcidin-1 (fish, chordates, animals) Q801Y3 Belongs to the hepcidin family hamp1 Salmo salar (Atlantic salmon) Unknown Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12697315 Dev Comp Immunol. 2003 Jun-Jul;27(6-7):589-601. Douglas SE, Gallant JW, Liebscher RS, Dacanay A, Tsoi SC. Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. DRAMP02319 FIGGIISLIKKLF 13 Grammistin Pp2a (Group II grammistin; fish, chordates, animals) P69843 Belongs to the grammistin family (Group 2 subfamily) Not found Pogonoperca punctata (Clown grouper) (Bearded grouper) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has lytic, hemolytic and antibacterial activities. No MICs found in DRAMP database [Swiss_Prot Entry P69843]has lytic, hemolytic and antibacterial activities Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phospholipids PubMed ID is not available Fish. Sci. 2001 Feb;67:163-169. Shiomi K, Yokota H, Nagashima Y, Ishida M. Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata. DRAMP18268 ATYYGNGLYCNSKKCWVEWGITGGCLAQYAIGGWLGGAVPGKC 43 Enterocin NKR-5-3C(Bacteriocin) I7H7S7 Belongs to the class IIa bacteriocin enkC Enterococcus faecium NKR-5-3 Antimicrobial, Antibacterial, Anti-Gram+ Not found Ent53C is a novel class IIa bacteriocin that contains a YGNVL motif sequence and two disul?de bridges. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25149515 Appl Environ Microbiol. 2014 Nov;80(21):6647-55. Ishibashi N, Himeno K, Masuda Y, Perez RH, Iwatani S, Zendo T, Wilaipun P, Leelawatcharamas V, Nakayama J, Sonomoto K. Gene cluster responsible for secretion of and immunity to multiple bacteriocins, the NKR-5-3 enterocins. DRAMP02323 LFGFLIPLLPHLIGAIPQVIGAIR 24 Grammistin Pp4b (Group I grammistin; fish, chordates, animals) P69838 Belongs to the grammistin family (Group 1 subfamily) Not found Pogonoperca punctata (Clown grouper) (Bearded grouper) Antimicrobial, Antibacterial Protein level Not found Not found MOA: Thanks to its abundant amphiphilic alpha-helices, it may integrate into membrane phospholipids, leading to lysis of the membrane. Has also ichthyotoxic activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phospholipids PubMed ID is not available Fish. Sci. 2001 Feb;67:163-169. Shiomi K, Yokota H, Nagashima Y, Ishida M. Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata. DRAMP02325 FFHHIFRGIVHVGKTIHKLVTGG 23 Moronecidin 1 (fish, chordates, animals) No entry found Belongs to the pleurocidin family Not found Morone chrysops (white bass) Antimicrobial, Antibacterial Not found Not found Not found Function: Exhibits antimicrobial activity against fish bacterial pathogens, especially against species of Aeromonas, which may to certain extent reflect the pathogenicity of these bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02326 FFHHIFRGIVHVGKTIHRLVTGG 23 Moronecidin 2 (fish, chordates, animals) No entry found Belongs to the pleurocidin family Not found Morone chrysops (white bass) Antimicrobial, Antibacterial Not found Not found Not found Function: Exhibits antimicrobial activity against fish bacterial pathogens, especially against species of Aeromonas, which may to certain extent reflect the pathogenicity of these bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02327 FFHHIFRGIVHVGRTIHKLVTGG 23 Moronecidin 3 (fish, chordates, animals) No entry found Belongs to the pleurocidin family Not found Morone chrysops (white bass) Antimicrobial, Antibacterial Not found Not found Not found Function: Exhibits antimicrobial activity against fish bacterial pathogens, especially against species of Aeromonas, which may to certain extent reflect the pathogenicity of these bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02328 FFHHIFRGIVHVGRTIHRLVTGG 23 Moronecidin 4 (fish, chordates, animals) No entry found Belongs to the pleurocidin family Not found Morone chrysops (white bass) Antimicrobial, Antibacterial Not found Not found Not found Function: Exhibits antimicrobial activity against fish bacterial pathogens, especially against species of Aeromonas, which may to certain extent reflect the pathogenicity of these bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02329 IFHHIFKGIVHVGKTIHRLVTG 22 Moronecidin 5 (fish, chordates, animals) No entry found Belongs to the pleurocidin family Not found Morone chrysops (white bass) Antimicrobial, Antibacterial Not found Not found Not found Function: Exhibits antimicrobial activity against fish bacterial pathogens, especially against species of Aeromonas, which may to certain extent reflect the pathogenicity of these bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11739390 J Biol Chem. 2002 Feb 15;277(7):5030-5039. Lauth X, Shike H, Burns JC, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Nizet V, Taylor SW, Shimizu C, Bulet P. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. DRAMP02332 FIHHIFRGIVHAGRSIGRFLTG 22 Piscidin-3 (Pis-3; fish, chordates, animals) P0C006 Belongs to the pleurocidin family Not found Morone chrysops x Morone saxatilis (white bass x striped sea-bass) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Not found Not found "Function: Exhibits broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Has hemolytic activity. Tissue specificity: Mast cells in gill, skin and gut, and in lining blood vessels in the viscera." [Swiss_Prot Entry P0C006]broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria [Ref.11713517]5% hemolytic activity at 100 μg/mL against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11713517 Nature. 2001 Nov 15;414(6861):268-269. Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. DRAMP02333 FFRHLFRGAKAIFRGARQGWRAHKVVSRYRNRDVPETDNNQEEP 44 Piscidin-4 (Pis-4; fish, chordates, animals) E3UVF6 Belongs to the pleurocidin family Not found Morone chrysops x Morone saxatilis (white bass x striped sea-bass) Antimicrobial, Antibacterial, Antiviral Predicted Not found Not found "Function: Piscidin 4 demonstrates potent, broad-spectrum, antibacterial activity against a number of fish and human pathogens, including multi-drug resistant bacteria. Sequence similarity: It has considerable (to >65%) N-terminal sequence homology to piscidins 1-3." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19266617 Comp Biochem Physiol B Biochem Mol Biol. 2009 Apr;152(4):299-305. Noga EJ, Silphaduang U, Park NG, Seo JK, Stephenson J, Kozlowicz S. Piscidin 4, a novel member of the piscidin family of antimicrobial peptides. DRAMP02334 XSHLSLCRWCCNCCHNKGXGFCCKF 25 Hepcidin (fish, chordates, animals) Q9DFD6 Belongs to the hepcidin family hamp Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11164886 Dev Comp Immunol. 2001 Apr;25(3):205-217. Bayne CJ, Gerwick L, Fujiki K, Nakao M, Yano T. Immune-relevant (including acute phase) genes identified in the livers of rainbow trout, Oncorhynchus mykiss, by means of suppression subtractive hybridization. DRAMP02335 SKGKKANKDVELARG 15 Oncorhyncin I (Oncorhyncin 1; fish, chordates, animals) P83287 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database Planococcus citreus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10938737 Fish Shellfish Immunol. 2000 Apr;10(3):243-260. Smith VJ, Fernandes JM, Jones SJ, Kemp GD, Tatner MF. Antibacterial proteins in rainbow trout, Oncorhynchus mykiss. DRAMP02338 MVTLVLLVFLLLNVVEDEAASFPFSCPTLSGVCRKLCLPTEMFFGPLGCGKGFLCCVSHF 60 Beta-defensin 1 (fish, chordates, animals) A6YT28 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial Transcript level Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Falco A, Chico V, Marroqui L, Perez L, Coll J.M, Estepa A. Expression and antiviral activity of a beta-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences. DRAMP02339 PKRKSATKGDEPA 13 Histone H6-like protein (fish, chordates, animals) P83338 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted APR-2002 to the SWISS-PROT data bank. Fernandes JMO, Smith VJ. Antimicrobial properties of a histone H6-like peptide from skin secretions of rainbow trout, Oncorhynchus mykiss. DRAMP02340 XXSVPAFGHYLPAXP 15 Salmocidin-1 (fish, chordates, animals) P81369 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-1998) to UniProtKB. Henry M.A, Siegert K.J, Davidson I, Dunbar B, Mordue W, Secombes C.J. Isolation and N-terminal sequencing of an antibacterial peptide in rainbow trout, Oncorhynchus mykiss. DRAMP02341 SGFVLKGYTKTSQ 13 Salmocidin-2A (fish, chordates, animals) P82238 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted DEC-1999 to the SWISS-PROT data bank. Henry MA, Secombes CJ. Purification and partial characterization of antibacterial peptides from rainbow trout, Oncorhynchus mykiss. DRAMP02342 AGFVLKGYTKTSQ 13 Salmocidin-IIb (fish, chordates, animals) P82239 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted DEC-1999 to the SWISS-PROT data bank. Henry MA, Secombes CJ. Purification and partial characterization of antibacterial peptides from rainbow trout, Oncorhynchus mykiss. DRAMP02343 XXPQQLGHVKAAXSDY 16 Salmocidin-3 (fish, chordates, animals) P82240 Not found Not found Oncorhynchus mykiss (Rainbow trout) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-1999) to UniProtKB. Henry M.A, Secombes C.J. Purification and partial characterization of antibacterial peptides from rainbow trout, Oncorhynchus mykiss. DRAMP01375 GLGGAKKNFIIAANKTAPQSVKKTFSCKLYNG 32 Odorranain-E1 (OdE1; Frogs, amphibians, animals) A6MBK8 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Odorranain-E1 adopts 100% turn structure in water solution. Function: Odorranain-E1 exhibites antimicrobial activities against all of the tested microbes including Gram-positive and Gram-negative bacteria and fungi. Has no hemolytic activity against red cell. [Ref.17272268] Gram-negative bacterium: Escherichia coli (MIC=9.37 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=4.68 μg/ml), Bacillus subtilis (MIC=4.68 μg/ml).##Yeast: Candida albicans (MIC=9.37 μg/ml). [Ref:17272268]Non-hemolytic activity against rabbit red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP02345 PEGQRALKRMARMTPLWRTMGTKPYGAYCLNNYECSTGICRGGHCMFSQPIKS 53 Liver-expressed antimicrobial peptide 2A (LEAP-2A; fish, chordates, animals) Q64KQ7 Not found LEAP-2A Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) Antimicrobial Predicted Not found Not found LEAP-2 is a blood-derived peptide expressed predominantly in the liver. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15350756 Vet Immunol Immunopathol. 2004 Oct;101(3-4):259-269. Zhang YA, Zou J, Chang CI, Secombes CJ. Discovery and characterization of two types of liver-expressed antimicrobial peptide 2 (LEAP-2) genes in rainbow trout. DRAMP02346 GVCLVALILMHQVCASPIGSHDSRLSLQQGTKLLERRTRMTPLWRFMGTKPTGAYCRDHFECSTQICRRGHCALSGA 77 Liver-expressed antimicrobial peptide 2B No entry found Not found Not found Oncorhynchus mykiss (rainbow trout) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP02353 RSTEDIIKSISGGGFLNAMNA 21 Pleurocidin-like peptide WFX (fish, chordates, animals; Predicted) Q7T053 Not found ple6 Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Predicted Not found Not found Function: Has antibacterial and antifungal activity. Gram-negative bacteria: Aeromonas salmonicida A449 field isolate (MIC>64 µg/ml), A. salmonicida 97-4 field isolate (MIC>64 µg/ml), Pseudomonas aeruginosa K799 (MIC>64 µg/ml), Pseudomonas aeruginosa Z61 (MIC>64 µg/ml), Escherichia coli (MIC>64 µg/ml), Salmonella typhimurium 14028s (MIC>64 µg/ml), S. typhimurium MS7953s (MIC>64 µg/ml);##Gram-positive bacteria: Staphylococcus epidermidis (human clinical isolates) (MIC>64 µg/ml), Staphylococcus aureus (MRSA) (MIC>64 µg/ml).##Fungi: Candida albica (MIC>64 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12950255 Eur J Biochem. 2003 Sep;270(18):3720-3730. Douglas SE, Patrzykat A, Pytyck J, Gallant JW. Identification, structure and differential expression of novel pleurocidins clustered on the genome of the winter flounder, Pseudopleuronectes americanus (Walbaum). DRAMP18267 GLEESPGHPGQPGPPGPPGAPGP 23 BacFL31(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Enterococcus faecium FL31 Antimicrobial, Antibacterial, Anti-Gram+, Antilisterial Pro-rich It is usual that even in the N-terminal 23 residues sequenced, six prolines at positions 6,9,12,15,18, and 21 are hydroxylated. To our knowledge, BacFL31 is the first bacteriocin described as encompassing hydroxyproline residues. BacFL31 exerted bactericidal effect against L. monocytogenes and proved useful for the inhibition of the growth of L. monocytogenes in minced beef meat during storage at 4 Celsius degree. Gram-positive(certain) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24583094 Anaerobe. 2014 Jun;27:1-6. Chakchouk-Mtibaa A, Elleuch L, Smaoui S, Najah S, Sellem I, Abdelkafi S, Mellouli L. An antilisterial bacteriocin BacFL31 produced by Enterococcus faecium FL31 with a novel structure containing hydroxyproline residues. DRAMP02356 FLGLIFHGLVHAGKLIHGLIHRNRG 25 HKPLP (pleurocidin-like peptide; glycine-rich; fish, chordates, animals) No entry found Not found Not found Hippocampus kuda Bleeker (Sea horse) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22252202 J Antibiot (Tokyo). 2012 Mar;65(3):117-121. Sun D, Wu S, Jing C, Zhang N, Liang D, Xu A. Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker. DRAMP02369 LLAWCLVFLVIVQQVTSSPVPQSDTPLTSVQEVQRSLKRTARMTPLWRIMGTKPHGAYCQNHYECSTGICRKGHCSYS 78 Liver-expressed antimicrobial peptide 2 (fish, chordates, animals) D0Q093 Not found LEAP-2 Ctenopharyngodon idella (Grass carp) (Leuciscus idella) Antimicrobial, Antibacterial, Anti-Gram- Predicted Not found Not found Grass carp LEAP-2 gene is expressed in a wide range of tissues except blood, with the highest level of transcripts found in liver. Gram-negative bacteria: Escherichia coli XC-1 and Aeromonas hydrophila S2. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19716607 Vet Immunol Immunopathol. 2010 Feb 15;133(2-4):133-143. Liu F, Li JL, Yue GH, Fu JJ, Zhou ZF. Molecular cloning and expression analysis of the liver-expressed antimicrobial peptide 2 (LEAP-2) gene in grass carp. DRAMP02370 KCCKKGGPRKCPPEGMTXFYERIFRI 26 Mucus envelope protein (parrotfish, chordates, animals) P81557 Not found Not found Scarus vetula (Queen parrotfish) Antimicrobial Protein level Not found Not found "Function: May have antimicrobial activity. Tissue specificity: Produced by the opercular gland in the gill cavity and secreted as part of the mucus cocoon." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-1998) to UniProtKB Videler H, Geertjes G.J, Videler J.J. Biochemical characteristics and antibiotic properties of the mucus envelope of the queen parrotfish (Scarus vetula). DRAMP02371 MPVSVGSYGQQAQPSCFDRVKMGFMMGFAVGMAAGAMFGTFSCLRIGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC 80 Reactive oxygen species modulator 1 (ROS modulator 1; zebrafish, chordates, animals) Q6NYD1 Belongs to the MGR2 family romo1 Danio rerio (Zebrafish) (Brachydanio rerio) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity against a variety of bacteria. Acts by inducing bacterial membrane breakage (By similarity). Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation." S. aureus, Pseudomonas aeruginosa and M. tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Unknown NIH - Zebrafish Gene Collection (ZGC) project DRAMP02372 QSHLSLCRFCCKCCRNKGCGYCCKF 25 Hepcidin-1 (zebrafish, chordates, animals) P61516 Belongs to the hepcidin family hamp1 Danio rerio (Zebrafish) (Brachydanio rerio) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15043943 Dev Comp Immunol. 2004 Jun;28(7-8):747-754. Shike H, Shimizu C, Lauth X, Burns JC. Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates. DRAMP18266 TYYGNGLYCNKEKCWVDWNQAKGEIGKIIVNGWVNH 36 Bacteriocin T8(Bacteriocin) Q27HG2 Belongs to the class IIa bacteriocin bacA Enterococcus faecium (Streptococcus faecium) Antimicrobial, Antibacterial, Anti-Gram+ Not found The predicted mature BacA protein (44 amino acids) showed sequence homology with the membrane-active class IIa bacteriocins of lactic acid bacteria and showed 86% homology with bacteriocin 31 from E. faecalis YI717 and 98% homology with bacteriocin RC714. Fuction: Bacteriocin T8 is active against E. faecalis isolated from patients diagnosed with vaginosis, against Lactobacillus sakei, and against a Propionibacterium sp. The peptide is heat stable (60 min at 100 degrees C) and remains active in phosphate buffer from pH 4.0 to 10.0. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16820469##17088377 Appl Environ Microbiol. 2006 Jul;72(7):4761-6.##Appl Environ Microbiol. 2006 Nov;72(11):6955-64. De Kwaadsteniet M, Fraser T, Van Reenen CA, Dicks LM.##Todokoro D, Tomita H, Inoue T, Ike Y. Bacteriocin T8, a novel class IIa sec-dependent bacteriocin produced by Enterococcus faecium T8, isolated from vaginal secretions of children infected with human immunodeficiency virus.##Genetic analysis of bacteriocin 43 of vancomycin-resistant Enterococcus faecium. DRAMP02375 RQRVEELSKFSKKGAAARRRK 21 Misgurin (weatherfish, chordates, animals) P81474 Not found Not found Misgurnus anguillicaudatus (Oriental weatherfish) (Oriental weatherloach) Antimicrobial, Antibacterial, Antifungal Protein level Alpha helix Not found Comment: No comments found on DRAMP database B.subtilus, Staphylococcus aureus, Streptococcus mutans, Streptococcus pneumoniae, Pseudomonas putida, Escherichia coli, Salmonella typhimurium, Serratia spps, Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9271200 FEBS Lett. 1997 Jul 14;411(2-3):173-178. Park CB, Lee JH, Park IY, Kim MS, Kim SC. A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus. DRAMP02383 ASFPWSCPSLSGVCRKVCLPTELFFGPLGCGKGFLCGVSHFL 42 saBD (seabream beta defensin; fish, chordates, animals) No entry found Not found Not found Sparus aurata (Teleost fish gilthead seabream) Antimicrobial, Antibacterial Not found Not found Not found Its gene is constitutively expressed and upregulated by CpG ODNs. It is also chemotactic activity to leukocytes. Vibrio anguillarum (a seabream pathogenic bacterium), Bacillus subtilis (strong activity); Vibrio harvey and Photobacterium damselae (little activity). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21497909 Mol Immunol. 2011 Jul;48(12-13):1432-1438. Cuesta A, Meseguer J, Esteban MÃ. Molecular and functional characterization of the gilthead seabream ?-defensin demonstrate its chemotactic and antimicrobial activity. DRAMP02384 SPAGCRFCCGCCPNMRGCGVCCRF 24 Hepcidin AS-hepc2 (fish, chordates, animals) Q68M56 Not found Not found Acanthopagrus schlegelii (Black porgy) Not found Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21073978 Comp Biochem Physiol B Biochem Mol Biol. 2011 Feb;158(2):155-163. Yang M, Chen B, Cai JJ, Peng H, Ling-Cai, Yuan JJ, Wang KJ. Molecular characterization of hepcidin AS-hepc2 and AS-hepc6 in black porgy (Acanthopagrus schlegelii): expression pattern responded to bacterial challenge and in vitro antimicrobial activity. DRAMP02385 CRFCCRCCPRMRGCGLCCRF 20 Hepcidin AS-hepc6 (fish, chordates, animals) Q68M52 Not found Not found Acanthopagrus schlegelii (Black porgy) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database Pdp11 (IC50=2.20 µM), 51M6 (IC50=14.61 µM), Bacillus subtilis CECT 35 (IC50=11.41 µM), Escherichia coli DH5α (IC50=18.66 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18164062 Mol Immunol. 2008 Apr;45(8):2333-2342. Cuesta A, Meseguer J, Esteban MA. The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish giltherad seabream. DRAMP02387 PDPAKTAPKKKSKKAVT 17 Histone HIIb-3 (Antibacterial histone-like protein 3, HLP-3; catfishes, chordates, animals) P81904 Belongs to the histone H2B family Not found Ictalurus punctatus (Channel catfish) Antimicrobial, Antifungal Protein level Not found Not found Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Aeromonas hydrophila, Saprolegnia spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9645227 Cell Mol Life Sci. 1998 May;54(5):467-475. Robinette D, Wada S, Arroll T, Levy MG, Miller WL, Noga EJ. Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins. DRAMP02388 PDPAKTAPKKGSKKAVTKXA 20 Histone HIIb-1 (Antibacterial histone-like protein 1, HLP-1; catfishes, chordates, animals) P81903 Belongs to the histone H2B family Not found Ictalurus punctatus (Channel catfish) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Aeromonas hydrophila, vibrio alginolyticus, Escherichia coli D31, Saprolegnia spp. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9645227 Cell Mol Life Sci. 1998 May;54(5):467-475. Robinette D, Wada S, Arroll T, Levy MG, Miller WL, Noga EJ. Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins. DRAMP02389 FKVQNQHGQVVKIFHH 16 Astacidin 1 (crayfish, Arthropods, animals) No entry found Not found Not found Not found Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17049601 Dev Comp Immunol. 2007;31(5):441-455. Jiravanichpaisal P, Lee SY, Kim YA, Andrén T, Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern. DRAMP02392 GWFKKAWRKVKNAGRVLKGVGIHYGVGLIG 30 Hematopoietic antimicrobial peptide-29 (MgCath29; hagfishes, chordates, animals) Q71MD5 Not found CATH29 Myxine glutinosa (Atlantic hagfish) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019197 Peptides. 2003 Nov;24(11):1655-1667. Uzzell T, Stolzenberg ED, Shinnar AE, Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. DRAMP02245 GLFLDTLKGLAGKLLQGLKCIKAGCKP 27 Ranatuerin-2Cb (Ranatuerin 2Cb; Frogs, amphibians, animals) P82879 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=40 μg/ml);##Gram-negative bacterium: Escherichia coli (MIC=2 μg/ml).##Yeast: Candida albicans (MIC=46 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP02398 GPVGLLSSPGSLPPVGGAP 19 Antimicrobial peptide GP-19 (GP-19) B3A0L2 Not found Not found Xenorhabdus budapestensis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: GP-19 displays broad-spectrum antimicrobial activity against the tested bacteria and fungi. Gram-positive bacteria: Bacillus subtilis (IZ=19.04±0.2 mm), Bacillus megaterium (IZ=7.3±0.28 mm), Prototheca wickerhamii (IZ=10.3±0.33 mm);##Gram-negative bacteria: Xanthomonas campestris pv. vesicatoria (IZ=16.47±0.35 mm), Pseudomonas solanacearum (IZ=10.75±0.41 mm).##fungi: Phytophthora capsici (CD=16.62±1.07 mm), Verticillium dahlia (EC50=17.54 µg/ml), Fusarium graminearum (CD=12.04±0.87 mm), Fusarium omysporum (CD=21.64±0.4 mm).##NOTE: IZ = Inhibition Zone and CD = Colony diameter. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497806 Peptides. 2012 Jun;35(2):253-260. Xiao Y, Meng F, Qiu D, Yang X. Two novel antimicrobial peptides purified from the symbiotic bacteria Xenorhabdus budapestensis NMC-10. DRAMP02399 EGPVGLADPDGPASAPLGAP 20 Antimicrobial peptide EP-20 (EP-20) B3A0L3 Not found Not found Xenorhabdus budapestensis Antimicrobial, Antifungal Protein level Not found Not found Function: EP-20 showes high inhibition against P. capsici but lower antibacterial activity. Fungi: Phytophthora capsici (EC50=3.14 µg/ml), Verticillium dahlia (CD=19.32±1.31 mm), Fusarium graminearum (CD=12.45±1.6 mm), Fusarium oxysporum (CD=21.29±1.1 mm).##NOTE: CD = Colony diameter. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497806 Peptides. 2012 Jun;35(2):253-260. Xiao Y, Meng F, Qiu D, Yang X. Two novel antimicrobial peptides purified from the symbiotic bacteria Xenorhabdus budapestensis NMC-10. DRAMP02400 GCPQTPRCTNYAEKGQCPPN 20 Antimicrobial peptide AJN-10 (AJN-10) P0DJ30 Not found Not found Anguilla japonica (Japanese eel) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Displays antimicrobial activity against the Gram-negative bacterium A.hydrophila. Gram-negative bacterium: Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21796440 Protein J. 2011 Aug;30(6):413-421. Liang Y, Guan R, Huang W, Xu T. Isolation and identification of a novel inducible antibacterial peptide from the skin mucus of Japanese eel, Anguilla japonica. DRAMP18265 MAKEFGIPAAVAGTVLNVVEAGGWVTTIVSILTAVGSGGLSLLAAAGRESIKAYLKKEIKKKGKRAVIAW 70 Enterocin RM6 (Bacteriocin) No entry found Belongs to the class IIc bacteriocin Not found Enterococcus faecalis OSY-RM6 Antimicrobial, Antibacterial, Anti-Gram+ Not found Tandem mass spectrometry (MS/MS) analysis revealed that enterocin RM6 is a 70-residue cyclic peptide with a head-to-tail linkage between methionine and tryptophan residues. 1E68 Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23844357 Biomed Res Int. 2013;2013:206917. Huang E, Zhang L, Chung YK, Zheng Z, Yousef AE. Characterization and application of enterocin RM6, a bacteriocin from Enterococcus faecalis. DRAMP02404 CPAIQRCCQQLRNIQPPCRCCQ 22 Chitin-binding protein 3 (Mo-CBP3) P86528 Not found Not found Moringa oleifera (Horseradish tree) (Moringa pterygosperma) Antimicrobial, Antifungal Protein level Not found Not found "Function: Chitin binding protein. Has antifungal activity against F. solani. Not toxic to mice. Acts as a flocculent. PTM: Glycosylated; contains 2.5% carbohydrates. Miscellaneous: On the 2D-gel the determined pI of this protein is: 10.8, its MW is: 14.34 kDa." Fungi: Fusarium solani. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding PubMed ID is not available Thesis (2010), Federal University of Ceara, Brazil Gifoni J.M. Isolation and biochemical characterization of a new thermostable antifungal chitin-binding protein from Moringa oleifera seeds. DRAMP02405 QSERFEQQMQGQDFSHDERFLSQAA 25 Antifungal protein 1 (Pf-AFP1; Plants) P84884 Belongs to the 2S seed storage albumins family Not found Passiflora edulis (Passion fruit) Antimicrobial, Antifungal Protein level Not found Not found "Function: Function: Has strong antifungal activity against T. harzianum, F. oxysporum and A. fumigatus. Lacks antifungal activity against R. solani, P. brasiliensis and C. albicans. Tissue specificity: Expressed in seed (at protein level). Not detected in pulp, stems and leaves. Developmental stage: Expressed in dormant seed." Fungi: Trichoderma harzianum (IC50=32 µg/ml), Fusarium oxysporum (IC50=34 µg/ml), Aspergillus fumigatus (IC50=40 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16766236 Biochim Biophys Acta. 2006 Jun;1764(6):1141-6. Pelegrini PB, Noronha EF, Muniz MA, Vasconcelos IM, Chiarello MD, Oliveira JT, Franco OL. An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins. DRAMP02406 QEGCEWESRPCNRGCWLPRQWESVHMRFGVLVLWRAPQFEHFRECCNELRCEALRCMMRMRMEYWPRGLQDQQVYQRARDLEPRKHCGMSYPVECRMPR 99 Antimicrobial protein 2 (Si-AMP2; Plants) B3EWE9 Belongs to the 2S seed storage albumins family Not found Sesamum indicum (Oriental sesame) (Sesamum orientale) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has antibacterial activity against Gram-negative Klebsiella sp. but not against E. coli, Proteus sp., Salmonella sp. and Xanthomonas sp. or against Gram-positive bacteria S.pyogenes, S. aureus and Rathayibacter sp. Has no antifungal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21691771 Protein J. 2011 Jun;30(5):340-350. Maria-Neto S, Honorato RV, Costa FT, Almeida RG, Amaro DS, Oliveira JT, Vasconcelos IM, Franco OL. Bactericidal activity identified in 2S Albumin from sesame seeds and in silico studies of structure-function relations. DRAMP02407 PAQPFRIKKRQGPFERP 17 Napin-like polypeptide (Contains: Napin-like polypeptide small chain and large chain) P84782 Belongs to the 2S seed storage albumins family Not found Brassica oleracea var. alboglabra (Chinese kale) (Brassicaalboglabra) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Inhibits cell-free protein synthesis. Inhibits trypsin and chymotrypsin. Does not inhibit ribonuclease of protease activity. Has antibacterial activity except Gram-positive bacterium S. aureus or the Gram-negative bacteria E. coli, E. aerogenes, P. aeruginosa and P. vulgaris. Inhibits the proliferation of leukemia cells in vitro. Subunit structure: The mature protein consists of a small and a large chain linked by disulfide bonds (sequence shown is small chain). Biophysicochemical properties: This activity is preserved between pH 5 and pH 11, and between 10 and 40 degrees C. It falls to a low level at pH 3 and pH 13 and at 70 degrees C." Gram-negative bacterium: Pseudomonas fluorescens (IC50=89±6.1 µM);##Gram-positive bacteria: Bacillus subtilis (IC50=278±12.9 µM), B. cereus (IC50=145±83 µM), Bacillus megaterium (IC50=156±8.4 µM), Megabacterium phlei (IC50=104±27 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15485558 J Pept Res. 2004 Nov;64(5):202-208. A napin-like polypeptide with translation-inhibitory, trypsin-inhibitory, antiproliferative and antibacterial activities from kale seeds. A napin-like polypeptide with translation-inhibitory, trypsin-inhibitory, antiproliferative and antibacterial activities from kale seeds. DRAMP02408 PVSRQQCSQRIQGERFNQCRSQMQDGQLQSCCQELQNVEEQCQC 44 2S albumin (To-A1) P86783 Belongs to the 2S seed storage albumins family Not found Taraxacum officinale (Common dandelion) (Leontodon taraxacum) Antimicrobial, Antifungal Protein level Not found Not found "Function: This is a 2S seed storage protein. Has antifungal activity. Inhibits growth of H.sativum, V.albo-atrum and P. infestans. Subunit structure: The sequence shown is the mature protein which consists of a small and a large chain linked by 2 disulfide bonds." Fungi: Helminthosporium sativum (IC50=62.5 µg/ml), Pemphigus betae (IC50=62.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19594427 Protein Pept Lett. 2010 Apr;17(4):522-529. Odintsova TI, Rogozhin EA, Sklyar IV, Musolyamov AK, Kudryavtsev AM, Pukhalsky VA, Smirnov AN, Grishin EV, Egorov TA. Antifungal activity of storage 2S albumins from seeds of the invasive weed dandelion Taraxacum officinale Wigg. DRAMP02413 GYGCPFNQYQCHSHCRGIRGYKGGYCTGRFKQTCKCY 37 Ornithodoros defensin B (Ticks, Arthropods, animals) Q9BLJ4 Not found omdef-B Ornithodoros moubata (Soft tick) (Argasid tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11378409 Insect Biochem Mol Biol. 2001 Jun 22;31(8):747-751. Nakajima Y, van der Goes van Naters-Yasui A, Taylor D, Yamakawa M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). DRAMP02414 GYGCPFNQYQCHSHCSGIRGYKGGYCKGLFKQTCNCY 37 Ornithodoros defensin C (Ticks, Arthropods, animals) Q8MY08 Not found omdef-C Ornithodoros moubata (Soft tick) (Argasid tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11378409 Insect Biochem Mol Biol. 2001 Jun 22;31(8):747-751. Nakajima Y, van der Goes van Naters-Yasui A, Taylor D, Yamakawa M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). DRAMP02415 GFGCPFNQYECHAHCSGVPGYKGGYCKGLFKQTCNCY 37 Ornithodoros defensin D (Ticks, Arthropods, animals) Q8MY07 Not found omdef-D Ornithodoros moubata (Soft tick) (Argasid tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11378409 Insect Biochem Mol Biol. 2001 Jun 22;31(8):747-751. Nakajima Y, van der Goes van Naters-Yasui A, Taylor D, Yamakawa M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). DRAMP02416 GYGCPFNQYQCHSHCSGIRGYKGGYCKGTFKQTCKCY 37 Orinthodoros defensin A (Ticks, Arthropods, animals) Q9BLJ3 Not found omdef-A Ornithodoros moubata (Soft tick) (Argasid tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11378409 Insect Biochem Mol Biol. 2001 Jun 22;31(8):747-751. Nakajima Y, van der Goes van Naters-Yasui A, Taylor D, Yamakawa M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). DRAMP02417 MVRARRGCGCPLNQGACHRHCKSIGRRGGYCAGFLKQTCTCYRN 44 Defensin (Ticks, Arthropods, animals) B2D2C0 Belongs to the invertebrate defensin family Not found Ornithodoros coriaceus (Soft tick) (Argasid tick) Antimicrobial, Antibacterial Homology Not found Not found Function: Antibacterial peptide mostly active against Gram-positive bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18725333 J Proteomics. 2008 Dec 2;71(5):493-512. Francischetti IM, Meng Z, Mans BJ, Gudderra N, Hall M, Veenstra TD, Pham VM, Kotsyfakis M, Ribeiro JM. An insight into the salivary transcriptome and proteome of the soft tick and vector of epizootic bovine abortion, Ornithodoros coriaceus. DRAMP02418 GFGCPLNQGACHNHCRSIGRRGGYCAGIIKQTCTCYRK 38 Longicin (Ticks, Arthropods, animals) No entry found Not found Not found Haemaphysalis longicornis (Tick) Antimicrobial, Antibacterial, Antifungal, Antiparasitic Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17485458 Infect Immun. 2007 Jul;75(7):3633-3640. Tsuji N, Battsetseg B, Boldbaatar D, Miyoshi T, Xuan X, Oliver JH Jr, Fujisaki K. Babesial vector tick defensin against Babesia sp. parasites. DRAMP02420 FDNPFGCPADEGKCFDHCNNKAYDIGYCGGSYRATCVCYRK 41 Amblyomma defensin peptide 1 (ADP-1; Ticks, Arthropods, animals) No entry found Not found Not found Amblyomma hebraeum (Tick) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14705963 Biochem J. 2004 May 1;379(Pt 3):681-685. Lai R, Lomas LO, Jonczy J, Turner PC, Rees HH. Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, Amblyomma hebraeum. DRAMP02424 GFGCPFNQGACHRHCRSIRRRGGYCAGLIKQTCTCYRN 38 Defensin (Ticks, Arthropods, animals) Q86LE4 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Boophilus microplus (Cattle tick) Antimicrobial, Antibacterial Protein level Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14642886 Dev. Comp. Immunol. 2004;28:191-200. Fogaca A.C, Lorenzini D.M, Kaku L.M, Esteves E, Bulet P, Daffre S. Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile. DRAMP02426 GFGCPLNQGACHNHCRSIRRRGGYCSGIIKQTCTCY 36 Defensin (Varisin A1; Ticks, Arthropods, animals) Q86QI5 Belongs to the invertebrate defensin family (Type 2 subfamily) VSNA1 Dermacentor variabilis (American dog tick) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. PTM: Problely contains three disulfide bonds 4-25; 11-33; 15-35." Gram-positive bacteria: Bacillus subtilis, Borrelia burgdorferi. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11439245##14563361 Insect Biochem Mol Biol. 2001 Jul 26;31(9):857-865.##Insect Biochem Mol Biol. 2003 Nov;33(11):1099-1103. Johns R, Sonenshine D.E, Hynes W.L.##Ceraul SM, Sonenshine DE, Ratzlaff RE, Hynes WL. Identification of a defensin from the hemolymph of the American dog tick, Dermacentor variabilis.##An arthropod defensin expressed by the hemocytes of the American dog tick, Dermacentor variabilis (Acari: Ixodidae). DRAMP02431 HHVELCKKNDAELKEALTCITSKLPAALGCNDKSCVFEKLCKEGDLDEALKKHFTEAEVQTLHTTATDCDHSHGHEHSHGHEHGHGHH 88 Antimicrobial peptide microplusin (Ticks, Arthropods, animals) B7PCF6 Not found Not found Ixodes scapularis (Black-legged tick) (Deer tick) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Has bacteriostatic activity against Gram-positive bacteria, but not against Gram-negative bacteria. Has fungistatic activity against some but not all fungi. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M. luteus. PTM: Contains three disulfide bonds 6-41; 19-69; 30-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Caler E, Hannick L I, Bidwell S. et al. Annotation of Ixodes scapularis. DRAMP02435 LSKFGGECSLKHNTCTYLKGGKNHVVNCGSAANKKCKSDRHHCEYDEHHKRVDCQTPV 58 Antifungal protein (PgAFP; Cys-rich) D0EXD3, B6GXZ8 Not found afp Penicillium chrysogenum (Penicillium notatum) Antimicrobial, Antibacterial, Antifungal, Antiparasitic Protein level Not found Not found 7BAD##7BAE##7BAF##2NC2 "Function: Has strong antifungal activity against the molds Polytrichum commune Pc332, Penicillium echinulatum Pe321, and Aspergillus niger An261. PTM: Contains three disulfide bonds (By similarity)." Fungi: Polytrichum commune Pc332, Penicillium echinulatum Pe321, Aspergillus niger An261. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19914321##19683356 Peptides. 2010 Apr;31(4):541-547.##Int J Food Microbiol. 2009 Sep 30;135(1):39-46. Rodríguez-Martín A, Acosta R, Liddell S, Núñez F, Benito MJ, Asensio MA.##Acosta R, Rodríguez-Martín A, Martín A, Núñez F, Asensio MA. Characterization of the novel antifungal protein PgAFP and the encoding gene of Penicillium chrysogenum.##Selection of antifungal protein-producing molds from dry-cured meat products. DRAMP02436 EQPGGDKVNLGYFTN 15 Chitinase P84754 Belongs to the glycosyl hydrolase 18 family Chitinase (class Not found Streptomyces violaceus (Streptomyces venezuelae) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Enzyme regulation: Inhibited by divalent metal ions. Maximum inhibition observed with Ca2+ while the least inhibition was observed with Fe2+. Inhibited by high concentrations of GlcNAc. Biophysicochemical properties: pH dependence (Optimum pH is 6-8. There is a 37.7% decrease in activity at pH 5 and a 39.8% decrease in activity at pH 9); Temperature dependence (Optimum temperature is 35 degrees Celsius)." Fungi: Aspergillus niger, Alternaria alternata, Hordeum sativum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding PubMed ID is not available##16972135 Thesis (2005), Visva Bharati (Central University), India.##Curr Microbiol. 2006 Oct;53(4):265-269. Mukherjee G.##Mukherjee G, Sen SK. Extracellular production of chitinase by Streptomyces venezuelae.##Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P(10). DRAMP02437 GFWKKVGSAAWGGVKAAAKGAAVGGLNALAKHIQ 34 Papillosin P86416 Not found Not found Halocynthia papillosa (Red sea-squirt) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has strong antibacterial activity against the Gram-positive bacteria M. luteus, S. aureus, B. megaterium, A. viridans and E. faecalis, and against the Gram-negative bacteria K. pneumoniae, E. coli DH5alpha, S. typhimurium, P. aeruginosa and E. aerogenes. Lacks hemolytic activity against sheep erythrocytes. [Ref.19085906]Gram-positive bacteria (Native, Synthetic): Micrococcus luteus A270 (MBC=0.13-0.25, 0.19-0.39 µM), Aerococcus viridans 54.145 T (MBC=ND, 0.19-0.39 µM), Bacillus megaterium 66.20 T (MBC=ND, 0.05-0.10 µM), Staphylococcus aureus 65.8 T (MBC=0.5-1.00, 1.56-3.13 µM), Enterococcus faecalis 103015 T (MBC=ND, 0.78-1.56 µM);##Gram-negative bacteria (Native, Synthetic): Enterobacter aerogenes 30.86 T (MBC=ND, 0.78-1.56 µM), Pseudomonas aeruginosa 100720 T (MBC=ND, 3.13-6.25 µM), Salmonella thyphimurium 60.62 T (MBC=ND, 0.78-1.56 µM), Klebsiella pneumoniae 82.91 T (MBC=ND, 0.39-0.78 µM), Escherichia coli (MBC=0.25-0.50, 0.78-1.56 µM) [Ref.19085906]0% hemolytic activity at 50 μM against sheep erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19085906 J Pept Sci. 2009 Jan;15(1):48-55. Galinier R, Roger E, Sautiere PE, Aumelas A, Banaigs B, Mitta G. Halocyntin and papillosin, two new antimicrobial peptides isolated from hemocytes of the solitary tunicate, Halocynthia papillosa. DRAMP02438 FWGHIWNAVKRVGANALHGAVTGALS 26 Halocyntin P86415 Not found Not found Halocynthia papillosa (Red sea-squirt) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has strong antibacterial activity against the Gram-positive bacteria M. luteus, S. aureus, B. megaterium, A. viridans and E. faecalis, and against the Gram-negative bacterium K. pneumoniae. Has less potent antibacterial activity against the Gram-negative bacteria E. coli DH5alpha, S. typhimurium, P. aeruginosa, E. aerogenes and N. gonorrhoeae. Has moderate hemolytic activity against sheep erythrocytes. [Ref.19085906]Gram-positive bacteria (Native, Synthetic): Micrococcus luteus A270 (MBC=0.39-0.78, 0.39-0.78 µM), Aerococcus viridans 54.145 T (MBC=3.13-6.25, 0.78-1.56 µM), Bacillus megaterium 66.20 T (MBC=0.75-1.56, 0.39-0.78 µM), Staphylococcus aureus 65.8 T (MBC=6.25-12.50, 1.56-3.13 µM), Enterococcus faecalis 103015 T (MBC=6.25-12.50, 1.56-3.13 µM);##Gram-negative bacteria (Native, Synthetic): Enterobacter aerogenes 30.86 T (MBC=25-50, 6.25-12.50 µM), Pseudomonas aeruginosa 100720 T (MBC>100, 25-50 µM), Salmonella thyphimurium 60.62 T (MBC=50-100, 12.50-25 µM), Klebsiella pneumoniae 82.91 T (MBC=12.50-25, 1.56-3.13 µM), Neisseria gonorrhoeae 103711 (MBC=25-50, ND µM), Escherichia coli (MBC=6.25-12.50, 6.25-12.50 µM). [Ref.19085906]8% hemolytic activity at 6.25 μM, 13% hemolytic activity at 12.5 μM, 14% hemolytic activity at 25 μM, 22% hemolytic activity at 50 μM against sheep erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19085906 J Pept Sci. 2009 Jan;15(1):48-55. Galinier R, Roger E, Sautiere PE, Aumelas A, Banaigs B, Mitta G. Halocyntin and papillosin, two new antimicrobial peptides isolated from hemocytes of the solitary tunicate, Halocynthia papillosa. DRAMP02440 MKRNQKEWESVSKKGLMKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI 55 Sporulation-killing factor SkfA O31422 Not found Not found Bacillus subtilis (strain 168) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Induces the lysis of other B. subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation. Can also inhibit growth of other bacteria at high concentrations. Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor. Induction: By Spo0A and PhoP, during nutrient starvation, especially phosphate starvation. Repressed by AbrB during normal growth when nutrients are plentiful, in association with the transcriptional repressor Abh." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12817086##15812018##16816204 Science. 2003 Jul 25;301(5632):510-513.##Appl Environ Microbiol. 2005 Apr;71(4):1899-1908.##J Bacteriol. 2006 Jul;188(14):5299-5303. González-Pastor JE, Hobbs EC, Losick R.##Westers H, Braun PG, Westers L, Antelmann H, Hecker M, Jongbloed JD, Yoshikawa H, Tanaka T, van Dijl JM, Quax WJ.##Allenby NE, Watts CA, Homuth G, Prágai Z, Wipat A, Ward AC, Harwood CR. Cannibalism by sporulating bacteria.##Genes involved in SkfA killing factor production protect a Bacillus subtilis lipase against proteolysis.##Phosphate starvation induces the sporulation killing factor of Bacillus subtilis. DRAMP02442 WKSESVCTPGCVTGVLQTCFLQTITCNCHISK 32 Ericin S (lantibiotic-like peptide) No entry found Not found Not found Bacillus subtilis A1/3 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Rich Not found Comment: No comments found on DRAMP database B. amyloliquefaciens ATCC 15841, B. brevis ATCC 7577, B. cereus ATCC 14579, B. firmus ATCC 14575, B. polymyxa ATCC 842, B. sphaericus ATCC 14577, Bacillus subtilis natto DSM 1088, Bacillus subtilis DSM 3256, Bacillus subtilis DSM 3258, L. lactis IL-1403. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11872722 J. Bacteriol. 2002; 184:1703-1711. Stein T, Borchert S, Conrad B, Feesche J, Hofemeister B, Hofemeister J, Entian KD. Two different lantibiotic-like peptides originate from the ericin gene cluster of Bacillus subtilis A1/3. DRAMP02443 VLSKSLCTPGCITGPLQTCYLCFPTFAKC 29 Ericin A (lantibiotic-like peptide) No entry found Not found Not found Bacillus subtilis A1/3 (Gram-positive bacteria) Antimicrobial, Antibacterial Not found Rich Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11872722 J. Bacteriol. 2002; 184:1703-1711. Stein T, Borchert S, Conrad B, Feesche J, Hofemeister B, Hofemeister J, Entian KD. Two different lantibiotic-like peptides originate from the ericin gene cluster of Bacillus subtilis A1/3. DRAMP18264 VTTSIPCTVMVSAAVCPTLVCSNKCGGRG 29 Enterocin W beta(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Enterococcus faecalis NKR-4-1 Antimicrobial, Antibacterial, Anti-Gram+ Not found Enterocin Wbeta was proven to have 3 dehydrated amino acids as well as 2 and 2 Lan and MeLan residues, respectively. The amino acid sequences of the prepeptides of enterocin W showed the highest identity with those of plantaricins Walpha and Wbeta (63.3 and 44.7%, respectively). Comment: No comments found on DRAMP database Gram-positive (Narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 22138996 Appl Environ Microbiol. 2012 Feb;78(3):900-3. Sawa N, Wilaipun P, Kinoshita S, Zendo T, Leelawatcharamas V, Nakayama J, Sonomoto K. Isolation and characterization of enterocin W, a novel two-peptide lantibiotic produced by Enterococcus faecalis NKR-4-1. DRAMP02447 FCKSLPLPLSVK 12 Antimicrobial protein 2 (Antimicrobial protein AN5-2) B3EWQ7 Not found Not found Paenibacillus alvei (Bacillus alvei) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity Gram-positive bacteria as well as against Gram-negative bacteria. Gram-positive bacteria: Lactobacillus plantarum strain ATCC 8014 and Bacillus cereus strain ATCC 14579;##Gram-negative bacteria: Escherichia coli strain ATCC 25922 and Salmonella enteritidis strain ATCC 13076. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2012) to UniProtKB Alkotaini B, Anuar N, Kadhum AAH. Unknown DRAMP02448 ASGGTVGXYGAWMRSXSLVSXSTITTFS 28 Antibacterial protein LC3 (Antibacterial protein LCIII) Q9R5C6 Not found Not found Bacillus subtilis Antimicrobial, Antibacterial, Antifungal, Antiparasitic Protein level Not found Not found "Function: Has antibacterial activity. Miscellaneous: On a 2D-GEL the determined pI of this protein is: 9.12." X. campestris strain G and P. solacearum PO1. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1295599 Chin J Biotechnol. 1992;8(3):187-193. Liu J, Li Z, Pan N, Chen Z. Purification and partial characterization of an antibacterial protein LCIII. DRAMP02450 KIFTKCELARKLRAEGMDGF 20 Lysozyme C (1,4-beta-N-acetylmuramidase C) P37155 Belongs to the glycosyl hydrolase 22 family LYZ Felis catus (Cat) (Felis silvestris catus) Antimicrobial Protein level Not found Not found "Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents By similarity. Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Miscellaneous: Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides By similarity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2344734 Comp Biochem Physiol B. 1990;95(4):773-779. Halliday JA, Bell K, McKenzie HA, Shaw DC. Feline whey proteins: identification, isolation and initial characterization of alpha-lactalbumin, beta-lactoglobulin and lysozyme. DRAMP02451 SKMKKCEFAKIAKEQHMDGYHGVSLADWVCLVNNESDFNTKAINRNKGI 49 Lysozyme C (1,4-beta-N-acetylmuramidase C) P21776 Belongs to the glycosyl hydrolase 22 family LYZ Pseudocheirus peregrinus (Common ring-tailed possum) Antimicrobial Protein level Not found Not found "Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents By similarity. Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Miscellaneous: Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides By similarity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2605916 Comp Biochem Physiol B. 1989;94(4):775-778. Nicholas K, Loughnan M, Messer M, Munks S, Griffiths M, Shaw D. Isolation, partial sequence and asynchronous appearance during lactation of lysozyme and alpha-lactalbumin in the milk of a marsupial, the common ringtail possum (Pseudocheirus peregrinus). DRAMP02452 KYFATRCDLVRELRKXGF 18 Lysozyme P82175 Belongs to the glycosyl hydrolase 22 family Not found Estigmene acrea (Salt marsh moth) Antimicrobial Protein level Not found Not found Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte- macrophage system and enhance the activity of immunoagents (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9303271 Dev Comp Immunol. 1997 Jul-Aug;21(4):323-336. Wittwer D, Weise C, Götz P, Wiesner A. LPS (lipopolysaccharide)-activated immune responses in a hemocyte cell line from Estigmene acraea (Lepidoptera). DRAMP02453 GKIPVKAIKKAGAAIGKGLRAINIASTAHDVYSFFKPKHKKK 42 S. litura moricin (Sl moricin; Insects, animals) Q7YZB4 Not found Not found Spodoptera litura (Lepidopteran insect) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (1 helices; 31 residues) The solution structure of Sl moricin is determined by two-dimensional (2D) 1H-nuclear magnetic resonance (NMR) spectroscopy and hybrid distance geometry-simulated annealing calculation. The tertiary structure reveales a long alpha-helix containing eight turns along nearly the full length of the peptide like that of moricin, confirming that Sl moricin is a new moricin-like antibacterial peptide. 1X22 resolved by NMR. Function: Sl moricin showes a broad antibacterial spectrum against Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Pseudomonas aeruginosa (LD50=67.4 µg/ml), Escherichia coli JM109 (LD50=5.2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (LD50=2.7 µg/ml), Methicillin-resistant S. aureus (LD50=9.8 µg/ml), Micrococcus luteus (LD50=28.4 µg/ml), Bacillus thuringiensis HD-1 (LD50=0.5 µg/ml), Enterococcus faecium IFO3128 (LD50=6.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16115804 Biochim Biophys Acta. 2005 Aug 31;1752(1):83-92. Oizumi Y, Hemmi H, Minami M, Asaoka A, Yamakawa M. Isolation, gene expression and solution structure of a novel moricin analogue, antibacterial peptide from a lepidopteran insect, Spodoptera litura. DRAMP02454 GCFEDWSRCSPSTASATGVLWRSCDSYCKVCFKADRGECYDSPSLNCPHRLPNNKQCRCINARTAKDNRNPTCWA 75 Theromacin (Arthropods, animals) A8I0L8, A8IK85 Not found Not found Hirudo medicinalis (Medicinal leech) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Structural features of Theromacin: the characteristic additional N-terminal helix and two long flexible loops separating the two helices. 2LN8 resolved by NMR. "Function: It showes antimicrobial activity against Gram-positive bacteria and Gram-negative bacteria in the low microgram concentration range. PTM: Problely contains five disulfide bonds 2-9; 24-28; 31-73; 39-47; 57-59." Gram-negative bacterium: Escherichia coli ATCC 35218 (LD90=6.25 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 12600 (LD90=25 µg/ml), Bacillus megaterium ATCC 14581 (MBC=0.2-0.39 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22396551##PubMed ID is not available J Biol Chem. 2012 Apr 20;287(17):14246-58.##Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Jung S, Sönnichsen FD, Hung CW, Tholey A, Boidin-Wichlacz C, Haeusgen W, Gelhaus C, Desel C, Podschun R, Waetzig V, Tasiemski A, Leippe M, Grötzinger J.##Schikorski D, Salzet M, Tasiemski A. Macin family of antimicrobial proteins combines antimicrobial and nerve repair activities.##Antimicrobial peptides isolated from the medicinal leech. DRAMP02455 ADSRNPLEEEFRETNYEEF 19 L-amino-acid oxidase (ACL-LAO; LAAO; LAO) P0CC16 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Agkistrodon contortrix laticinctus (Broad-banded copperhead)(Agkistrodon mokasen laticinctus) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Ile followed by L-Phe, L-Met, L-Val, L-Arg, L-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage (minimum hemorrhagic dose of 10 µg), and apoptosis. May also induce hemolysis, edema, antibacterial and antiparasitic activities. May also regulate platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10441379 Arch Biochem Biophys. 1999 Aug 15;368(2):285-290. Souza DH, Eugenio LM, Fletcher JE, Jiang MS, Garratt RC, Oliva G, Selistre-de-Araujo HS. Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data. DRAMP02457 ADVRNPLEEFRETDYEVL 18 L-amino-acid oxidase (Balt-LAAO-I; LAAO; LAO; snakes, reptils, animals) P0DI86 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops alternatus (Urutu) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as slight hemorrhage, Induction: of platelet aggregation, edema in the mouse paw and bactericidal activity against both Gram-positive (S.aureus) and Gram-negative (E.coli) bacteria. May also induce hemolysis, apoptosis of vascular endothelial cells or tumor cell lines, and may have antiparasitic activities. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Tissue specificity: Expressed by the venom gland." Gram-positive bacterium: S. aureus;##Gram-negative bacterium: E. coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15142548 Bioorg Med Chem. 2004 Jun 1;12(11):2881-2886. Stábeli RG, Marcussi S, Carlos GB, Pietro RC, Selistre-de-Araújo HS, Giglio JR, Oliveira EB, Soares AM. Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom. DRAMP02458 ADDKNPLEECFREDDYEGFLEIAKNGLSTTSNPKRVVIVGAGMSGLAAY 49 L-amino-acid oxidase (BiLAO; LAAO; LAO; snakes, reptils, animals) P0DI87 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops insularis (Golden lancehead) (Queimada jararaca) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). In addition, this protein induces apoptosis and necrosis and has inhibitory effects on rat kidney Function: (decrease of blood flow and glomerular filtration). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17983639 Toxicon. 2008 Feb;51(2):199-207. Braga MD, Martins AM, Amora DN, de Menezes DB, Toyama MH, Toyama DO, Marangoni S, Alves CD, Barbosa PS, de Sousa Alves R, Fonteles MC, Monteiro HS. Purification and biological effects of L-amino acid oxidase isolated from Bothrops insularis venom. DRAMP02459 ADDKNPLEECFRETDYEEFLEIARNGLKATSNPKRVV 37 L-amino-acid oxidase (BjarLAAO-I; LAAO; LAO; snakes, reptils, animals) P0DI88 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops jararaca (Jararaca) Antimicrobial, Antibacterial, Anti-Gram+, Antiparasitic, Antitumor Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Met, L-Leu, L-Phe, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, edema, apoptosis of vascular endothelial cells or tumor cell lines, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. This protein induce hemolysis and has antibacterial and antiparasitic activities (against the Gram-positive S.aureus). Tested in vivo, this protein significantly inhibits Ehrlich ascite tumors growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of hydrogen peroxide from peritoneal macrophages. Tissue specificity: Expressed by the venom gland. Miscellaneous: Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production." Gram-positive bacterium: S. aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18346051##19101583##20615423 Basic Clin Pharmacol Toxicol. 2008 Jun;102(6):533-542.##Toxicon. 2009 Mar 1;53(3):330-341.##Toxicon. 2010 Nov;56(6):944-955. de Vieira Santos MM, Sant'Ana CD, Giglio JR, da Silva RJ, Sampaio SV, Soares AM, Fecchio D.##Ciscotto P, Machado de Avila RA, Coelho EA, Oliveira J, Diniz CG, Farías LM, de Carvalho MA, Maria WS, Sanchez EF, Borges A, Chávez-Olórtegui C.##olindo P, Teixeira-Ferreira AS, DaMatta RA, Alves EW. Antitumoural effect of an L-amino acid oxidase isolated from Bothrops jararaca snake venom.##Antigenic, microbicidal and antiparasitic properties of an L-amino acid oxidase isolated from Bothrops jararaca snake venom.##L-amino acid oxidase activity present in fractions of Bothrops jararaca venom is responsible for the Induction: of programmed cell death in Trypanosoma cruzi. DRAMP02460 ADDRNPLEECFRETDYEEFLEIAKNGLSTT 30 L-amino-acid oxidase (LAAO; LAO; snakes, reptils, animals) P0DI89 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops leucurus (White-tailed jararaca) (White-tailed lancehead) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (high activity against L-Met, L-Leu, L-Nle, L-Trp, L-Phe and moderate activity against L-Tyr), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities (By similarity). In addition, this protein induces apoptosis. It also interacts with endothelial cells, and inhibits collagen- and ADP-induced platelet aggregation. L-LAAO family effects on platelets are controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions. Tissue specificity: Expressed by the venom gland. Miscellaneous: Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production. Biophysicochemical properties: pH dependence (Optimum pH is 7.5-8.8 for L-Leu)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21539897 Biochim Biophys Acta. 2011 Jul;1810(7):683-694. Naumann GB, Silva LF, Silva L, Faria G, Richardson M, Evangelista K, Kohlhoff M, Gontijo CM, Navdaev A, de Rezende FF, Eble JA, Sanchez EF. Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom. DRAMP02461 AHDGNPLEECFREDDEEFFLEIAKNGLTATSNPKRVVIV 39 L-amino-acid oxidase (BmarLAAO; LAAO; LAO; snakes, reptils, animals) P0CJ40 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops marajoensis (Marajo lancehead) Antimicrobial, Antibacterial, Antifungal, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram-negative bacteria and yeast, probably by the generation of hydrogen peroxide. Tissue specificity: Expressed by the venom gland. Miscellaneous: Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19944711 Toxicon. 2010 Apr 1;55(4):795-804. Costa Torres AF, Dantas RT, Toyama MH, Diz Filho E, Zara FJ, Rodrigues de Queiroz MG, Pinto Nogueira NA, Rosa de Oliveira M, de Oliveira Toyama D, Monteiro HS, Martins AM. Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidase. DRAMP02462 DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK 95 L-amino-acid oxidase (LAAO; LAO; snakes, reptils, animals) P0DI91 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Naja oxiana (Central Asian cobra) (Oxus cobra) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial activity against both Gram-positive (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of ADP- or collagen-induced platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic activities. Tissue specificity: Expressed by the venom gland. Biophysicochemical properties: Kinetic parameters (KM=0.885 mM for L-Met; KM=0.051 mM for L-Phe; KM=0.147 mM for L-Trp; KM=0.75 mM for L-Leu)" Gram-positive bacterium: Bacillus subtilis;##Gram-negative bacterium: E. coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18294891 Comp Biochem Physiol B Biochem Mol Biol. 2008 Apr;149(4):572-580. Samel M, Tõnismägi K, Rönnholm G, Vija H, Siigur J, Kalkkinen N, Siigur E. L-Amino acid oxidase from Naja naja oxiana venom. DRAMP02463 ADDKNPLEEAFREADYEVFLEIAKNGL 27 L-amino-acid oxidase (LAAO, LAO, LN-AAO; Reptiles, animals) P0C2D3 Not found Not found Eristocophis macmahoni (Leaf-nosed viper) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemolysis, edema, apoptosis, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also have antibacterial and antiparasitic activities. Catalytic activity: An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Subunit structure: Homodimer; non-covalently linked. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet FAD and Flavoprotein 11368308 Arch Biochem Biophys. 2000 Dec 15;384(2):216-226. Ali SA, Stoeva S, Abbasi A, Alam JM, Kayed R, Faigle M, Neumeister B, Voelter W. Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom. DRAMP02464 GPMRIPEKHRIVREYIRKFGLQLNEFVQETENAWYYIKNIRKKVHEVKKDPGLLKYPVKP 60 L-amino-acid oxidase (LAAO, LAO; reptilia, animals) Q6T627 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bitis gabonica (Gaboon adder) (Gaboon viper) Antimicrobial, Antibacterial, Antiparasitic Transcript level Not found Not found Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15276202 Gene. 2004 Aug 4;337:55-69. Francischetti IM, My-Pham V, Harrison J, Garfield MK, Ribeiro JM. Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins. DRAMP02465 ADDINPKEECFFEDDYYEFE 20 L-amino-acid oxidase L1 (LAAO; LAAO-L1; LAO; Reptiles, animals) P86535 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Daboia russelii (Russel's viper) (Vipera russelii) Antimicrobial, Antibacterial, Antitumor, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. Tissue specificity: Expressed by the venom gland. Biophysicochemical properties: Kinetic parameters (KM=0.297 mM for L-Met; KM=1.44 mM for L-Ile; KM=0.750 mM for L-Leu; KM=0.066 mM for L-Phe; KM=0.210 mM for L-Trp; KM=0.052 mM for L-Tyr; Vmax=8.96 µmol/min/mg enzyme toward L-Phe)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18384385##20203422 FEBS J. 2008 May;275(9):2078-2095.##Biomed Res. 2010 Feb;31(1):71-81. Mandal S, Bhattacharyya D.##Suzuki M, Itoh T, Anuruddhe BM, Bandaranayake IK, Shirani Ranasinghe JG, Athauda SB, Moriyama A. Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs.##Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka. DRAMP02466 ADDKNPLEECFCEDDDYCEG 20 L-amino-acid oxidase L2 (LAAO; LAAO-L2; LAO; Reptiles, animals) P0DI90 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Daboia russelii (Russel's viper) (Vipera russelii) Antimicrobial, Antibacterial, Antitumor, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. Tissue specificity: Expressed by the venom gland. Biophysicochemical properties: Kinetic parameters (KM=1.89 mM for L-Ile; KM=599.7 µM for L-Leu; KM=222.8 µM for L-Met; KM=49.3 µM for L-Phe; KM=235.1 µM for L-Trp; KM=538.2 µM for L-Tyr; Vmax=6.94 µmol/min/mg enzyme toward L-Phe)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18384385 FEBS J. 2008 May;275(9):2078-2095. Mandal S, Bhattacharyya D. Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs. DRAMP02467 ADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVYPVKPSEQLYEESLRDQLPTSMHRYPSMIQKIFFAGEYTANAHGWIDSTIK 88 L-amino-acid oxidase (LAAO; LAO; Reptiles, animals) P0C2D7 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Vipera berus berus (Common viper) Antimicrobial, Antibacterial, Antitumor, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (the most specific substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg and L-His), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities By similarity. In addition, this protein has an ability to induce apoptosis in cultured HeLa and K562 cells, and inhibits ADP-induced platelet aggregation dose-dependently. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Tissue specificity: Expressed by the venom gland. Biophysicochemical properties: Kinetic parameters (KM=0.361 mM for L-Leu; KM=0.286 mM for L-Met; KM=0.058 mM for L-Phe)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16574513 Biochim Biophys Acta. 2006 Apr;1764(4):707-714. Samel M, Vija H, Rönnholm G, Siigur J, Kalkkinen N, Siigur E. Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom. DRAMP02468 DLLQFXDMMK 10 Acidic phospholipase A2 PnPLA2 (svPLA2; Reptiles, animals) B3EWG8 Belongs to the phospholipase A2 family (Group II subfamily) Not found Porthidium nasuta (Hognosed viper) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Snake venom phospholipase A2 (PLA2) that has antibacterial activity against S.aureus ATCC 25923 and ATCC 29213, acts by inducing bacterial membrane breakage. Displays a potent inhibitory effect on collagen-induced human platelet aggregation and has indirect hemolytic activity. Does not show cytotoxicity to murine skeletal muscle myoblasts. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Tissue specificity: Expressed by the venom gland. Miscellaneous: The determined pI of this protein is: 4.6." [Ref.22251437]Gram-positive bacteria: S. aureus ATCC 25923 and S. aureus ATCC 29213. [Ref.22251437]MHD=7.5 μg against agarose erythrocyte-egg yolk gels Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22251437 Comp Biochem Physiol B Biochem Mol Biol. 2012 Apr;161(4):341-347. Vargas LJ, Londoño M, Quintana JC, Rua C, Segura C, Lomonte B, Núñez V. An acidic phospholipase A(2) with antibacterial activity from Porthidium nasutum snake venom. DRAMP02469 VNVLGGIEYSINNATLCSVGFSVRVFNYAEGAVRGLTQGNACMGRGDSGGSWFTLFERQYGL 62 Alpha-lytic protease L1 P85142 Belongs to the peptidase S1 family Not found Lysobacter sp. (strain XL1) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has bacteriolytic activity. Biophysicochemical properties: pH dependence (Optimum pH is 8.0. Active from pH 7.0 to 11.0); Temperature dependence (Optimum temperature is 70 degrees Celsius)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2007) to UniProtKB Muranova T.A, Stepnaya O.A, Tsfasman I.M, Kulaev I.S. Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1. DRAMP02471 IASASCTTCICTCSCSS 17 Thiostrepton (Alaninamide; Bryamycin; Gargon; Thiactin) P0C8P8, C4NCM0 Belongs to the thiocillin family tpdA Streptomyces azureus Antimicrobial, Antibacterial Protein level No secondary structure Not found 1E9W, 3CF5 resolved by X-ray.##1OLN, 2JQ7 resolved by NMR. "Function: Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity). PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings. Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser. Pharmaceutical use: Available under the names Animax (Dechra) and Panolog (Fort Dodge), that combine thiostrepton with nystatin (antifungal), neomycin (antibiotic) and triamcinolone (corticosteroid). Used to treat cat and dog skin and ear disorders caused by" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13355325##11320328 Antibiot Annu. 1955-1956;3:554-559.##Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):755-758. DONOVICK R, PAGANO JF, STOUT HA, WEINSTEIN MJ.##Bond CS, Shaw MP, Alphey MS, Hunter WN. Thiostrepton, a new antibiotic. I. In vitro studies.##Structure of the macrocycle thiostrepton solved using the anomalous dispersion contribution of sulfur. DRAMP02472 LCPLDVLQLSSELLDIDGNEVEASRILSDITAFGGIRCPLTVVQSRGIGTIISSPYRFIAEGHPLSLKDMDGWFRVSDDEFNNYK 85 Turmerin (Plants) P85278 Not found Not found Curcuma longa (Turmeric) (Curcuma domestica) Anti-cancer, Antiplasmodial Protein level Not found Not found "Function: Has anticarcinogenic activity, prevents transformation of DMBA-treated JB6 cells. Has antipromoter activity, prevents promotion by tetradecanoyl phorbal acetate (TPA) in JB6 cells. Prevents tertiary butyl hydroperoxide-induced mutagenesis. Protects AT base pairs and shows antimutagenesis activity in TA102 and TA104 S.typhimurium mutagenesis tests. Inhibits paw edema formation induced by phospholipase A2 in Swiss Wistar mice. Prevents the release of arachidonate, the parent compound for the synthesis of prostaglandins and prostacyclins. Has antimalarial activity, kills P. falciparum. Has antivenom activity, nullifies the lethal effects of N.naja venom and inhibits phospholipase A2 present in N.naja venom. Has antifungal activity, inhibits cilia formation by A.niger. Is not toxic or allergenic. Sequence similarities: Belongs to the protease inhibitor I3 (leguminous Kunitz-type inhibitor) family. [View classification] Biophysicochemical properties: Temperature dependence (Stable for 7 days at room temperature and for 30 days at 4 degrees Celsius. Remains active after incubation at 100 degrees Celsius for 3 hours). Caution: The order of the first peptide shown is Not found." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1731625##18177267 Arch Biochem Biophys. 1992 Feb 1;292(2):617-623.##Biol Chem. 2008 Mar;389(3):299-303. Srinivas L, Shalini VK, Shylaja M.##Chethankumar M, Srinivas L. Turmerin: a water soluble antioxidant peptide from turmeric [Curcuma longa].##New biological activity against phospholipase A2 by Turmerin, a protein from Curcuma longa L. DRAMP02475 NEKSGSCPDMSMPIPPLGICKTLCNSDSGCPNVQKCCKNGCGFMTCTTPVP 51 Nawaprin (Snakes, reptiles, animals) P60589, P83769 Belongs to the snake waprin family Not found Naja nigricollis (Black-necked spitting cobra) Antimicrobial, Antibacterial Protein level Not found Not found 1UDK Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12878611 J Biol Chem. 2003 Oct 10;278(41):40097-104. Torres AM, Wong HY, Desai M, Moochhala S, Kuchel PW, Kini RM. Identification of a novel family of proteins in snake venoms. Purification and structural characterization of nawaprin from Naja nigricollis snake venom. DRAMP02476 KTTKQLRLPKVKPGECPKVKIPPDYPCNQYCVWDFDCEGNKKCCPVGCAKECFPPGPL 58 Waprin-Phi3 (Snakes, reptiles, animals) A7X4M7 Belongs to the snake waprin family Not found Philodryas olfersii (Green snake) Antimicrobial Transcript level Not found Not found "PTM: four disulfide bonds: 6-44; 27-48; 31-43; 37-52. Damages membranes of susceptible bacteria. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02477 EQEKPGSCPNVDMPIPPLGLCKTTCSKDSDCSETKKCCKNGCGFMTCTTARP 52 Waprin-Phi2 (Snakes, reptiles, animals) A7X4K7 Belongs to the snake waprin family Not found Philodryas olfersii (Green snake) Antimicrobial Transcript level Not found Not found "PTM: four disulfide bonds 8-38; 21-42; 25-37; 31-47. Damages membranes of susceptible bacteria. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02479 QDRPKKPGLCPPRPQKPPCVKECKNDWSCPGQQKCCSYGCIDECRDPIFVN 51 Scuwaprin-a (Snakes, reptiles, animals) B5G6G8 Belongs to the snake waprin family Not found Oxyuranus scutellatus scutellatus (Australian taipan) (Coastaltaipan) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02480 KDRPKKPGLCPPRPQKPCVKECKNDWSCPGQQKCCNYGCIDECRDPIFVN 50 Omwaprin-b (Oxywaprin-b; Snakes, reptiles, animals) B5G6G7 Belongs to the snake waprin family Not found Oxyuranus microlepidotus (Inland taipan) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02481 QDRPKKPGLCPPRPQKPCVKECKNDWSCPGQQKCCNYGCIDECRDPIFVN 50 Omwaprin-c (Oxywaprin-c; Snakes, reptiles, animals) B5L5M9 Belongs to the snake waprin family Not found Oxyuranus microlepidotus (Inland taipan) Antimicrobial, Antibacterial, Antimalarial Homology Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02482 KDRPKKPGLCPPRPQKPCVKECKNDDSCPGQQKCCNYGCKDECRDPIFVG 50 Omwaprin-a (Oxywaprin; Oxywaprin-a; Snakes, reptiles, animals) P83952 Belongs to the snake waprin family Not found Oxyuranus microlepidotus (Inland taipan) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Omwaprin is closest in structure to the 50 amino acid residue C-terminal WAP domain of the human protein secretory leukocyte protease inhibitor (SLPI) (PDB ID: 2Z7F). This domain of SLPI has eight Cys residues that align well with the Cys residues of omwaprin, suggesting a similar fold. 3NGG resolved by NMR. "Function: Damages membranes of susceptible bacteria. Has antibacterial activity against the Gram-positive bacteria. Has no antibacterial activity against the Gram-positive bacteria. Tissue specificity: Expressed by the venom gland. Domain: Contains 1 WAP domain. PTM: Contains four disulfide bonds 10-35; 18-39; 22-34; 28-43." Gram-positive bacteria: Bacillus megaterium, Bacillus anthracis, Staphylococcus warneri. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17044815##20669184 Biochem J. 2007 Feb 15;402(1):93-104.##Protein Sci. 2010 Oct;19(10):1840-1849. Nair DG, Fry BG, Alewood P, Kumar PP, Kini RM.##Banigan JR, Mandal K, Sawaya MR, Thammavongsa V, Hendrickx AP, Schneewind O, Yeates TO, Kent SB. Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins.##Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography. DRAMP02483 KFFKKLKNSVKKRAKKFFKKPKVIGVTFPF 30 Cathelicidin-NA (Cathelicidin-related protein; Snakes, reptiles, animals) B6S2X0 Not found Not found Naja atra (Chinese cobra) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Alpha helix Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli ATCC 25922, Escherichia coli ML-35P, Escherichia coli clinic strain, Pseudomonas aeruginosa ATCC 27853, Pseudomonas aeruginosa PA 01, Pseudomonas aeruginosa clinic strain, Enterobacter aerogenes clinic strain, Enterobacter cloacae clinic strain. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18620012 Peptides. 2008 Oct;29(10):1685-91. Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y. Identification and characterization of novel reptile cathelicidins from elapid snakes. DRAMP02484 ENEKAGSCPDVNQPIPPLGLCRNMCESDSGCPNNEKCCKNGCGFMTCSRPR 51 Waprin-Thr1 (Snakes, reptiles, animals) A7X4I7 Belongs to the snake waprin family Not found Thrasops jacksonii (Jackson's black tree snake) Antimicrobial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). PTM: Contains four disulfide bonds 8-38; 21-42; 25-37; 31-47 (By similarity). Tissue specificity: Expressed by the venom gland. Domain: Contains 1 WAP domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02485 QDGKAGSCPDVNQPIPPLGVCKTTCATDSNCPDIQKCCKNGCGHMSCTRPST 52 Waprin-Rha1 (Snakes, reptiles, animals) A7X4J4 Belongs to the snake waprin family Not found Rhabdophis tigrinus tigrinus (Tiger keelback snake) Antimicrobial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). PTM: Contains four disulfide bonds 8-38; 21-42; 25-37; 31-47 (By similarity). Tissue specificity: Expressed by the venom gland. Domain: Contains 1 WAP domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02486 QVVRPGSCPNVDVPIPPLGLCRTTCQTDANCQEGRKCCKNGCGFMTCETARF 52 Waprin-Lio1 (Snakes, reptiles, animals) A7X4L4 Belongs to the snake waprin family Not found Liophis poecilogyrus (Water snake) Antimicrobial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). PTM: Contains four disulfide bonds 8-38; 21-42; 25-37; 31-47 (By similarity). Tissue specificity: Expressed by the venom gland. Domain: Contains 1 WAP domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02487 KILFGCGISPGNPFPCSLPGLTGNRCRRDYDCPQTLRCCNFRCSRSCRIPPVLPWSCPRNPFKCTIPGIDRCRYDYDCPGRQRCCYYSCSRICK 94 Waprin-Enh1 (Snakes, reptiles, animals) A7X4M1 Belongs to the snake waprin family Not found Enhydris polylepis (Macleay's water snake) Antimicrobial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). PTM: Contains eight disulfide bonds (By similarity). Tissue specificity: Expressed by the venom gland. Domain: Contains 2 WAP domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17855442 Mol Cell Proteomics. 2008 Feb;7(2):215-246. Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, Vidal N, Poelmann RE, Norman JA. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). DRAMP02488 ADDRNPLEEFRENNYEEFL 19 L-amino-acid oxidase ACTX-8 (LAAO; LAO; Snakes, reptiles, animals) P0DI85 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) Antimicrobial, Antibacterial, Antitumor, Antiparasitic Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). Induces apoptosis in HeLa cervical cancer cells. Both the caspase-dependent and the mitochondrial pathways seem to be involved in apoptosis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17275856 Life Sci. 2007 Mar 6;80(13):1189-1197. Zhang L, Wei LJ. ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells. DRAMP02489 QDRPKKPGLCPPRPQKPPCVRECKNDWSCPGEQKCCRYGCIFECRDPIFVK 51 Supwaprin-a (Snakes, reptiles, animals) B5KGY9 Belongs to the snake waprin family Not found Austrelaps superbus (Lowland copperhead snake) (Hoplocephalussuperbus) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). PTM: Contains four disulfide bonds (By similarity). Domain: Contains 1 WAP domain." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases St Pierre L. Identification and characterization of Waprins from the venom of Australian elapid snakes. DRAMP18263 KCPWWNLSCHLGNDGKICTYSHECTAGCNA 30 Enterocin W alpha(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Enterococcus faecalis NKR-4-1 Antimicrobial, Antibacterial, Anti-Gram+ Not found The cysteine, serine, and threonine residues in this peptide form a disulfide bridge and 3 dehydrated residues with or without monosulfide bridges. The amino acid sequences of the prepeptides of enterocin W showed the highest identity with those of plantaricins Walpha and Wbeta (63.3 and 44.7%, respectively). The two peptides acted synergistically, and their order of binding to the cell membrane was important for their inhibitory activity. Gram-positive (Narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 22138996 Appl Environ Microbiol. 2012 Feb;78(3):900-3. Sawa N, Wilaipun P, Kinoshita S, Zendo T, Leelawatcharamas V, Nakayama J, Sonomoto K. Isolation and characterization of enterocin W, a novel two-peptide lantibiotic produced by Enterococcus faecalis NKR-4-1. DRAMP02491 QDHPKKPGLCPPRPQKPPCVRECKNDWSCPGEQKCCRYGCIFECRDPIFVK 51 Stewaprin-a (Snakes, reptiles, animals) B5G6H3 Belongs to the snake waprin family Not found Hoplocephalus stephensii (Stephens' banded snake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02492 LDRPKKPGLCPPRPQKPPCVRECKNDWRCPGEQKCCRYGCIYECRDPIFVK 51 Notewaprin-a (Snakes, reptiles, animals) B5G6H4 Belongs to the snake waprin family Not found Notechis scutatus scutatus (Mainland tiger snake) (Common tigersnake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02493 KDRPKKPGLCPPRPQKPCVKECKNDWSCSGQQKCCNYGCIDECRDPIFVN 50 Auswaprin-a (Snakes, reptiles, animals) B5G6G9 Belongs to the snake waprin family Not found Pseudechis australis (Mulga snake) (King brown snake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database [Swiss_Prot Entry B5G6G9]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02494 KDRPKKLGLCPPRPQKPCVKECKNDWSCPGQQKCCNYGCIDECRDPIFVN 50 Porwaprin-a (Snakes, reptiles, animals) B5G6H0 Belongs to the snake waprin family Not found Pseudechis porphyriacus (Red-bellied black snake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database [Swiss_Prot Entry B5G6H0]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02496 QDRPVKPGLCPPRPQKPPCVKECKNDWSCRGEQKCCRYGCIYECRDPIFVK 51 Nigwaprin-a (Snakes, reptiles, animals) B5G6H1 Belongs to the snake waprin family Not found Rhinoplocephalus nigrescens (Eastern small-eyed snake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database [Swiss_Prot Entry B5G6H1]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02497 QDRPKKPGLCPPRPQKPPCVRECKNDWRCPGEQKCCRYGCIYECRDPIFVK 51 Carwaprin-a (Snakes, reptiles, animals) B5G6H2 Belongs to the snake waprin family Not found Tropidechis carinatus (Australian rough-scaled snake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). No MICs found in DRAMP database [Swiss_Prot Entry B5G6H2]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP18262 MGAIAKLVAKFGWPIVKKYYKQIMQFIGEGWAINKIIDWIKKHI 44 Enterocin 7A(Bacteriocin) Q1A2D3 Belongs to the class IId bacteriocin mr10A Enterococcus faecalis MRR 10-3; Enterococcus faecalis 710C Antimicrobial, Antibacterial, Anti-Gram+ Helix Both peptides are primarily alpha-helical, adopting a similar overall fold. The structures can be divided into three separate alpha-helical regions: the N- and C-termini are both alpha-helical, separated by a central kinked alpha-helix. The overall structures bear an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold. 2M5Z resolved by NMR leaderless, i.e. no signal peptide. The amino acid sequence of enterocin 7A is identical to that of MR10A. However, enterocin 7A is N-terminally formylated. Remarkably, the peptide is helical in aqueous solution.Enterocins 7A and 7B each display strong activity by themselves without their partner. Gram-positive (broad-spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 16751538##23725536 Appl Environ Microbiol. 2006 Jun;72(6):4245-9.##Biochemistry. 2013 Jun 11;52(23):3987-94. Mart Characterization of antimicrobial substances produced by Enterococcus faecalis MRR 10-3, isolated from the uropygial gland of the hoopoe (Upupa epops).##Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide. DRAMP02499 QDRPKKPGLRPPRPQKPPCVRECKNDWRCPGEQKCCRYGCIYECRDPIFVK 51 Veswaprin-b (Snakes, reptiles, animals) B5L5P5 Belongs to the snake waprin family Not found Demansia vestigiata (Lesser black whip snake) (Demansia atra) Antimicrobial, Antibacterial, Antimalarial Homology Not found Not found "Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database [Swiss_Prot Entry B5L5P5]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02500 QDRPKKPGLCPPRPQKPPCVRECKNDWICPGEQKCCRYGCIYECRDPIFVK 51 Notewaprin-b (Snakes, reptiles, animals) B5G6H5 Belongs to the snake waprin family Not found Notechis scutatus scutatus (Mainland tiger snake) (Common tigersnake) Antimicrobial, Antibacterial, Antimalarial Transcript level Not found Not found "Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database [Swiss_Prot Entry B5G6H5]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02502 QDRPVKPGLCPPRPQKPPCVKECKNDWSCRGEQKCCHYGCIYECRDPIFVK 51 Porwaprin-b (Snakes, reptiles, animals) B5L5N2 Belongs to the snake waprin family Not found Pseudechis porphyriacus (Red-bellied black snake) Antimicrobial, Antibacterial, Antimalarial Homology Not found Not found "Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database [Swiss_Prot Entry B5L5N2]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP02503 QDRPIKPGLCPPRPQKPPCVKECKNDRSCPREQKCCRYGCIYECRDPIFVK 51 Nigwaprin-b (Snakes, reptiles, animals) B5L5N6 Belongs to the snake waprin family Not found Rhinoplocephalus nigrescens (Eastern small-eyed snake) Antimicrobial, Antibacterial, Antimalarial Homology Not found Not found "Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database [Swiss_Prot Entry B5L5N6]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP18261 MGAIAKLVAKFGWPFIKKFYKQIMQFIGQGWTIDQIEKWLKRH 43 Enterocin 7B (Bacteriocin) Q1A2D2 Belongs to the class IId bacteriocin mr10B Enterococcus faecalis 710C; Enterococcus faecalis MRR 10-3 Antimicrobial, Antibacterial, Anti-Gram+ Helix Both peptides are primarily alpha-helical, adopting a similar overall fold. The structures can be divided into three separate alpha-helical regions: the N- and C-termini are both alpha-helical, separated by a central kinked alpha-helix. The overall structures bear an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold. 2M60 leaderless, i.e. no signal peptide. Although MR10B and Enterocin 7B share the same amino acid sequence, enterocin 7B is N-terminally formylated Met. Remarkably, the peptides are helical in aqueous solution. Enterocins 7A and 7B each display strong activity by themselves without their partner. broad-spectrum( mainly Gram-positive) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 21469734##23725536 J Agric Food Chem. 2011 May 25;59(10):5602-8.##Biochemistry. 2013 Jun 11;52(23):3987-94. Liu X, Vederas JC, Whittal RM, Zheng J, Stiles ME, Carlson D, Franz CM, McMullen LM, van Belkum MJ.##Lohans CT, Towle KM, Miskolzie M, McKay RT, van Belkum MJ, McMullen LM, Vederas JC. Identification of an N-terminal formylated, two-peptide bacteriocin from Enterococcus faecalis 710C.##Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide. DRAMP18260 ATYYGNGLYCNKQKCWVDWNKASREIGKIIVNGWVQHGPWAPR 43 Bacteriocin 31 (Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Enterococcus faecalis Y1717 Antimicrobial, Antibacterial, Anti-Gram+ Not found These bacteriocins are heat-stable, nonlanthionine, membrane-active peptides characterized by a Gly (22) The deduced amino acid sequence of the mature protein of BacA showed a high degree of homology of the identical residues with the class II bacteriocin of lactic acid bacteria. Gram-positive(narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8655558 J Bacteriol. 1996 Jun;178(12):3585-93. Tomita H, Fujimoto S, Tanimoto K, Ike Y. Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17. DRAMP02506 LDRPKKPGLCPPRPQKPPCVRECKNDWRCPGERKCCRYGCIYECRDPIFVK 51 Veswaprin-c (Snakes, reptiles, animals) B5L5P6 Belongs to the snake waprin family Not found Demansia vestigiata (Lesser black whip snake) (Demansia atra) Antimicrobial, Antibacterial, Antimalarial Homology Not found Not found "Function: Damages membranes of susceptible bacteria. Has no hemolytic activity. Does not inhibit the proteinases elastase and cathepsin G (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database [Swiss_Prot Entry B5L5P6]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18979207 Cell Mol Life Sci. 2008 Dec;65(24):4039-4054. St Pierre L, Earl ST, Filippovich I, Sorokina N, Masci PP, De Jersey J, Lavin MF. Common evolution of waprin and Kunitz-like toxin families in Australian venomous snakes. DRAMP18259 LGSCVANKIKDEFFAMISISAIVKAAQKKAWKELAVTVLRFAKANGLKTNAIIVAGQLALWAVQCGLS 68 Enterocin O16 (Bacteriocin) No entry found Not found Not found Enterococcus faecalis Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found the enterocin O16 antimicrobial peptide is translated as a large precursor pre-proprotein. The precursor is secreted via the general secretory pathway, and a 30-residues proprotein is released from the cells Gram-positive(certain) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25733609 J Bacteriol. 2015 Jul;197(13):2112-21. Dundar H, Brede DA, La Rosa SL, El-Gendy AO, Diep DB, Nes IF. The fsr Quorum-Sensing System and Cognate Gelatinase Orchestrate the Expression and Processing of Proprotein EF_1097 into the Mature Antimicrobial Peptide Enterocin O16. DRAMP18355 MAAFMKLIQFLATKGQKYVSLAWKHKGTILKWINAGQSFEWIYKQIKKLWA 51 Lacticin Z (bacteriocin) No entry found Belongs to the lantibiotic family. Not found Lactococcus lactis QU 14 Antimicrobial, Antibacterial Not found Not found 2N8P PTM: N-terminal Met is formylated. Active against S. saprophyticus (MIC 82.3-160 nM), S. hominis, S. warneri, E. faecalis (MIC 160 nM), including multidrug-resistant S. epidermidis strains causing biofilm-related infections (MIC 10-658 nM), S. aureus 1195 (MRSA), and vancomycin-resistant enterococci (VRE) (MIC 160-329 nM). THe recombinant peptide shows activity against M. luteus and S. aureus strains in lawn assays. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17690480 Biosci Biotechnol Biochem. 2007 Aug;71(8):1984-92. Iwatani S, Zendo T, Yoneyama F, Nakayama J, Sonomoto K. Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14. DRAMP18258 PNWTKIGKCAGSIAWAIGSGLFGGAKLIKIKKYIAELGGLQKAAKLLVGATTWEEKLHAGGYALINLAAELTGVAGIQANCF 82 Closticin 574(Bacteriocin) Q8GCU9 Belongs to the class IIc bacteriocin cloA Clostridium tyrobutyricum ADRIAT 932 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Closticin 574 is, on the basis of the nucleotide sequence of its structural gene, produced as preproprotein of 309 amino acid residues. After secretion and processing, it gives rise to an antimicrobial peptide of 82 amino acid residues. Gram-positive(narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12620847 Appl Environ Microbiol. 2003 Mar;69(3):1589-97.##Appl Environ Microbiol. 2003 Oct;69(10):5839-48. Kemperman R, Kuipers A, Karsens H, Nauta A, Kuipers O, Kok J. Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574. DRAMP18256 GLCAVNEFVALAAIPGGAATFAVCQMPNLDEIVSNAAYV 39 Boticin B (Bacteriocin) Q9KGZ4 Not found btcB Clostridium botulinum Antimicrobial, Antibacterial, Anti-Gram+ Not found Boticin B appears to be unique since it shows no detectable homology to other bacteriocins, including those from clostridial species. Amino acid analysis of purified boticin B estimated that the active protein contained 39 amino acids. Boticin B is a heat-stable bacteriocin produced by Clostridium botulinum strain 213B that has inhibitory activity against various strains of C. botulinum and related clostridia. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11097932 Appl Environ Microbiol. 2000 Dec;66(12):5480-3. Dineen SS, Bradshaw M, Johnson EA. Cloning, nucleotide sequence, and expression of the gene encoding the bacteriocin boticin B from Clostridium botulinum strain 213B. DRAMP02511 YKQCHKKGGHCFPKEKICLPPSSDFGKMDCRWRWKCCKKGSG 42 Crotamine (defensin-like toxin; Snakes, reptiles, animals) Q9PWF3 Belongs to the crotamine-myotoxin family CRO2 Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytotoxic, Antifungal Protein level Combine helix and strand structure Crotamine contains an alpha-helix with residues 1-7 and a two-stranded anti-parallel beta-sheet with residues 9-13 and 34-38 as the only regular secondary structures. These are connected with each other and the remainder of the polypeptide chain by the three disulfide bonds, which also form part of a central hydrophobic core (Ref.2). 1Z99 resolved by NMR. "Function: It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism. As a cell-penetrating peptide, crotamine has high specificity for actively proliferating cells, and interacts inside the cell with subcellular and subnuclear structures, like vesicular compartments, chromosomes and centrioles. Crotamine has marked activity against the eukaryotic pathogen Candida albicans at pH 7.5 or 5.5. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 1.5 mg/kg by intravenous injection. LD50 is 32.8 mg/kg by intraperitoneal injection into mice.(Ref.3)(Ref.4) Pharmaceutical use: Has high potential for use as an anticancer agent. In vivo treatment with this protein significantly delays tumor implantation, inhibits tumor growth and prolongs the lifespan of the mice with melanoma tumors. It has also potent and specific toxicity against tumor cell lines of aggressive mouse and human tumors, but low cytotoxicity against non-tumoral cell lines. In addition, this protein can act as a carrier capable of delivering DNA into replicating cells with low cytotoxicity against normal proliferative cells.(Ref.5)(Ref.6) Miscellaneous: Has no hemolytic activity ." [Swiss_Prot Entry Q9PWF3]Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Escherichia coli;##Yeast: Candida albicans [Ref.210622]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Eukaryotic ion channels 19706485##16185738##1176086##9839677##22142367##210622 Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14972-14977.##Toxicon. 2005 Dec 1;46(7):759-767.##Hoppe Seylers Z Physiol Chem. 1975 Feb;356(2):213-215.##Toxicon. 1998 Dec;36(12):1927-1937.##Mol Pharm. 2012 Feb 6 Yount NY, Kupferwasser D, Spisni A, Dutz SM, Ramjan ZH, Sharma S, Waring AJ, Yeaman MR.##Fadel V, Bettendorff P, Herrmann T, de Azevedo WF Jr, Oliveira EB, Yamane T, Wüthrich K.##Laure CJ.##Mancin AC, Soares AM, Andrião-Escarso SH, Faça VM, Greene LJ, Zuccolotto S, Pelá IR, Giglio JR.##Nascimento FD, Sancey L, Pereira A, Rome C, Oliveira V, Oliveira EB, Nader HB, Yamane T, Kerkis I, Tersariol IL, Coll JL, Hayashi MA.##Kerkis I, Silva Selective reciprocity in antimicrobial activity versus cytotoxicity of hBD-2 and crotamine.##Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus.##The primary structure of crotamine (author's transl).##he analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: a biochemical and pharmacological study.##The natural cell-penetrating peptide crotamine targets tu DRAMP02512 ADDRNPLEQCFRETDYEEFLEIARNNLKATSNPKHVVIVGAGMAGLSAAYVLSGGGHQVTV 61 L-amino-acid oxidase (Casca LAO, LAAO, LAO; Snakes, reptiles, animals) P0C2D2 Not found Not found Crotalus durissus cascavella (Northeastern Brazilian rattlesnake) Antimicrobial, Antibacterial, Antiparasitic, Cytotoxic Protein level Not found Not found Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and edema. Also has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production, and the 50% inhibitory concentration was estimated in 2.39 microg/ml. Xanthomonas axonopodis pv passiflorae, Streptococcus mutans, Leishmania amazonensis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16307769 Toxicon. 2006 Jan;47(1):47-57. Toyama MH, Toyama Dde O, Passero LF, Laurenti MD, Corbett CE, Tomokane TY, Fonseca FV, Antunes E, Joazeiro PP, Beriam LO, Martins MA, Monteiro HS, Fonteles MC. Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom. DRAMP02513 KRRGSVTTRYQFLMIHLLRPKKLFA 25 EA-CATH1 No entry found Not found Not found Equus asinus Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20423460 FEBS J. 2010 May;277(10):2329-2339. Lu Z, Wang Y, Zhai L, Che Q, Wang H, Du S, Wang D, Feng F, Liu J, Lai R, Yu H. Novel cathelicidin-derived antimicrobial peptides from Equus asinus. DRAMP02514 RIKRFWPVVIRTVVAGYNLYRAIKKK 26 Cathelicidin Pc-CATH1 No entry found Not found Not found Phasianus colchicus Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Dong L, Yang JJ, Wang Y, Liu H, Mu LX, Lin DH, Lai R. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP18398 ISQSDAILSAIWSGIKSLF 19 Um2 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Urodacus manicatus Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against M. luteus (MIC 4 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28067810 Toxins (Basel). 2017 Jan 6;9, 22. doi: 10.3390/toxins9010022. Luna-Ramirez K, Tonk M, Rahnamaeian M, Vilcinskas A. Bioactivity of Natural and Engineered Antimicrobial Peptides from Venom of the Scorpions Urodacus yaschenkoi and U. manicatus DRAMP02516 LVQRGRFGRFLKKVRRFIPKVIIAAQIGSRFG 32 Cc-CATH2 No entry found Not found Not found Coturnix coturnix Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21375690 FEBS J. 2011 May;278(9):1573-1584. Feng F, Chen C, Zhu W, He W, Guang H, Li Z, Wang D, Liu J, Chen M, Wang Y, Yu H. Gene cloning, expression, and characterization of avian cathelicidin orthologue, Cc-CATHs, from Coturnix coturnix. DRAMP02517 RVRRFWPLVPVAINTVAAGINLYKAIRRK 29 Cc-CATH3 No entry found Not found Not found Coturnix coturnix Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21375690 FEBS J. 2011 May;278(9):1573-1584. Feng F, Chen C, Zhu W, He W, Guang H, Li Z, Wang D, Liu J, Chen M, Wang Y, Yu H. Gene cloning, expression, and characterization of avian cathelicidin orthologue, Cc-CATHs, from Coturnix coturnix. DRAMP04532 GIHDILKYGKPS 12 Myxinidin (Hagfish, animals) No entry found Not found Not found Myxine glutinosa (Atlantic hagfish) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Myxinidin showed activity against a broad range of bacteria and yeast pathogens at minimum bactericidal concentration (MBC) ranging from 1.0 to 10.0 [Ref.19330556] Gram-negative bacteria: Escherichia coli D31 (MBC=2.0 μg/ml), Salmonella enterica serovar Typhimurium C610 (MBC=2.5 μg/mL), Pseudomonas aeruginosa Z61 (MBC=7.0μg/ml), Pseudomonas aeruginosa K799 (MBC=10.0 μg/ml), Aeromonas salmonicida sub sp. salmonicida A449 (MBC=2.0 μg/ml), Listonella anguillarum 02-11 (MBC=1.0 μg/ml), Yersinia ruckeri 96-4 (MBC=2.0 μg/ml);##Gram-positive bacterium: Staphylococcus epidermis C621(MBC=8.5 μg/ml);##Yeast: Candida albicans C627 (MBC=10.0 μg/ml). [Ref.19330556] Non-hemolytic activity against rabbit red blood cells at concentrations 50-fold higher than its antimicrobial activity. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19330556 Mar Biotechnol (NY). 2009 Nov-Dec;11(6):748-757. Subramanian S, Ross NW, MacKinnon SL. Myxinidin, a novel antimicrobial peptide from the epidermal mucus of hagfish, Myxine glutinosa L. DRAMP02519 KRFKKFFKKLKKSVKKRAKKFFKKPRVIGVSIPF 34 BF-CATH No entry found Not found Not found Bungarus fasciatus Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18620012 Peptides. 2008 Oct;29(10):1685-1691. Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y. Identification and characterization of novel reptile cathelicidins from elapid snakes. DRAMP02521 KFFKKLKNSVKKRAKKFFKKPRVIGVSIPF 30 Cathelicidin-OH (Cathelicidin-related protein; Snakes, reptiles, animals) B6S2X2 Belongs to the cathelicidin family. Not found Ophiophagus hannah (King cobra) (Naja hannah) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram+, Antifungal Transcript level Alpha helix Not found 2mwt resolved by NMR [Ref.22491685]Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.18620012]Gram-negative bacteria: Escherichia coli ATCC 25922, Escherichia coli ML-35P, Escherichia coli clinic strain, Pseudomonas aeruginosa ATCC 27853, Pseudomonas aeruginosa PA 01, Pseudomonas aeruginosa clinic strain, Enterobacter aerogenes clinic strain, Enterobacter cloacae clinic strain.##[Ref.22491685]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=3.125 μg/ml), Staphylococcuss aureus ATCC 43300 MRSA (MIC=6.25 μg/ml), Staphylococcuss aureus clinical strain 1 (MIC=3.125 μg/ml), Staphylococcuss aureus clinical strain 2 (MIC=6.25 μg/ml), Staphylococcuss aureus clinical strain 3 (MIC=6.25 μg/ml), Enterococcus faecalis ATCC 29212 (MIC=25 μg/ml) ;##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=6.25 μg/ml), Escherichia coli ML-35p (MIC=3.125 μg/ml), Escherichia coli clinical strain 1 (MIC=6.25 μg/ml), Escherichia coli clinical strain 2 (MIC=3.125 μg/ml), Escherichia coli clinical strain 3 (MIC=1.56 μg/ml), Escherichia coli clinical strain 4 (MIC=12.5 μg/ml), Escherichia coli clinical strain 5 (MIC=3.125 μg/ml), Escherichia coli clinical strain 6 (MIC=3.125 μg/ml), Enterobacter cloacae ATCC 13047 (MIC=25 μg/ml), Enterobacter cloacae clinical strain (MIC=3.125 μg/ml), Enterobacter aerogenes clinical strain (MIC=6.25 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=6.25 μg/ml), Pseudomonas aeruginosa PA 01 (MIC=6.25 μg/ml), Pseudomonas aeruginosa clinical strain 1 (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain 2 (MIC=6.25 μg/ml), Haemophilus influenzae ATCC 49247 (MIC=3.125 μg/ml), Haemophilus influenzae ATCC 49766 (MIC=3.125 μg/ml), Klebsiella pneumoniae ATCC 13883 (MIC=6.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=3.125 μg/ml) ;##Fungi : Candida albicans ATCC 2002 (MIC>200 μg/ml), Candida albicans clinical strain (MIC>200 μg/ml) [Ref.22491685] 3% hemolysis at 100 μg/ml , 5% hemolysis at 200 μg/ml , 6% hemolysis at 300 μg/ml , 7% hemolysis at 400 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18620012##22491685 Peptides. 2008 Oct;29(10):1685-91. ##Antimicrob Agents Chemother. 2012 Jun;56(6):3309-17. doi: 10.1128/AAC.06304-11. Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y.##Sheng-An Li, Wen-Hui Lee, and Yun Zhang Identification and characterization of novel reptile cathelicidins from elapid snakes.##Efficacy of OH-CATH30 and Its Analogs against Drug-ResistantBacteria In Vitro and in Mouse Models DRAMP02523 MLHLVVYDISDDGSRARLAKLLEKFGLQRVQYSAFRGELNPNDREVLARQVGKFVRDDRDCIFIIPLCQRCSSTAIVISNTGVELVKEKGVEFV 94 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) O28403 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas21 Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM9628 / NBRC 100126) Antimicrobial, Antiviral Protein level Not found Not found Function: CRISPR is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 9389475##18482976 Nature. 1997 Nov 27;390(6658):364-370.##J Biol Chem. 2008 Jul 18;283(29):20361-71. Klenk HP, Clayton RA, Tomb JF, White O, Nelson KE, Ketchum KA, Dodson RJ, Gwinn M, Hickey EK, Peterson JD, Richardson DL, Kerlavage AR, Graham DE, Kyrpides NC, Fleischmann RD, Quackenbush J, Lee NH, Sutton GG, Gill S, Kirkness EF, Dougherty BA, McKenney K, Adams MD, Loftus B, et al.##Beloglazova N, Brown G, Zimmerman MD, Proudfoot M, Makarova KS, Kudritska M, Kochinyan S, Wang S, Chruszcz M, Minor W, Koonin EV, Edwards AM, Savchenko A, Ya The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.##A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats. DRAMP02524 MFYLISYDISVDQRRLKIAKLLEGYGQRVLESVFECDLELPAYRQLRQKLNRLIKDEEGDRLRIYRLCASCREQIEIIGDGPPPETSQDIYII 93 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) A9WEP1 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Copeland A, Lucas S, Lapidus, Barry K, Glavina del Rio T, Hammon N, Israni S, Dalin E, Tice H, Pitluck S, Chertkov O, Brettin T, Bruce D, Detter JC, Han C, Schmutz J, Larimer F, Land M, Hauser L, Kyrpides N, Mikhailova N, Pierson BK, Blankenship RE, Richardson P. Complete sequence of Chloroflexus aurantiacus J-10-fl. DRAMP02525 MTVKHLIVCYDVEKTKDRNKVIKVLEYYGLIRVQYSVFMGSLTETRLHQMNARIKREFTKPSIKILVIEVCNACMERALLVHEELPKVNRQFEVI 95 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) Q2FL79 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC100397 / JF-1) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Copeland A, Lucas S, Lapidus A, Barry K, Detter JC, Glavina T, Hammon N, Israni S, Pitluck S, Brettin T, Bruce D, Han C, Tapia R, Gilna P, Kiss H, Schmutz J, Larimer F, Land M, Kyrpides N, Ivanova N, McInerney MJ, Brockman F, Culley D, Ferry JG, Gunsalus RP, Morrison M, Plugge C, Scholten J, Stams AJM, Boone DR, Richardson P. Complete sequence of Methanospirillum hungatei JF-1. DRAMP02526 MIWLAVYDIEDDGERAKASAILQAWGFVRVQRSFYVGRMPRGKAADLLKILQRHVKSGHIALIPITDELLAKALELGRPPYAPLKPPKYAQIYVV 95 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) Q8ZZU2 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630/ NBRC 100827) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 11792869 Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):984-989. Fitz-Gibbon ST, Ladner H, Kim UJ, Stetter KO, Simon MI, Miller JH. Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. DRAMP02527 MLYLIIYDVPATKAGNKRRTRLFDLLSGYGKWRQFSVFECFLSVKQFAKLQTAMEKLIKLDEDAVCIYVLDENTVQRTITYGTPQPEKPGSIII 94 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) Q6ZEI1 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Synechocystis sp. (strain PCC 6803 / Kazusa) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 14686584 DNA Res. 2003 Oct 31;10(5):221-228. Kaneko T, Nakamura Y, Sasamoto S, Watanabe A, Kohara M, Matsumoto M, Shimpo S, Yamada M, Tabata S. Structural analysis of four large plasmids harboring in a unicellular cyanobacterium, Synechocystis sp. PCC 6803. DRAMP02528 MRELYLVIAYDTPDDRRRARLAKLLKGFGERRQYSVFEARLTREQWAHLKGKLEALVNKEEDVLAVYFLPPEAVGRTWRIGHEGLKRLEDPDFV 94 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) Q745W0 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2a Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 15064768 Nat Biotechnol. 2004 May;22(5):547-553. Henne A, Brüggemann H, Raasch C, Wiezer A, Hartsch T, Liesegang H, Johann A, Lienard T, Gohl O, Martinez-Arias R, Jacobi C, Starkuviene V, Schlenczeck S, Dencker S, Huber R, Klenk HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ. The genome sequence of the extreme thermophile Thermus thermophilus. DRAMP02529 MRVLYIIAYDITDARRLGQIRYFLKGYSTGGQKSVYECFLEREELKFIISKIKRLINPNEDRVHIFRIDGRSKVITLGIAVPPIDPEYFYIG 92 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) B5YJS1 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /YP87) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Dodson R.J, Durkin A.S, Wu M, Eisen J, Sutton G. The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87. DRAMP02530 MVVIVYVIVAYDVNVERVNRVKKFLRRYLNWVQNSLFEGELSSADLEEVKMGLREIINEDEDMVVIYRFRSADAFKREVMGIEKGLGGEEVI 92 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) O30237 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas22 Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM9628 / NBRC 100126) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 9389475 Nature. 1997 Nov 27;390(6658):364-370. Klenk HP, Clayton RA, Tomb JF, White O, Nelson KE, Ketchum KA, Dodson RJ, Gwinn M, Hickey EK, Peterson JD, Richardson DL, Kerlavage AR, Graham DE, Kyrpides NC, Fleischmann RD, Quackenbush J, Lee NH, Sutton GG, Gill S, Kirkness EF, Dougherty BA, McKenney K, Adams MD, Loftus B, et al. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. DRAMP02531 MQCLVIYDIPNDRARQRVADACLDYGLQRIQYSAFAGNLSRTHQRALFGEITRRVKGHTANVQLFVFDSKTWSDRRILEQQYDDA 85 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) A9WFZ7 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Copeland A, Lucas S, Lapidus, Barry K, Glavina del Rio T, Hammon N, Israni S, Dalin E, Tice H, Pitluck S, Chertkov O, Brettin T, Bruce D, Detter JC, Han C, Schmutz J, Larimer F, Land M, Hauser L, Kyrpides N, Mikhailova N, Pierson BK, Blankenship RE, Richardson P. Complete sequence of Chloroflexus aurantiacus J-10-fl. DRAMP02532 MVRLVITYDIRKDKIRNKLFRLLERYGAWKQYSVFELEINPVHKVELFHSIADLIEDTDRVRIYDLCERCQGKITELGEVSPDKMQVVI 89 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) Q2FQQ4 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC100397 / JF-1) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Copeland A, Lucas S, Lapidus A, Barry K, Detter JC, Glavina T, Hammon N, Israni S, Pitluck S, Brettin T, Bruce D, Han C, Tapia R, Gilna P, Kiss H, Schmutz J, Larimer F, Land M, Kyrpides N, Ivanova N, McInerney MJ, Brockman F, Culley D, Ferry JG, Gunsalus RP, Morrison M, Plugge C, Scholten J, Stams AJM, Boone DR, Richardson P. Complete sequence of Methanospirillum hungatei JF-1. DRAMP02533 MILIYDINTEDNDGKRRLVKIMKTSRKYLSHVQKSVFEGDITEGQISLLKKEIMAIVNMKKDFVIIYSLRDGVKLNREILTDTPDPTDNFL 91 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) Q2RHR2 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Moorella thermoacetica (strain ATCC 39073) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 18631365 Environ Microbiol. 2008 Oct;10(10):2550-2573. Pierce E, Xie G, Barabote RD, Saunders E, Han CS, Detter JC, Richardson P, Brettin TS, Das A, Ljungdahl LG, Ragsdale SW. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). DRAMP02534 MYVVVAYDITEDEVRNKVADALKAYGLERIQRSVFVGRINPALLKDLVERLKRITKGANADITIFKVDRRAIDTAIRIGPPPPARKNVDLY 91 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) Q8ZZL9 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630/ NBRC 100827) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 11792869 Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):984-989. Fitz-Gibbon ST, Ladner H, Kim UJ, Stetter KO, Simon MI, Miller JH. Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. DRAMP02535 MKLLVVYDVSDDSKRNKLANNLKKLGLERIQRSAFEGDIDSQRVKDLVRVVKLIVDTNTDIVHIIPLGIRDWERRIVIGREGLEEWLV 88 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) Q97Y85 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas22 Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /P2) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 3EXC resolved by X-ray. Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 11427726##18482976##PubMed ID is not availbale Proc Natl Acad Sci U S A. 2001 Jul 3;98(14):7835-7840.##J Biol Chem. 2008 Jul 18;283(29):20361-71.##To be Published She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez MJ, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A, Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, Van der Oost J.##Beloglazova N, Brown G, Zimmerman MD, Proudfoot M, Makarova KS, Kud The complete genome of the crenarchaeon Sulfolobus solfataricus P2.##A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats.##Structure of the RNA'se SSO8090 from Sulfolobus solfataricus. DRAMP02536 MDFWLVCYDVRDDKRRRKLAKLLEQRCQRVQYSVFECPLPEKVLTDLLHRRWLKELNLKEDSLRAYPLQRQSRSQAKIFGSPDLYEPPDFLIL 93 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) Q6ZEC6 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Synechocystis sp. (strain PCC 6803 / Kazusa) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 14686584 DNA Res. 2003 Oct 31;10(5):221-228. Kaneko T, Nakamura Y, Sasamoto S, Watanabe A, Kohara M, Matsumoto M, Shimpo S, Yamada M, Tabata S. Structural analysis of four large plasmids harboring in a unicellular cyanobacterium, Synechocystis sp. PCC 6803. DRAMP02537 MGKRLYAVAYDIPDDTRRVKLANLLKSYGERVQLSVFECYLDERLLEDLRRRARRLLDLGQDALRIYPVAGQVEVLGVGPLPELREVQVL 90 CRISPR-associated endonuclease Cas2 2 (Antiviral defensin) Q746F4 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2b Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 1ZPW resolved by X-ray. Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 15064768##22942283##PubMed ID is not availbale Nat Biotechnol. 2004 May;22(5):547-553.##J Biol Chem. 2012 Oct 19;287(43):35943-52.##To be Published Henne A, Brüggemann H, Raasch C, Wiezer A, Hartsch T, Liesegang H, Johann A, Lienard T, Gohl O, Martinez-Arias R, Jacobi C, Starkuviene V, Schlenczeck S, Dencker S, Huber R, Klenk HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ.##Nam KH, Ding F, Haitjema C, Huang Q, DeLisa MP, Ke A.##Ihsanawati, Murayama K, Shirouzu M, Yokoyama S. The genome sequence of the extreme thermophile Thermus thermophilus.##Double-stranded endonuclease activity in Bacillus halodurans clustered regularly interspaced short palindromic repeats (CRISPR)-associated Cas2 protein.##Crystal structure of a hypothetical protein TT1823 from Thermus thermophilus. DRAMP02538 MRLPYLVCYDISDEGRLNRVYRFMKGKGFHIQYSVFYCILTDVELKEMKAEILKLIHSRYDDVRIYPLPNNSLVAVLGVGDRIPDGVEVFY 91 CRISPR-associated endoribonuclease Cas2 2 (Antiviral defensin) B5YJS4 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-2 Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /YP87) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Dodson R.J, Durkin A.S, Wu M, Eisen J, Sutton G. The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87. DRAMP02539 MKMFTVISYDIVDDQRRTSVMKVLKGYGVRVQYSVFEAILDAREFHDLSNQLRKIIDPGQDSIRCYRLDQVAAQRTVIYGIGLTTTDPTHYMV 93 CRISPR-associated endoribonuclease Cas2 3 (Antiviral defensin) A9WJV5 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-3 Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Copeland A, Lucas S, Lapidus, Barry K, Glavina del Rio T, Hammon N, Israni S, Dalin E, Tice H, Pitluck S, Chertkov O, Brettin T, Bruce D, Detter JC, Han C, Schmutz J, Larimer F, Land M, Hauser L, Kyrpides N, Mikhailova N, Pierson BK, Blankenship RE, Richardson P. Complete sequence of Chloroflexus aurantiacus J-10-fl. DRAMP02540 MLIIVTYDVSTETRAGRKRLRRVAKLCESIGQRVQKSVFECRINLMQYEELERRLLSEIDEQEDNLRLYRLTEPAELHVKEYGNFKAIDFEGPLTI 96 CRISPR-associated endoribonuclease Cas2 3 (Antiviral defensin) Q82W51 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas23 Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298) Antimicrobial, Antiviral Protein level Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 12700255##18482976 J Bacteriol. 2003 May;185(9):2759-2773.##J Biol Chem. 2008 Jul 18;283(29):20361-71. Chain P, Lamerdin J, Larimer F, Regala W, Lao V, Land M, Hauser L, Hooper A, Klotz M, Norton J, Sayavedra-Soto L, Arciero D, Hommes N, Whittaker M, Arp D.##Beloglazova N, Brown G, Zimmerman MD, Proudfoot M, Makarova KS, Kudritska M, Kochinyan S, Wang S, Chruszcz M, Minor W, Koonin EV, Edwards AM, Savchenko A, Yakunin AF. Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea.##A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats. DRAMP02541 MILVTYDVNTVEPGGRRRLRQVAKACQDYGQRVQNSVFEVEVDPARWVALKARLEAIIDPALDSLRYYDLGANWQRRVDHVGAKPAVDLHGPLIL 95 CRISPR-associated endoribonuclease Cas2 3 (Antiviral defensin) Q2RW60 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-3 Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2005) to the EMBL/GenBank/DDBJ database Copeland A, Lucas S, Lapidus A, Barry K, Detter JC, Glavina T, Hammon N, Israni S, Pitluck S, Munk AC, Brettin T, Bruce D, Han C, Tapia R, Gilna P, Schmutz J, Larimer F, Land M, Kyrpides N, Mavrommatis K, Richardson P, Zhang Y, Roberts G, Reslewic S, Zhou S, Schwartz DC. Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170. DRAMP02542 MFLYVIAYDIPDDRRRKKMADLLEGYGQRVQYSVFECTLSKSKFNELQKRLRKIYQSEEDSLRFYPLSGHTLTQVDIWGEPPLTKPPGSVIV 92 CRISPR-associated endoribonuclease Cas2 3 (Antiviral defensin) Q6ZEA5 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-3 Synechocystis sp. (strain PCC 6803 / Kazusa) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 14686584 DNA Res. 2003 Oct 31;10(5):221-228. Kaneko T, Nakamura Y, Sasamoto S, Watanabe A, Kohara M, Matsumoto M, Shimpo S, Yamada M, Tabata S. Structural analysis of four large plasmids harboring in a unicellular cyanobacterium, Synechocystis sp. PCC 6803. DRAMP02543 MPYLIVTYDIAEERVNKVRKILKKYFMWVQNSVFEGEITEGKLLKCKLELEKVIDKEVDSVYFYSLENRLNYRKTVLGIEKEITGNIL 88 CRISPR-associated endoribonuclease Cas2 3 (Antiviral defensin) B5YIU7 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-3 Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /YP87) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Dodson R.J, Durkin A.S, Wu M, Eisen J, Sutton G. The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87. DRAMP02544 MVYVLIAYDISNDSKRLKAAQKLLQMGFARVQKSVYIAKGGRSLAKEAYRALQRLADSGKDKIMVMVIPGDSVRDAYGLGGSLEDGKRVVVV 92 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q05E21 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC100138 / K1) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 10382966 DNA Res. 1999 Apr 30;6(2):83-101, 145-152. Kawarabayasi Y, Hino Y, Horikawa H, Yamazaki S, Haikawa Y, Jin-no K, Takahashi M, Sekine M, Baba S, Ankai A, Kosugi H, Hosoyama A, Fukui S, Nagai Y, Nishijima K, Nakazawa H, Takamiya M, Masuda S, Funahashi T, Tanaka T, Kudoh Y, Yamazaki J, Kushida N, Oguchi A, Kikuchi H, et al. Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1. DRAMP02545 MSSRLAVFAYDIRDDRVRRHALKTLREWRLDGQLSVHECQVDAIQARRLFEQLGDELDPATDAWLFTWVEGHRAVLARGKGRTTALQDGLLLAA 94 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) D3RW30 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D)(Chromatium vinosum) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Lucas S, Copeland A, Lapidus A, Cheng J-F, Bruce D, Goodwin L, Pitluck S, Munk AC, Detter JC, Han C, Tapia R, Larimer F, Land M, Hauser L, Kyrpides N, Ivanova N, Zigann R, Dahl C, Woyke T. Complete sequence of plasmid 1 of Allochromatium vinosum DSM 180. DRAMP02546 MLVLITYDVQTSSMGGTKRLRKVAKACQNYGQRVQNSVFECIVDSTQLTSLKLELTSLIDEEKDSLRIYRLGNNYKTKVEHIGAKPSIDLEDPLIF 96 CRISPR-associated endonuclease Cas2 (Antiviral defensin) Q9KFX8 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM9153 / C-125) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 4ES1, 4ES2, 4ES3 resolved by X-ray. Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 11058132##22942283##PubMed ID is not availbale Nucleic Acids Res. 2000 Nov 1;28(21):4317-4331.##J Biol Chem. 2012 Oct 19;287(43):35943-52.##To be Published Takami H, Nakasone K, Takaki Y, Maeno G, Sasaki R, Masui N, Fuji F, Hirama C, Nakamura Y, Ogasawara N, Kuhara S, Horikoshi K.##Nam KH, Ding F, Haitjema C, Huang Q, DeLisa MP, Ke A.##Ke A, Nam KH. Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.##Double-stranded endonuclease activity in Bacillus halodurans clustered regularly interspaced short palindromic repeats (CRISPR)-associated Cas2 protein.##Crystal structure of BH0342 protein. DRAMP02547 MLVLVTYDVNTETPAGRRRLRRIAKTCQNYGQRVQFSVFECNVDPAQWVKLRSKLLNEMDPKLDSLRFYFLGSNWQGRVEHEGAKEPRDLEGTLIL 96 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q8KDC5 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 12093901 Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9509-9514. Eisen JA, Nelson KE, Paulsen IT, Heidelberg JF, Wu M, Dodson RJ, Deboy R, Gwinn ML, Nelson WC, Haft DH, Hickey EK, Peterson JD, Durkin AS, Kolonay JL, Yang F, Holt I, Umayam LA, Mason T, Brenner M, Shea TP, Parksey D, Nierman WC, Feldblyum TV, Hansen CL, Craven MB, Radune D, Vamathevan J, Khouri H, White O, Gruber TM, Ketchum KA, Venter JC, Tettelin H, Bryant DA, Fraser CM. The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium. DRAMP02548 MYVIMVYDVNQRRINKVLNTARKYLEWIQNSVLEGEITEAKFEMLKREIEIIINEEEDSVIFYIMRTTKYSERQILGIEKNKREQIL 87 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) B8DZH3 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Dictyoglomus turgidum (strain Z-1310 / DSM 6724) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Lucas S, Copeland A, Lapidus A, Glavina del Rio T, Tice H, Bruce D, Goodwin L, Pitluck S, Sims D, Brettin T, Detter J.C, Han C, Larimer F, Land M, Hauser L, Kyrpides N, Mikhailova N, Mead D. Complete sequence of Dictyoglomus turgidum DSM 6724. DRAMP02549 MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIREMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTPVDLDGLRLVSFLPV 94 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) P45956, Q2MA75 Belongs to the CRISPR-associated endoribonuclease Cas2 prote ygbF Escherichia coli (strain K12) Antimicrobial, Antiviral Protein level Not found Not found "Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). Induction: Repressed by H-NS, activated by LeuO. Activated by the BaeSR two-component regulatory system, possibly due to envelope stress. Part of the casABCDE-ygbT-ygbF operon." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 2656660##9278503##16738553 J Bacteriol. 1989 Jun;171(6):3553-6.##Science. 1997 Sep 5;277(5331):1453-1462.##Mol Syst Biol. 2006;2:2006.0007. Nakata A, Amemura M, Makino K.##Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y.##Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T. Unusual nucleotide arrangement with repeated sequences in the Escherichia coli K-12 chromosome.##The complete genome sequence of Escherichia coli K-12.##Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. DRAMP02550 MFVVLVYDTAAERNPNALRTCRKYLHWVQRSVFEGELSAAQYRALMTTLRDQLDLTYDSIRVYRTRSPALVETEWLGVPLGNQDSVL 87 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q0RE94 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Frankia alni (strain ACN14a) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 17151343 Genome Res. 2007 Jan;17(1):7-15. Normand P, Lapierre P, Tisa LS, Gogarten JP, Alloisio N, Bagnarol E, Bassi CA, Berry AM, Bickhart DM, Choisne N, Couloux A, Cournoyer B, Cruveiller S, Daubin V, Demange N, Francino MP, Goltsman E, Huang Y, Kopp OR, Labarre L, Lapidus A, Lavire C, Marechal J, Martinez M, Mastronunzio JE, Mullin BC, Niemann J, Pujic P, Rawnsley T, Rouy Z, Schenowitz C, Sellstedt A, Tavares F, Tomkins JP, Vallenet D, Valverde C, Wall LG, Wang Y, Medigue C, B Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography. DRAMP02551 MEHLYIVSYDIRNQRRWRRLFKTMHGFGCWLQLSVFQCRLDRIRIIKMEAAINEIVNHAEDHVLILDLGPAENVKPKVSSIGKTFDPILRQAVIV 95 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q74H35 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 14671304 Science. 2003 Dec 12;302(5652):1967-1969. Methé BA, Nelson KE, Eisen JA, Paulsen IT, Nelson W, Heidelberg JF, Wu D, Wu M, Ward N, Beanan MJ, Dodson RJ, Madupu R, Brinkac LM, Daugherty SC, DeBoy RT, Durkin AS, Gwinn M, Kolonay JF, Sullivan SA, Haft DH, Selengut J, Davidsen TM, Zafar N, White O, Tran B, Romero C, Forberger HA, Weidman J, Khouri H, Feldblyum TV, Utterback TR, Van Aken SE, Lovley DR, Fraser CM. Genome of Geobacter sulfurreducens: metal reduction in subsurface environments. DRAMP02552 MPYVVVFYDVSDNKRRDLLAKTLQSLGLVRVQRSVFMGRGGYTKAKEAIRAASRIVDARTDSVVALVVPEDYARRMLVYGGIMSDPKQKQAVRVV 95 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) A2BKJ6 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Hyperthermus butylicus (strain DSM 5456 / JCM 9403) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 17350933 Archaea. 2007 May;2(2):127-135. Brügger K, Chen L, Stark M, Zibat A, Redder P, Ruepp A, Awayez M, She Q, Garrett RA, Klenk HP. The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C. DRAMP02553 MRGGNLKVLVVYDITDDSLRLKVAEILKDLGLFRIQKSAFIGEMTSQERENMEEILRRQNLGPSDRIDVFPICDRDLKMHSQIGRGKFGRGPP 93 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) B1L402 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Korarchaeum cryptofilum (strain OPF8) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 18535141 Proc Natl Acad Sci U S A. 2008 Jun 10;105(23):8102-8107. Elkins JG, Podar M, Graham DE, Makarova KS, Wolf Y, Randau L, Hedlund BP, Brochier-Armanet C, Kunin V, Anderson I, Lapidus A, Goltsman E, Barry K, Koonin EV, Hugenholtz P, Kyrpides N, Wanner G, Richardson P, Keller M, Stetter KO. A korarchaeal genome reveals insights into the evolution of the Archaea. DRAMP02554 MKHWRLVSYDIREPKRLRRVAKIMEGFGERIQYSVFRIYSTDKELEKLRWKLAKVTEEEDNIFYLTLCTKCASGAHTQEKKSAWPEAPKTLKIL 94 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q8F1F4 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai(strain 56601) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 12712204 Nature. 2003 Apr 24;422(6934):888-893. Ren SX, Fu G, Jiang XG, Zeng R, Miao YG, Xu H, Zhang YX, Xiong H, Lu G, Lu LF, Jiang HQ, Jia J, Tu YF, Jiang JX, Gu WY, Zhang YQ, Cai Z, Sheng HH, Yin HF, Zhang Y, Zhu GF, Wan M, Huang HL, Qian Z, Wang SY, Ma W, Yao ZJ, Shen Y, Qiang BQ, Xia QC, Guo XK, Danchin A, Saint Girons I, Somerville RL, Wen YM, Shi MH, Chen Z, Xu JG, Zhao GP. Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. DRAMP02555 MYVVIVYDVGVERVNKVRSFLREYMNWVQNSVFEGELTKAEFLKIKSRLKELIQESSDHIIFYSSRDRKYLGIEDLGTPKADTSNII 87 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q8TJV8 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /C2A) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 11932238 Genome Res. 2002 Apr;12(4):532-542. Galagan JE, Nusbaum C, Roy A, Endrizzi MG, Macdonald P, FitzHugh W, Calvo S, Engels R, Smirnov S, Atnoor D, Brown A, Allen N, Naylor J, Stange-Thomann N, DeArellano K, Johnson R, Linton L, McEwan P, McKernan K, Talamas J, Tirrell A, Ye W, Zimmer A, Barber RD, Cann I, Graham DE, et al. The genome of M. acetivorans reveals extensive metabolic and physiological diversity. DRAMP02556 MAVFLIAYDLVNERRGTHDYQPLWDELKRLGAHRTQFSLWLVSANNTTAEVRQHFQQFVDSNDRIWVTRLRKSQYDYANAIGGTNNWLSNNPPEA 95 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) B7KNJ8 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Methylobacterium extorquens (strain CM4 / NCIMB 13688)(Methylobacterium chloromethanicum) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding PubMed ID is not availbale Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Lucas S, Copeland A, Lapidus A, Glavina del Rio T, Dalin E, Tice H, Bruce D, Goodwin L, Pitluck S, Chertkov O, Brettin T, Detter J.C, Han C, Larimer F, Land M, Hauser L, Kyrpides N, Mikhailova N, Marx C, Richardson P. Complete sequence of chromosome of Methylobacterium chloromethanicum CM4. DRAMP18356 MAGLLRFLLSKGRALYNWAKSHVGKVWEWLKSGATYEQIKEWIENALGWR 50 BacSP222 (bacteriocin) No entry found Not found Not found isolated from dog skin lesions, Staphylococcus pseudintermedius strain 222 Antibacterial, Mammalian cells, Antimicrobial Not found Not found 5LWC Fuction: No acitivtiy against two Gram-negative bacteria tested (see the article). N-terminal formylation is not needed for antibacterial effects since a synthetic peptide without this modification works better. Active against B. subtilis ATCC 6633 (MIC 0.16 uM), L. lactis subsp. lactis LOCK 0871 strain 239 (MIC 0.89 uM), M. luteus ATCC 4698 (MIC 0.11 uM), S. aureus DSM 26258 (CH91), S. aureus MRSA USA300 strain FPR3757, S. aureus KB/8658, S. aureus ATCC 25923 (MIC 0.89-1.3 uM), S. epidermidis ATCC 35547 (MIC 4.4 uM), S. intermedius ATCC 29663, S. intermedius R-2725 (MIC 1.2-2 uM), S. pseudintermedius 222, S. pseudintermedius LMG 22219 (MIC 2.1 and 0.16 uM), S. saprophyticus ATCC 15305 (MIC 0.93 uM), S. pyogenes PCM 465 (MIC 7.8 uM), S. sanguinis PCM 2335 (MIC 3.5 uM), and C. albicans ATCC 10231 (MIC 100 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26411997 Sci Rep. 2015 Sep 28;5:14569 Wladyka B, Piejko M, Bzowska M, Pieta P, Krzysik M, Mazurek ?, Guevara-Lora I, Bukowski M, Sabat AJ, Friedrich AW, Bonar E, Mi?dzobrodzki J, Dubin A, Mak P.2015 A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors DRAMP18255 VAGALGVQTAAATTIVNVILNAGTLVTVLGIIASIASGGAGTLMTIGWATFKATVQKLAKQSMARAIAY 69 Circularin A(Bacteriocin) Q8GB47 Belongs to the class IIc bacteriocin cirA Clostridium beijerinckii ATCC 25752 Antimicrobial, Antibacterial, Anti-Gram+ Not found nonmodified, head-to-tail-ligated cyclic antibacterial peptides digestion products of circularin A are not the cause of the residual antibacterial activity Gram-positive(broad) No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 12620847##14532033 Appl Environ Microbiol. 2003 Mar;69(3):1589-97.##Appl Environ Microbiol. 2003 Oct;69(10):5839-48. Kemperman R, Kuipers A, Karsens H, Nauta A, Kuipers O, Kok J.##Kemperman R, Jonker M, Nauta A, Kuipers OP, Kok J. Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574.##Functional analysis of the gene cluster involved in production of the bacteriocin circularin A by Clostridium beijerinckii ATCC 25752. DRAMP02558 MKVLVSFEIKFKTNKEKIISILKHFGFRRMQENLYFGDVEYDELYAMQSDIMENIREYDSILTIPICKSCYLKLNVFGRNLSFKDELYKIF 91 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) D3E4V5 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM13430 / M1) (Methanobacterium rumi Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 20126622 PLoS One. 2010 Jan 28;5(1):e8926. Leahy SC, Kelly WJ, Altermann E, Ronimus RS, Yeoman CJ, Pacheco DM, Li D, Kong Z, McTavish S, Sang C, Lambie SC, Janssen PH, Dey D, Attwood GT. The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions. DRAMP02559 MVVTVYLLIVYDVGVERVNRVKSYLRTELHWVQNSVFEGEVTESQFRRIETNLERIIDRERDSVIIYSFRSERAMNRNVLGLEKSPLDVIL 91 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) O27155 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /JCM 10044 / NBRC 100330 / Delt Antimicrobial, Antiviral Protein level Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 9371463##18482976 J Bacteriol. 1997 Nov;179(22):7135-7155.##J Biol Chem. 2008 Jul 18;283(29):20361-71. Smith DR, Doucette-Stamm LA, Deloughery C, Lee H, Dubois J, Aldredge T, Bashirzadeh R, Blakely D, Cook R, Gilbert K, Harrison D, Hoang L, Keagle P, Lumm W, Pothier B, Qiu D, Spadafora R, Vicaire R, Wang Y, Wierzbowski J, Gibson R, Jiwani N, Caruso A, Bush D, Reeve JN, et al.##Beloglazova N, Brown G, Zimmerman MD, Proudfoot M, Makarova KS, Kudritska M, Kochinyan S, Wang S, Chruszcz M, Minor W, Koonin EV, Edwards AM, Savchenko A, Yakunin AF Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.##A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats. DRAMP02560 MAEPRRWYLITYDIRDPKRWRKVHALLKGYGEWLQLSVFRCSLTDRDREKLRWELSRRMDAVDTLLVIGLCGGCVERVRAINAKEDWPEEPAPFKVL 97 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q1CW51 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Myxococcus xanthus (strain DK 1622) Antimicrobial, Antiviral Transcript level Not found Not found "Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). Induction: Part of an operon going from at least MXAN_7266 to MXAN_7259 that includes a CRISPR operon with transcription continuing into the pre-crRNA locus." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 17015832##17369305 Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15200-5.##J Bacteriol. 2007 May;189(10):3738-3750. Goldman BS, Nierman WC, Kaiser D, Slater SC, Durkin AS, Eisen JA, Ronning CM, Barbazuk WB, Blanchard M, Field C, Halling C, Hinkle G, Iartchuk O, Kim HS, Mackenzie C, Madupu R, Miller N, Shvartsbeyn A, Sullivan SA, Vaudin M, Wiegand R, Kaplan HB.##Viswanathan P, Murphy K, Julien B, Garza AG, Kroos L. Evolution of sensory complexity recorded in a myxobacterial genome.##Regulation of dev, an operon that includes genes essential for Myxococcus xanthus development and CRISPR-associated genes and repeats. DRAMP02561 MQYKINMYAIVVYDVNVSRQNQIREFLRKYLYHVQRSVFEGEISPSSLYYMKKILQSYIGETDSLIIYVLRDKSCLMDKIVLGEDKDLQIY 91 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q74N46 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Nanoarchaeum equitans (strain Kin4-M) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 14566062 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12984-8. Waters E, Hohn MJ, Ahel I, Graham DE, Adams MD, Barnstead M, Beeson KY, Bibbs L, Bolanos R, Keller M, Kretz K, Lin X, Mathur E, Ni J, Podar M, Richardson T, Sutton GG, Simon M, Soll D, Stetter KO, Short JM, Noordewier M. The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism. DRAMP02562 MYIVVVYDVGVERVNKVKKFLRMHLNWVQNSVFEGEVTLAEFERIKEGLKKIIDENSDSVIIYKLRSMPPRETLGIEKNPIEEII 85 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q8U1T8 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) Antimicrobial, Antiviral Protein level Combine helix and strand structure Not found 2I0X resolved by X-ray. Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 10430560##PubMed ID is not availbale Genetics. 1999 Aug;152(4):1299-1305.##Submitted (AUG-2006) to the PDB data bank. Maeder DL, Weiss RB, Dunn DM, Cherry JL, González JM, DiRuggiero J, Robb FT.##Chen LQ, Fu ZQ, Hwang J, Chang J, Chen L, Wang Y, Zhang H, Liu ZJ, Rose JP, WangBC. Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.##Crystal Structure of Hypothetical Protein Pf1117 from Pyrococcus furiosus. DRAMP02563 MYIIVVYDVSVERVNRVKKFLRQHLHWVQNSVFEGEVTLAEFERIKAGIGELIDGDEDSVVIYKLRSMPKREVMGVEKNPIEDII 85 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q5JD44 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Pyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)(Thermococcus kodakaraensis (strain Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 15710748 Genome Res. 2005 Mar;15(3):352-363. Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S, Imanaka T. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. DRAMP02564 MYVIMVYDVNEKRVAKILKIARKYLKWVQNSVLEGELSPGKYEKLKLEVSRLIDEKEDSVRFYVMDSQKVFNLETLGVEKGEDGFIF 87 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) Q9X2B6 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) Antimicrobial, Antiviral Protein level Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 10360571 Nature. 1999 May 27;399(6734):323-329. Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM. Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. DRAMP02565 MIVIVAYDISDEDRRGRLRRYLRRLGLARVNRSVYAGPGTATTAELVAERAKEIVEEGDSVFVIVVREDEYQRAHVFDGRDYYIVSERKYEVY 93 CRISPR-associated endoribonuclease Cas2 (Antiviral defensin) A1RZT9 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2 Thermofilum pendens (strain Hrk 5) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 18263724 J Bacteriol. 2008 Apr;190(8):2957-2965. Anderson I, Rodriguez J, Susanti D, Porat I, Reich C, Ulrich LE, Elkins JG, Mavromatis K, Lykidis A, Kim E, Thompson LS, Nolan M, Land M, Copeland A, Lapidus A, Lucas S, Detter C, Zhulin IB, Olsen GJ, Whitman W, Mukhopadhyay B, Bristow J, Kyrpides N. Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction. DRAMP18253 KYYGNGLSXNKKGXTVDWGTAIGIIGNNAAANXATGGAAGXNK 43 Piscicocin CS526(Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Carnobacterium piscicola CS526 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found In this study, we found that piscicocin CS526, which possessed YGNGL sequence, had anti-Listeria activity typical of class IIa bacteriocins. Accordingly, the presence of Val7 within the YGNGV7 motif could not be a prerequisite for the antimicrobial activity of class IIa bacteriocins. The bacteriocin piscicocin CS526 was inactivated by proteolytic enzymes, was stable at 100 Celsius degree for 30 min, had a pH range of 2 to 8, and was active against Enterococcus, Listeria, Pediococcus, and Leuconostoc. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15640235##15836484 Appl Environ Microbiol. 2005 Jan;71(1):554-7.##J Appl Microbiol. 2005;98(5):1146-51. Yamazaki K, Suzuki M, Kawai Y, Inoue N, Montville TJ.##Suzuki M, Yamamoto T, Kawai Y, Inoue N, Yamazaki K. Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526.##Mode of action of piscicocin CS526 produced by Carnobacterium piscicola CS526. DRAMP02567 MYILITYDVSTETEAGKKRLRKVAQVCKDFGQRVQKSVFECSVNEAQFEQLKHRLLQCIDEKSDSLRIYRLREPAKKYIQEYGVNLTIDFDAPLVL 96 CRISPR-associated endoribonuclease Cas2 1 (Antiviral defensin) Q2RL67 Belongs to the CRISPR-associated endoribonuclease Cas2 prote cas2-1 Moorella thermoacetica (strain ATCC 39073) Antimicrobial, Antiviral Homology Not found Not found Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 18631365 Environ Microbiol. 2008 Oct;10(10):2550-2573. Pierce E, Xie G, Barabote RD, Saunders E, Han CS, Detter JC, Richardson P, Brettin TS, Das A, Ljungdahl LG, Ragsdale SW. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). DRAMP02568 KGGYTRPISRPPYGGGYGNVCTSCHVLTTSQARSCCSRFGRCCVPRRGYSG 51 Penaeidin 3-1 Q7Z286 Not found PEN3-1 Fenneropenaeus chinensis (Fleshy prawn) (Penaeus chinensis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15123293 Fish Shellfish Immunol. 2004 Apr;16(4):513-525. Kang CJ, Wang JX, Zhao XF, Yang XM, Shao HL, Xiang JH. Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis. DRAMP02569 MRLVVCLVFLASFALVCQAQGYQGGYTRPFPRPPYGGGYHPVPVCTSCHRLSPLQARACCRQLGRCCDAKQTYG 74 Penaeidin Q6H2Z5 Not found PEN3a Penaeus monodon (Giant tiger prawn) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 20379756 Mar Biotechnol (NY). 2010 Oct;12(5):487-505. Tassanakajon A, Amparyup P, Somboonwiwat K, Supungul P. Cationic antimicrobial peptides in penaeid shrimp. DRAMP02570 YRGGYTGPIPRPPPIGRPPLRLVVCACYRLSVSDARNCCIKFGSCCHLVK 50 Penaeidin-1 (Pen-1; shrimps, Arthropods, animals) P81056 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. Tissue specificity: Higher expression in hemocytes and to a lesser extent in heart, testis, gills, intestine, lymphonoid organ and hepatopancreas. Traces in eyes and subcuticular epithelium. Not present in the brain. Developmental stage: Expression decreases 3 hours after microbial challenge to return to control levels after 12 hours and slightly increases after 24 hours. PTM: Contains three disulfide bonds 25-38; 27-45; 39-46." Gram-positive bacterium: Micrococcus luteus;##Gram-negative bacterium: Escherichia coli.##Fungi: Neurospora crassa, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 9353298##10639333 Biol Chem. 1997 Nov 7;272(45):28398-28406.##J Cell Sci. 2000 Feb;113 (Pt 3):461-469. Destoumieux D, Bulet P, Loew D, Van Dorsselaer A, Rodriguez J, Bachère E.##Destoumieux D, Muñoz M, Cosseau C, Rodriguez J, Bulet P, Comps M, Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda).##Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. DRAMP02571 YRGGYTGPIPRPPPIGRPPFRPVCNACYRLSVSDARNCCIKFGSCCHLVK 50 Penaeidin-2a (Pen-2a; shrimps, Arthropods, animals) P81057 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. Tissue specificity: Higher expression in hemocytes and to a lesser extent in heart, testis, gills, intestine, lymphonoid organ and hepatopancreas. Traces in eyes and subcuticular epithelium. Not present in the brain. Developmental stage: Expression decreases 3 hours after microbial challenge to return to control levels after 12 hours and slightly increases after 24 hours. PTM: Contains three disulfide bonds 24-38; 27-45; 39-46 and Lysine amide at position 50." Gram-positive bacterium: Micrococcus luteus;##Gram-negative bacterium: Escherichia coli.##Fungi: Neurospora crassa, Fusarium oxysporum, Saccharomyces cerevisiae TGY. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 11028917##9353298##10561573 Cell Mol Life Sci. 2000 Aug;57(8-9):1260-1271.##J Biol Chem. 1997 Nov 7;272(45):28398-28406.##Eur J Biochem. 1999 Dec;266(2):335-346. Destoumieux D, Munoz M, Bulet P, Bachère E.##Destoumieux D, Bulet P, Loew D, Van Dorsselaer A, Rodriguez J, Bachère E.##Destoumieux D, Bulet P, Strub JM, Van Dorsselaer A, Bachère E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda).##Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda).##Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. DRAMP02572 YRGGYTGPIPRPPPIGRPPLRPVCNACYRLSVSDARNCCIKFGSCCHLVK 50 Penaeidin-2b (Pen-2b; shrimps, Arthropods, animals) Q963C4 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 24-38; 27-45; 39-46 and lysine amide at K50." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02575 QVYKGGYTRPVPRPPPFVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYS 62 Penaeidin-3b (Pen-3b; shrimps, Arthropods, animals) P81059 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. Tissue specificity: Higher expression in hemocytes and to a lesser extent in heart, testis, gills, intestine, lymphonoid organ and hepatopancreas. Traces in eyes and subcuticular epithelium. Not present in the brain. Developmental stage: Expression decreases 3 hours after microbial challenge to return to control levels after 12 hours and slightly increases after 24 hours. PTM: Contains three disulfide bonds 32-47; 36-54; 48-55, Pyrrolidone carboxylic acid and Lysine amide at position 1 and 62 respectively." Gram-positive bacterium: Micrococcus luteus;##Gram-negative bacterium: Escherichia coli.##Fungi: Neurospora crassa, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 11028917##10639333 Cell Mol Life Sci. 2000 Aug;57(8-9):1260-1271.##J Cell Sci. 2000 Feb;113 (Pt 3):461-469. Destoumieux D, Munoz M, Bulet P, Bachère E.##Destoumieux D, Muñoz M, Cosseau C, Rodriguez J, Bulet P, Comps M, Bachère E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda).##Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. DRAMP02576 QVYKGGYTRPIPRPPFVRPVPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYS 61 Penaeidin-3c (Pen-3c; shrimps, Arthropods, animals) P81060 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. Tissue specificity: Higher expression in hemocytes and to a lesser extent in heart, testis, gills, intestine, lymphonoid organ and hepatopancreas. Traces in eyes and subcuticular epithelium. Not present in the brain. Developmental stage: Expression decreases 3 hours after microbial challenge to return to control levels after 12 hours and slightly increases after 24 hours. PTM: Contains three disulfide bonds 31-46; 35-53; 47-54, Pyrrolidone carboxylic acid and Lysine amide at position 1 and 62 respectively." Gram-positive bacterium: Micrococcus luteus;##Gram-negative bacterium: Escherichia coli.##Fungi: Neurospora crassa, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 11028917##10639333 Cell Mol Life Sci. 2000 Aug;57(8-9):1260-1271.##J Cell Sci. 2000 Feb;113 (Pt 3):461-469. Destoumieux D, Munoz M, Bulet P, Bachère E.##Destoumieux D, Muñoz M, Cosseau C, Rodriguez J, Bulet P, Comps M, Bachère E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda).##Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. DRAMP02577 QVYKGGYTRPIPRPPPFVRPLPGGPIGPYNGCPISCRGISFSQARSCCSRLGRCCHVGKGYS 62 Penaeidin-3d (Pen-3d; shrimps, Arthropods, animals) Q963D0 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 32-47; 36-54; 48-55, Pyrrolidone carboxylic acid and Serine amide at position 1 and 62 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP18252 GDVMPESTPICAGFATLMSSIGLVKTIKGKC 31 Carnolysin A2(Bacteriocin) W0FGJ7 Belongs to the lantibiotics family (Class I bacteriocin) crnA2 Carnobacterium maltaromaticum C2 Antimicrobial, Antibacterial, Anti-Gram+ Not found Altogether, there are six dehydrated ser or thr, and five thioether bonds in the two chains. For Carnolysin A1, residues 8, 10, and 25 are dehydrated; thioether bonds exist between residues 9, 13; 24,28; 41,45; residues 16, 21, 33, 36, are D-amino acids. For Carnolysin A2, residues 8, 16, and 20 are dehydrated; thioether bonds exist between 7, 11; 26, 31; residues 16 and 19 are D-amino acids, which is the first D-Abu in ribosomally synt Comment: No comments found on DRAMP database Gram-positive(broad) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24412962 Int J Food Microbiol. 2014 Mar 3;173:81-8. Tulini FL, Lohans CT, Bordon KC, Zheng J, Arantes EC, Vederas JC, De Martinis EC. Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2. DRAMP02580 QVYKGGYTRPIPRPPPFVRPLPGGPISPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYS 62 Penaeidin-3g (Pen-3g; shrimps, Arthropods, animals) Q963C7 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 32-47; 36-54; 48-55, Pyrrolidone carboxylic acid and Serine amide at position 1 and 62 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02581 QVYKGGYTRPIPRPPPFVRPLPGGPIGPYNGCPISCRGISFSQARSYCSRLGRCCHVGKGYS 62 Penaeidin-3h (Pen-3h; shrimps, Arthropods, animals) Q963C6 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains two disulfide bonds 36-54; 48-55, Pyrrolidone carboxylic acid and Serine amide at position 1 and 62 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02582 QVYKGGYTRPIPRPPPFVRPLPGGPIGPYNGRPVSCRGISFSQARSCCSRLGRCCHVGKGYS 62 Penaeidin-3i (Pen-3i; shrimps, Arthropods, animals) Q963C5 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains two disulfide bonds 36-54; 48-55, Pyrrolidone carboxylic acid and Serine amide at position 1 and 62 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02583 QVYKGGYTRPVPRPPFVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYS 61 Penaeidin-3j (Pen-3j; shrimps, Arthropods, animals) Q963D9 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 31-46; 35-53; 47-54, Pyrrolidone carboxylic acid and Serine amide at position 1 and 61 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02585 YSSGYTRPLPKPSRPIFIRPIGCDVCYGIPSSTARLCCFRYGDCCHR 47 Penaeidin-4c (Pen-4c; shrimps, Arthropods, animals) Q963C3 Belongs to the penaeidin family Not found Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity (By similarity). PTM: Contains three disulfide bonds 23-37; 26-44; 38-45 and C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02587 QGYKGPYTRPILRPYVRPVVSYNACTLSCRGITTTQARSCCTRLGRCCHVAKGYS 55 Penaeidin-3k (Pen-3k; shrimps, Arthropods, animals) Q962B2 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 25-40; 29-47; 41-48, Pyrrolidone carboxylic acid and Serine amide at position 1 and 55 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02588 QGYKGPYTRPILRPYVRPVVSYNVCTLSCRGITTTQARSCCTRLGRCCHVAKGYS 55 Penaeidin-3l (Pen-3l; shrimps, Arthropods, animals) Q962A8 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 25-40; 29-47; 41-48, Pyrrolidone carboxylic acid and Serine amide at position 1 and 55 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02589 QGCKGPYTRPILRPYVRPVVSYNACTLSCRGITTTQARSCCTRLGRCCHVAKGYS 55 Penaeidin-3m (Pen-3m; shrimps, Arthropods, animals) Q962B1 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity. Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains three disulfide bonds 25-40; 29-47; 41-48, Pyrrolidone carboxylic acid and Serine amide at position 1 and 55 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02590 QGYKGPYTRPILRPYVRPVVSYNACTLSCRGITTTQARSCSTRLGRCCHVAKGYS 55 Penaeidin-3n (Pen-3n; shrimps, Arthropods, animals) Q962B0 Belongs to the penaeidin family Not found Litopenaeus setiferus (Atlantic white shrimp) (Penaeus setiferus) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Posesses antibacterial and antifungal activity. Presents chitin-binding activity (By similarity). Subcellular location: Cytoplasmic granule. Note: Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. PTM: Contains two disulfide bonds 25-40; 29-47, Pyrrolidone carboxylic acid and Serine amide at position 1 and 55 respectively." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12242595 Immunogenetics. 2002 Sep;54(6):442-445. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. DRAMP02592 GXFGKAFXSVSNFAKKHKTA 20 Styelin-A (Styelin A; invertebrates, animals) P81469 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Bactericidal against several Gram-positive and Gram-negative bacteria. Tissue specificity: Hemocytes and pharyngeal tissues." Psychrobacter immobilis, Planococcus citreus No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9467865 Comp Biochem Physiol B Biochem Mol Biol. 1997 Nov;118(3):515-521. Lee IH, Cho Y, Lehrer RI. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. DRAMP02593 GXFGPAFHSVSNFAKKHKTA 20 Styelin-B (Styelin B; invertebrates, animals) P81470 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Bactericidal against several Gram-positive and Gram-negative bacteria. Tissue specificity: Hemocytes and pharyngeal tissues." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9467865 Comp Biochem Physiol B Biochem Mol Biol. 1997 Nov;118(3):515-521. Lee IH, Cho Y, Lehrer RI. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. DRAMP02594 GWFGKAFRSVSNFYKKHKTYIHAGLSAATLL 31 Styelin-C (Styelin C; chordates, animals) O18494 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial Homology Alpha helix Not found Function: Bactericidal against several Gram-positive and Gram- negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9257708 FEBS Lett. 1997 Jul 21;412(1):144-148. Zhao C, Liaw L, Lee IH, Lehrer RI. cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava. DRAMP02596 GWLRKAAKSVGKFYYKHKYYIKAAWKIGRHAL 32 Styelin-E (Styelin E; chordates, animals) O18496 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bactericidal against several Gram-positive and Gram- negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9257708 FEBS Lett. 1997 Jul 21;412(1):144-148. Zhao C, Liaw L, Lee IH, Lehrer RI. cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava. DRAMP02597 VFQFLGKIIHHVGNFVHGFSHVF 23 Clavanin-A (His-rich; chordates, animals) P80710, O18490 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix Not found Function: Has antimicrobial activity. Gram-negative bacterium: Escherichia coli;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9001389##9237689 FEBS Lett. 1997 Jun 30;410(2-3):490-492.##FEBS Lett. 1997 Jan 3;400(2):158-162. Lee IH, Zhao C, Cho Y, Harwig SSL, Cooper EL, Lehrer RI.##Zhao C, Lian H, Lee I.H, Lehrer R.I. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes.##cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes. DRAMP02598 VFQFLGRIIHHVGNFVHGFSHVF 23 Clavanin-B (His-rich; chordates, animals) P80711 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Antifungal Protein level Alpha helix Not found "Function: Has antimicrobial activity. PTM: C-terminal amidation." Escherichia coli, L. monocytes, Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9001389 FEBS Lett. 1997 Jan 3;400(2):158-162. Lee IH, Zhao C, Cho Y, Harwig SS, Cooper EL, Lehrer RI. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. DRAMP02599 VFHLLGKIIHHVGNFVYGFSHVF 23 Clavanin-C (His-rich; chordates, animals) O18493, P80712 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix Not found "Function: Has antimicrobial activity. Tissue specificity: Hemocytes and pharyngeal tissues." Gram-negative bacterium: Escherichia coli;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9001389##9237689 FEBS Lett. 1997 Jun 30;410(2-3):490-492.##FEBS Lett. 1997 Jan 3;400(2):158-162. Lee IH, Zhao C, Cho Y, Harwig SSL, Cooper EL, Lehrer RI.##Zhao C, Lian H, Lee I.H, Lehrer R.I. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes.##cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes. DRAMP02600 AFKLLGRIIHHVGNFVYGFSHVF 23 Clavanin-D (His-rich; chordates, animals) P80713, O18491 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix Not found "Function: Has antimicrobial activity. Tissue specificity: Hemocytes and pharyngeal tissues." Gram-negative bacterium: Escherichia coli;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9237689##9001389 FEBS Lett. 1997 Jun 30;410(2-3):490-492.##FEBS Lett. 1997 Jan 3;400(2):158-162. Zhao C, Liaw L, Lee IH, Lehrer RI.##Lee IH, Zhao C, Cho Y, Harwig SS, Cooper EL, Lehrer RI. cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes.##Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. DRAMP02601 LFKLLGKIIHHVGNFVHGFSHVF 23 Clavanin E (His-rich; chordates, animals) O18492 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Has antimicrobial activity. Gram-negative bacterium: Escherichia coli;##yeast Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9237689 FEBS Lett. 1997 Jun 30;410(2-3):490-492. Zhao C, Liaw L, Lee IH, Lehrer RI. cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes. DRAMP02602 FLRFIGSVIHGIGHLVHHIGVAL 23 Clavaspirin (chordates, animals) O97395 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix Not found Function: Has potent hemolytic activity. [Swiss_Prot Entry O97395]Exhibits broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria [Ref.12005415]has potent hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12005415 J Pept Res. 2001 Dec;58(6):445-456. Lee IH, Zhao C, Nguyen T, Menzel L, Waring AJ, Sherman MA, Lehrer RI. Clavaspirin, an antibacterial and haemolytic peptide from Styela clava. DRAMP18251 GDINGEFTTSPACVYSVMVVSKASSAKCAAGASAVSGAILSAIRC 45 Carnolysin A1(Bacteriocin) W0FC94 Belongs to the lantibiotics family (Class I bacteriocin) crnA1 Carnobacterium maltaromaticum C2 Antimicrobial, Antibacterial, Anti-Gram+ Not found Altogether, there are six dehydrated ser or thr, and five thioether bonds in the two chains. For Carnolysin A1, residues 8, 10, and 25 are dehydrated; thioether bonds exist between residues 9, 13; 24,28; 41,45; residues 16, 21, 33, 36, are D-amino acids. For Carnolysin A2, residues 8, 16, and 20 are dehydrated; thioether bonds exist between 7, 11; 26, 31; residues 16 and 19 are D-amino acids, which is the first D-Abu in ribosomally synt Comment: No comments found on DRAMP database Gram-positive(broad) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24412962 Int J Food Microbiol. 2014 Mar 3;173:81-8. Tulini FL, Lohans CT, Bordon KC, Zheng J, Arantes EC, Vederas JC, De Martinis EC. Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2. DRAMP02606 RLGNFFRKAKEKIGRGLKKIGQKIKDFWGNLVPRTES 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) Q1KLX5 Belongs to the cathelicidin family CAMP Trachypithecus cristatus (Silvered leaf-monkey) (Presbytis cristata) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02607 QLGDVLQKAGEKIVRGLKNIGQRIKDFFGKLTPRTES 37 Antibacterial protein LL-37 (AFRLL-37; cathelicidin; primates, mammals, animals) Q1KLY8, Q1KLY7 Belongs to the cathelicidin family CAMP Ateles fusciceps robustus (Colombian black-faced spider monkey) (Brown-headed spider monkey) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02608 RLGKFFRKVKKKIGGGLKKIGQKIKDFLGNLVPRTAS 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) Q1KLY6 Belongs to the cathelicidin family CAMP Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02610 VKGGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKKLEEGGNKDEDVSGPCPEPGWEAKSPGSSSTGCPQK 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2Y4 Not found WFDC12 Cercopithecus aethiops (Green monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 3 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02611 DHYNCVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; primates, mammals, animals) Q95J24 Belongs to the beta-defensin family DEFB1 Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) Unknown Homology Not found Not found Function: Has bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11862391 Immunogenetics. 2002 Feb;53(10-11):907-913. Del Pero M, Boniotto M, Zuccon D, Cervella P, Spano A,Amoroso A, Crovella S. Beta-defensin 1 gene variability among non-human primates. DRAMP02613 DSHEERRQGRHGHHEYGRKFHEKHHSHRGY 30 Mfa-hst 5 (M.fascicularis histatin 5; primates, mammals, animals) No entry found Not found Not found Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antifungal Not found Alpha helix (CD) Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20423320 Protein Pept Lett. 2010 Jul;17(7):909-918. Padovan L, Segat L, Pontillo A, Antcheva N, Tossi A, Crovella S. Histatins In Non-Human Primates: Gene Variations and Functional Effects. DRAMP02614 GLEFSEPFPSGRFAVCESCKLGRGKCRKECLENEKPDGSCRLNFLCCRPRM 51 Beta-defensin 105A (Defensin, beta 105; Defensin, beta 105A; primates, mammals, animals) A4H209 Belongs to the beta-defensin family DEFB105A Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02615 DHYNCVRSGGQCLYSACPIYTRIQGTCYHGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; primates, mammals, animals) P61261, A4H1Z6 Belongs to the beta-defensin family DEFB1 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16700051 Proteins. 2006 Aug 1;64(2):524-531. Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S. Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity. DRAMP02616 NLYVKRCLNDIGICKKTCKPEEVRSEHGWVMCGKRKACCVPAD 43 Beta-defensin 126 (Defensin, beta 126; Epididymal secretory protein 13.2, ESP13.2; primates, mamm Q9BEE3 Belongs to the beta-defensin family DEFB126 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). Tissue specificity: High-level and epididymis-specific expression. Detected in epithelial cells lining the efferent ductules, initial segment, and cauda regions of the epididymis, but not on spermatozoa. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10491631 Biol Reprod. 1999 Oct;61(4):965-972. Perry AC, Jones R, Moisyadi S, Coadwell J, Hall L. The novel epididymal secretory protein ESP13.2 in Macaca fascicularis. DRAMP02617 AIHRALICKRMEGHCEAECLTFEVKIGGCRAELTPYCCKKRKKD 44 Beta-defensin 107A (Defensin, beta 107; Defensin, beta 107A; primates, mammals, animals) A4H218 Belongs to the beta-defensin family DEFB107A Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Problely contains two disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02618 AYGGEKKCWNRSGHCRKQCKDGEAVKETCKNHRACCVPSNEDH 43 Beta-defensin 118 (Defensin, beta 118; primates, mammals, animals) A4H223 Belongs to the beta-defensin family DEFB118 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02619 KRHNLRCMGNSGICRASCKKNEQPYLYCRNYQACCLQSYMRISISGKEENTDWSYEKQWPRLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; Defensin, beta 120; primates, mammals, A4H228, A4H233 Belongs to the beta-defensin family DEFB119 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02620 ARLKKCFNNVTGYCRKKCKVGEIHEIGCLSGKLCCVNDEENKKHVPFKKPHQQPVEKLSVQQDYVILPTITIFTV 75 Beta-defensin 128 (Defensin, beta 128; primates, mammals, animals) A4H255 Belongs to the beta-defensin family DEFB128 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02621 GGSKCVSDTPGYCRTHCHRGETALFMCSPFRKCCISYSFLPQPDLPQLIGNHWPSRSRNTQRKNKKQQTTVTP 73 Beta-defensin 132 (Defensin, beta 132; primates, mammals, animals) A4H265 Belongs to the beta-defensin family DEFB132 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02622 RLGNFFRKVKEKIGGGLKKVGQKIKDFLGNLVPRTAS 37 Antibacterial protein LL-37 (primates, mammals, animals) Q1KLX7 Belongs to the cathelicidin family CAMP Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial Homology Not found Not found Function: Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02623 DSHEERHHGRHGHHKYGRKFHEKHHSHRGYRSNYLYDN 38 Macaque histatin (His-rich; M-Histatin 1; primates, mammals, animals) P34084 Belongs to the histatin family HTN1 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2229609 J Dent Res. 1990 Nov;69(11):1717-1723. Xu T, Telser E, Troxler RF, Oppenheim FG. Primary structure and anticandidal activity of the major histatin from parotid secretion of the subhuman primate, Macaca fascicularis. DRAMP02624 VKGGIEKAGVCPADNVRCFKSNPPQCHTDQDCLGERKCCYLHCGFKCVIPVKKLEEGGNKDEDVSGPHPEPGWEAKSPGSSSTGCPQI 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2P8 Not found WFDC12 Colobus guereza (Black-and-white colobus monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 2 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02625 VKGNIEKPEVCPADNVRCIKSDPPQCHTDQDCQGIRKCCYLHCGFKCVIPVKELEEGGNQDEDVSRPCP 69 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2W8 Not found WFDC12 Aotus nancymaae (Ma's night monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 5 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02626 VKGNTEKPGVCPADNVRCIKSDPPQCHTDQDCQGIRKCCYLHCGFKCVIPVKELEEGGSKDEDVSRPCPESGWEVKPPGFFSTRCPQK 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2X6 Not found WFDC12 Saimiri boliviensis boliviensis (Bolivian squirrel monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 6 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02627 DHYICVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; primates, mammals, animals) Q95M67 Belongs to the beta-defensin family DEFB1 Cercopithecus erythrogaster (Red-bellied monkey) (White-throated monkey) Antimicrobial, Antibacterial Homology Bridge Not found Function: Has bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11862391 Immunogenetics. 2002 Feb;53(10-11):907-913. Del Pero M, Boniotto M, Zuccon D, Cervella P, Spanò A, Amoroso A, Crovella S. Beta-defensin 1 gene variability among non-human primates. DRAMP18250 MACQCPDAISGWTHTDYQCHGLENKMYRHVYAICMNGTQVYCRTEWGSSC 50 Laterosporulin (Bacteriocin) H1ZZ98 Belongs to the class IId bacteriocin laterosporulin Brevibacillus sp. Strain GI-9 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Beta strand The crystal structure of LS at 2.0 A resolution reveals an all-bconformation of this peptide, with four beta-strands forming a twisted b-sheet. All six intrinsic cysteines are intramolecularly disulfide-bonded, with two disulfides constraining the N terminus of the peptide and the third disulfide crosslinking the extreme C terminus, resulting in the formation of a closed structure. Despite a low overall sequence similarity, LS has disul 4OZK resolved by X-ray This peptide is thermal stable, pH tolerant, and resistant to proteases. Reducing agent DTT had no effect on peptide activity or migration on gel. Gram-positive, Gram-negative (broad spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22403615##25345978 PLoS One. 2012;7(3):e31498. doi: 10.1371/journal.pone.0031498.##FEBS J. 2015 Jan;282(2):203-14. Singh PK, Chittpurna, Ashish, Sharma V, Patil PB, Korpole S.##Singh PK, Solanki V, Sharma S, Thakur KG, Krishnan B, Korpole S. Identification, purification and characterization of laterosporulin, a novel bacteriocin produced by Brevibacillus sp. strain GI-9.##The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module. DRAMP02630 GIGDPVTCLKNGAICHPVFCPRRYKQIGTCGLPGTKCCKKP 41 Rhesus monkey beta-defensin 2 (RhBD-2; Defensin, beta 2; primates, mammals, animals) Q9BDS9 Belongs to the beta-defensin family DEFB4A Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11238224 Clin Diagn Lab Immunol. 2001 Mar;8(2):370-375. Bals R, Lang C, Weiner DJ, Vogelmeier C, Welsch U, Wilson JM. Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. DRAMP18248 KYGDVPLY 8 Bifidin I(Bacteriocin) No entry found Belongs to the class IIa bacteriocin Not found Bifidobacterium infantis BCRC 14602 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found The N-terminal sequencing may also be blocked partially or totally which could be due to the structure of the peptide (circular) or N terminal capping. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Food Control. 2010 May;21(5):746-753. Cheikhyoussef A,Cheikhyoussef N,Chen HQ,Zhao JX,Tang J,Zhang H,Chen W. Bifidin I - A new bacteriocin produced by Bifidobacterium infantis BCRC 14602: Purification and partial amino acid sequence DRAMP18249 DWTFANWSCLVCDDCSVNLTV 21 Bac-GM100 (Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Brevibacillus brevis strain GM100 Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Not found The 21 N-terminal residues of Bac-GM100 displayed 65% homology with thurincin H from Bacillus thuringiensis. Bac-GM100 was extremely heat-stable and was stable within a pH range of 3-10. It proved sensitive to various proteases. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23291759 Biosci Biotechnol Biochem. 2013;77(1):151-60. Ghadbane M, Harzallah D, Laribi AI, Jaouadi B, Belhadj H. Purification and biochemical characterization of a highly thermostable bacteriocin isolated from Brevibacillus brevis strain GM100. DRAMP02632 QVTPVTKCWGKSGRCRTTCKKSEVYYILCKTEAKCCVDPKYVPVRSKLTDTNTSLESTSAV 61 Beta-defensin 121 (Defensin, beta 121; primates, mammals, animals) Q5J600 Belongs to the beta-defensin family DEFB121 Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Yashwanth R, Hamil K.G, Yenugu S, French F.S, Hall S.H. Differential expression of a primate beta defensin gene cluster specific to male reproductive tract. DRAMP02633 VGSIEKCWNFRGSCRDECLKNEKVYVFCMSGKLCCLKPKDQPHLPQRTKN 50 Beta-defensin 122 (Defensin, beta 122; primates, mammals, animals) Q5J5Z9 Belongs to the beta-defensin family DEFB122 Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Yashwanth R, Hamil K.G, Yenugu S, French F.S, Hall S.H. Differential expression of a primate beta defensin gene cluster specific to male reproductive tract. DRAMP02634 GTQRCWNLYGKCRHRCSKKERVYVYCLNNKMCCVKPKYQPKEKWWPF 47 Beta-defensin 123 (Defensin, beta 123; primates, mammals, animals) Q5J5D0 Belongs to the beta-defensin family DEFB123 Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Yashwanth R, Hamil K.G, Yenugu S, French F.S, Hall S.H. Differential expression of a primate beta defensin gene cluster specific to male reproductive tract. DRAMP02635 KRHILRCMGNSGICRASCKKNEQPYLYCRNYQACCLQSYMRISISGKEENTDWSYEKQWPRLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; Defensin, beta 120; primates, mammals, Q5J602, Q5J601 Belongs to the beta-defensin family DEFB119 Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. Yashwanth R, Hamil K.G, Yenugu S, French F.S, Hall S.H. Differential expression of a primate beta defensin gene cluster specific to male reproductive tract. DRAMP18246 GWVAXVGAXGTAALASGGV 19 Thuricin 439A,439B(Bacteriocin) No entry found Not found Not found Bacillus thuringiensis strain B439 Antimicrobial, Antibacterial, Anti-Gram+ Not found Based on its unique physical and biological characteristics we can conclude that thuricin 439 is a novel bacteriocin. The two active peptides are likely to be encoded by a single gene, whose product may undergo one or more post translational modifications that result in two active products of different molecular masses. Gram-positive (Narrow) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644238 FEMS Microbiol Lett. 2003 Mar 14;220(1):127-31. Ahern M, Verschueren S, van Sinderen D. Isolation and characterisation of a novel bacteriocin produced by Bacillus thuringiensis strain B439. DRAMP18247 DWTXWSXL 8 Bacthuricin F4(Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Bacillus thuringiensis subsp. kurstaki strain BUPM4 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found No proteins were shown to have similar sequences in either their N-terminal regions or any other region. This bacteriocin was heat-stable up to 70 degrees C and resisted up to pH 3.0. Bacthuricin F4 was sensitive to proteases demonstrating its proteinaceous nature. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752334 J Appl Microbiol. 2005;98(4):881-8. Kamoun F, Mejdoub H, Aouissaoui H, Reinbolt J, Hammami A, Jaoua S. Purification, amino acid sequence and characterization of Bacthuricin F4, a new bacteriocin produced by Bacillus thuringiensis. DRAMP02637 SARLGNFFRKVKEKIGGGLKKVGQKIKDFLGNLVPRTAS 39 Antibacterial protein FALL-39 (FALL-39 peptide antibiotic; primates, mammals, animals) Q9GLV5 Belongs to the histatin family CAMP Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial Transcript level Not found Not found Tissue specificity: Expressed in epithelia of various organs. Most abundant peptide levels are found in organs lining outer or inner body surfaces, such as organs of the respiratory or gastrointestinal tract. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 11238224 Clin Diagn Lab Immunol. 2001 Mar;8(2):370-375. Bals R, Lang C, Weiner DJ, Vogelmeier C, Welsch U, Wilson JM. Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. DRAMP02638 MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE 40 Liver-expressed antimicrobial peptide 2 (LEAP-2; primates, mammals, animals) Q95M25 Not found LEAP2 Macaca mulatta (Rhesus macaque) Antimicrobial Homology Not found Not found 2L1Q PTM: Contains two disulfide bonds 17-28; 23-33. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12493837 Protein Sci. 2003 Jan;12(1):143-152. Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-García JR, Forssmann WG, Schulz-Knappe P, Nehls MC, Wattler F, Wattler S, Adermann K. Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver. DRAMP02639 RCICVLGIC 9 Demidefensin-3 (primates, mammals, animals) Q9GLR2 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found "Function: Has antimicrobial activities against bacteria and fungi (By similarity). Subunit structure: Forms a cyclic homodimer; disulfide-linked (By similarity). PTM: This is a cyclic peptide (By similarity). Caution: The mature 9-residue peptide is expected to be found in 18-residue cyclopeptides produced by combinatorial peptide splicing either with itself or with other demidefensins. However among cyclopeptides screened for antimicrobial activity, no peptides that would have been produced from this sequence were detected." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11527997 J Leukoc Biol. 2001 Sep;70(3):461-464. Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI. Circular minidefensins and posttranslational generation of molecular diversity. DRAMP02640 RCLCRRGVC 9 Rhesus theta defensin-1/2 subunit B (RTD-1b; primates, mammals, animals) P82271 Belongs to the alpha-defensin family (Theta subfamily) RTD1B Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found PTM: contains one disulfide bond 4-9. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10521339##1152799##11675394 Science. 1999 Oct 15;286(5439):498-502.##J Leukoc Biol. 2001 Sep;70(3):461-464.##J Biol Chem. 2002 Feb 1;277(5):3079-3084. Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.##Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.##Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.##Circular minidefensins and posttranslational generation of molecular diversity.##Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. DRAMP02641 RCICTRGFC 9 Rhesus theta defensin-1/3 subunit A (RTD-1a; primates, mammals, animals) P82270, Q9TU01 Belongs to the alpha-defensin family (Theta subfamily) RTD1A Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found PTM: contains one disulfide bond 4-9. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10521339##1152799##11675394 Science. 1999 Oct 15;286(5439):498-502.##J Leukoc Biol. 2001 Sep;70(3):461-464.##J Biol Chem. 2002 Feb 1;277(5):3079-3084. Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.##Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.##Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.##Circular minidefensins and posttranslational generation of molecular diversity.##Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. DRAMP02642 GFCRCLCRRGVCRCICTR 18 Rhesus theta-defensin 1 (RTD-1; primates, mammals, animals) P82271, P82270, Q9TU01 Belongs to the alpha-defensin family (Theta subfamily) Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Beta strand (4 strands; 10 residues) Not found 1HVZ resolved by NMR. "Function: RTD-1 and RTD-2 have similar antimicrobial activities against the Gram-positive bacteria S. aureus 502A and L. monocytogenes, the Gram-negative bacterium S. typhimurium, and the fungi C. albicans 16820 and C. neoformans 271A. RTD-2 is 2-3-fold less active than RTD-1 against E. coli ML35. Subunit structure: RTD-1 is a cyclic heterodimer composed of subunits A and B; disulfide-linked. Tissue specificity: RTD-1 is expressed in bone marrow. Detected in promyelocytes, myelocytes and mature neutrophils and monocytes. Developmental stage: RTD-1 expression begins early during granulocyte myelopoiesis. PTM: Forms a cyclic peptide with 1 subunit B (RTD-2) or with 1 subunit A (RTD-1). An additional intersubunit disulfide bond is formed. Miscellaneous: RTD-1 is 10-fold more present in cells than RTD-2." Gram-positive bacteria: Staphylococcus aureus 502a and Listeria monocytogenes;##Gram-negative bacteria: Salmonella typhimurium, Escherichia coli ML35.##Fungi: Candida albicans 16820, Cryptococcus neoformans 271A (the activity of RTD-2 against Escherichia coli ML35 was 2-3-fold less than those of RTD-1 and RTD-3). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10521339##1152799##11675394 Science. 1999 Oct 15;286(5439):498-502.##J Leukoc Biol. 2001 Sep;70(3):461-464.##J Biol Chem. 2002 Feb 1;277(5):3079-3084. Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.##Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.##Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.##Circular minidefensins and posttranslational generation of molecular diversity.##Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. DRAMP02643 RCLCRRGVCRCLCRRGVC 18 Rhesus theta-defensin 2 (RTD-2; primates, mammals, animals) P82271 Belongs to the alpha-defensin family (Theta subfamily) Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: RTD-1 and RTD-2 have similar antimicrobial activities against the Gram-positive bacteria S. aureus 502A and L. monocytogenes, the Gram-negative bacterium S. typhimurium, and the fungi C. albicans 16820 and C. neoformans 271A. RTD-2 is 2-3-fold less active than RTD-1 against E. coli ML35. Subunit structure: RTD-2 is a cyclic homodimer composed of two subunits B; disulfide-linked. PTM: Forms a cyclic peptide with 1 subunit B (RTD-2) or with 1 subunit A (RTD-1). An additional intersubunit disulfide bond is formed. Miscellaneous: RTD-1 is 10-fold more present in cells than RTD-2." Gram-positive bacteria: Staphylococcus aureus 502a, Listeria monocytogenes; ##Gram-negative bacteria: Salmonella typhimurium, Escherichia coli ML35.##Fungi: Candida albicans 16820, Cryptococcus neoformans 271A (the activity of RTD-2 against Escherichia coli ML35 was 2-3-fold less than those of RTD-1 and RTD-3). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10521339##1152799##11675394 Science. 1999 Oct 15;286(5439):498-502.##J Leukoc Biol. 2001 Sep;70(3):461-464.##J Biol Chem. 2002 Feb 1;277(5):3079-3084. Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.##Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.##Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.##Circular minidefensins and posttranslational generation of molecular diversity.##Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. DRAMP02644 RCICTRGFCRCICTRGFC 18 Rhesus theta-defensin 3 (RTD-3; primates, mammals, animals) P82270, Q9TU01 Belongs to the alpha-defensin family (Theta subfamily) Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Bridge Not found "Function: RTD-1 and RTD-3 have similar antimicrobial activities against the Gram-positive bacteria, the Gram-negative bacteria and the fungi C. albicans 16820 and C. neoformans 271A. Subunit structure RTD-1 is a cyclic heterodimer composed of subunits A and B; disulfide-linked. RTD-3 is a cyclic homodimer composed of two subunits A; disulfide-linked. PTM: Forms a cyclic peptide with subunit A (RTD-3) or with subunit B (RTD-1). An additional intersubunit disulfide bond is formed. Miscellaneous: RTD-1 is 10-fold more present in cells than RTD-3." Gram-positive bacteria: Staphylococcus aureus 502a, Listeria monocytogenes;##Gram-negative bacteria: Salmonella typhimurium, Escherichia coli ML35.##Fungi: Candida albicans 16820, Cryptococcus neoformans 271A (the activity of RTD-2 against Escherichia coli ML35 was 2-3-fold less than those of RTD-1 and RTD-3). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10521339##1152799##11675394 Science. 1999 Oct 15;286(5439):498-502.##J Leukoc Biol. 2001 Sep;70(3):461-464.##J Biol Chem. 2002 Feb 1;277(5):3079-3084. Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.##Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.##Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.##Circular minidefensins and posttranslational generation of molecular diversity.##Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. DRAMP02645 GICRCICTRGFCRCICVL 18 Rhesus theta-defensin 4 (RTD-4; primates, mammals, animals) No entry found Belongs to the alpha-defensin family (Theta subfamily) Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: RTD-1 and RTD-5 are 3-fold more active than RTD-4. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21084627 J Leukoc Biol. 2011 Feb;89(2):283-290. Tongaonkar P, Tran P, Roberts K, Schaal J, Osapay G, Tran D, Ouellette AJ, Selsted ME. Rhesus macaque {theta}-defensin isoforms: expression, antimicrobial activities, and demonstration of a prominent role in neutrophil granule microbicidal activities. DRAMP02646 GICRCLCRRGVCRCICVL 18 Rhesus theta-defensin 5 (RTD-5; primates, mammals, animals) No entry found Belongs to the alpha-defensin family (Theta subfamily) Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Function: RTD-1 and RTD-5 are 3-fold more active than RTD-4. RTD-6 has not be collected due to the lack of activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21084627 J Leukoc Biol. 2011 Feb;89(2):283-290. Tongaonkar P, Tran P, Roberts K, Schaal J, Osapay G, Tran D, Ouellette AJ, Selsted ME. Rhesus macaque {theta}-defensin isoforms: expression, antimicrobial activities, and demonstration of a prominent role in neutrophil granule microbicidal activities. DRAMP02647 DPVTCLKNGAICHPVFCPRRYKQIGTCGLPGTKCCK 36 Beta-defensin 2 No entry found Not found Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP02648 GDFFRKSKEKIGKEFKRIVQRIKDFLRN 28 Cationic antimicrobial protein No entry found Not found Not found Macaca mulatta (Rhesus monkey) Antimicrobial Not found Not found Not found 2K6O Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Not found Not found Not found DRAMP02649 MKVFFLFAVLFCLVRRNSVHISHQEARGP 29 EP2B protein Q8SQD5 Not found EP2 Macaca mulatta (Rhesus monkey) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12606416 Biol Reprod. 2003 Jul;69(1):294-300. Fröhlich O, Ibrahim NM, Young LG. EP2 splicing variants in rhesus monkey (Macaca mulatta) epididymis. DRAMP02651 GDVPPGIRNTICLMQQGTCRLFFCHSGEKKRDICSDPWNRCCVSNRDEEGKEKPKTDGRSGI 62 Sperm associated antigen 11 isoform E (primates, mammals, animals) No entry found Not found Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15229135 Biol Reprod. 2004 Nov;71(5):1453-1460. Avellar MC, Honda L, Hamil KG, Yenugu S, Grossman G, Petrusz P, French FS, Hall SH. Differential expression and antibacterial activity of epididymis protein 2 isoforms in the male reproductive tract of human and rhesus monkey (Macaca mulatta). DRAMP02652 VKGGIEKAGVCPADNIRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKKLEEGGNKDEDVSGPCPEPGWEAKSPGSSSTGCPQK 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2T3 Not found WFDC12 Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 1 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02653 ACYCRIPACLAGERRYGTCFYLGRVWAFCC 30 Neutrophil defensin 1 (RMAD-1; primates, mammals, animals) P60030 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacterium: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02654 ACYCRIPACLAGERRYGTCFYMGRVWAFCC 30 Neutrophil defensin 2 (RMAD-2; primates, mammals, animals) P82317 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Has antibacterial and antifungal activiy. Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacterium: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02655 MRTFALLTAVLLVALQAQAGPLQARCDEAAGQEQPGVDDQDISISFAWDKISALQASGERGQYEEPQSLQGWMGDRLWNRVSMVHVT 87 Alpha defensin (primates, mammals, animals) Q6KFT8 Not found DEFA1 Macaca mulatta (Rhesus macaque) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019196 ptides. 2003 Nov;24(11):1647-1654. Nguyen TX, Cole AM, Lehrer RI. Evolution of primate theta-defensins: a serpentine path to a sweet tooth. DRAMP02656 MRTLAILAAILLFALLAQAKSLQETADDAATQEQPGEDDQDLAVSFEENGLSTLRASGSQARRTCRCRFGRCFRRESYSGSCNINGRIFSLCCR 94 Alpha-defensin 2 (primates, mammals, animals) Q9TTZ8 Not found MNP2 Macaca mulatta (Rhesus macaque) Antimicrobial Predicted Not found Not found 6KRA Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019196 Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Zhao C, Nguyen T, Lehrer RI. cDNA cloning of three alpha-defensins and three demidefensins from rhesus monkey bone marrow. DRAMP02657 MRTIAILAAILLFALLAQAKSLQETADEAATQEQPGEDDQDLAVSFEENGLSTLRDSGSQARRTCRCRIRRCRGLESSFGNCILHGQFAKLCCR 94 Alpha-defensin 1 (primates, mammals, animals) Q5I2Q2 Not found Not found Macaca mulatta (Rhesus macaque) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14977952 Infect Immun. 2004 Mar;72(3):1470-1478. Tanabe H, Yuan J, Zaragoza MM, Dandekar S, Henschen-Edman A, Selsted ME, Ouellette AJ. Paneth cell alpha-defensins from rhesus macaque small intestine. DRAMP02658 MRTLTILAAILLFALLAQAKSLQETADDAATQEQPGEDDQDLAVSFEENGLSTLRASGSQARRNCHCRIGHCRRPAAPMGVCIIHGQFGKLCCR 94 Alpha-defensin 6 (primates, mammals, animals) Q5I2P7 Not found Not found Macaca mulatta (Rhesus macaque) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14977952 Infect Immun. 2004 Mar;72(3):1470-1478. Tanabe H, Yuan J, Zaragoza MM, Dandekar S, Henschen-Edman A, Selsted ME, Ouellette AJ. Paneth cell alpha-defensins from rhesus macaque small intestine. DRAMP02659 ACYCRIPACLAGERRYGTCFYRRRVWAFCC 30 Neutrophil defensin 3 (RMAD-3; primates, mammals, animals) P60031, P82318 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bacteriostatic and antifungal activity. PTM: Contains three disulfide bonds: 2-30; 4-19; 9-29." Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacteria: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02660 RRTCRCRFGRCFRRESYSGSCNINGRIFSLCCR 33 Neutrophil defensin 4 (RMAD-4; primates, mammals, animals) P82319 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found 6KRA "Function: Defensins 4 has bacteriostatic and antifungal activity. PTM: Contains three disulfide bonds 4-32; 6-21; 11-31." Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacteria: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02661 RTCRCRFGRCFRRESYSGSCNINGRIFSLCCR 32 Neutrophil defensin 5 (RMAD-5; primates, mammals, animals) P82319 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found 6KRA "Function: Defensins 5 has bacteriostatic and antifungal activity. PTM: Contains three disulfide bonds 3-31; 5-20; 10-30." Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacteria: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02662 RRTCRCRFGRCFRRESYSGSCNINGRISSLCCR 33 Neutrophil defensin 6 (RMAD-6; primates, mammals, animals) P82320 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Defensins 6 has bacteriostatic and antifungal activity. PTM: Contains three disulfide bonds 65-93; 67-82; 72-92." Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacteria: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02663 RTCRCRFGRCFRRESYSGSCNINGRISSLCCR 32 Neutrophil defensin 7 (RMAD-7; primates, mammals, animals) P82320 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Defensins 7 has bacteriostatic and antifungal activity. PTM: Contains three disulfide bonds 65-93; 67-82; 72-93." Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes;##Gram-negative bacteria: Escherichia coli.##Fungi: Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02664 ACYCRIPACLAGERRYGTCFYLRRVWAFCC 30 Neutrophil defensin 8 (RMAD-8; primates, mammals, animals) P60032, P82318 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Antifungal Homology Bridge Not found "Function: Probable antibiotic and antifungal activity. PTM: Contains three disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531277 Infect Immun. 1999 Nov;67(11):6139-6144. Tang YQ, Yuan J, Miller CJ, Selsted ME. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. DRAMP02665 EPLQARADEMPAQKQPPADDQDVVIYFSGDDSSSLQVPGSTKGLICHCRVLYCLFGEHLGGTSFIHGERYPICCY 75 Defensin-7 (Defensin, alpha 7; primates, mammals, animals) Q5G859 Not found DEFA7 Pan troglodytes (chimpanzee) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). Miscellaneous: The human orthologous protein seems not to exist, its coding region does not have a start codon. PTM: Problely contains two disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP02666 VKEDIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRPYPEPGWEAKCPGSSSTRCPQK 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2P0 Not found WFDC12 Pan troglodytes (chimpanzee) Antimicrobial, Antibacterial Homology Not found Not found PTM: Contains four disulfide bonds 11-39; 18-43; 26-38; 32-47. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02668 STRAFTCHCRRSCYSTEYSYGTCTVMGINHRFCCL 35 Defensin-6 (Defensin, alpha 6; primates, mammals, animals) Q5G860 Belongs to the alpha-defensin family DEFA6 Pan troglodytes (chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains three disulfide bonds 4-31; 6-20; 10-30. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP02669 ACYCRIPACLAGERRYGTCIYQGRLWAFCC 30 Neutrophil defensin 1 (Defensin, alpha 1; primates, mammals, animals) Q5G863 Belongs to the alpha-defensin family DEFA1 Pan troglodytes (chimpanzee) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Bridge Not found MOA: Defensins are thought to kill microbes by permeabilizing their plasma membrane. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Epub 2004 Oct 19. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP02670 VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRVD 34 Neutrophil defensin 4 (Defensin, alpha 4; primates, mammals, animals) Q5G862 Belongs to the alpha-defensin family DEFA4 Pan troglodytes (chimpanzee) Antimicrobial, Antibacterial, Antifungal Homology Bridge Not found 1ZMM Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Inhibits corticotropin (ACTH)-stimulated corticosterone production. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP02671 DHYNCVSSGGQCLYSACPIFTKIQGTCYGGKAKCCK 36 Beta-defensin 1 (BD-1; primates, mammals, animals) P60023, A4H1Z2, Q09753, Q95M69, Q95M68 Belongs to the beta-defensin family DEFB1 Pan troglodytes (Chimpanzee); also Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Problely has antimicrobial activity. PTM: Problely contains three disulfide bonds 5-34; 12-27; 17-35. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11862391##11168821 Immunogenetics. 2002 Feb;53(10-11):907-913.##J Med Primatol. 2000 Oct;29(5):318-323. Del Pero M, Boniotto M, Zuccon D, Cervella P, Spanò A, Amoroso A, Crovella S.##Duits LA, Langermans JA, Paltansing S, van der Straaten T, Vervenne RA, Frost PA, Hiemstra PS, Thomas AW, Nibbering PH. Beta-defensin 1 gene variability among non-human primates.##Expression of beta-defensin-1 in chimpanzee (Pan troglodytes) airways. DRAMP02672 GISDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP 41 Beta-defensin 4A (Beta-defensin 2, BD-2; primates, mammals, animals) Q9TT12 Belongs to the beta-defensin family DEFB4A Pan troglodytes (Chimpanzee) Antimicrobial Homology Bridge Not found "Function: Problely has antimicrobial activity. PTM: Problely contains three disulfide bonds 8-37; 15-30; 20-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Duits LA, Langermans JAM, van der Straaten T, Vervenne RAW, Paltansing S, Frost PA, Hiemstra PS, Thomas AW, Nibbering PH. Expression of beta-defensin-2 in chimpanzee (Pan troglodytes). DRAMP02673 GIINTLQKYYCRVRGGRCAVLTCLPKEEQIGKCSTRGRKCCRRKK 45 Beta-defensin 103A (Beta-defensin 3, BD-3; primates, mammals, animals) Q95JD2, A4H1Z8, Q30KM2, Q5IAC2 Belongs to the beta-defensin family DEFB103A Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria. PTM: Problely contains three disulfide bonds 11-40; 18-33; 23-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15904491 Physiol Genomics. 2005 Sep 21;23(1):5-17.##BMC Evol Biol. 2005 May 18;5:32. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Semple CAM, Maxwell A, Gautier P, Kilanowski FM, Eastwood H, Barran PE, Dorin JR. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. The complexity of selection at the major primate beta-defensin locus. DRAMP18245 SLGVTLGAAGVYTATQTIATQIWKCGAVLTTSAECSRTGKSC 42 Ticin A4(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus thuringiensis BMB3201 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Comment: Active against the tested Gram-positive bacteria, including B. amyloliquefaciens, B. cereus, B. firmus, B. thuringiensis, B. subtilis, B. pumilus, E. faecalis, L. monocytogenes, Microbacterium, Paenibacillus, S. aureus, and S. sciuri. However, they are more active against food-borne pathogens such as B. cereus and L. monocytogenes. Chemical modifications such as dehydration are to be determined. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26231642 Appl Environ Microbiol. 2015 Oct;81(20):6964-72. Xin B, Zheng J, Xu Z, Li C, Ruan L, Peng D, Sun M. Three Novel Lantibiotics, Ticins A1, A3, and A4, Have Extremely Stable Properties and Are Promising Food Biopreservatives. DRAMP02675 GLDFSQPFPSGEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFLCCRQRI 51 Beta-defensin 105A (Beta-defensin 5, BD-5; primates, mammals, animals) Q5IAB6, A4H205, Q30KM0 Belongs to the beta-defensin family DEFB105A Pan troglodytes (Chimpanzee) Antimicrobial Homology Bridge Not found "Function: Problely has antimicrobial activity. PTM: Problely contains three disulfide bonds 16-47; 26-40; 30-46." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15904491##16033865 BMC Evol Biol. 2005 May 18;5:32.##Physiol Genomics. 2005 Sep 21;23(1):5-17. Semple CA, Maxwell A, Gautier P, Kilanowski FM, Eastwood H, Barran PE, Dorin JR.##Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. The complexity of selection at the major primate beta-defensin locus.##Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02676 FFDEKCNKLKGTCKNNCGKNEELIALCQKSLKCCRTIQPCGSIID 45 Beta-defensin 106A (Beta-defensin 6, BD-6; primates, mammals, animals) Q5IAB3, A4H210, Q30KL9 Belongs to the beta-defensin family DEFB106A Pan troglodytes (Chimpanzee) Antimicrobial Homology Bridge Not found "Function: Problely has antimicrobial activity. PTM: Problely contains three disulfide bonds 6-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15904491##16033865 BMC Evol Biol. 2005 May 18;5:32.##Physiol Genomics. 2005 Sep 21;23(1):5-17. Semple CA, Maxwell A, Gautier P, Kilanowski FM, Eastwood H, Barran PE, Dorin JR.##Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. The complexity of selection at the major primate beta-defensin locus.##Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02677 AIHRALISKRMEGHCEAECLTFEVKTGGCRAELAPFCCKNRKKH 44 Beta-defensin 107A (Beta-defensin 7; BD-7, DEFB-7, cBD-7; primates, mammals, animals) Q5IAA9, A4H214, Q30KL8 Belongs to the beta-defensin family DEFB107A Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains two disulfide bonds 15-29; 19-38. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15904491 Physiol Genomics. 2005 Sep 21;23(1):5-17.##BMC Evol Biol. 2005 May 18;5:32. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Semple C.A.M, Maxwell A, Gautier P, Kilanowski F.M, Eastwood H, Barran P.E, Dorin J.R. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. The complexity of selection at the major primate beta-defensin locus. DRAMP02678 KFKEICERPDGSCRDFCLETEIHVGRCLNSRPCCLPLGHQPRIESTTPKKD 51 Beta-defensin 108B (Beta-defensin 8; BD-8, DEFB-8, hBD-8; primates, mammals, animals) Q5IAA6 Belongs to the beta-defensin family DEFB108B Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found PTM: contains three disulfide bonds 6-33; 13-27; 17-34. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15904491 BMC Evol Biol. 2005 May 18;5:32. Semple C.A.M, Maxwell A, Gautier P, Kilanowski F.M, Eastwood H, Barran P.E, Dorin J.R. The complexity of selection at the major primate beta-defensin locus. DRAMP02679 GLGPAEGHCLNLSGVCRRDVCKVVEDQIGACRRRMKCCRAWWILMPIPTPLIMSDYQEPLKRKLK 65 Beta-defensin109 (Defensin, beta 109; Defensin, beta 109; primates, mammals, animals) Q30KL7 Belongs to the beta-defensin family DEFB109 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (By similarity). PYM: Problely contrains three disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02680 KMKYPEYGSLDLRRECRMGNGRCKNQCHENEIRIAYCIRPGTHCCLQQ 48 Beta-defensin 110 (Defensin, beta 110; Beta-defensin 111; primates, mammals, animals) Q30KL6 Belongs to the beta-defensin family DEFB110 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains three disulfide bonds 16-44; 23-37; 27-45. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02681 GPSVPQKKTREVAEKKRECQLVRGACKPECNSWEYVYYYCNVNPCCVVQEYQKPIINKITSKLHQK 66 Beta-defensin 113 (Defensin, beta 113; primates, mammals, animals) Q30KL4 Belongs to the beta-defensin family DEFB113 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 19-45; 26-40; 30-46." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02682 GLFRSHNGKSREPWNPCELYQGMCRNACREYEIQYLTCPNDQKCCLKLSVKITSSKNVKEDYDSNSNLSVTNSSSYSHI 79 Beta-defensin 116 (Defensin, beta 116; primates, mammals, animals) Q30KL1 Belongs to the beta-defensin family DEFB116 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 17-44; 24-38; 28-45." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02683 QVTPVMKCWGKSGRCRTTCKESEVYYILCKTEAKCCVDPKYVPVKPKLTDRNTSLESTSAV 61 Beta-defensin 121 (Defensin, beta 121; primates, mammals, animals) Q30KK6 Belongs to the beta-defensin family DEFB121 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 8-35; 15-29; 19-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02684 EFKRCWKGQGACRTYCTRQETYMHLCPDASLCCLSYALKPPPVPKHEYE 49 Beta-defensin 124 (Defensin, beta 124; Defensin, beta 126; primates, mammals, animals) Q30KK4 Belongs to the beta-defensin family DEFB124 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 5-32; 12-26; 16-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02685 VKCAVKDTYSCFIVRGKCRHECHDFEKPIGFCTKLNANCYM 41 Beta-defensin 133 (Defensin, beta 133; primates, mammals, animals) Q30KJ6 Belongs to the beta-defensin family DEFB133 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains two disulfide bonds 11-39; 18-32." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02686 EMHKKCYKNGICRLECYESEMLVAYCMFQLECCVKGNPAP 40 Beta-defensin 134 (Defensin, beta 134; primates, mammals, animals) Q30KJ5 Belongs to the beta-defensin family DEFB134 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 6-32; 12-26; 16-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02687 GPNVYIQKIFASCWRLQGTCRPKCLKNETISYFGVILYICGCVNPKYLPILTGK 54 Beta-defensin 135 (Defensin, beta 135; primates, mammals, animals) Q30KJ4 Belongs to the beta-defensin family DEFB135 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains two disulfide bonds 13-40; 24-42." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02688 MFGNDGVKVRTCTSQKAVCFFGCPPGYRWIAFCHNILSCCKNMTRFQPLQAKDPWVH 57 Beta-defensin 136 (Defensin, beta 136; primates, mammals, animals) Q30KJ3 Belongs to the beta-defensin family DEFB136 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 12-39; 19-33; 23-40." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02689 AYSGEKKCWNRSGHCRKQCKDGEAVKDTCKNLRACCVPSNEDH 43 Beta-defensin 118 (Defensin, beta 118; primates, mammals, animals) Q30KK9, A4H219 Belongs to the beta-defensin family DEFB118 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 8-35; 15-29; 19-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02690 KRHILRRMGNSGICRASCKKNEQPYLYCRNYQSCCLQSYMRISISGKEENTDWSYEKQWPRLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; primates, mammals, animals) Q30KK8, A4H224, A4H229, Q30KK7 Belongs to the beta-defensin family DEFB119 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains two disulfide bonds 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02691 GTQRCWNLYGKCRYRCSKKERVYVYCINNKMCCVKPKYQPKERWWPF 47 Beta-defensin 123 (Defensin, beta 123; primates, mammals, animals) Q30KK5, A4H234 Belongs to the beta-defensin family DEFB123 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 5-32; 12-26; 16-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02692 NWYVKKCLNDVGICKKKCKPGEMHIKNGWATCGKQRDCCVPAD 43 Beta-defensin 126 (Defensin, beta 126; primates, mammals, animals) Q30KK2, A4H242 Belongs to the beta-defensin family DEFB126 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 7-37; 14-32; 18-39." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02693 LKKCWNNYVQGHCRKICRVNEVPEALCENGRYCCLNIKELEAC 43 Beta-defensin 127 (Defensin, beta 127; primates, mammals, animals) Q30KK1 Belongs to the beta-defensin family DEFB127 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 5-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02694 GVIPGQKQCIALKGVCRDKLCSTLDDTIGICNEGKKCCRRWWILEPYPTPVPKGKSP 57 Beta-defensin 130 (Defensin, beta 130; primates, mammals, animals) Q30KJ9 Belongs to the beta-defensin family DEFB130 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains two disulfide bonds 16-31; 21-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02695 FISNDECPSEYYYHCRLKCNADEHAIRYCADFSICCKLKIIEIHGQKKW 49 Beta-defensin 131 (Defensin, beta 131; primates, mammals, animals) Q30KJ8 Belongs to the beta-defensin family DEFB131 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 7-35; 15-29; 19-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02696 GGSKCVSNTPGYCRTYCHWGETALFMCNASRKCCVSYSFLPKADLPRLIGNHWQSRRRNTQRKDKKQQTTVTS 73 Beta-defensin 132 (Defensin, beta 132; primates, mammals, animals) Q30KJ7, A4H261 Belongs to the beta-defensin family DEFB132 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 5-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##PubMed ID is not available Physiol Genomics. 2005 Sep 21;23(1):5-17.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Hollox EJ, Armour JAL. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Evolution and sequence variation of human beta-defensin genes. DRAMP02697 ESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRIGHCTILESLSGVCEISGRLYRLCCR 75 Defensin-5 (Defensin, alpha 5; primates, mammals, animals) Q5G861 Not found DEFA5 Pan troglodytes (Chimpanzee) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing (By similarity). Subcellular location: Secreted. Cytoplasmic vesicle › secretory vesicle (By similarity). Note: Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are detected intracellularly. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP02698 RRTCHCRSRCLRRESNSGSCNINGRIFSLCCR 32 Rhesus macaque oral alpha-defensins (ROADs; primates, mammals, animals) B5AKV3 Belongs to the alpha-defensin family Not found Macaca mulatta (Rhesus monkey) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand (3 strands; 19 residues) NMR spectroscopy shows that Synthetic ROAD-1 adopts the canonical disulfide pairing and alpha-defensin fold. 2K1I resolved by NMR. "Function: ROAD-1 is active against Staphylococcus aureus, Escherichia coli, and Candida albicans in a concentration-dependent manner. The antimicrobial mechanism of defensins has been correlated with their ability to disrupt and permeabilize the cell envelope, activities that depend on the surface features of the folded peptide. PTM: Contains three disulfide bonds." Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli.##Fungi: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys4 and Cys31; Cys6 and Cys20; Cys10 and Cys30. L No cytotoxicity information found Not found 18930922 J Biol Chem. 2008 Dec 19;283(51):35869-35877. Vasudevan S, Yuan J, Osapay G, Tran P, Tai K, Liang W, Kumar V, Selsted ME, Cocco MJ. Synthesis, structure, and activities of an oral mucosal alpha-defensin from rhesus macaque. DRAMP02699 VKEGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRP 67 WAP four-disulfide core domain protein 12 (primates, mammals,animals) A4K2R5 Not found WFDC12 Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP02700 AIHRALICKRMEGHCEAECLTFEAKIGGCRAELAPFCCKNRKKH 44 Beta-defensin 107A (Defensin, beta 107; Defensin, beta 107A; primates, mammals,animals) A4H215 Belongs to the beta-defensin family DEFB107A Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains two disulfide bonds 15-29; 19-38. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP18244 SLGVTLGAAGVYTATQTIATQIWKCGAVLTTSAECSRTGNSC 42 Ticin A3(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus thuringiensis BMB3201 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Activity spectrum is similar to Ticin A4. Chemical modifications such as dehydration are to be determined. Chemical modifications such as dehydration are to be determined. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26231642 Appl Environ Microbiol. 2015 Oct;81(20):6964-72. Xin B, Zheng J, Xu Z, Li C, Ruan L, Peng D, Sun M. Three Novel Lantibiotics, Ticins A1, A3, and A4, Have Extremely Stable Properties and Are Promising Food Biopreservatives. DRAMP02702 KRHILRCMGNSGICRASCKKNEQPYLYCRNYQSCCLQSYMRISISGKEEDTDWSYEKQWPRLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; primates, mammals,animals) A4H225, A4H230 Belongs to the beta-defensin family DEFB119 Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 7-34; 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP18243 SLGVTLGAAGLYTATQTIATQIWKCGAVLTTSAECSRTGNSC 42 Ticin A1(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus thuringiensis BMB3201 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Activity spectrum is similar to Ticin A4. Chemical modifications such as dehydration are to be determined. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26231642 Appl Environ Microbiol. 2015 Oct;81(20):6964-72. Xin B, Zheng J, Xu Z, Li C, Ruan L, Peng D, Sun M. Three Novel Lantibiotics, Ticins A1, A3, and A4, Have Extremely Stable Properties and Are Promising Food Biopreservatives. DRAMP02704 NWYVKKCLNDVGICKKKCKPEEMHVKNGWAMCGKQRDCCVPAD 43 Beta-defensin 126 (Defensin, beta 126; primates, mammals,animals) A4H243 Belongs to the beta-defensin family DEFB126 Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains three disulfide bonds 7-38; 14-32; 18-39." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02705 GGSKCVSNTPAYCRTYCHWGETALFMFNASRKCCISYSFLPKPDLPQLIGNHWQSRRNTQRKDKKQQTTVTS 72 Beta-defensin 132 (Defensin, beta 132; primates, mammals,animals) A4H262 Belongs to the beta-defensin family DEFB132 Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Contains two disulfide bonds 5-33; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02706 EFELDRICGYGTARCRKKCRSQEYRIGRCPNTFACCLRKWDESLLNRTKP 50 Beta-defensin 104A (Defensin, beta 104; Defensin, beta 104A; primates, mammals, animals) A4H202 Belongs to the beta-defensin family DEFB104A Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP18242 EKYTEVPEYV 10 Fengycin B2 (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus thuringiensis Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found K2 is Orn. The C-terminal V forms an ester bond with the side chain of Y3. Fuction: Active against fungi C. Albicans and A.niger. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24312083##22847390 Front Microbiol. 2013 Nov 21;4:332.##J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31. Roy A, Mahata D, Paul D, Korpole S, Franco OL, Mandal SM.##Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1.##Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins. DRAMP02709 LLGDFFRKAKEKIGKESKRIVQRIKDFLRNLVPRTES 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) Q1KLY3 Belongs to the cathelicidin family CAMP Gorilla gorilla gorilla (Lowland gorilla) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP18240 EKYTEIPEYV 10 Fengycin C(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis K1 Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found K2 is Orn. Comment: No comments found on DRAMP database Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22847390 J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31. Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins. DRAMP18241 TWATIGKTIVQSVKKCRTFTCGCSLGSCSNCN 32 Subtilomycin(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) subA Bacillus subtilis MMA7 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found There are extensive post-translational modifications: T1, T4 and T8 are dehydrated into Dhb. The N-terminal Dhb was unstable and further oxidized by deamination into 2-oxo butyrate. In addition, thioether or methylthioether bonds occur between the following residue pairs: S11-C15, T17-C21, T20-C23, S24-C28, and S27-C31. Therefore the most likely sequence for the lantibiotic is Dhb*-W-A-Dhb-I-G-K-Dhb-I-V-Q-Dha-V-K-K-C-R-Dhb-F-Dhb-C-G-C-Dha-L-G-Dha-C-Dha-N-C-N, where the underlined amino acids have been experimentally confirmed by mass spectrometric analysis and the subsequent sequence predicted from the genomic sequence of strain MMA7. Gram-positive, Gram-negative (broad spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23736764 Mar Drugs. 2013 Jun 3;11(6):1878-98. Phelan RW, Barret M, Cotter PD, O'Connor PM, Chen R, Morrissey JP, Dobson AD, O'Gara F, Barbosa TM. Subtilomycin: a new lantibiotic from Bacillus subtilis strain MMA7 isolated from the marine sponge Haliclona simulans. DRAMP18239 EKYTEAPEYV 10 Fengycin A2(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis K1 Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found K2 is Orn. The C-terminal V forms an ester bond with the side chain of Y3. Comment: No comments found on DRAMP database Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22847390 J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31. Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins. DRAMP18238 EKYTEVPEYI 10 Fengycin B(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis K1 Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found K2 is Orn. The structure consists of a cyclic peptide lactone formed between the phenolic -OH of Tyr3 and the C-terminal -COOH of an amino acid at position 10. The N-terminus of the decapeptide segment is acylated with a beta-hydroxy fatty acid (beta-OH FA). Comment: No comments found on DRAMP database Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22847390 J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31. Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins. DRAMP02713 DTHFPIYIFCCGCCHRSKCGMCCKT 25 Hepcidin (primates, mammals, animals) Q5NVR8 Belongs to the glycosyl hydrolase 22 family HAMP Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains three disulfide bonds 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases The German cDNA consortium Unknown DRAMP02714 LLGDFFRKAREKIGEEFKRIVQRIKDFLRNLVPRTES 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals,animals) Q1KLX2 Belongs to the beta-defensin family CAMP Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Not found Not found Function: Problrly has antibacterial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharides (LPS) 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02715 FFDEKCGKLKGTCKNNCGKNEELIALCQKSLKCCRTIQPCGSIID 45 Beta-defensin 106A (Defensin, beta 106; Defensin, beta 106A; primates, mammals,animals) A4H212 Belongs to the beta-defensin family DEFB106A Pongo pygmaeus (Bornean orangutan) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02716 GLDFSQPFPSDEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFLCCRERI 51 Beta-defensin 105A (Defensin, beta 105; Defensin, beta 105A; primates, mammals,animals) A4H207 Belongs to the beta-defensin family DEFB105A Pongo pygmaeus (Bornean orangutan) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ database Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02717 KRYILRCMGNSGICRASCKRNEQPYLYCKNYQSCCLQSYMRISISGKEENTDWSYEKQWPKLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; Defensin, beta 120; primates, mammals, A4H226 Belongs to the beta-defensin family DEFB119 Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 7-34; 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02718 GTQRCWNLYGKCRHRCSKKERVYVYCVNNKMCCVKPKYQPKERWWRF 47 Beta-defensin 123 (Defensin, beta 123; primates, mammals, animals) A4H236 Belongs to the beta-defensin family DEFB123 Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 5-32; 12-26; 16-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02719 SWYVKKCLNDVGICKKKCKPEELHVKNGWAMCGKQRDCCVPAD 43 Beta-defensin 126 (Defensin, beta 126; primates, mammals, animals) A4H244 Belongs to the beta-defensin family DEFB126 Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 7-38; 14-32; 18-39." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02720 ARLKKCFNNVTGYCRKKCKVGERYEIGCLSGKLCCINYEEEKEHVSFKKPHQHSGEKLSVQQDYIILPTVTIFTV 75 Beta-defensin 128 (Defensin, beta 128; primates, mammals, animals) A4H253 Belongs to the beta-defensin family DEFB128 Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 6-34; 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02721 GGSKCVSNTPGYCRTYCHQGETALFMCNASRKCCVSYSFLPKPDLPQLIGNHWQSRRRNTQRKDKKQQTTVTS 73 Beta-defensin 132 (Defensin, beta 132; primates, mammals, animals) A4H263 Belongs to the beta-defensin family DEFB132 Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 5-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox E.J, Armour J.A.L. Evolution and sequence variation of human beta-defensin genes. DRAMP02722 DHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; primates, mammals,animals) P61263, A4H1Z4 Belongs to the beta-defensin family Not found Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found 1E4S "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds 5-34; 12-27; 17-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11862391##PubMed ID is not available Immunogenetics. 2002 Feb;53(10-11):907-913.##Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. Del Pero M, Boniotto M, Zuccon D, Cervella P, Spanò A, Amoroso A, Crovella S.##Hollox E.J, Armour J.A.L. Beta-defensin 1 gene variability among non-human primates.##Evolution and sequence variation of human beta-defensin genes. DRAMP18237 EKYTEAPEYI 10 Fengycin A(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis K1 Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found K2 is Orn. The structure consists of a cyclic peptide lactone formed between the phenolic -OH of Tyr3 and the C-terminal -COOH of an amino acid at position 10. The N-terminus of the decapeptide segment is acylated with a beta-hydroxy fatty acid (beta-OH FA). Comment: No comments found on DRAMP database Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22847390 J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31. Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins. DRAMP02724 LPGNFFRKAREKIGKEFKRIVQRIKDFLQHLVPRTEA 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) Q1KLY2 Belongs to the cathelicidin family CAMP Nomascus gabriellae (Red-cheeked gibbon) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02725 LLGNFFRKAREKIGKEFKRIVQRIKDFLQHLVPRTEA 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) No entry found Not found Not found Nomascus leucogenys (White-cheeked Gibbon) Antimicrobial, Antibacterial Not found Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP02729 AIHRALICKRMEGHCEAECLTFEVKIGGCRAELAPFCCKNRKKH 44 Beta-defensin 107A (Defensin, beta 107; Defensin, beta 107A; primates, mammals, animals) A4H216, A4H217 Belongs to the beta-defensin family DEFB107A Hylobates lar (Common gibbon) (White-handed gibbon); also Pongo pygmaeus (Bornean orangutan) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains two disulfide bonds 15-29; 19-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02730 EFEWDRICGYGTARCRNKCRSQEYRIGRCPNTFACCLRKWDESLLNSTKP 50 Beta-defensin 104A (Defensin, beta 104; Defensin, beta 104A; primates, mammals, animals) A4H204 Belongs to the beta-defensin family DEFB104A Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02731 GLDFSQPFPSGEFAVFESCKFSRGKCRKECLENEKPDGNCRLNFLCCRQSI 51 Beta-defensin 105A (Defensin, beta 105; Defensin, beta 105A; primates, mammals, animals) A4H208 Belongs to the beta-defensin family DEFB105A Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02732 FFDDKCDKLRGTCKNSCEKNEELTSFCQKSLKCCRTIQTCGNTTD 45 Beta-defensin 106A (Defensin, beta 106; Defensin, beta 106A; primates, mammals, animals) A4H213 Belongs to the beta-defensin family DEFB106A Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial Homology Not found Not found "Function: Has antimicrobial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP18236 NRWCFAGDD 9 NRWC(Bacteriocin) No entry found Not found Not found Bacillus subtilis ATCC 6633 Antimicrobial, Antibacterial Not found The sequence showed no homology with other known antimicrobial peptides. The antimicrobial activity was affected by the action of the proteases pronase E and proteinase K, but the absence of the inhibition zone against H. parasuis was only observed when the enzymes were used at 10 mg/ml. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23519163 Microbiology. 2013 May;159(Pt 5):980-8. Teixeira ML, Dalla Rosa A, Brandelli A. Characterization of an antimicrobial peptide produced by Bacillus subtilis subsp. spizezinii showing inhibitory activity towards Haemophilus parasuis. DRAMP02734 KHHILRCMGNSGICRASCKKNEQPYLYCRNYQHCCLQSYMRISISGEEENTDWSYEKQWPRLP 63 Beta-defensin 119 (Defensin, beta 119; Beta-defensin 120; primates, mammals, animals) A4H227, A4H232 Belongs to the beta-defensin family DEFB119 Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 7-34; 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02735 NWYVKKCLNDVGICKKKCKPEELHVKNGRAMCGKQRDCCVPAD 43 Beta-defensin 126 (Defensin, beta 126; primates, mammals, animals) A4H245 Belongs to the beta-defensin family DEFB126 Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 7-38; 14-32; 18-39." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02736 ARLKKCFNNITGYCRKKCKVGERYEIGCLSGKLCCVNDEEEKKHVSFKKPHQHSGEKLSVQQDYIILPTITIFAV 75 Beta-defensin 128 (Defensin, beta 128; primates, mammals, animals) A4H254 Belongs to the beta-defensin family DEFB128 Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 6-34; 14-28; 18-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02737 GGSKCVSDTQGYCRTYCHQGETALFMCNASRKCCASYSFLPKPDLPQLIGNHWQSRRRNTQRKDKKQQTTVTSS 74 Beta-defensin 132 (Defensin, beta 132; primates, mammals, animals) A4H264 Belongs to the beta-defensin family DEFB132 Hylobates lar (Common gibbon) (White-handed gibbon) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Potentially has antibacterial activity. PTM: Problely contains three disulfide bonds 5-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hollox EJ, Armour JAL. Evolution and sequence variation of human beta-defensin genes. DRAMP02738 DHYNCVRSGGQCLYSACPIYTKIQGTCYQGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; primates, mammals, animals) Q7JGM2, Q95J22, Q7JGM1, A4H1Z5 Belongs to the beta-defensin family DEFB1 Nomascus concolor (Black crested gibbon) (Hylobates moloch) (Hylobates lar) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16700051##11862391 Proteins. 2006 Aug 1;64(2):524-531.##Immunogenetics. 2002 Feb;53(10-11):907-913. Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S.##Del Pero M, Boniotto M, Zuccon D, Cervella P, Spano A, Amoroso A, Crovella S. Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity.##Beta-defensin 1 gene variability among non-human primates. DRAMP02739 EKKCPGRCTLKCGKHERPTLPYNCGKYICCVPVKVK 36 TEWP (turtle egg-white protein; Reptiles, animals) No entry found Not found Not found Caretta caretta (Loggerhead turtle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Not found Beta strand (2 strands; 2 residues) The protein has no α-helix and consists of two antiparallel β-sheets. 2B5B resolved by NMR. Function: The protein showes strong antibacterial activity against Escherichia coli and Salmonella typhimurium. The protein also showes significant antiviral activity against an enveloped rhabdovirus, Chandipura virus, Gram-negative bacteria: Escherichia coli (IC50=2.3 µM), Salmonella typhimurium (IC50=2.8 µM);##Gram-positive bacterium: Staphylococcus aureus (IC50=5.1 µM).##Virus: enveloped rhabdovirus, Chandipura virus, Vesicular stomatitis virus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16700051 Proteins. 2006 Aug 1;64(2):524-531. Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S. Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity. DRAMP02741 DDTPSSRCGSGGWGPCLPIVDLLCIVHVTVGCSGGFGCCRIG 42 Pelovaterin (defensin-like AMP; Gly-rich; Reptiles, animals) P84818 Not found Not found Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure An analysis of the ensemble of pelovaterin structures reveals that hydrophilic residues Asp1 Arg7 begin with a random coil structure leading to a short 310 helix between Cys8 and Gly12, whereas antiparallel â-strands are formed by the residues Leu17 Val20 (β), His27 Val28 (â2), and Gly34 Cys39 (â3) arranged in a βâ2â3 topology. 2JR3 resolved by NMR. "Function: Induces the nucleation and stabilization of vaterite, one of the crystalline polymorphs of calcium carbonate. Exhibits strong antimicrobial activity against Pseudomonas aeruginosa and Proteus vulgaris. PTM: Contains three disulfide bonds 8-38; 16-32; 24-39." Gram-negative bacteria: Pseudomonas aeruginosa (EC50=0.42 µg/mL), Proteus vulgaris (EC50=0.37 µg/mL), Proteus mirabilis (EC50=8.4 µg/mL);##Gram-positive bacterium: Staphylococcus aureus (EC50=42 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15877362##18341335 Biomacromolecules. 2005 May-Jun;6(3):1429-37.##J Am Chem Soc. 2008 Apr 9;130(14):4660-8. Lakshminarayanan R, Chi-Jin EO, Loh XJ, Kini RM, Valiyaveettil S.##minarayanan R, Vivekanandan S, Samy RP, Banerjee Y, Chi-Jin EO, Teo KW, Jois SD, Kini RM, Valiyaveettil S. Purification and characterization of a vaterite-inducing peptide, pelovaterin, from the eggshells of Pelodiscus sinensis (Chinese soft-shelled turtle).##Structure, self-assembly, and dual role of a beta-defensin-like peptide from the Chinese soft-shelled turtle eggshell matrix. DRAMP02742 QKKCPGRCTLKCGKHERPTLPYNCGKYICCVPVKVK 36 Defensin-like turtle egg white protein TEWP (TEWP; Reptiles, animals) P0CAP0 Belongs to the beta-defensin family Not found Caretta caretta (Loggerhead sea turtle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Beta strand (2 strands; 2 residues) Three-dimensional structure of TEWP was determined by distance geometry and simulated annealing. The protein has no α-helix and consists of two antiparallel β-sheets. The secondary structure is consistent with the previously obtained circular dichroism spectra. 2B5B resolved by NMR. "Function: The protein showes strong antibacterial activity against Escherichia coli and Salmonella typhimurium and also showes significant antiviral activity against an enveloped rhabdovirus, Chandipura virus, which is an emerging human pathogen. Tissue specificity: Detected in egg white (at protein level)." Gram-negative bacteria: Escherichia coli (IC50=3.3 µM), Salmonella typhimurium (IC50=2.8 µM);##Gram-positive bacterium: Staphylococcus aureus (IC50=5. 1µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16700051 Proteins. 2006 Aug 1;64(2):524-531. Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S. Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity. DRAMP02743 AVRIGPCDQVCPRIVPERHECCRAHGRSGYAYCSGGGMYCN 41 Diapause-specific peptide (Dsp) Q8T0W8 Belongs to the diapausin family Not found Gastrophysa atrocyanea Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 2E2F resolved by NMR. "Function: Has antifungal activity against Trichophyton rubrum. Blocks voltage-dependent N-type calcium channels (Cav2.2 / CACNA1B). Tissue specificity: Highly expressed in the fat body. Developmental stage: Produced throughout adult diapause, and to a minor extent in pupae, but not in eggs, larvae, or post-diapausing adults. Inhibition of DSP expression does not affect the onset or maintenance of diapause, indicating that the expression of DSP accompanies but does not play a direct role in the induction or maintenance of diapause." Trichophyton rubrum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17994764 Appl. Entomol. Zool. 1998; 33: 535-543. Tanaka H et al. Suzuki K A specific peptide produced during adult diapause of the leaf beetle, Gastrophysa atrocyanea Moschulsky (Coleoptara: Chrysomelidae) DRAMP02744 FWGTLAKLALKAVPAVMGMIKKE 23 Dinoponeratoxin Da-2501 (ants, insects, animals) P0CF01 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Dinoponeratoxin Da-2051 may have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02745 ALKAVPAVMGMIKKE 15 Dinoponeratoxin Da-1585 (ants, insects, animals) P0CF01 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Dinoponeratoxin Da-1585 may have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02746 GLKDWWNKHKDKIIAVAKEMGKAGLQAA 28 Dinoponeratoxin Da-3105 (ants, insects, animals) P0CF02 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02747 FLGGLIGPLMSLIPGLLK 18 Dinoponeratoxin Da-1837 (ants, insects, animals) P0CF03 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02748 GVVPHDFRI 9 Dinoponeratoxin Da-1039 (ants, insects, animals) P0CF04 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02749 GLKDWWNKHKDKIIDVVKEMGKAGLQAA 28 Dinoponeratoxin Da-3177 (ants, insects, animals) P0CF05 Not found Not found Dinoponera australis (Giant neotropical hunting ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May have antibacterial activity, since it is predicted to form an amphipathic alpha helix. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19879289 Toxicon. 2010 Apr 1;55(4):702-710. Johnson SR, Copello JA, Evans MS, Suarez AV. A biochemical characterization of the major peptides from the venom of the giant Neotropical hunting ant Dinoponera australis. DRAMP02750 FTCDLLSGAGVDHSACAAHCILRGKTGGRCNSDRVCVCRA 40 Defensin (ants, insects, animals) Q5BU36 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Formica aquilonia (Red wood ant) Antimicrobial, Antibacterial Homology Bridge Not found Function: Antibacterial peptide mostly active against Gram-positive bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033427 Insect Mol Biol. 2005 Aug;14(4):335-338. Viljakainen L, Pamilo P. Identification and molecular characterization of defensin gene from the ant Formica aquilonia. DRAMP03743 RSVCRQIKICRRRGGCYYKCTNRPY 25 Androctonin (Arthropods, animals) P56684 Not found Not found Androctonus australis (Sahara scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand (2 strands; 8 residues) The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn. 1CZ6 resolved by NMR. "Function: Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria (Gram-positive and Gram-negative) and filamentous fungi. Acts on the membrane of the bacterial cells. It destabilize a membrane by modifying its properties. PTM: Contains two disulfide bonds 4-20; 10-16." [Ref.10942757] Gram-positive bacteria: Micrococcus luteus (MIC=0.6-1.5 μM), Aerococcus viridans (MIC=0.3-0.6 μM), Staphylococcus aureus (MIC=15-30 μM);##Gram-negative bacteria: Escherichia coli D31 (MIC=3-6 μM), Escherichia coli D22 (MIC=6-15 μM), Escherichia coli 1106 (MIC=6-15 μM), Salmonella typhimurium (MIC=3-6 μM).##Fungi: Alternaria brassicola (MIC=3-6 μM), Fusarium culmorum (MIC=3-6 μM), Fusarium oxysporum (MIC=6-12 μM), Neurospora crassa (MIC=6-12 μM), Nectria haematococca (MIC=6-12 μM), Trichoderma viridae (MIC=6-12 μM);##Yeast: Candida albicans (MIC=1.6-3.15 μM).##[Ref.8939880] Gram-positive bacteria: Bacillus subtilis (MIC=1.5-3.0 μM);##Gram-negative bacteria: Escherichia coli D22 (MIC>30 μM), Pseudomonas syringae (MIC=1.5-3.0 μM), Pseudomonas syringae pv.syringae (MIC=15-22 μM), Pseudomonas syringae phaseoli (MIC=1.5-3.0 μM), Pseudomonas syringae pv.pisi (MIC=6-15 μM), Pseudomonas syringae pv. maculicola (MIC=3-6 μM), Phoma valerianella (MIC=15-22 μM), Xanthomonas compestris pv.compestris (MIC=3-6 μM), Xanthomonas vesicatoria 687.3 (MIC=1.5-3.0 μM), Xanthomonas vesicatoria B229RI (MIC=1.5-3.0 μM);##Fungi: Alternaria dauci (MIC=8-16 μM), Stemphylium (MIC=4-8 μM), Fusarium oxysporum M. (MIC=2-4 μM), Fusarium oxysporum L. (MIC=2-4 μM), Botrytis cinerea (MIC=6-12 μM), B. petunia (MIC=4-8 μM), Verticilium toreilis (MIC=2-4 μM), Aspergillus fumigatus (MIC=25-50 μM). [Ref.8939880] It exhibits no hemolytic activity on porcine or bovine erythrocytes at a concentration of up to 150 μM. Cyclic Free Free Disulfide bond between Cys4 and Cys20,Cys10 and Cys16. L No cytotoxicity information found Cell membrane 8939880##10563585##10942757 J Biol Chem. 1996 Nov 22;271(47):29537-29544.##J Biomol Struct Dyn. 1999 Oct;17(2):367-380.##J Biol Chem. 2000 Oct 27;275(43):33464-70. Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann JA, van Dorsselaer A, Bulet P.##Mandard N, Sy D, Maufrais C, Bonmatin JM, Bulet P, Hetru C, Vovelle F.##Silva PI Jr, Daffre S, Bulet P. Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood.##Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer.##Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. DRAMP02753 GWKDWAKKAGGWLKKKGPGMAKAALKAAMQ 30 Ponericin G1 (ants, insects, animals) P82414 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found MOA: The comparison of ponericins with those well-studied peptides suggests that ponericins may adopt an amphipathic alpha-helical structure on cell membranes. B. cereus CIP 6624a, Bacillus megaterium ATCC 9885b, B.stearothermophilus CIP 675, B.stearothermophilus CIP 675, Bacillus subtilis ATCC 6623, Enterococcus faecalis CIP 636, Lactococcus lactis ssp. cremoris I116, Streptococcus pyogenes CIP 561, S. sanguinis CIP 55128, Listeria ivanovii LMA 94d, Listeria monocytogenes ATCC 15313, Micrococcus luteus CIP 5345, Staphylococcus aureus CIP 677, Staphylococcus aureus LMA, S. epidermidis CIP 53134, Escherichia coli, Enterobacter cloacae CIP 6085, Klebsiella pneumoniae CIP 8291, Proteus mirabilis LMA TP, Salmonella enterica CIP 813, Serratia marcescens LMA TP, Alcaligenes faecalis CIP 6723, Pseudomonas aeruginosa CIP A22, Proteus mirabilis LMA TP, Flavobacterium meningosepticum CIP 6057, Pseudomonas aeruginosa CIP A22, Yersinia entericolitica CIP 6529, P. putida LMA, Saccharomyces cerevisiae LMA 720 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02754 GWKDWLKKGKEWLKAKGPGIVKAALQAATQ 30 Ponericin G2 (ants, insects, animals) P82415 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found MOA: The comparison of ponericins with those well-studied peptides suggests that ponericins may adopt an amphipathic alpha-helical structure on cell membranes. Saccharomyces cerevisae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02755 GWKDWLNKGKEWLKKKGPGIMKAALKAATQ 30 Ponericin G3 (ants, insects, animals) P82416 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found MOA: The comparison of ponericins with those well-studied peptides suggests that ponericins may adopt an amphipathic alpha-helical structure on cell membranes. Gram-positive bacteria: Bacillus cereus CIP 6624a, B. megaterium ATCC 9885b, B. stearothermophilus CIP 675, B. stearothermophilus CIP 675, B. subtilis ATCC 6623, Enterococcus faecalis CIP 636, Lactococcus lactis ssp. cremoris I116, Streptococcus pyogenes CIP 561, S. sanguinis CIP 55128, Listeria ivanovii LMA 94d, Listeria monocytogenes ATCC 15313, Micrococcus luteus CIP 5345, Staphylococcus aureus CIP 677, Staphylococcus aureus LMA, S. epidermidis CIP 53134;##Gram-negative bacteria: Escherichia coli, Enterobacter cloacae CIP 6085, Klebsiella pneumoniae CIP 8291, Proteus mirabilis LMA TP, Salmonella enterica CIP 813, Serratia marcescens LMA TP, Alcaligenes faecalis CIP 6723, Pseudomonas aeruginosa CIP A22, Proteus mirabilis LMA TP, Flavobacterium meningosepticum CIP 6057, Pseudomonas aeruginosa CIP A22, Yersinia entericolitica CIP 6529, P. putida LMA, Saccharomyces cerevisiae LMA 720. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02756 DFKDWMKTAGEWLKKKGPGILKAAMAAAT 29 Ponericin G4 (ants, insects, animals) P82417 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found MOA: The comparison of ponericins with those well-studied peptides suggests that ponericins may adopt an amphipathic alpha-helical structure on cell membranes. Gram-positive bacteria: B. cereus CIP 6624a, Bacillus megaterium ATCC 9885b, B.stearothermophilus CIP 675, B.stearothermophilus CIP 675, Bacillus subtilis ATCC 6623, Lactococcus lactis ssp. cremoris I116, Streptococcus pyogenes CIP 561, S. sanguinis CIP 55128, Micrococcus luteus CIP 5345;##Gram-negative bacteria: Klebsiella pneumoniae CIP 8291, Pseudomonas aeruginosa CIP A22, Saccharomyces cerevisae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02757 GLKDWVKIAGGWLKKKGPGILKAAMAAATQ 30 Ponericin G5 (ants, insects, animals) P82418 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P82418]has antibacterial activity No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02758 GLVDVLGKVGGLIKKLLP 18 Ponericin G6 (ants, insects, animals) P82419 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has activity against Gram-positive bacteria and S. cerevisiae. Has non-hemolytic activity. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a, B. megaterium ATCC 9885b, B. stearothermophilus CIP 675, B. stearothermophilus CIP 675, B. subtilis ATCC 6623, Lactococcus lactis ssp. cremoris I116, Streptococcus pyogenes CIP 561, S. sanguinis CIP 55128, Listeria monocytogenes ATCC 15313, Micrococcus luteus CIP 5345, Staphylococcus aureus CIP 677, S. epidermidis CIP 53134;##Gram-negative bacteria: Klebsiella pneumoniae CIP 8291, Pseudomonas aeruginosa CIP A22, Saccharomyces cerevisiae LMA 720. [Ref.11279030]Non-hemolytic activity against horse and sheep erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02759 GLVDVLGKVGGLIKKLLPG 19 Ponericin G7 (ants, insects, animals) P82420 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Has activity against Gram-positive bacteria and S. cerevisiae. Tissue specificity: Expressed by the venom gland. [Swiss_Prot Entry P82420]has activity against Gram-positive bacteria and S.cerevisiae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chafotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02760 LLKELWTKMKGAGKAVLGKIKGLL 24 Ponericin-L1 (ants, insects, animals) P82421 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P82421]Broad spectrum of activity against both Gram-positive and Gram-negative bacteria No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02761 LLKELWTKIKGAGKAVLGKIKGLL 24 Ponericin-L2 (ants, insects, animals) P82422 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral Protein level Alpha helix Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 6.5mm), B. megaterium ATCC 9885b(Inhibition zone = 14mm), B. stearothermophilus CIP 675(Inhibition zone = 21mm), B. subtilis ATCC 6623(Inhibition zone = 13.5mm), Enterococcus faecalis CIP 636(Inhibition zone = 4mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 15.5mm), Streptococcus pyogenes CIP 561(Inhibition zone = 12.5mm), S. sanguinis CIP 55128(Inhibition zone = 6mm), Listeria ivanovii LMA 94d(Inhibition zone = 9.5mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 9.5mm), Micrococcus luteus CIP 5345(Inhibition zone = 10.5mm), Staphylococcus aureus CIP 677(Inhibition zone = 4.5mm), Staphylococcus aureus LMA(Inhibition zone = 11mm), S. epidermidis CIP 53134(Inhibition zone = 11.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 4mm), Enterobacter cloacae CIP 6085(Inhibition zone = 5mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 3.5mm), Proteus mirabilis LMA TP(Inhibition zone = 9mm), Salmonella enterica CIP 813(Inhibition zone = 1.5mm), Serratia marcescens LMA TP(Inhibition zone = 9mm), Flavobacterium meningosepticum CIP 6057(Inhibition zone = 7mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 14mm). [Ref.11279030]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02762 WLGSALKIGAKLLPSVVGLFKKKKQ 25 Ponericin-W1 (ants, insects, animals) P82423 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal Protein level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 10mm), B. megaterium ATCC 9885b(Inhibition zone = 12.5mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 12mm), Enterococcus faecalis CIP 636(Inhibition zone = 6mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 15mm), Streptococcus pyogenes CIP 561(Inhibition zone = 10mm), S. sanguinis CIP 55128(Inhibition zone = 7.5mm), Listeria ivanovii LMA 94d(Inhibition zone = 11.5mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 9.5mm), Micrococcus luteus CIP 5345(Inhibition zone = 11.5mm), Staphylococcus aureus CIP 677(Inhibition zone = 10mm), Staphylococcus aureus LMA(Inhibition zone = 13.5mm), S. epidermidis CIP 53134(Inhibition zone = 13.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 8mm), Enterobacter cloacae CIP 6085(Inhibition zone = 3mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 6.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(Inhibition zone = 3mm), Serratia marcescens LMA TP(no detected), Flavobacterium meningosepticum CIP 6057(Inhibition zone = 6mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 16mm). [Ref.11279030]2mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 μl of the peptide solution and placed overnight at 4℃ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02763 WLGSALKIGAKLLPSVVGLFQKKKK 25 Ponericin-W2 (ants, insects, animals) P82424 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) Antibacterial, Antifungal, Insecticidal, Antimicrobial Protein level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Has insecticidal activities. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02764 GIWGTLAKIGIKAVPRVISMLKKKKQ 26 Ponericin-W3 (ants, insects, animals) P82425 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal Protein level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 10mm), B. megaterium ATCC 9885b(Inhibition zone = 13.5mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 8mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 17.5mm), Streptococcus pyogenes CIP 561(Inhibition zone = 11.5mm), S. sanguinis CIP 55128(Inhibition zone = 10mm), Listeria ivanovii LMA 94d(Inhibition zone = 14mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 11mm), Micrococcus luteus CIP 5345(Inhibition zone = 11mm), Staphylococcus aureus CIP 677(Inhibition zone = 13mm), Staphylococcus aureus LMA(Inhibition zone = 18mm), S. epidermidis CIP 53134(Inhibition zone = 15mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 10mm), Enterobacter cloacae CIP 6085(Inhibition zone = 4mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 7.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(Inhibition zone = 4mm), Serratia marcescens LMA TP(Inhibition zone = 11mm), Flavobacterium meningosepticum CIP 6057(no detected), Pseudomonas aeruginosa CIP A22(Inhibition zone = 18.5mm). [Ref.11279030]1mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 μl of the peptide solution and placed overnight at 4℃ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02765 GIWGTALKWGVKLLPKLVGMAQTKKQ 26 Ponericin-W4 (ants, insects, animals) P82426 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal Protein level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 8.5mm), B. megaterium ATCC 9885b(Inhibition zone = 13.5mm), B. stearothermophilus CIP 675(Inhibition zone = 18mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 3mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 14mm), Streptococcus pyogenes CIP 561(Inhibition zone = 8mm), S. sanguinis CIP 55128(Inhibition zone = 7mm), Listeria ivanovii LMA 94d(Inhibition zone = 10mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 10mm), Micrococcus luteus CIP 5345(Inhibition zone = 12.5mm), Staphylococcus aureus CIP 677(Inhibition zone = 11.5mm), Staphylococcus aureus LMA(Inhibition zone = 13.5mm), S. epidermidis CIP 53134(Inhibition zone = 11.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 8.5mm), Enterobacter cloacae CIP 6085(Inhibition zone = 16.5mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 9mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(no detected), Serratia marcescens LMA TP(Inhibition zone = 13mm), Flavobacterium meningosepticum CIP 6057(no detected), Pseudomonas aeruginosa CIP A22(Inhibition zone = 17mm). [Ref.11279030]2mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 μl of the peptide solution and placed overnight at 4℃ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02766 FWGALIKGAAKLIPSVVGLFKKKQ 24 Ponericin-W5 (ants, insects, animals) P82427 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal Protein level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 7mm), B. megaterium ATCC 9885b(Inhibition zone = 12mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 3mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 11mm), Streptococcus pyogenes CIP 561(Inhibition zone = 6.5mm), S. sanguinis CIP 55128(Inhibition zone = 4.5mm), Listeria ivanovii LMA 94d(Inhibition zone = 8mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 6.5mm), Micrococcus luteus CIP 5345(Inhibition zone = 11mm), Staphylococcus aureus CIP 677(Inhibition zone = 7.5mm), Staphylococcus aureus LMA(Inhibition zone = 9mm), S. epidermidis CIP 53134(Inhibition zone = 7.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 3mm), Enterobacter cloacae CIP 6085(Inhibition zone = 11mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 6.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(no detected), Serratia marcescens LMA TP(Inhibition zone = 11mm), Flavobacterium meningosepticum CIP 6057(Inhibition zone = 5mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 14mm). [Ref.11279030]4mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 μl of the peptide solution and placed overnight at 4℃ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02767 FIGTALGIASAIPAIVKLFK 20 Ponericin-W6 (ants, insects, animals) P82428 Not found Not found Pachycondyla goeldii (Ponerine ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Activity against Gram-positive bacteria. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." [Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 9.5mm), B. megaterium ATCC 9885b(Inhibition zone = 17mm), B. stearothermophilus CIP 675(Inhibition zone = 18mm), B. subtilis ATCC 6623(Inhibition zone = 15mm), Enterococcus faecalis CIP 636(Inhibition zone = 3mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 11mm), Streptococcus pyogenes CIP 561(Inhibition zone = 9.5mm), S. sanguinis CIP 55128(Inhibition zone = 4mm), Listeria ivanovii LMA 94d(Inhibition zone = 5mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 4mm), Micrococcus luteus CIP 5345(Inhibition zone = 11mm), Staphylococcus aureus CIP 677(Inhibition zone = 7mm), Staphylococcus aureus LMA(Inhibition zone = 10mm), S. epidermidis CIP 53134(Inhibition zone = 7mm);##Gram-negative bacteria: Serratia marcescens LMA TP(Inhibition zone = 13mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 14mm). [Ref.11279030]3mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 μl of the peptide solution and placed overnight at 4℃ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J. Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. DRAMP02769 GLLSKFGRLARKLARVIPKV 20 Pilosulin 2 (ants, insects, animals) No entry found Not found Not found Not found Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9813247 Arch Biochem Biophys. 2005 Feb 15;434(2):358-364. Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A. Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin. DRAMP02770 IIGLVSKGTCVLVKTVCKKVLKQG 24 Pilosulin 3 (ants, insects, animals) Q68Y23 Belongs to the pilosulin family Not found Myrmecia banksi (Jack jumper ant) (Australian jumper ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Shows moderate activity against E. coli and S. aureus (MIC<25 µM), slight activity against B. subtilis (MIC<50 µM), and no activity against L. garvieae, P. aeruginosa, C. albicans, and S. cerevisiae. Has no hemolytic nor cytolytic activity. Causes an IgE-independent histamine release. Tissue specificity: Expressed by the venom gland." [Ref.15246874]Gram-negative bacteria: Escherichia coli (MIC<25 µM);##Gram-positive bacteria: Staphylococcus aureus(MIC<25 µM), Bacillus subtilis (MIC<50 µM). [Ref.15246874]Non-hemolytic activity at 50 μM against human whole blood Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 15246874 Arch Biochem Biophys. 2004 Aug 15;428(2):170-178. Inagaki H, Akagi M, Imai HT, Taylor RW, Kubo T. Molecular cloning and biological characterization of novel antimicrobial peptides, pilosulin 3 and pilosulin 4, from a species of the Australian ant genus Myrmecia. DRAMP02771 FDITKLNIKKLTKATCKVISKGASMCKVLFDKKKQE 36 Pilosulin 4 (ants, insects, animals) Q68Y22 Belongs to the pilosulin family Not found Myrmecia banksi (Jack jumper ant) (Australian jumper ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Shows activity against E.coli and S.aureus, moderate activity against P.aeruginosa, weak activity against B.subtilis, and has no effect against L.garvieae, C.albicans, and S.cerevisiae. Has no hemolytic nor cytolytic activity. Causes an IgE-independent histamine release. Tissue specificity: Expressed by the venom gland." [Ref.15246874]Gram-positive bacteria: Staphylococcus aureus (MIC<6.25 µM), Bacillus subtilis (MIC<50 µM);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC<25 µM), Escherichia coli (MIC<6.25 µM). [Ref.15246874]Non-hemolytic activity at 50 μM against human whole blood Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 15246874 Arch Biochem Biophys. 2004 Aug 15;428(2):170-178. Inagaki H, Akagi M, Imai HT, Taylor RW, Kubo T. Molecular cloning and biological characterization of novel antimicrobial peptides, pilosulin 3 and pilosulin 5, from a species of the Australian ant genus Myrmecia. DRAMP02772 IDWKKVDWKKVSKKTCKVMLKACKFL 26 Pilosulin-3a (Allergen Myr p II; Pilosulin-2; ants, insects, animals) Q26464 Not found Not found Myrmecia pilosula (Jack jumper ant) (Australian jumper ant) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has hemolytic activity. Tissue specificity: Expressed by the venom gland. Allergenic properties: Causes an allergic reaction in human. PTM: Contains one disulfide bond and C-terminal amidation." No MICs found in DRAMP database [Ref.15639237]15% hemolytic activity at 10 μM, 40% hemolytic activity at 100 μM against human erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 15639237##8866004 Toxicon. 2004 Feb;43(2):173-183.##Biochem Mol Biol Int. 1996 Aug;39(5):877-885. Davies NW, Wiese MD, Brown SG.##Donovan GR, Street MD, Tetaz T, Smith AI, Alewood D, Alewood P, Sutherland SK, Baldo BA. Characterisation of major peptides in 'jack jumper' ant venom by mass spectrometry.##Expression of jumper ant (Myrmecia pilosula) venom allergens: post-translational processing of allergen gene products. DRAMP02773 DVKGMKKAIKGILDCVIEKGYDKLAAKLKKVIQQLWE 37 Pilosulin 5 (Myr b III; ants, insects, animals) A9CM07 Not found Myrb5 Myrmecia banksi (Jack jumper ant) (Australian jumper ant) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Causes a significant and dose-dependent histamine release, probably by influencing the signal transduction of mast cells through a non-IgE-mediated pathway. This peptide does not have cytotoxic activities. Subunit structure: Homodimer; disulfide-linked. Tissue specificity: Expressed by the venom gland. PTM: Contains one disulfide bond." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18544336##16376960 Arch Biochem Biophys. 2008 Sep 15;477(2):411-416.##Toxicon. 2006 Feb;47(2):208-217. Inagaki H, Akagi M, Imai HT, Taylor RW, Wiese MD, Davies NW, Kubo T.##Wiese MD, Chataway TK, Davies NW, Milne RW, Brown SG, Gai WP, Heddle RJ. Pilosulin 5, a novel histamine-releasing peptide of the Australian ant, Myrmecia pilosula (Jack Jumper Ant).##Proteomic analysis of Myrmecia pilosula (jack jumper) ant venom. DRAMP02775 CIANRNGCQPDGSQGNCCSGYCHKEPGWVAGYCR 34 Antimicrobial peptide Alo-2 (Alo-2; knottin-type peptide; Insects, animals) P83652 Belongs to the AMP family Not found Acrocinus longimanus (Giant harlequin beetle) Antimicrobial, Antifungal Protein level Bridge Not found "Function: Has antifungal activity against C. glabrata. Domain: The presence of a disulfide through disulfide knot' structurally defines this protein as a knottin. PTM: Contains three disulfide bonds 1-18; 8-22; 17-33." Fungi: Candida glabrata patient 1 (MIC>64 µg/mL), C. albicans IHEM 8060 (MIC>64 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14661954 Biochemistry. 2003 Dec 16;42(49):14434-14442. Barbault F, Landon C, Guenneugues M, Meyer JP, Schott V, Dimarcq JL, Vovelle F. Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus. DRAMP02781 SLQGGAPNFPQPSQQNGGWQVSPDLGRDDKGNTRGQIEIQNKGKDHDFNAGWGKVIRGPNKAKPTWHVGGTYRR 74 Coleoptericin (Insects, animals) P80032 Belongs to the coleoptericin family Not found Zophobas atratus (Giant mealworm beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Responsible for the anti Gram-negative activity of immune hemolymph of Z. atratus. Gram-negative bacteria: Escherichia coli D31, E. coli D22 (highly activity), Acinetobacter baumannii, Pseudomonas maltophilia (lower activity);##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1761552 J Biol Chem. 1991 Dec 25;266(36):24520-24525. Bulet P, Cociancich S, Dimarcq JL, Lambert J, Reichhart JM, Hoffmann D, Hetru C, Hoffmann JA. Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family. DRAMP02782 FTCDVLGFEIAGTKLNSAACGAHCLALGRRGGYCNSKSVCVCR 43 Defensin, isoforms B and C (Insects, animals) P80033 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Zophobas atratus (Giant mealworm beetle) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Involved in anti Gram-positive activity of immune hemolymph of Z. atratus. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1761552 J Biol Chem. 1991 Dec 25;266(36):24520-24525. Bulet P, Cociancich S, Dimarcq JL, Lambert J, Reichhart JM, Hoffmann D, Hetru C, Hoffmann JA. Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family. DRAMP02783 FTCDVLGFEIAGTKLNSAACGAHCLALGRTGGYCNSKSVCVCR 43 Peptide C (Insects, animals) No entry found Not found Not found Zophobas atratus (Giant mealworm beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli D22;##Gram-positive bacteria: Micrococcus luteus, Corynebacterium D2, Streptococcus pyogenes, Bacillus subtilis QB935. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1761552 J Biol Chem. 1991 Dec 25;266(36):24520-24525. Bulet P, Cociancich S, Dimarcq JL, Lambert J, Reichhart JM, Hoffmann D, Hetru C, Hoffmann JA. Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family. DRAMP02784 SLQPGAPNVNNKDQPWQVSPHISRDDSGNTRTDINVQRHGENNDFEAGWSKVVRGPNKAKPTWHIGGTHRW 71 Acaloleptin-A1 (chain of Acaloleptin A; Insects, animals) P81592, Q76K70 Belongs to the coleoptericin family Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Acaloleptins A1 show antibacterial activity against Gram-negative bacteria but not against Gram-positive bacteria. Tissue specificity: Hemolymph (at protein level). Larval fat body. Induction: By bacterial infection. Expression detected 2 hours post-injection, with expression increasing until 48 hours post-injection and remaining considerably high at least until 72 hours post-injection." Gram-negative bacteria: Escherichia coli, Aeromonas hydrophila, Erwinia persicinus, Serratia marcescens, Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10077828##19527748 Arch Insect Biochem Physiol. 1999;40(2):88-98.##Dev Comp Immunol. 2009 Oct;33(10):1120-1127. Imamura M, Wada S, Koizumi N, Kadotani T, Yaoi K, Sato R, Iwahana H.##Imamura M, Wada S, Ueda K, Saito A, Koizumi N, Iwahana H, Sato R. Acaloleptins A: inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa.##Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa. DRAMP02785 SLQPGAPNINNKDQPWQVSPHISRDDNGNTRTNINVQRHGENNDFEAGWSKVVRGPNKAKPTWHIGGTHRW 71 Acaloleptin-A2 (chain of Acaloleptin A; Insects, animals) P81592, Q76K70 Belongs to the coleoptericin family Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Acaloleptins A2 show antibacterial activity against Gram-negative bacteria but not against Gram-positive bacteria. Induction: By bacterial infection. Expression detected 2 hours post-injection, with expression increasing until 48 hours post-injection and remaining considerably high at least until 72 hours post-injection." Gram-negative bacteria: Escherichia coli, Aeromonas hydrophila, Erwinia persicinus, Serratia marcescens, Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10077828##19527748 Arch Insect Biochem Physiol. 1999;40(2):88-98.##Dev Comp Immunol. 2009 Oct;33(10):1120-1127. Imamura M, Wada S, Koizumi N, Kadotani T, Yaoi K, Sato R, Iwahana H.##Imamura M, Wada S, Ueda K, Saito A, Koizumi N, Iwahana H, Sato R. Acaloleptins A: inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa.##Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa. DRAMP02786 SLQPGAPNVNNKDQPWQVSPHISRDDSGNTRTNINVQRHGENNDFEAGWSKVVRGPNKAKPTWHIGGTHRW 71 Acaloleptin-A3 (chain of Acaloleptin A; Insects, animals) P81592, Q76K70 Belongs to the coleoptericin family Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Acaloleptins A3 show antibacterial activity against Gram-negative bacteria but not against Gram-positive bacteria. Induction: By bacterial infection. Expression detected 2 hours post-injection, with expression increasing until 48 hours post-injection and remaining considerably high at least until 72 hours post-injection." Gram-negative bacteria: Escherichia coli, Aeromonas hydrophila, Erwinia persicinus, Serratia marcescens, Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10077828##19527748 Arch Insect Biochem Physiol. 1999;40(2):88-98.##Dev Comp Immunol. 2009 Oct;33(10):1120-1127. Imamura M, Wada S, Koizumi N, Kadotani T, Yaoi K, Sato R, Iwahana H.##Imamura M, Wada S, Ueda K, Saito A, Koizumi N, Iwahana H, Sato R. Acaloleptins A: inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa.##Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa. DRAMP02787 SLQPGAPNVNNKDQPWQVSPHISRDDSGNTNTDINLQRHGENHDFDAGWSKVVRGPNKAKPTWHVGGTYRW 71 Acaloleptin-A4 (chain of Acaloleptin A; Insects, animals) P81592, Q76K70 Belongs to the coleoptericin family Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Acaloleptins A4 show antibacterial activity against Gram-negative bacteria but not against Gram-positive bacteria. Induction: By bacterial infection. Expression detected 2 hours post-injection, with expression increasing until 48 hours post-injection and remaining considerably high at least until 72 hours post-injection." Gram-negative bacteria: Escherichia coli, Aeromonas hydrophila, Erwinia persicinus, Serratia marcescens, Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10077828##19527748 Arch Insect Biochem Physiol. 1999;40(2):88-98.##Dev Comp Immunol. 2009 Oct;33(10):1120-1127. Imamura M, Wada S, Koizumi N, Kadotani T, Yaoi K, Sato R, Iwahana H.##Imamura M, Wada S, Ueda K, Saito A, Koizumi N, Iwahana H, Sato R. Acaloleptins A: inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa.##Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa. DRAMP02788 SDDEDEEEEEDQPWQLNPNIARGDDGNTRADVNIKRRGENHDFEAGWSKVVDGPDRAKPTWHVGGTFRW 69 Acaloleptin-A5 (chain of Acaloleptin A; Insects, animals) P81592, Q76K70 Belongs to the coleoptericin family Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Acaloleptin A5 shows antibacterial activity against Gram-positive bacteria but not against Gram-negative bacteria, and may also have antifungal activity. Induction: By bacterial infection. Expression detected 2 hours post-injection, with expression increasing until 48 hours post-injection and remaining considerably high at least until 72 hours post-injection." Gram-negative bacteria: Escherichia coli, Aeromonas hydrophila, Erwinia persicinus, Serratia marcescens, Aeromonas hydrophila. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10077828##19527748 Arch Insect Biochem Physiol. 1999;40(2):88-98.##Dev Comp Immunol. 2009 Oct;33(10):1120-1127. Imamura M, Wada S, Koizumi N, Kadotani T, Yaoi K, Sato R, Iwahana H.##Imamura M, Wada S, Ueda K, Saito A, Koizumi N, Iwahana H, Sato R. Acaloleptins A: inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa.##Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa. DRAMP02789 VTCDILSVEAKGVKLNDAACAAHCLFRGRSGGYCNGKRVCVCR 43 Tenecin-1 (Insects, animals) Q27023 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Tenebrio molitor (Yellow mealworm beetle) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Bactericidal protein produced in response to injury. It is cytotoxic to Gram-positive bacteria. PTM: Contains three disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7798186 J. Biochem. 1994; 116:53-58 Moon HJ, Lee SY, Kurata S, Natori S, Lee BL. Purification and molecular cloning of cDNA for an inducible antibacterial protein from larvae of the coleopteran, Tenebrio molitor. DRAMP02790 DHHDGHLGGHQTGHQGGQQGGHLGGQQGGHLGGHQGGQPGGHLGGHQGGIGGTGGQQHGQHGPGTGAGHQGGYKTHGH 78 Tenecin-3 (Insects, animals) Q27270 Not found Not found Tenebrio molitor (Yellow mealworm beetle) Antimicrobial, Antifungal Protein level Not found Not found "Function: Antifungal heat stable protein produced in response to injury. It is active against C.albicans. No antibacterial activity against Gram-positive and Gram-negative bacteria. Developmental stage: Highest expression in larvae and adult. To a much lesser extent in pupae." Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8573176##PubMed ID is not available Biochem Biophys Res Commun. 1996 Jan 5;218(1):6-11.##Mol. Cells 1995;5:287-292. Lee YJ, Chung TJ, Park CW, Hahn Y, Chung JH, Lee BL, Han DM, Jung YH, Kim S, Lee Y.##Jung HY, Park BY, Lee DK, Hahn Y, Chung JH, Han DM, Moon HJ, Lee BL, Lee Y. Structure and expression of the tenecin 3 gene in Tenebrio molitor.##Biochemical and molecular characterization of an antifungal protein from Tenebrio molitor larvae. DRAMP02791 VTCDLLSFEAKGFAANHSLCAAHCLAIGRRGGSCERGVCICRR 43 A.dichotoma defensin (defensins; Insects, animals) Q10745 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Allomyrina dichotoma (Japanese rhinoceros beetle) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus, Bacillus subtilis, Staphylococcus aureus (MRSA). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8607799 Biochem Biophys Res Commun. 1996 Mar 27;220(3):526-531. Miyanoshita A, Hara S, Sugiyama M, Asaoka A, Taniai K, Yukuhiro F, Yamakawa M. Isolation and characterization of a new member of the insect defensin family from a beetle, Allomyrina dichotoma. DRAMP02792 ELPKLPDDKVLIRSRSNCPKGKVWNGFDCKSPFAFS 36 Scarabaecin, major form (Insects, animals) Q86SC0 Not found scar Oryctes rhinoceros (Coconut rhinoceros beetle) Antimicrobial, Antibacterial, Antifungal Protein level Combine helix and strand structure The solution structure consists of a two-stranded antiparallel beta-sheet connected by a type-I beta-turn after a short helical turn. All secondary structures and a conserved disulfide bond are located in the C-terminal half of the peptide, residues 18-36. Overall folding is stabilized by a combination of a disulfide bond, seven hydrogen bonds, and numerous hydrophobic interactions.(Ref.2) 1IYC resolved by NMR. Comment: No comments found on DRAMP database Fungi: P. oryzae (IC50=16 µM), R. solani (IC50=32 µM), Botrytis cinerea (IC50=4 µM), S.tritici (IC50=16 µM), P. syringae pv.mori S6804 (IC50=25 µM); And Staphylococcus aureus, B. bassiana (weak activity). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 12859949##12676931 Biochem Biophys Res Commun. 2003 Jul 25;307(2):261-266.##J Biol Chem. 2003 Jun 20;278(25):22820-22827. Tomie T, Ishibashi J, Furukawa S, Kobayashi S, Sawahata R, Asaoka A, Tagawa M, Yamakawa M.##Hemmi H, Ishibashi J, Tomie T, Yamakawa M. Scarabaecin, a novel cysteine-containing antifungal peptide from the rhinoceros beetle, Oryctes rhinoceros.##Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros. DRAMP02793 MQKLAEAIAAAVSAGQDKDWGKMGTSIVGIVENGITVLGKIFGF 44 Antibacterial protein1 (Gonococcal growth inhibitor I) P11697 Belongs to the staphylococcal hemolytic protein family Not found Staphylococcus haemolyticus Antimicrobial, Antibacterial Protein level Not found Not found Function: Has haemolytic activity. Gonococci No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3138972 Biochem J. 1988 May 15;252(1):87-93. Watson DC, Yaguchi M, Bisaillon JG, Beaudet R, Morosoli R. The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus. DRAMP02794 MEKIANAVKSAIEAGQNQDWTKLGTSILDIVSNGVTELSKIFGF 44 Antibacterial protein 2 (Gonococcal growth inhibitor II) P11698 Belongs to the staphylococcal hemolytic protein family Not found Staphylococcus haemolyticus Antimicrobial, Antibacterial Protein level Not found Not found Function: Has haemolytic activity. Gonococci No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3138972 Biochem J. 1988 May 15;252(1):87-93. Watson DC, Yaguchi M, Bisaillon JG, Beaudet R, Morosoli R. The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus. DRAMP02795 MSKLVQAISDAVQAQQNQDWAKLGTSIVGIVENGVGILGKLFGF 44 Antibacterial protein 3 (Gonococcal growth inhibitor III) P11699 Belongs to the staphylococcal hemolytic protein family Not found Staphylococcus haemolyticus (strain JCSC1435) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has haemolytic activity. Gonococci No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3138972 Biochem J. 1988 May 15;252(1):87-93. Watson DC, Yaguchi M, Bisaillon JG, Beaudet R, Morosoli R. The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus. DRAMP02796 ATCDILSFQSQWVTPNHAGCALHCVIKGYKGGQCKITVCHCRR 43 Defensin (Type 1 invertebrate defensin; Insects, animals) P37364, P80308 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Pyrrhocoris apterus (Sap sucking bug) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found "Function: Has antibacterial activity against Gram-positive bacteria and the Gram-negative bacterium E.coli D22. PTM: Contains three disulfide bonds 3-34; 20-39; 24-41 (By similarity)." Gram-positive bacteria: Micrococcus luteus, Bacillus megaterium, Aerococcus viridans, Staphylococcus aureus, S. saprophyticus, Pediococcus acidilactici, Bacillus subtilis QB935, Escherichia coli D22. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8002963 Biochem J. 1994 Jun 1;300 (Pt 2):567-575. Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru C, Hoffmann JA, Bulet P. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus. DRAMP02797 GIINMLQKSYCKIRKGRCALLGCLPKEEQIGSCSVSGRKCCRKKK 45 Beta-defensin 103A (Defensin, beta 103; Defensin, beta 103A; houses, mammals, animals) Q0W9P9 Belongs to the beta-defensin family DEFB103A Equus caballus (Horse) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria (By similarity). PTM: Contains three disulfide bonds 11-40; 18-33; 23-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16723195 Gene. 2006 Jul 19;376(2):192-198. Looft C, Paul S, Philipp U, Regenhard P, Kuiper H, Distl O, Chowdhary BP, Leeb T. Sequence analysis of a 212 kb defensin gene cluster on ECA 27q17. DRAMP02798 GIACWSCRKILQKLEDLVGEQPNEATINEAASRVCRNLGLLRGACKKIMRTCLRLISRDILAGKKPQEVCVDIKLCKH 78 Antimicrobial peptide NK-lysin (houses, mammals, animals) Q8HZQ3 Not found NKL Equus caballus (Horse) Antimicrobial Transcript level Not found Not found "Function: May be an effector molecule of cytotoxic activity. Has antimicrobial activity. PTM: Contains three disulfide bonds 4-76; 7-70; 35-45." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Davis E.G, Zhang G, Sang Y, Rush B.R, Ross C, Blecha F. cDNA sequence of equine NK-lysin. DRAMP02799 DVQCGEGHFCHDQTCCRASQGGACCPYSQGVCCADQRHCCPVGF 44 Antimicrobial peptide eNAP-1 (houses, mammals, animals) P80930 Belongs to the granulin family Not found Equus caballus (Horse) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antimicrobial activity against Gram-negative and Gram-positive bacteria. PTM: Contains two disulfide bonds 4-16; 10-26." Streptococcus zooepidemicus, Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1639474 Infect Immun. 1992 Aug;60(8):3065-3071. Couto MA, Harwig SS, Cullor JS, Hughes JP, Lehrer RI. Identification of eNAP-1, an antimicrobial peptide from equine neutrophils. DRAMP02800 EVERKHPLGGSRPGRCPTVPPGTFGHCACLCTGDASEPKGQKCCSN 46 Antimicrobial peptide eNAP-2 (houses, mammals, animals) P56928 Not found Not found Equus caballus (Horse) Antimicrobial, Antibacterial Protein level Not found Not found Function: Selectively inactivates microbial serine proteases (subtilisin A and proteinase K) without inhibiting mammalian serine proteases (human neutrophil elastase, human cathepsin G and bovine pancreatic trypsin). Streptococcus zooepidemicus, Escherichia coli, Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1452336##8514405 Infect Immun. 1992 Dec;60(12):5042-5047.##Infect Immun. 1993 Jul;61(7):2991-2994. Couto MA, Harwig SS, Cullor JS, Hughes JP, Lehrer RI.##Couto MA, Harwig SS, Lehrer RI. eNAP-2, a novel cysteine-rich bactericidal peptide from equine leukocytes.##Selective inhibition of microbial serine proteases by eNAP-2, an antimicrobial peptide from equine neutrophils. DRAMP02801 KVFERXELARTLKRLGLDGFRGVSLPNXVXLAR 33 Lysozyme C, spleen isozyme (1,4-beta-N-acetylmuramidase C; houses, mammals, animals) P81710 Belongs to the glycosyl hydrolase 22 family Not found Equus caballus (Horse) Antimicrobial Protein level Not found Not found "Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents By similarity. Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Miscellaneous: Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides By similarity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8080284 Arch Biochem Biophys. 1994 Sep;313(2):360-366. Grobler JA, Rao KR, Pervaiz S, Brew K. Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily. DRAMP02803 GCASRCKAKCAGRRCKGWASASFRGRCYCKCFRC 34 Mytilin-A (molluscas, animals) P81612 Not found Not found Mytilus edulis (Blue mussel) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity. It is active against the marine species Alteromonas carrageenovora, Pseudomonas alginovora and Cytophaga drobachiensis. Gram-positive bacteria: Aerococcus viridans, Bacillus megaterium, Micrococcus luteus, Enterococcus faecalis, Staphylococcus aureus;##Gram-negative bacteria: Escherichia coli, Alteromonas carrageenovora, Pseudomonas alginovora, Cytophaga drobachiensis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702979 J Biol Chem. 1996 Sep 6;271(36):21808-21813. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. DRAMP02804 GFGCPNDYPCHRHCKSIPGRYGGYCGGXHRLRCTC 35 Mytilus defensin-B (molluscas, animals) P81611 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Mytilus edulis (Blue mussel) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Has antibacterial activity. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702979 J Biol Chem. 1996 Sep 6;271(36):21808-21813. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. DRAMP02805 SCASRCKGHCRARRCGYYVSVLYRGRCYCKCLRC 34 Mytilin-B (molluscas, animals) P81613 Not found Not found Mytilus edulis (Blue mussel) Antimicrobial, Antibacterial, Antiviral Protein level Combine helix and strand structure Not found 2EEM resolved by NMR. Function: Has antibacterial and antiviral activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702979##17628674 J Biol Chem. 1996 Sep 6;271(36):21808-21813.##Dev Comp Immunol. 2008;32(3):227-238. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P.##Roch P, Yang Y, Toubiana M, Aumelas A. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis.##NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides. DRAMP02806 GFGCPNDYPCHRHCKSIPGRXGGYCGGXHRLRCTCYR 37 Mytilus defensin-A (molluscas, animals) P81610 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Mytilus edulis (Blue mussel) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." Micrococcus luteus, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702979 J Biol Chem. 1996 Sep 6;271(36):21808-21813. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. DRAMP02807 DCCRKPFRKHCWDCTAGTPYYGYSTRNIFGCTC 33 Mytimycin (molluscas, animals) P81614 Not found Not found Mytilus edulis (Blue mussel) Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Neurospora crassa, Fusarium culmorum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8702979 J Biol Chem. 1996 Sep 6;271(36):21808-21813. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. DRAMP02808 HSHACTSYWCGKFCGTASCTHYLCRVLHPGKMCACVHCSR 40 Myticin-A (Myt A; Cys-rich; molluscas, animals) P82103 Not found Not found Mytilus galloprovincialis (Mediterranean mussel) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Rich Not found "Function: Bacteriolytic activity against Gram-positive bacteria M. luteus, Bacillus megaterium and A. viridans. PTM: contains four disulfide bonds." Gram-positive bacteria: Micrococcus luteus (MBC=2.25-4.5 µM), Bacillus megaterium (MBC=2.25-4.5 µM), Aerococcus viridans (MBC=9-4.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10491159 Eur J Biochem. 1999 Oct 1;265(1):71-78. Mitta G, Hubert F, Noël T, Roch P. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. DRAMP02810 QEAQSVACTSYYCSKFCGSAGCSLYGCYLLHPGKICYCLHCSR 43 Myticin C No entry found Not found Not found Mytilus galloprovincialis (Mediterranean mussel) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17628673 Dev Comp Immunol. 2008;32(3):213-226. Pallavicini A, Costa Mdel M, Gestal C, Dreos R, Figueras A, Venier P, Novoa B. High sequence variability of myticin transcripts in hemocytes of immune-stimulated mussels suggests ancient host-pathogen interactions. DRAMP02812 AVVNGVNYVGETTAA 15 Endopeptidase L4 P85155 Not found Not found Lysobacter sp. strain XL1 (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Biophysicochemical properties: Optimum pH is 8.0; Optimum temperature is 50-55 degrees Celsius. Retains 50% of its maximal activity after incubation at 52 degrees Celsius for 15 min. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16266276 Biochemistry (Mosc). 2005 Sep;70(9):1031. Stepnaya OA, Tsfasman IM, Logvina IA, Ryazanova LP, Muranova TA, Kulaev IS. Isolation and characterization of a new extracellular bacteriolytic endopeptidase of Lysobacter sp. XL1. DRAMP02814 FHPSLWVLIPQYIQLIRKILKS 22 Conolysin-Mt2 No entry found Not found Not found Conus mustelinus (Weasel cone) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17927208 Biochemistry. 2007 Nov 6;46(44):12586-12593. Biggs J.S, Rosenfeld Y, Shai Y, Olivera B.M. Conolysin-Mt: a conus peptide that disrupts cellular membranes. DRAMP18235 LLEL 4 Gageopeptide D(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Glu-Leu-3-beta-hydroxy-9,11-dimethyltetradecanoic acid Non-cytotoxic antifungal agents. It was revealed that compounds 1 and 2 exhibited stronger antifungal activity than 3 and 4. Compounds 1 and 2 were structurally different from compounds 3 and 4 in terms of having less side chains in the fatty acid units, suggesting that the side chain length and the additional methyl group in the aliphatic chain are important for antifungal activity. These compounds also showed potent antimicrobial activity against Gram positive and Gram negative bacteria with MIC values of 0.04?0.08 uM. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2485741 Yan Ke Xue Bao. 1989 Jun;5(1-2):32-5. Lin N, Gong XM, Xie QJ, Shao MR. Study in cytotoxicity of gentamycin to corneal epithelium and endothelium in tissue culture. DRAMP02816 RQKDKRPYSERKNQYTGPQFLYPPERIPP 29 Lumbrican No entry found Not found Not found Lumbricus rubellus (humus earthworm) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis ATCC 62037, Staphylococcus aureus ATCC 15752, Streptococcus mutans ATCC 25175;##Gram-negative bacteria: Escherichia coli ATCC 27325, Pseudomonas putida ATCC 17426, Serratia sp. ATCC 21074.##Fungi: Candida albicans ATCC 10231, Cryptococcus neoformans ATCC 34881, Saccharomyces cerevisiae ATCC 44774. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9784609 Biochim Biophys Acta. 1998 Oct 22;1408(1):67-76. Cho JH, Park CB, Yoon YG, Kim SC. Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization. DRAMP02818 ILQKAVLDCLKAAGSSLSKAAITAIYNKIT 30 Dicynthaurin P0C007 Not found Not found Halocynthia aurantium (Sea peach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix (CD) CD spectra of the cynthaurin monomer (Fig. 5A) and homodimer (Fig. 5B) in PBS showes properties characteristic of helical peptides. In structure-promoting environments, such as TFE:phosphate buffer or SDS micelles, the helical conformations are enhanced and accounted for the dominant structural component of both the monomeric and the homodimeric peptides. "Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Its antimicrobial activity is optimal at NaCl concentrations below 100 mM, suggesting that the antimicrobial actions of this peptide may take place intracellularly rather than extracellularly. Has no activity against the fungus C.albicans. Has hemolytic activity. PTM: Contians one disulfide bond and C-terminal amidation." [Ref.11479030]Gram-positive bacteria: Micrococcus luteus, Staphylococcus aureus(50 units at 100ug/ml), Listeria monocytogenes(50 units at 40ug/ml);##Gram-negative bacteria: Escherichia coli(50 units at 10ug/ml), Pseudomonas aeruginosa(25 units at 20ug/ml). [Ref.11479030]10% hemolytic activity at 50 μg/ml, 20% hemolytic activity at 100 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11479030 Biochim Biophys Acta. 2001 Aug 15;1527(3):141-148. Lee IH, Lee YS, Kim CH, Kim CR, Hong T, Menzel L, Boo LM, Pohl J, Sherman MA, Waring A, Lehrer RI. Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. DRAMP01820 FLPLFASLIGKLL 13 Temporin-1Cb (Temporin 1Cb; Frogs, amphibians, animals) P82881 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacterium Staphylococcus aureus. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=140 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP01822 FLPFLASLLSKVL 13 Temporin-1Cd (Temporin 1Cd; Frogs, amphibians, animals) P82883 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacterium Staphylococcus aureus. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP02820 VTCDLLSLQIKGIAINDSACAAHCLAMRRKGGSCKQGVCVCRN 43 Holotricin-1 (Gly-rich; His-rich; invertebrate defensin; animals) Q7M426 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Holotrichia diomphalia (Korean black chafer) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Shows potent antibacterial activity against Gram-positive bacteria. PTM: Contians three disulfide bonds 3-34; 20-39; 24-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7550103 Biol Pharm Bull. 1995 Mar;18(3):457-459. Lee S.Y, Moon H.J, Kawabata S, Kurata S, Natori S, Lee B.L. A sapecin homologue of Holotrichia diomphalia: purification, sequencing and determination of disulfide pairs. DRAMP02821 SLQPGAPSFPMPGSQLPTSVSGNVEKQGRNTIATIDAQHKTDRYDVRGTWTKVVDGPGRSKPNFRIGGSYRW 72 Holotricin-2 (Gly-rich; His-rich; invertebrate defensin; animals) Q25054 Belongs to the coleoptericin family Not found Holotrichia diomphalia (Korean black chafer) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibacterial activity against Gram-negative bacteria but not against Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8188641 J Biochem. 1994 Jan;115(1):82-86. Lee SY, Moon HJ, Kurata S, Kurama T, Natori S, Lee BL. Purification and molecular cloning of cDNA for an inducible antibacterial protein of larvae of a coleopteran insect, Holotrichia diomphalia. DRAMP02822 YGPGDGHGGGHGGGHGGGHGNGQGGGHGHGPGGGFGGGHGGGHGGGGRGGGGSGGGGSPGHGAGGGYPGGHGGGHHGGYQTHGY 84 Holotricin-3 (Gly-rich; His-rich; invertebrate defensin; animals) Q25055 Not found Not found Holotrichia diomphalia (Korean black chafer) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity against C. albicans. Yeast: Candida ablicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8535393 Biol. Pharm. Bull. 1995; 18:1049-1052. Lee S.Y, Moon H.J, Kurata S, Natori S, Lee B.L. Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae. DRAMP02824 VRNSQSCRRNKGICVPIRCPGSMRQIGTCLGAQVKCCRRK 40 Lingual antimicrobial peptide (mammals, animals) A3RJ36 Belongs to the beta-defensin family Not found Bubalus bubalis (Domestic water buffalo) Antimicrobial, Antibacterial, Antiviral Protein level Bridge Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds 7-36; 14-29; 19-37." Escherichia coli, Staphylococcus aureus, Streptococcus pyogenes, Candida albicans, Rinderpest Virus (RPV) and Newcastle Disease Virus (NDV) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18826332 Altern Lab Anim. 2008 Sep;36(4):429-440. Das H, Swamy N, Sahoo G, Ahmed S.U, More T. Beta-defensin antibiotic peptides in the innate immunity of the buffalo: in vivo and in vitro studies. DRAMP02825 SSMKLSFRARAYGFRGPGPQL 21 Catestatin No entry found Not found Not found Bos taurus (Bovine) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15723172 Cell Mol Life Sci. 2005 Feb;62(3):377-385. Briolat J, Wu SD, Mahata SK, Gonthier B, Bagnard D, Chasserot-Golaz S, Helle KB, Aunis D, Metz-Boutigue MH. New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A. DRAMP02826 RPKHPIKHQGLPQEVLNENLLRF 23 Isracidin No entry found Not found Not found Bos taurus (Bovine) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19054235 J Appl Microbiol. 2009 Jan;106(1):233-240. Birkemo GA, O'Sullivan O, Ross RP, Hill C. Antimicrobial activity of two peptides casecidin 15 and 17, found naturally in bovine colostrum. DRAMP02827 FLSFPTTKTYFPHFDLSHGSAQVKGHGAK 29 BHP (pepsin-derived bovine hemoglobin fragment) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11226440 FEBS Lett. 2001 Feb 23;491(1-2):159-163. Froidevaux R, Krier F, Nedjar-Arroume N, Vercaigne-Marko D, Kosciarz E, Ruckebusch C, Dhulster P, Guillochon D. Antibacterial activity of a pepsin-derived bovine hemoglobin fragment. DRAMP02829 SDEKASPDKHHRFSLSRYAKLANRLANPKLLETFLSKWIGDRGNRSV 47 Seminalplasmin No entry found Not found Not found Bos taurus (Bovine) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16453469 EMBO J. 1983;2(7):1159-1163. Theil R, Scheit KH. Amino acid sequence of seminalplasmin, an antimicrobial protein from bull semen. DRAMP02830 AAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQR 60 Chrombacin No entry found Not found Not found Bos taurus (Bovine) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18181560 J Proteome Res. 2008 Feb;7(2):795-802. Taylor SW, Sun C, Hsieh A, Andon NL, Ghosh SS. A sulfated, phosphorylated 7 kDa secreted peptide characterized by direct analysis of cell culture media. DRAMP02831 MLTDLECAINSLIDVYHKYSLKKGNYHAVYRDDLKQLLETECPKFMKKKDADTWFKELDINQDGGINFEEFLVLVIKVGLEAHEEIHKE 89 Protein S100-A8 (Calgranulin-A; MRP-8; mammals, animals) P28782, Q2NKR8 Belongs to the S-100 family S100A8 Bos taurus (Bovine) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn2+ which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect. Tissue specificity: Found essentially in phagocytic cells. Miscellaneous: Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 1610833##8505358 Biochemistry. 1992 Jun 30;31(25):5898-5905.##J Cell Sci. 1993 Feb;104 ( Pt 2):237-247. Dianoux AC, Stasia MJ, Garin J, Gagnon J, Vignais PV.##Tang TK, Hong TM, Lin CY, Lai ML, Liu CH, Lo HJ, Wang ME, Chen LB, Chen WT, Ip W, et al. The 23-kilodalton protein, a substrate of protein kinase C, in bovine neutrophil cytosol is a member of the S100 family.##Nuclear proteins of the bovine esophageal epithelium. I. Monoclonal antibody W2 specifically reacts with condensed nuclei of differentiated superficial cells. DRAMP02832 MPVAVGPYGQSQPSCFDRVKMGFVMGCAVGMAAGALFGTFSCLRIGMRGRELMGGIGKTMMQSGGTFGTFMAIGMGIRC 79 Reactive oxygen species modulator 1 (ROS modulator 1; mammals, animals) Q3SZV8 Belongs to the MGR2 family ROMO1 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found "Function: Has antibacterial activity against a variety of bacteria. Acts by inducing bacterial membrane breakage (By similarity). Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation." Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Pseudomonas aeruginosa, Mycobacterium tuberculosis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Unknown NIH - Mammalian Gene Collection (MGC) project DRAMP02833 SALYALYDFSPPARKMRAYTVRAYVHGSYSRRGPWYDFEPVPGASMDGL 49 Glycolactin (Antiviral defensin; mammals, animals) P59760 Belongs to the pancreatic ribonuclease family Not found Bos taurus (Bovine) Antimicrobial, Antiviral Protein level Not found Not found "Function: MManifests poly C-specific RNase activity toward yeast tRNA, elicits a dose-dependent inhibition of cell-free translation, inhibits formation of superoxide ions in vitro and inhibits the hemagglutinating activities of soybean lectin and Ricinus communis agglutinin 120. Inhibits HIV-1 reverse transcriptase. Tissue specificity: Milk." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10486275##11105990 Biochem Biophys Res Commun. 1999 Sep 16;263(1):187-191.##Life Sci. 2000 Oct 20;67(22):2745-2752. Ye XY, Cheng KJ, Ng TB.##Wang H, Ye X, Ng TB. Isolation and characterization of angiogenin-1 and a novel protein designated lactogenin from bovine milk.##First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation. DRAMP02834 SDEKASPDKHHRFSLSRYAKLANRLANPKLLETFLSKWIGDRGNRSVK 48 Seminalplasmin (Calcium transport inhibitor; Peptide YY-2; mammals, animals) P06833 Not found PYY2 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Function: Inhibits calcium transport into spermatozoa; it does not bind directly to calcium. Binds to calmodulin. Inhibits the growth of microorganisms. Seem to act as an antibiotic by permeabilizing the bacterial membrane. Gram-negative bacterium: Escherichia coli.##Fungi: Saccharomyces cerevisiae, Candida ablicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Does not bind directly to calcium. It binds to calmodulin in the presence of Ca2+. 16453469##2334517##3863108 EMBO J. 1983;2(7):1159-1163.##Biol Chem Hoppe Seyler. 1990 Feb;371(2):111-116.##Proc Natl Acad Sci U S A. 1985 Oct;82(19):6490-6491. Theil R, Scheit KH.##Krauhs E, Preuss KD, Scheit KH.##Lewis RV, Agustin JS, Kruggel W, Lardy HA. Amino acid sequence of seminalplasmin, an antimicrobial protein from bull semen.##Functional properties of peptides derived from seminalplasmin: binding to monospecific anti-seminalplasmin immunoglobulins G and calmodulin.##The structure of caltrin, the calcium-transport inhibitor of bovine seminal plasma. DRAMP02836 QCVGTITLDQSDDLFDLNCNELQSVR 26 Cathelicidin antimicrobial peptide (cathelicidin; mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial Not found Not found Not found One chain of Cathelicidin antimicrobial peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8706679 Eur J Biochem. 1996 Jun 15;238(3):769-776. Storici P, Tossi A, Lenarcic B, Romeo D. Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. DRAMP02837 PLSCRRKGGICILIRCPGPMRQIGTCFGRPVKCCR 35 Beta-defensin C7 (BBD(C7); mammals, animals) O18815 Belongs to the beta-defensin family Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram- Homology Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9488394 Infect Immun. 1998 Mar;66(3):1045-1056. Tarver AP, Clark DP, Diamond G, Russell JP, Erdjument-Bromage H, Tempst P, Cohen KS, Jones DE, Sweeney RW, Wines M, Hwang S, Bevins CL. Enteric beta-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection. DRAMP18233 LLLE 4 Gageopeptide B(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Leu-OMeGlu-3-beta-hydroxy-12-methyltetradecanoic acid Non-cytotoxic antifungal agents. It was revealed that compounds 1 and 2 exhibited stronger antifungal activity than 3 and 4. Compounds 1 and 2 were structurally different from compounds 3 and 4 in terms of having less side chains in the fatty acid units, suggesting that the side chain length and the additional methyl group in the aliphatic chain are important for antifungal activity. These compounds also showed potent antimicrobial activity against Gram positive and Gram negative bacteria with MIC values of 0.04?0.08 uM. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2485741 Yan Ke Xue Bao. 1989 Jun;5(1-2):32-5. Lin N, Gong XM, Xie QJ, Shao MR. Study in cytotoxicity of gentamycin to corneal epithelium and endothelium in tissue culture. DRAMP18234 LLEL 4 Gageopeptide C(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Glu-Leu-3-beta-hydroxy-9,11-dimethyltridecanoic acid Non-cytotoxic antifungal agents. It was revealed that compounds 1 and 2 exhibited stronger antifungal activity than 3 and 4. Compounds 1 and 2 were structurally different from compounds 3 and 4 in terms of having less side chains in the fatty acid units, suggesting that the side chain length and the additional methyl group in the aliphatic chain are important for antifungal activity. These compounds also showed potent antimicrobial activity against Gram positive and Gram negative bacteria with MIC values of 0.04?0.08 uM. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2485741 Yan Ke Xue Bao. 1989 Jun;5(1-2):32-5. Lin N, Gong XM, Xie QJ, Shao MR. Study in cytotoxicity of gentamycin to corneal epithelium and endothelium in tissue culture. DRAMP02839 NPLSCRLNRGICVPIRCPGNLRQIGTCFTPSVKCCRWR 38 Enteric Beta-defensin (mammals, animals) O02775, Q1RMP8 Belongs to the beta-defensin family (LAP/TAP subfamily) EBD Bos taurus (Bovine) Antimicrobial, Antibacterial Transcript level Not found Not found "Tissue specificity: Inducibly expressed in enteric epithelial cells. PTM: Contains three disulfide bonds 5-34; 12-27; 17-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9488394##8589529 Infect Immun. 1998 Mar;66(3):1045-1056.##Mamm Genome. 1995 Aug;6(8):554-556. Tarver AP, Clark DP, Diamond G, Russell JP, Erdjument-Bromage H, Tempst P, Cohen KS, Jones DE, Sweeney RW, Wines M, Hwang S, Bevins CL.##Gallagher DS Jr, Ryan AM, Diamond G, Bevins CL, Womack JE. Enteric beta-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection.##Somatic cell mapping of beta-defensin genes to cattle syntenic group U25 and fluorescence in situ localization to chromosome 27. DRAMP02846 QKIAEKFSGTRRG 13 Secretolytin (mammals, animals) P23389, O02707 Belongs to the chromogranin/secretogranin protein family CHGB Bos taurus (Bovine) Antimicrobial, Antibacterial Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7744058##8603705 Eur J Biochem. 1995 Apr 15;229(2):356-368.##FEBS Lett. 1996 Feb 5;379(3):273-278. Strub JM, Hubert P, Nullans G, Aunis D, Metz-Boutigue MH.##Strub JM, Garcia-Sablone P, Lonning K, Taupenot L, Hubert P, Van Dorsselaer A, Aunis D, Metz-Boutigue MH. Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.##Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity. DRAMP02847 QAEESNLQSLVSQYFQTVADYGKDLVEKAKGSELQTQAKAYFEKTQEELTPFFKKAGTDLLNFLSSFIDPKKQPATR 77 Apolipoprotein A-II (Antimicrobial peptide BAMP-1; mammals, animals) P81644, Q2NKV9 Belongs to the apolipoprotein A2 family APOA2 Bos taurus (Bovine) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function:May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. Has antimicrobial activity. Escherichia coli and yeasts. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9538260 J Biochem. 1998 Apr;123(4):675-679. Motizuki M, Itoh T, Yamada M, Shimamura S, Tsurugi K. Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II. DRAMP02848 QAEESNLQSLVSQYFQTVADYGKDLVEKAKGSELQTQAKAYFEKTQEELTPFFKKAGTDLLNFLSSFIDPKKQPAT 76 Apolipoprotein A-II(1-76)(mammals, animals) P81644, Q2NKV9 Belongs to the apolipoprotein A2 family APOA2 Bos taurus (Bovine) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function:May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. Has antimicrobial activity. Escherichia coli and yeasts. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9538260 J Biochem. 1998 Apr;123(4):675-679. Motizuki M, Itoh T, Yamada M, Shimamura S, Tsurugi K. Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II. DRAMP02850 KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK 39 Casocidin-1 (mammals, animals) P02663, Q1RMQ6, Q9TR51 Belongs to the alpha-casein family CSN1S2 Bos taurus (Bovine) Antimicrobial, Antibacterial Protein level Not found Not found 6FS5##6FS4 Comment: No comments found on DRAMP database Staphylococcus carnosus, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7556666 FEBS Lett. 1995 Sep 25;372(2-3):185-188. Zucht HD, Raida M, Adermann K, Mägert HJ, Forssmann WG. Casocidin-I: a casein-alpha s2 derived peptide exhibits antibacterial activity. DRAMP02852 RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPPFRPPLGPFP 43 Cathelicidin-2 (Bactenecin-5, Bac5; PR-42; mammals, animals) P19660, A5PJA3, Q24JY5 Belongs to the cathelicidin family CATHL2 Bos taurus (Bovine) Antimicrobial, Antibacterial Protein level Not found BAC5 sequence consists almost exclusively of X-P-P-Y repeats. "Function: Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms. Tissue specificity: Large granules of neutrophils. Domain: BAC5 sequence consists almost exclusively of X-P-P-Y repeats. PTM: Contains two disulfide bonds and C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2229048 J Biol Chem. 1990 Nov 5;265(31):18871-18874. Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. DRAMP02853 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRP 59 Cathelicidin-3 (Bactenecin-7, Bac7; PR-59; mammals, animals) P19661, A5PJ95 Belongs to the cathelicidin family CATHL3 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found 5HAU "Function: Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms. Tissue specificity: Large granules of neutrophils. PTM: Contains two disulfide bonds." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2229048 J Biol Chem. 1990 Nov 5;265(31):18871-18874. Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. DRAMP02856 AGLFRRLRDSIRRGQQKILEKARRIGERIKDIFR 34 Cathelicidin-7 (Antibacterial peptide BMAP-34; mammals, animals) P56425, A6QPU1, B9TUC8 Belongs to the cathelicidin family CATHL7 Bos taurus (Bovine) Antimicrobial Transcript level Not found Not found "Function: Exerts a potent antimicrobial activity. Tissue specificity: Expressed in bone marrow myeloid cells, spleen and testis." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9409740##19136450 FEBS Lett. 1997 Nov 17;417(3):311-315.##J Hered. 2009 Mar-Apr;100(2):241-245. Scocchi M, Wang S, Zanetti M.##Gillenwaters EN, Seabury CM, Elliott JS, Womack JE. Structural organization of the bovine cathelicidin gene family and identification of a novel member.##Sequence analysis and polymorphism discovery in 4 members of the bovine cathelicidin gene family. DRAMP01356 FLGGLMKAFPALICAVTKKC 20 Ranalexin-1Ca (Ranatuerin 1Ca; Frogs, amphibians, animals) P82876 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=17 μM);##Gram-negative bacterium: Escherichia coli (MIC=4 μM).##Yeast: Candida albicans (MIC=14 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP02864 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPRIKCCR 40 Bovine Beta-defensin 7 (bBD-7; BNBD-7; BNDB-7; mammals, animals) P46165, Q32P80 Belongs to the beta-defensin family DEFB7 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has bactericidal activity. Active against E. coli ML35 and S. aureus 502A. Tissue specificity: Neutrophilic granules. PTM: Contains three disulfide bonds 9-38; 16-31; 21-39. (By similarity)" Gram-positive bacterium: Staphylococcus aureus 502A;##Gram-negative bacterium: Escherichia coli ML35 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8454635 J Biol Chem. 1993 Mar 25;268(9):6641-6648. Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of Beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP02871 RRHMLRCMGDLGICRPACRQSEEPYLYCRNYQPCCLPFYVRIDISGKEGKNDWSRENRWPKVS 63 Beta-defensin 119 (Defensin, beta 119; mammals, animals) Q32P86, A7LM95 Belongs to the beta-defensin family DEFB119 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Bridge Not found "Function Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." Gram-negative bacteria: Escherichia coli, Salmonella typhimurium;##Gram-positive bacteria: Staphylococcus aureus and Listeria monocytogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cormican P, Meade K.G, Lloyd A.T, Cahalane S, Narciandi F, O'Farrelly C. Novel bovine AMPs exhibit constitutive tissue-specific gene expression and significant in vitro antimicrobial efficacy against Escherichia coli, Salmonella typhimurium, Stapylococcus aureus and Listeria monocytogenes. DRAMP02874 YPGPQAKEDSEGPSQGPASREK 22 Chromacin (mammals, animals) P05059, P79392, Q2KJ52 Belongs to the chromogranin/secretogranin protein family CHGA Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has antibacterial activity against the Gram-positive bacterium M. luteus. Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binds calcium with a low-affinity. 8910482 J Biol Chem. 1996 Nov 8;271(45):28533-28540. Strub JM, Goumon Y, Lugardon K, Capon C, Lopez M, Moniatte M, van Dorsselaer A, Aunis D, Metz-Boutigue MH. Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. DRAMP02876 SYSMEHFRWGKPV 13 Alpha-melanocyte-stimulating hormone (Alpha-MSH; mammals, animals) P01190, Q05B64, Q28166, Q28167, Q28168 Belongs to the POMC family POMC Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found The last three residues KPV are antimicrobial. "Function: Has antibacterial activity against Gram-positive bacterium S. aureus. Also has antifungl activity against yeast C. albicans. Miscellaneous: Alpha-MSH has potent anti-inflammatory influences in models of acute, chronic, and systemic inflammation. Its wide spectrum of activity and low toxicity suggest that a-MSH may be useful for treatment of inflammation in human and veterinary disorders." Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10670585 J Leukoc Biol 2000; 67(2): 233-239. Cutuli M, Cristiani S, Lipton JM, Catania A. Antimicrobial effects of alpha-MSH peptides. DRAMP02879 NPVSCVRNKGICVPIRCPGNMKQIGTCVGRAVKCCR 36 Tracheal antimicrobial peptide (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database Yeast: Candida ablicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8506305 Proc Natl Acad Sci U S A. 1993 May 15;90(10):4596-600. Diamond G, Jones DE, Bevins CL. Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene. DRAMP02881 NPVSCVRNKGICVPIRCPGSMKQIGTCVGRAVKCCR 36 Antimicrobial protein exons 1-2 (mammals, animals) No entry found Not found Not found Bos taurus (Bovine) Antimicrobial, Antibacterial, Antifungal Not found dulsulfide-bond link Not found Comment: No comments found on DRAMP database Yeast: Candida ablicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8506305 Proc Natl Acad Sci U S A. 1993 May 15;90(10):4596-600. Diamond G, Jones DE, Bevins CL. Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene. DRAMP02882 MTPFWRAVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE 40 Liver-expressed antimicrobial peptide 2 (LEAP-2; mammals, animals) Q95JC3, Q32P98 Not found LEAP2 Bos taurus (Bovine) Antimicrobial Homology Not found Not found PTM: Contains two disulfide bonds 16-28; 23-33. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12493837 Protein Sci. 2003 Jan;12(1):143-152. Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-García JR, Forssmann WG, Schulz-Knappe P, Nehls MC, Wattler F, Wattler S, Adermann K. Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver. DRAMP02883 MIQIKFLCLFLAIMTIVVLDSNVAEARDCLSGTFKGPCWAWSGEKCRRLCIEEGRVSGHCSGGSKCWCEGC 71 Drosomycin-like A (Predicted) Q95NH5 Not found Drsl-B Drosophila triauraria Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11707335 Gene. 2001 Oct 31;278(1-2):177-184. Daibo S, Kimura MT, Goto SG. Upregulation of genes belonging to the drosomycin family in diapausing adults of Drosophila triauraria. DRAMP02884 DCLSGRYRGSCAVWHRKKCVDICQREGRTSGHCSPSLKCWCEGC 44 Drosomycin-like C Q86GH7 Not found Drsl1 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02885 MVQMIFLFAILAVMTIVLMEANTVLARDCLSGTFGGPCWAWSGEKCRRLCIEEGHVSGHCSGAMKCWCEGC 71 Drosomycin-like 3 (Drosomycin-like E; Drosomycin-like G; Predicted) Q8IRD7 Not found Drsl3 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02886 MQIKFLYLFLAVMTIFILGAKEADADCLSGRYGGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC 69 Drosomycin-like 5 (Drosomycin-like E; Drosomycin-like G; Predicted) Q9VZR2 Not found Drsl5 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02887 MEIKFLIVLSAVLMIIFLGAEESHADCLSGRYRGSCAVWHRKKCVDICQREGRTSGHCSPSLKCWCEGC 69 Dro1 protein (Drosomycin-like 1; Drosomycin-like C1; Predicted) Q9VZQ5, C9QPF6 Not found Drsl1 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02888 MVQIKFLFVFLAVMTIVVLAANMADADCLSGKYKGPCAVWDNEMCRRICKEEGHISGHCSPSLKCWCEGC 70 Dro2 protein (Drosomycin 2; Drosomycin-like 2; Drosomycin-like D; Drosomycin-like H; Predicted) Q7YXH9, Q9VZR3 Not found Drsl2 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02889 MAQIKGLFALLAVVTIVLMVANSASAVDCPSGRFSGPCWAWDGEQCRRLCREEGRVSGHCSASLKCWCEQC 71 Dro4 protein (Drosomycin 4; Drosomycin-like 4; Drosomycin-like F; Predicted) Q8IRD6 Not found Drsl4 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02890 MMQIKFLFTFLALLMMVILGAKEADADCLSGRYRGPCAVWDNETCRRVCREEGRGRVSGHCSARLQCWCEGC 72 Dro6 protein (Drosomycin-like 6; Drosomycin-like D; Drosomycin-like I; Predicted) Q9VZQ4 Not found Drsl6 Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16824706 Gene. 2006 Sep 1;379:26-32. Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, Xia QY, Cao Y. Functional divergence of six isoforms of antifungal peptide Drosomycin in Drosophila melanogaster. DRAMP02891 WSGFTQGVGNPVSCVRNKGICVPIRCPGNMKQIGTC 36 Tracheal antimicrobial peptide B3VHN0 Not found Not found Bos taurus (Bovine) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19181355 Res Vet Sci. 2009 Aug;87(1):59-63. López-Meza JE, Gutiérrez-Barroso A, Ochoa-Zarzosa A. Expression of tracheal antimicrobial peptide in bovine mammary epithelial cells. DRAMP02892 MKAFSIAVAVTLVLAFICILESSAVPLNGVQELEEAGSNDTPVAAHQEMSMESWMMPSRVREKRQSHISMCYWCCNCCRANKGCGYCCKF 90 Hepcidin antimicrobial peptide 1 B6ZJU9 Not found HAMP1 Pagrus auriga Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Fish Shellfish Immunol. 2009,26:483-491. Martin-Antonio B, Jimenez-Cantizano RM, Salas-Leiton E, Infante C, Manchado M. Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga). DRAMP02893 MKTFSVAVAVAVVLTFICLQESSADSVTEVQELEEPMSIGSPVAAYEEMPEESWKMPYASRSSSDRRRRRWRCRTCCRCCPRMKGCGICCRRR 93 Hepcidin antimicrobial peptide 2 B6ZJV0 Not found HAMP2 Pagrus auriga Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Fish Shellfish Immunol. 2009,26:483-491. Martin-Antonio B, Jimenez-Cantizano RM, Salas-Leiton E, Infante C, Manchado M. Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga). DRAMP02894 MKTFSVAVAVAVVLTFICLQESSAVPVTEVPELEEEISNDDAAASYEETSVETWMMPFDIRQKPHSGLIKCSYCCDCCVLGVCGMCCQ 88 Hepcidin antimicrobial peptide 3 B6ZJV1 Not found HAMP3 Pagrus auriga Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Fish Shellfish Immunol. 2009,26:483-491. Martin-Antonio B, Jimenez-Cantizano RM, Salas-Leiton E, Infante C, Manchado M. Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga). DRAMP02895 MKTFSVAVAVAVVLTFICLQESSAVSFTEVQEQEEPMSNDSPVAAHEEMSEESWKMPYNNRHKRSPAGRNKRRRRCRFCCGCCPNMIGCGTCCKF 95 Hepcidin antimicrobial peptide 4 B6ZJV2 Not found HAMP4 Pagrus auriga Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Fish Shellfish Immunol. 2009,26:483-491. Martin-Antonio B, Jimenez-Cantizano RM, Salas-Leiton E, Infante C, Manchado M. Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga). DRAMP02896 MFTLKKSLLLLFFLGTINLSLCEQERNADEEERRDDSDKRDVEVEKRFLSTLLKVAFKVVPTLFCPITKKC 71 Brevinin-1-AJ1 antimicrobial peptide K7Z430 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial, Antibacterial, Antifungal Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database [Ref.22828809] 7.62% hemolytic activity at 25 μg/ml,24.58% hemolytic activity at 50 μg/ml, 83.05% hemolytic activity at 100 μg/ml, 87.65% hemolytic activity at 200 μg/ml against rabbit red blood cells Cyclic Free Cyclization (Cys65 and Cys71) Disulfide bond between Cys65 and Cys71. L No cytotoxicity information found Not found 22828809 Amino Acids. 2012 Jul 25 He X, Yang S, Wei L, Liu R, Lai R, Rong M. Antimicrobial peptide diversity in the skin of the torrent frog, Amolops jingdongensis. DRAMP02897 MFTLKKSLLLLFFLGTINLFFCEQERDADEEERRDDDEMDVEVEKRFLPLAVSLAANFLPKLFCKITKKC 70 Brevinin-1-AJ2 antimicrobial peptide K7ZJ55 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Amino Acids. 2012 Jul 25 He X, Yang S, Wei L, Liu R, Lai R, Rong M. Antimicrobial peptide diversity in the skin of the torrent frog, Amolops jingdongensis. DRAMP02898 MFTLKKSLLLLFFLGTINLSLCEQERDADEEERRDDDEMDVEVEKRFLPLAVSLAANFLPKLFCKITKNVETLEMELEII 80 Brevinin-1-AJ3 antimicrobial peptide K7Z8Z4 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Amino Acids. 2012 Jul 25 He X, Yang S, Wei L, Liu R, Lai R, Rong M. Antimicrobial peptide diversity in the skin of the torrent frog, Amolops jingdongensis. DRAMP02899 MFTLKKSLLLLFFLGTINLSLCEQERDADEEERRDDDEMDVEVEKRFLPLVASLAANFLPKLFCKITKKC 70 Brevinin-1MT1 antimicrobial peptide E1B240 Not found Not found Amolops mantzorum Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops mantzorum. DRAMP02900 MFTLKKSMLLLFFLGTINLSLCEQERNADEEERRDDDEMDVEVEKRFLPMLAGLAANFLPKLFCKITKKC 70 Brevinin-1MT2 antimicrobial peptide E1B241 Not found Not found Amolops mantzorum Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops mantzorum. DRAMP02901 CLGVGSCNNFAGCGYAIVCFW 21 Tricyclic peptide MS-271 P85078 Not found Not found Streptomyces sp. Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Inhibits chicken myosin light chain kinase with an IC50 of 8 M. Antibacterial activity against the Gram-positive bacteria. No antibacterial activity against the Gram-negative bacteria E. coli, K. pneumoniae, P. aeruginosa, P. vulgaris, S. sonnei and S. typhosa. No antifungal activity against C. albicans. Caution: The isopeptide linked residue 9 is shown as Asn rather than Asp as mentioned in Ref.1, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible. PTM: Contains two disulfide bonds and D-amino acid at position 21." Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus, Enterococcus faecium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8689231 Bioorg Med Chem. 1996 Jan;4(1):115-120. Yano K, Toki S, Nakanishi S, Ochiai K, Ando K, Yoshida M, Matsuda Y, Yamasaki M. MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271. DRAMP02902 ADDKNPLEEFRETNYEVFLEIAKNGLKATSNPKRVVIVGAGMAGLSAAY 49 L-amino-acid oxidase (LAAO, LAO; BpirLAAO-I; reptilia, animals) P0C2D1 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Bothrops pirajai (Piraja's lance head) Antimicrobial, Antibacterial, Anti-Gram-, Antiparasitic Protein level Not found Not found "FunctionCatalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. This protein may also have activities in hemorrhage, hemolysis, and apoptosis. Tissue specificity: Expressed by the venom gland. Miscellaneous: Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production." Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa. Leishmania sp.. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16809041 Bioorg Med Chem. 2006 Oct 15;14(20):7034-7043. Izidoro LF, Ribeiro MC, Souza GR, Sant'Ana CD, Hamaguchi A, Homsi-Brandeburgo MI, Goulart LR, Beleboni RO, Nomizo A, Sampaio SV, Soares AM, Rodrigues VM. Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom. DRAMP02904 AAGNPSETGGAVATYSTAVGSFLDGTVKVVATGGASRVPGNCGTAAVLECDNPESFDGTRAWGDLSADQGTGEDAPPETASLIFAVN 87 Antibacterial substance A P01548 Not found Not found Streptomyces carzinostaticus Antimicrobial Protein level Not found Not found "Function: May have antibacterial activity. PTM: Contains one disulfide bond 42-50." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 5353565 Chem Pharm Bull (Tokyo). 1969 Oct;17(10):2188-2191. Sato H, Tanimura T, Nakajima T, Tamura Z. The total amino acid sequence of substance A produced by Streptomyces carzinostaticus. DRAMP02905 KWKIFKKIEHMGQNIRDGLIKAGPAVQVVGQAATIYKG 38 Hinnavin II Q68KS5 Not found Not found Artogeia rapae Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16616565 Comp Biochem Physiol B Biochem Mol Biol. 2006 Jun;144(2):199-205. Yoe SM, Kang CS, Han SS, Bang IS. Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae. DRAMP02906 RRLRPRRPRLPRPRPRPRPRPRSLPLPRPQPRRIPRPILLPWRPPRPIPRPQIQPIPRWL 60 OaBac7.5 (mammals, animals) No entry found Not found Not found Ovis aries (Sheep) Unknown Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14651991 Biochem Biophys Res Commun. 2003 Dec 26;312(4):1139-1146. Anderson RC, Yu PL. Isolation and characterisation of proline/arginine-rich cathelicidin peptides from ovine neutrophils. DRAMP02907 RRLRPRRPRLPRPRPRPRPRPRSLPLPRPKPRPIPRPLPLPRPRPKPIPRPLPLPRPRPRRIPRPLPLPRPRPRPIPRPLPLPQPQPSPIPRPL 94 OaBac11 (mammals, animals) No entry found Not found Not found Ovis aries (Sheep) Unknown Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14651991 Biochem Biophys Res Commun. 2003 Dec 26;312(4):1139-1146. Anderson RC, Yu PL. Isolation and characterisation of proline/arginine-rich cathelicidin peptides from ovine neutrophils. DRAMP02908 QGVRNRLSCHRNKGVCVPSRCPRHMRQIGTCRGPPVKCCRKK 42 Beta-defensin 1 (BD-1; sBD-1; mammals, animals) O19038 Belongs to the beta-defensin family DEFB1 Ovis aries (Sheep) Antimicrobial, Antibacterial Homology Bridge Not found Function: Has bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9478010##9461419 J Nutr. 1998 Feb;128(2 Suppl):297S-299S.##Gene. 1998 Jan 5;206(1):85-91. Huttner K.M, Brezinski-Caliguri D.J, Mahoney M.M, Diamond G.##Huttner K.M, Lambeth M.R, Burkin H.R, Broad T.E. Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract.##Localization and genomic organization of sheep antimicrobial peptides genes. DRAMP02909 HGVTDSLSCRWKKGICVLTRCPGTMRQIGTCFGPPVKCCRLK 42 Beta-defensin 2 (BD-2; sBD-2; mammals, animals) O19039 Belongs to the beta-defensin family DEFB2 Ovis aries (Sheep) Antimicrobial, Antibacterial Homology Bridge Not found Function: Has bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9478010##9461419 J Nutr. 1998 Feb;128(2 Suppl):297S-299S.##Gene. 1998 Jan 5;206(1):85-91. Huttner K.M, Brezinski-Caliguri D.J, Mahoney M.M, Diamond G.##Huttner K.M, Lambeth M.R, Burkin H.R, Broad T.E. Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract.##Localization and genomic organization of sheep antimicrobial peptides genes. DRAMP02914 RICRIIFLRVCR 12 Cathelicidin-1 (Bactenecin-1, Bac1; Cyclic dodecapeptide; ma P54230 Belongs to the cathelicidin family CATHL1A Ovis aries (Sheep) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Bridge Not found Function: Potent microbicidal activity; active against S. aureus and E. coli (By similarity). Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7498547##9461419 FEBS Lett. 1995 Dec 4;376(3):225-228.##Gene. 1998 Jan 5;206(1):85-91. Bagella L, Scocchi M, Zanetti M.##Huttner KM, Lambeth MR, Burkin HR, Burkin DJ, Broad TE. cDNA sequences of three sheep myeloid cathelicidins.##Localization and genomic organization of sheep antimicrobial peptide genes. DRAMP02915 RFRPPIRRPPIRPPFRPPFRPPVRPPIRPPFRPPFRPPIGPFP 43 Cathelicidin-2 (Bactenecin-5, Bac5; OaBac5; mammals, animals) P79362, P79363 Belongs to the cathelicidin family CATHL2 Ovis aries (Sheep) Antimicrobial Transcript level Not found Not found Function: Has potent antimicrobial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipipolysaccharides (LPS)-binding 9461419 Gene. 1998 Jan 5;206(1):85-91. Huttner KM, Lambeth MR, Burkin HR, Burkin DJ, Broad TE. Localization and genomic organization of sheep antimicrobial peptide genes. DRAMP02916 RRLRPRHQHFPSERPWPKPLPLPLPRPGPRPWPKPLPLPLPRPGLRPWPKPL 52 OaBac6 No entry found Not found Not found Ovis aries (Sheep) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14651991 Biochem Biophys Res Commun. 2003 Dec 26;312(4):1139-1146. Anderson RC, Yu PL. Isolation and characterisation of proline/arginine-rich cathelicidin peptides from ovine neutrophils. DRAMP02917 DTHFPICIFCCGCCKTPKCGLCCKT 25 Hepcidin (dogs, mammals, animals) Q5U9D2, Q5EES0 Belongs to the glycosyl hydrolase 22 family HAMP Canis familiaris (Dog) (Canis lupus familiaris) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##PubMed ID is not available Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases##Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Shi J, Wei Y, Boothe D.##Li XD, Zhao TZ, Sun M, Tian KG, Chen XZ. Identification of dog hepcidin.##Identification of dog hepcidin in China. DRAMP02918 MRPLYLLLLLLCLLFSYLPPGAGFLTGIGQRSDQYICARKGGTCNFSPCPLFTRIDGTCYRGKAKCCMP 69 Beta-defensin 1 Q30KV2 Not found CBD1 Canis familiaris (Dog) (Canis lupus familiaris) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02919 NFDPKYRFERCAKVKGICKTFCDDDEYDYGYCIKWRNQCCI 41 Beta-defensin 110 (Defensin, beta 110; dogs, mammals, animals) Q30KU3 Belongs to the glycosyl hydrolase 22 family DEFB110 Canis familiaris (Dog) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02920 KHHILRCMGNTGICRPSCRKTEQPYLYCLNYQSCCLQSYMRISISGREEKDDWSQQNRWPKIS 63 Beta-defensin 119 (Defensin, beta 119; dogs, mammals, animals) Q30KT5 Belongs to the glycosyl hydrolase 22 family DEFB119 Canis familiaris (Dog) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02921 MRLLFLLFLLLVCLVQMTSGREKRRKSLECERMGGVCKHQKTHGCSILPAECKSRNKHCCRV 62 Beta-defensin 138 Q30KR8 Not found CBD138 Canis familiaris (Dog) (Canis lupus familiaris) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP02927 NKDCKYWCKDNLGLNYCCGQPGVTYPPFTKKHLGRCPAVRDTCTGVRTQLPTYCPHDGACQFRSKCCYDTCLKHHVCKTAEYPY 84 Antibacterial 11.5 kDa protein (crabs, Arthropods, animals) Q9Y099 Not found 11.5 kDa Carcinus maenas (Common shore crab) (Green crab) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16712935 Mol Immunol. 2007 Feb;44(5):943-949. Brockton V, Hammond JA, Smith VJ. Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas. DRAMP02928 XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS 30 Antibacterial 6.5 kDa protein (crabs, Arthropods, animals) P82964 Not found Not found Carcinus maenas (Common shore crab) (Green crab) Antimicrobial, Antibacterial Protein level Not found Not found Function: Strong antimicrobial activity against Psychrobacter immobilis and M. luteus, less active against E. coli D22. Psychrobacter immobilis, Micrococcus luteus, Escherichia coli D22. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8856051 Eur J Biochem. 1996 Sep 15;240(3):532-539. Schnapp D, Kemp GD, Smith VJ. Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas. DRAMP02929 GQALNKLMPKIVSAIIYMIGQPNAGVTFLGHQCLVESTRQPDGFYTAKMWCTSWTSDNPIVGEGRSRVELEALKGSIRNFVQTASDYKKFTIEEVEDWIAS 102 Antimicrobial protein 1 A1YV58 Not found AP Scylla serrata (Mud crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Tissue specificity: Strongly expressed in gills, hemocytes and reproductive tract, with weaker expression in muscle, heart and digestive tract. Not detected in eyes and hepatopancreas (at protein level). Gram-positive bacteria: Escherichia coli (MIC<50 µg/ml), Pseudomonas aeruginosa (MIC<25 µg/ml);##Gram-negative bacteria: Staphylococcus aureus (MIC<100 µg/ml), Streptococcus pyogenes (MIC<50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19219229 Acta Biochim Pol. 2009;56(1):71-82. Yedery RD, Reddy KV. Purification and characterization of antibacterial proteins from granular hemocytes of Indian mud crab, Scylla serrata. DRAMP02930 HSPGGA 6 Antimicrobial protein 2 (crabs, Arthropods, animals) B3A0L8 Not found Not found Scylla serrata (Mud crab) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity. Gram-positive bacterium: Bacillus flexus;##Gram-negative bacteria: Escherichia coli, Vibrio harveyi. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2011) to UniProtKB Meiyalagan V, Arumugam M. Antibacterial protein (Scylla serrata). DRAMP02935 RRWCFRVCYKGFCYRKCR 18 Polyphemusin-2 (Polyphemusin II; crabs, Arthropods, animals) P14216 Belongs to the tachyplesin/polyphemusin family Not found Limulus polyphemus (Atlantic horseshoe crab) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found "Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria. Tissue specificity: Hemocytes. PTM: Contains two disulfide bonds 4-17; 8-13." Yeast: Candida albicans M9. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys4 and Cys17,Cys8 and Cys13. L No cytotoxicity information found Not found 2514185##15134657 J Biochem. 1989 Oct;106(4):663-668.##Biochim Biophys Acta. 2004 May 6;1698(2):239-250. Miyata T, Tokunaga F, Yonega T, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y.##Powers J.P, Rozek A, Hancock R.E. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity.##Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I. DRAMP02936 NPLIPAIYIGATVGPSVWAYLVALVGAAAVTAANIRRASSDNHSCAGNRGWCRSKCFRHEYVDTYYSAVCGRYFCCRSR 79 Big defensin (crabs, Arthropods, animals) P80957 Belongs to the big defensin family Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Not found 2RNG resolved by NMR. "Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro. Tissue specificity: Expressed in all tissues examined, including hemocytes, heart, hepatopancreas, stomach, intestine and skeletal muscle. PTM: Contains three disulfide bonds." Gram-negative bacteria: Escherichia coli 09:K39 (IC50=5 µg/ml), Salmonella typhimurium LT2 (IC50=20 µg/ml), S. minnesota R595 (IC50=1.3 µg/ml), Klebsiella pneumoniae (IC50>10 µg/ml);##Gram-positive bacteria: Staphylococcus aureus (IC50<2.5 µg/ml).##Yeast: Candida albicans (IC50>20 µg/ml)(Ref.1).##Note: Washed with a phosphate buffered saline (PBS, pH 7.0). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 8586631##18785751 J Biochem. 1995 May;117(5):1131-1137.##Biochemistry. 2008 Oct 7;47(40):10611-9. Saito T, Kawabata S, Shigenaga T, Takayenoki Y, Cho J, Nakajima H, Hirata M, Iwanaga S.##Kouno T, Fujitani N, Mizuguchi M, Osaki T, Nishimura S, Kawabata S, Aizawa T, Demura M, Nitta K, Kawano K. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity.##A novel beta-defensin structure: a potential strategy of big defensin for overcoming resistance by Gram-positive bacteria. DRAMP02937 YLAFRCGRYSPCLDDGPNVNLYSCCSFYNCHKCLARLENCPKGLHYNAYLKVCDWPSKAGCTSVNKECHLWKT 73 Tachycitin (crabs, Arthropods, animals) P91818 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Beta strand Not found 1DQC resolved by NMR. Comment: No comments found on DRAMP database Gram-positive bacteria: Staphylococcus aureus (IC50=56 µg/ml);##Gram-negative bacteria: Escherichia coli 363 (IC50=33 µg/ml), Escherichia coli B (IC50=2 µg/ml), Salmonella typhimurium LT2 (IC50=44 µg/ml), S. minnesota R595 (IC50=41 µg/ml), Klebsiella pneumoniae (IC50=32 µg/ml).##Yeast: Candida albicans (IC50=52 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 9010778##10770921 J Biochem. 1996 Dec;120(6):1253-1260.##J Biol Chem. 2000 Jun 16;275(24):17929-17932. Kawabata S, Nagayama R, Hirata M, Shigenaga T, Agarwala KL, Saito T, Cho J, Nakajima H, Takagi T, Iwanaga S.##Suetake T, Tsuda S, Kawabata S, Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K. Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity.##Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. DRAMP18230 LLLE 4 Gageotetrin B (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Leu-OMeGlu-3-hydroxy-11-methyltridecanoic acid (HTDA) Noncytotoxic Antimicrobial Linear Lipopeptides Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24502521 Org Lett. 2014 Feb 7;16(3):928-31. Tareq FS, Lee MA, Lee HS, Lee YJ, Lee JS, Hasan CM, Islam MT, Shin HJ. Gageotetrins A-C, noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis. DRAMP18231 LLLE 4 Gageotetrin C (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Leu-Glu-3-hydroxy-8,10-dimethyldodecanoic acid (HDDA) Noncytotoxic Antimicrobial Linear Lipopeptides Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24502521 Org Lett. 2014 Feb 7;16(3):928-31. Tareq FS, Lee MA, Lee HS, Lee YJ, Lee JS, Hasan CM, Islam MT, Shin HJ. Gageotetrins A-C, noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis. DRAMP18232 LLEL 4 Gageopeptide A(Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Glu-Leu-3-beta-hydroxy-11-methyltridecanoic acid Non-cytotoxic antifungal agents. It was revealed that compounds 1 and 2 exhibited stronger antifungal activity than 3 and 4. Compounds 1 and 2 were structurally different from compounds 3 and 4 in terms of having less side chains in the fatty acid units, suggesting that the side chain length and the additional methyl group in the aliphatic chain are important for antifungal activity. These compounds also showed potent antimicrobial activity against Gram positive and Gram negative bacteria with MIC values of 0.04?0.08 uM. Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2485741 Yan Ke Xue Bao. 1989 Jun;5(1-2):32-5. Lin N, Gong XM, Xie QJ, Shao MR. Study in cytotoxicity of gentamycin to corneal epithelium and endothelium in tissue culture. DRAMP02939 RWCFRVCYRGICYRKCR 17 Tachyplesin-2 (Tachyplesin II; crabs, Arthropods, animals) P14214 Belongs to the tachyplesin/polyphemusin family Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found Comment: No comments found on DRAMP database Yeast: Candida albicans M9. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation (Arg17) Disulfide bond between Cys3 and Cys16,Cys7 and Cys12. L No cytotoxicity information found Not found 2514185 J Biochem. 1989 Oct;106(4):663-668. Miyata T, Tokunaga F, Yonega T, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. DRAMP02940 KWCFRVCYRGICYRKCR 17 Tachyplesin-3 (Tachyplesin III; crabs, Arthropods, animals) P18252 Belongs to the tachyplesin/polyphemusin family Not found Tachypleus gigas (Southeast Asian horseshoe crab) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria. Tissue specificity: Hemocytes. PTM: Contains two disulfide bonds 3-16; 7-12, and Arginine amide at R17." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation (Arg17) Disulfide bond between Cys3 and Cys16,Cys7 and Cys12. L No cytotoxicity information found Not found 2229025 J Biochem. 1990 Aug;108(2):261-266. Muta T, Fujimoto T, Nakajima H, Iwanaga S. Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. DRAMP02941 YSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRF 44 Tachystatin-A1 (crabs, Arthropods, animals) P0C1Z7 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Exhibits stronger antimicrobial activity against the Gram-positive bacterium S. aureus and fungi C. albicans and P. pastoris than Gram-negative bacterium E. coli. Binds to chitin (8.4 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. Tissue specificity: Granular hemocytes, small secretory granules. PTM: Contains three disulfide bonds (By similarity)." Gram-negative bacterium: Escherichia coli (IC50=25 µg/ml);##Gram-positive bacterium: Staphylococcus aureus (IC50=4.2 µg/ml).##Fungi: Candida albicans (IC50=3.0 µg/ml), Pichia pastoris (IC50=0.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10473569 J Biol Chem. 1999 Sep 10;274(37):26172-26178. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins. DRAMP02942 YSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 44 Tachystatin-A2 (crabs, Arthropods, animals) Q9U8X3 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Beta strand Not found 1CIX resolved by NMR. "Function: Exhibits stronger antimicrobial activity against the Gram-positive bacterium S. aureus and fungi C. albicans and P. pastoris than Gram-negative bacterium E. coli. Binds to chitin (8.4 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. Tissue specificity: Granular hemocytes, small secretory granules. PTM: Contains three disulfide bonds." Gram-positive bacterium: Staphylococcus aureus (IC50=4.2 µg/ml);##Gram-negative bacterium: Escherichia coli (IC50=25 µg/ml).##Fungi: Candida albicans (IC50=3.0 µg/ml), Pichia pastoris (IC50=0.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10473569##11959852 J Biol Chem. 1999 Sep 10;274(37):26172-26178.##J Biol Chem. 2002 Jun 28;277(26):23651-23657. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S.##Fujitani N, Kawabata S, Osaki T, Kumaki Y, Demura M, Nitta K, Kawano K. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins.##Structure of the antimicrobial peptide tachystatin A. DRAMP02943 YVSCLFRGARCRVYSGRSCCFGYYCRRDFPGSIFGTCSRRNF 42 Tachystatin-B1 (crabs, Arthropods, animals) P0C1Z8 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Beta strand Not found 2DCV resolved by NMR. "Function: Exhibits stronger antimicrobial activity against the Gram-positive bacterium S. aureus and fungi C. albicans and P. pastoris than Gram-negative bacterium E. coli. Binds to chitin (4.3 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. Tissue specificity: Granular hemocytes, small secretory granules. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin." Gram-positive bacterium: Staphylococcus aureus (IC50=7.4 µg/ml).##Fungi: Candida albicans (IC50=3.0 µg/ml), Pichia pastoris (IC50=0.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10473569##17394123 J Biol Chem. 1999 Sep 10;274(37):26172-26178.##J Pept Sci. 2007 Apr;13(4):269-279. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S.##Fujitani N, Kouno T, Nakahara T, Takaya K, Osaki T, Kawabata S, Mizuguchi M, Aizawa T, Demura M, Nishimura S, Kawano K. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins.##The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. DRAMP02944 YITCLFRGARCRVYSGRSCCFGYYCRRDFPGSIFGTCSRRNF 42 Tachystatin-B2 (crabs, Arthropods, animals) P0C1Z9 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Beta strand Not found 2DCW resolved by NMR. "Function: Exhibits stronger antimicrobial activity against the Gram-positive bacterium S. aureus and fungi C. albicans and P. pastoris than Gram-negative bacterium E. coli. Binds to chitin (4.3 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. Tissue specificity: Granular hemocytes, small secretory granules. Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin." Gram-positive bacterium: Staphylococcus aureus (IC50=7.4 µg/ml).##Fungi: Candida albicans (IC50=3.0 µg/ml), Pichia pastoris (IC50=0.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10473569##17394123 J Biol Chem. 1999 Sep 10;274(37):26172-26178.##J Pept Sci. 2007 Apr;13(4):269-279. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S.##Fujitani N, Kouno T, Nakahara T, Takaya K, Osaki T, Kawabata S, Mizuguchi M, Aizawa T, Demura M, Nishimura S, Kawano K. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins.##The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. DRAMP02945 DYDWSLRGPPKCATYGQKCRTWSPPNCCWNLRCKAFRCRPR 41 Tachystatin-C (crabs, Arthropods, animals) P0C200 Not found Not found Tachypleus tridentatus (Japanese horseshoe crab) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Causes hemolysis on sheep erythrocytes, probably by forming ion-permeable pores. Gram-negative bacterium: Escherichia coli (IC50=1.2 µg/ml);##Gram-positive bacterium: Staphylococcus aureus (IC50=0.8 µg/ml).##Fungi: Candida albicans (IC50=0.9 µg/ml), Pichia pastoris (IC50=0.3 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 10473569 J Biol Chem. 1999 Sep 10;274(37):26172-26178. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins. DRAMP02946 YEALVTSILGKLTGLWHNDSVDFMGHICYFRRRPKIRRFKLYHEGKFWCPGWAPFEGRCKYCVVF 65 PtALF1 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 1; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CYFRRRPKIRRFKLYHEGKFWC) and two conserved cysteine residues which can form a disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21168510 Fish Shellfish Immunol. 2011 Feb;30(2):583-591. Liu Y, Cui Z, Luan W, Song C, Nie Q, Wang S, Li Q. Three isoforms of anti-lipopolysaccharide factor identified from eyestalk cDNA library of swimming crab Portunus trituberculatus. DRAMP02947 YEALVTSILGKLTGLWHNDSVDFMGHICYFRRRPKIRRFKLYHEGKFWCPGWAPFEGRSRTKSRSGSSREATKDFVRKALQNGLVTQQDASLWLN 95 PtALF2 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 2; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CYFRRRPKIRRFKLYHEGKFWC) and two conserved cysteine residues which can form a disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21168510 Fish Shellfish Immunol. 2011 Feb;30(2):583-591. Liu Y, Cui Z, Luan W, Song C, Nie Q, Wang S, Li Q. Three isoforms of anti-lipopolysaccharide factor identified from eyestalk cDNA library of swimming crab Portunus trituberculatus. DRAMP18228 LLDVLLE 7 Gageostatin C (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Asp-Val-Leu-Leu-Glu-(E)-7,9-dimethylundec-2-enoic acid surfactin like heptapeptides, cytotoxic. It is noteworthy that these compounds 1 Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85. Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis. DRAMP18229 LE 2 Gageotetrin A (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antifungal, Antibacterial, Anti-Gram+, Anti-Gram- Not found Leu-Glu-3-hydroxy-11-methyltridecanoic acid (HTDA) Noncytotoxic Antimicrobial Linear Lipopeptides Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24502521 Org Lett. 2014 Feb 7;16(3):928-31. Tareq FS, Lee MA, Lee HS, Lee YJ, Lee JS, Hasan CM, Islam MT, Shin HJ. Gageotetrins A-C, noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis. DRAMP02949 GWLDIVKAIVVPAARETIKTQEITLLDHYCTLSRSPYIKSLELHYRAEVTCPGWTIIRGRGSNHRNPTNSGKDALKDFMTQAVAAGLVTKEEAAPWLN 98 PtALF4 (Portunus trituberculatus anti-lipopolysaccharide factor isoform 4; crabs, Arthropods, ani No entry found Not found Not found Portunus trituberculatus (Swimming Crab) Antimicrobial, Antibacterial Not found Not found Not found Contains a signal peptide and an LPS-binding Domain: (CTLSRSPYIKSLELHYRAEVTC) and two conserved cysteine residues which can form a disulfide bridge. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 21362485##22333564 Fish Shellfish Immunol. 2011 Jul;31(1):29-42.##Fish Shellfish Immunol. 2012 May;32(5):724-731. Liu Y, Cui Z, Song C, Wang S, Li Q.##Liu Y, Cui Z, Li X, Song C, Li Q, Wang S. Multiple isoforms of immune-related genes from hemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.##A new anti-lipopolysaccharide factor isoform (PtALF4) from the swimming crab Portunus trituberculatus exhibited structural and functional diversity of ALFs. DRAMP02954 SRWPSPGRPRPFPGRPNPIFRPRPCICVRQPCPCDTY 37 Arasin 2 (Pro-rich, Arg-rich; crabs, Arthropods, animals) A6XMY1 Not found Not found Hyas araneus (Great spider crab) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17658600 Dev Comp Immunol. 2008;32(3):275-285. StensvÃ¥g K, Haug T, Sperstad SV, Rekdal O, Indrevoll B, Styrvold OB. Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. DRAMP02955 LGAWLAGKVAGTVATYAWNRYV 22 Hedistin (marine annelid, Metazoa) Q1PG44 Not found Not found Hediste diversicolor Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus (MRSA);##Gram-negative bacterium: Vibrio alginolyticus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17210178 Dev Comp Immunol. 2007;31(8):749-762. Tasiemski A, Schikorski D, Le Marrec-Croq F, Pontoire-Van Camp C, Boidin-Wichlacz C, Sautière PE. Hedistin: A novel antimicrobial peptide containing bromotryptophan constitutively expressed in the NK cells-like of the marine annelid, Nereis diversicolor. DRAMP02957 MWHLKLFAVLVICLLLAVQVHGSPIPELSSAKRRPRRITPFWRAVSLRPIGASCRDDSECLTRLCRKRRCSLSVAQE 77 Liver-expressed antimicrobial protein 2 (pigs, mammals, animals) Q8MJ79 Not found Not found Sus scrofa (Pig) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16051358 Dev Comp Immunol. 2006;30(4):357-366. Sang Y, Ramanathan B, Minton JE, Ross CR, Blecha F. Porcine liver-expressed antimicrobial peptides, hepcidin and LEAP-2: cloning and induction by bacterial infection. DRAMP02958 QLRYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTRQPPELCDFKEKQCVGTVTLNPSIHSLDISCNEIQSV 96 Cathelin (pigs, mammals, animals) P15175 Belongs to the cathelicidin family Not found Sus scrofa (Pig) Unknown Protein level Not found Not found "Function: Probably a microbicidal peptide. PTM: contains two disulfide bonds 55-66; 73-90." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8262248 FEBS Lett. 1993 Dec 27;336(2):289-292. Lenarcic B, Ritonja A, Dolenc I, Stoka V, Berbic S, Pungercar J, Strukelj B, Turk V. Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family. DRAMP02967 RADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK 32 Antibacterial peptide 3910 (AP 3910; pigs, mammals, animals) P80230, P37110 Belongs to the E(R) family ERH Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: May have a role in the cell cycle (By similarity). AP 3910 has antibacterial activity against B. megaterium. Subunit structure: Homodimer (By similarity)." Gram-positive bacterium: Bacillus megaterium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8375398 Eur J Biochem. 1993 Sep 1;216(2):623-629. Agerberth B, Boman A, Andersson M, Jörnvall H, Mutt V, Boman HG. Isolation of three antibacterial peptides from pig intestine: gastric inhibitory polypeptide (7-42), diazepam-binding inhibitor (32-86) and a novel factor, peptide 3910. DRAMP02968 AFPPPNVPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPPFPPPIFPGPWFPPPPPFRPPPFGPPRFP 79 Prophenin-1 (C6, PF-1; Pro-rich; pigs, mammals, animals) P51524 Belongs to the cathelicidin family Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria. Gram-positive bacterium: Listeria monocytogenes;##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7698355##7576250 FEBS Lett. 1995 Mar 27;362(1):65-69.##Biol Chem Hoppe Seyler. 1995 Aug;376(8):507-510. Harwig SS, Kokryakov VN, Swiderek KM, Aleshina GM, Zhao C, Lehrer RI.##Strukelj B, Pungercar J, Kopitar G, Renko M, Lenarcic B, Berbić S, Turk V. Prophenin-1, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes.##Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor. DRAMP02969 AFPPPNVPGPRFPPPNVPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPPFPPPIFPGPWFPPPPPFRPPPFGPPRFP 79 Prophenin-2 (C12, PF-2, PR-2; Pro-rich; pigs, mammals, animals) P51525 Belongs to the cathelicidin family Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria. Gram-positive bacterium: Listeria monocytogenes;##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8262247##7498526 FEBS Lett. 1993 Dec 27;336(2):284-288.##FEBS Lett. 1995 Dec 4;376(3):130-134. Pungercar J, Strukelj B, Kopitar G, Renko M, Lenarcic B, Gubensek F, Turk V.##Zhao C, Ganz T, Lehrer RI. Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow.##Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39. DRAMP02971 RGGRLCYCRRRFCICV 16 Protegrin-2 (Protegrin 2; PG-2; pigs, mammals, animals) P32195 Belongs to the cathelicidin family NPG2 Sus scrofa (Pig) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found 2MUH resolved by NMR. "Function: Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. PTM: Contains two disulfide bonds 6-15; 8-13 and Valine amide at V16." Gram-positive bacterium: Listeria moncyrogenes strain EGD (MIC>25 µg/ml);##Gram-negative bacterium: Escherichia coli ML-35 (MIC>25 µg/ml).##Yeast: Candida albicans strain 820 (MIC>25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8335113##8250892 FEBS Lett. 1993 Jul 26;327(2):231-236.##Biochem Biophys Res Commun. 1993 Nov 15;196(3):1363-1368. Kokryakov VN, Harwig SS, Panyutich EA, Shevchenko AA, Aleshina GM, Shamova OV, Korneva HA, Lehrer RI.##Storici P, Zanetti M. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins.##A novel cDNA sequence encoding a pig leukocyte antimicrobial peptide with a cathelin-like pro-sequence. DRAMP02972 RGGGLCYCRRRFCVCVGR 18 Protegrin-3 (Protegrin 3; PG-3; pigs, mammals, animals) P32196 Belongs to the cathelicidin family NPG3 Sus scrofa (Pig) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Bridge Not found 2MZ6 resolved by NMR. "Function: Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. PTM: Probablely contains two disulfide bonds 6-15; 8-13 and Arginine amide at R18." Gram-positive bacterium: Listeria moncyrogenes strain EGD;##Gram-negative bacterium: Escherichia coli ML-35.##Yeast: Candida albicans strain 820. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8335113 FEBS Lett. 1993 Jul 26;327(2):231-236. Kokryakov VN, Harwig SS, Panyutich EA, Shevchenko AA, Aleshina GM, Shamova OV, Korneva HA, Lehrer RI. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. DRAMP02973 RGGRLCYCRGWICFCVGR 18 Protegrin-4 (Protegrin 4; PG-4; pigs, mammals, animals) P49933 Belongs to the cathelicidin family NPG4 Sus scrofa (Pig) Antimicrobial, Antibacterial, Antifungal Protein level Bridge Not found "Function: Microbicidal activity (By similarity). PTM: Contains two disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8013647##12705830 FEBS Lett. 1994; 346: 285-288.##ochemistry. 2003 Apr 29;42(16):4669-4680. Zhao C, Liu L, Lehrer RI.##Yang Y, Sanchez JF, Strub MP, Brutscher B, Aumelas A. Identification of a new member of the protegrin family by cDNA cloning.##NMR structure of the cathelin-like domain of the protegrin-3 precursor. DRAMP02974 RGGRLCYCRPRFCVCVGR 18 Protegrin-5 (Protegrin 5; PG-5; pigs, mammals, animals) P49934 Belongs to the cathelicidin family NPG5 Sus scrofa (Pig) Antimicrobial, Antibacterial, Antifungal Homology Bridge Not found "Function: Microbicidal activity (By similarity). PTM: Contains two disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7628604 FEBS Lett. 1995 Jul 17;368(2):197-202. Zhao C, Ganz T, Lehrer RI. The structure of porcine protegrin genes. DRAMP02976 NIGNSVSCLRNKGVCMPGKCAPKMKQIGTCGMPQVKCCKRK 41 Beta-defensin 1 (BD-1; Defensin, beta 1; pigs, mammals, animals) O62697 Belongs to the beta-defensin family DEFB1 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds 8-37; 15-30; 20-38 (By similarity)." Gram-positive bacteria: Listeria monocytogenes, Streptococcus suis, Actinobacillus pleuropneumoniae;##Gram-negative bacterium: Escherichia coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16552064##9537511##10446172 Infect Immun. 2006 Apr;74(4):2338-2352.##FEBS Lett. 1998 Mar 6;424(1-2):37-40.## Biol Chem. 1999 Aug 20;274(34):24031-24037. Elahi S, Buchanan RM, Attah-Poku S, Townsend HG, Babiuk LA, Gerdts V.##Zhang G, Wu H, Shi J, Ganz T, Ross CR, Blecha F.##Zhang G, Hiraiwa H, Yasue H, Wu H, Ross CR, Troyer D, Blecha F. The host defense peptide Beta-defensin 1 confers protection against Bordetella pertussis in newborn piglets.##Molecular cloning and tissue expression of porcine beta-defensin-1.##Cloning and characterization of the gene for a new epithelial beta-defensin. Genomic structure, chromosomal localization, and evidence for its constitutive expression. DRAMP02977 SVSCLRNKGVCMPGKCAPKMKQIGTCGMPQVKCCKRK 37 pBD-1 (porcine beta-defensin 1; pigs, mammals, animals) No entry found Not found Not found Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17168333 Sheng Wu Gong Cheng Xue Bao. 2006 Nov;22(6):1036-9. Jiang LH, Lu HR, Huang DX, Yi JB, Li LY, Lin F. [Expression of porcine beta-defensin 1 gene in Pichia pastoris] In Chinese DRAMP02978 DHYICAKKGGTCNFSPCPLFNRIEGTCYSGKAKCCIR 37 pBD-2 (porcine beta-defensin 2; pigs, mammals, animals) No entry found Not found Not found Sus scrofa (Pig) Antimicrobial, Antibacterial Not found Combine helix and strand structure Not found Thought to be orthologue of hBD-1. The native pBD-2 has NOT been purified yet, so it's unclear to what extent the synthetic peptide corresponds to the in vivo form. Also of note is that the synthetic peptide does not have S-S bonds. pBD-2 (4-8 microM) killed these pathogens within 3h. Antimicrobial activity of pBD-2 was decreased at higher ionic strengths with no residual activity at 150mM NaCl. Salmonella typhimurium, Listeria monocytogenes and Erysipelothrix rhusiopathiae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17658606 Mol Immunol. 2008 Jan;45(2):386-394. Veldhuizen EJ, Rijnders M, Claassen EA, van Dijk A, Haagsman HP. Porcine beta-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. DRAMP02979 DTHFPICIFCCGCCRKAICGMCCKT 25 Hepcidin (pigs, mammals, animals) Q8MJ80 Belongs to the hepcidin family HAMP Sus scrofa (Pig) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Sang Y, Ross C.R, Blecha F. Cloning and characterization of porcine liver-expressed antimicrobial peptides, Hepcidin (pHAMP) and LEAP2. DRAMP02981 MTPFWRAVSLRPIGASCRDDSECLTRLCRKRRCSLSVAQE 40 Liver-expressed antimicrobial peptide 2 (LEAP-2; pigs, mammals, animals) Q95JB4 Belongs to the LEAP2 family LEAP2 Sus scrofa (Pig) Antimicrobial Homology Not found Not found PTM: Contains two disulfide bonds 17-28; 23-33. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12493837 Protein Sci. 2003 Jan;12(1):143-152. Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-García JR, Forssmann WG, Schulz-Knappe P, Nehls MC, Wattler F, Wattler S, Adermann K. Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver. DRAMP02982 MPVAVGPYGQSQPSCFDRVKMGFVMGCAVGMAAGALFGPFSCLRIGMRGRELMGGIGKTMMQSGGTFGPFMAIGMGIRC 79 Reactive oxygen species modulator 1 (ROS modulator 1; pigs, mammals, animals) A1XQR6 Belongs to the MGR2 family romo1 Sus scrofa (Pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found "Function: Has antibacterial activity against a variety of bacteria. Acts by inducing bacterial membrane breakage (By similarity). Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation (By similarity). Domain: Contains a transmembrane helix." Gram-positive bacteria: Staphylococcus aureus, Mycobacterium tuberculosis;##Gram-negative bacterium: Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cai G, Chen Y, Wang C, Li J, Peng G, Zhang H. Generation and analysis of cDNA sequences derived from a porcine skeletal muscle library. DRAMP02983 MTPFWRGVSLRPIGASCRDDSECITRLCKKRRCSLSVAQE 40 Liver-expressed antimicrobial peptide 2 (LEAP-2; pigs, mammals, animals) Q91X13 Not found LEAP2 Cavia porcellus (Guinea pig) Antimicrobial Homology Not found Not found PTM: Contains two disulfide bonds 17-28; 23-33. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12493837 Protein Sci. 2003 Jan;12(1):143-152. Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-García JR, Forssmann WG, Schulz-Knappe P, Nehls MC, Wattler F, Wattler S, Adermann K. Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver. DRAMP02984 GLRKKFRKTRKRIQKLGRKIGKTGRKVWKAWREYGQIPYPCRI 43 Neutrophil cationic antibacterial polypeptide of 11 kDa (CAP11; pigs, mammals, animals) Q91X12 Not found CAP11 Cavia porcellus (Domestic guinea pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Shows antibacterial activity against the Gram-positive bacteium S. aureus and Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (ED50=30-35 nM);##Gram-positive bacterium: Staphylococcus aureus (ED50=90-120 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8644997 Arch Biochem Biophys. 1996 Apr 15;328(2):219-226. Yomogida S, Nagaoka I, Yamashita T. Purification of the 11- and 5-kDa antibacterial polypeptides from guinea pig neutrophils. DRAMP02985 RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC 31 Neutrophil cationic peptide 2 (CP-2; GNCP-2; pigs, mammals, animals) P49112, Q9R0Z5 Belongs to the alpha-defensin family Not found Cavia porcellus (Guinea pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Homology Bridge Not found "Function: Has antibiotic, anti-fungi and antiviral activity. PTM: Contains three disulfide bonds (By similarity)." Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8173076##10738945 DNA Seq. 1993;4(2):123-128.##Inflamm Res. 2000 Feb;49(2):73-79. Nagaoka I, Nonoguchi A, Yamashita T.##Nagaoka I, Hirota S, Yomogida S, Ohwada A, Hirata M. Cloning and characterization of the guinea pig neutrophil cationic peptide-1 and -2 genes.##Synergistic actions of antibacterial neutrophil defensins and cathelicidins. DRAMP02986 RRCICTTRTCRFPYRRLGTCIFQNRVYTFCC 31 Neutrophil cationic peptide 1 (GPNP; Antiviral defensin; pigs, mammals, animals) Q64365, P11478 Belongs to the alpha-defensin family Not found Cavia porcellus (Guinea pig) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Bridge Not found "Function: Has antibiotic, anti-fungi and antiviral activity. Tissue specificity: Bone marrow." Gram-positive bacteria: Staphylococcus aureus, Streptococcus;##Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2473036##3623703 Infect Immun. 1989 Aug;57(8):2405-2409.##Infect Immun. 1987 Sep;55(9):2281-2286. Yamashita T, Saito K.##Selsted ME, Harwig SS. Purification, primary structure, and biological activity of guinea pig neutrophil cationic peptides.##Purification, primary structure, and antimicrobial activities of a guinea pig neutrophil defensin. DRAMP02987 AGFAAQAAASLAPVAIQQL 19 Tricholongin BII (Fungi) No entry found Not found Not found Trichoderma longibrachiatum Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1935961 Eur J Biochem. 1991 Nov 1;201(3):661-674. Rebuffat S, Prigent Y, Auvin-Guette C, Bodo B. Tricholongins BI and BII, 19-residue peptaibols from Trichoderma longibrachiatum. Solution structure from two-dimensional NMR spectroscopy. DRAMP02988 AGFAAQAAASLAPVAAQQL 19 Tricholongin BI (Fungi) No entry found Not found Not found Trichoderma longibrachiatum Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1935961 Eur J Biochem. 1991 Nov 1;201(3):661-674. Rebuffat S, Prigent Y, Auvin-Guette C, Bodo B. Tricholongins BI and BII, 19-residue peptaibols from Trichoderma longibrachiatum. Solution structure from two-dimensional NMR spectroscopy. DRAMP02989 VNWKKVLGKIIKVAK 15 Lasioglossin LL-I (Insects, animals) No entry found Not found Not found Lasioglossum laticeps (Eusocial Bee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found Function: Active against B. subtilis, S. aureus, P. aeruginosa, and E. coli. Low hemolytic toxicity. [Ref.19591185]Gram-positive bacteria: B. subtilis(MIC=0.8 μM), S. aureus(MIC=14.3 μM);##Gram-negative bacteria: P. aeruginosa(MIC=15.8 μM), E. coli(MIC=1.7 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2099. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP02990 VNWKKILGKIIKVAK 15 Lasioglossin LL-II (Insects, animals) No entry found Not found Not found Lasioglossum laticeps (Eusocial Bee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found Function: Active against B. subtilis, S. aureus, P. aeruginosa, and E. coli. Low hemolytic toxicity. [Ref.19591185]Gram-positive bacteria: B. subtilis(MIC=0.7 μM), S. aureus(MIC=9.0 μM);##Gram-negative bacteria: P. aeruginosa(MIC=14.4 μM), E. coli(MIC=1.4 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2099. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP02991 VNWKKILGKIIKVVK 15 Lasioglossin LL-III (Insects, animals) No entry found Not found Not found Lasioglossum laticeps (Eusocial Bee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Not found Not found Not found Function: Active against B. subtilis, S. aureus, P. aeruginosa, and E. coli. Low hemolytic toxicity. [Ref.19591185]Gram-positive bacteria: B. subtilis(MIC=0.7 μM), S. aureus(MIC=3.9 μM);##Gram-negative bacteria: P. aeruginosa(MIC=18.7 μM), E. coli(MIC=1.4 μM). [Ref.19591185]LC50>220 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2099. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP02992 GLPRKILCAIAKKKGKCKGPLKLVCKC 27 Lasiocepsin (Insects, animals) No entry found Not found Not found Lasioglossum laticeps (Eusocial Bee) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found 2MBD Function: The synthetic lasiocepsin possessed antimicrobial activity against both Gram-positive and -negative bacteria, antifungal activity against Candida albicans, and weak hemolytic activity against human erythrocytes. No MICs found in DRAMP database [Ref.22038181]LC50>200 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22038181 Amino Acids. 2012 Aug;43(2):751-761. Monincová L, Slaninová J, Fucík V, Hovorka O, Voburka Z, Bednárová L, Malon P, Stokrová J, Cerovský V. Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae). DRAMP02994 VTCDLLSFKGQVNDSACAANCLSLGKAGGHCEKVGCICRKTSFKDLWDKYF 51 Defensin-1 (Royalisin; Insects, animals) P17722, C7AHT1, Q5MY57, Q9BMA5 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Apis mellifera (Honeybee) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Found in royal jelly and in hemolymph, potent antibacterial protein against Gram-positive bacteria at low concentration. Tissue specificity: High expression in head, hypopharyngeal gland, and mandibular gland. Low expression in thorax and thoracic salivary gland. PTM: Contains three disulfide bonds 3-31; 17-36; 21-38 and Phenylalanine amide at F51." Bifidobacterium adolescentis ATCC15703, Bifidobacterium longum ATCC15707, Leuconostoc cremoris ATCC 19254, Lactobacillus spps, Staphylococcus aureus, Streptococcus spps No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2358464##15607651 J Biol Chem. 1990 Jul 5;265(19):11333-11337.##Insect Biochem Mol Biol. 2005 Jan;35(1):11-22. Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kawashima T, Kobayashi K.##Klaudiny J, Albert S, Bachanová K, Kopernický J, Simúth J. A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin.##Two structurally different defensin genes, one of them encoding a novel defensin isoform, are expressed in honeybee Apis mellifera. DRAMP03004 FVPYNPPRPGQSKPFPSFPGHGPFNPKIQWPYPLPNPGH 39 Abaecin (Insects, animals) P81463 Not found Not found Bombus pascuorum (Brown bumblebee) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide against Gram-positive and Gram-negative bacteria. Induction: By bacterial infection." Gram-negative bacteria: Micrococcus luteus;##Gram-negative bacteria: Escherichia coli D22. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9219367 Insect Biochem Mol Biol. 1997 May;27(5):413-22. Rees JA, Moniatte M, Bulet P. Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). DRAMP03005 GNRPVYIPPPRPPHPRL 17 Apidaecin (Insects, animals) P81464 Belongs to the apidaecin family Not found Bombus pascuorum (Brown bumblebee) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Antibacterial peptide against Gram-positive and Gram-negative bacteria. Induction: By bacterial infection." Gram-negative bacteria: Micrococcus luteus;##Gram-negative bacteria: Escherichia coli D22. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9219367 Insect Biochem Mol Biol. 1997 May;27(5):413-422. Rees JA, Moniatte M, Bulet P. Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). DRAMP03006 VTCDLLSIKGVAEHSACAANCLSMGKAGGRCENGICLCRKTTFKELWDKRF 51 Defensin (Insects, animals) P81462 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Bombus pascuorum (Brown bumblebee) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: Antibacterial peptide against Gram-positive and Gram-negative bacteria and fungi. Induction: By bacterial infection." Gram-negative bacteria: Micrococcus luteus;##Gram-negative bacteria: Escherichia coli D22. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9219367 Insect Biochem Mol Biol. 1997 May;27(5):413-422. Rees JA, Moniatte M, Bulet P. Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). DRAMP04531 AAGMGFFGAR 10 Urechistachykinin II (UII) P40752 Not found Not found Urechis unicinctus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. Antifungal. Has no hemolytic activity. [Ref.18570895] Gram-negative bacteria: Escherichia coli O-157 (MIC=12.7μM), Pseudomonas aeruginosa (MIC=12.7μM), Vibrio vulnificu (MIC=25.4μM) ;##Gram-positive bacteria: Streptococcus mutans (MIC=12.7μM), Staphylococcus aureus (MIC=25.4μM),Enterococcus faecium(MIC=25.4μM) ;##Fungi: Candida albicans(MIC=25.4μM), Trichosporon beigelii (MIC=12.7μM), Malassezia furfur (MIC=50.9μM). [Ref.18570895] Has no hemolytic activities against human erythrocyte cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18570895 FEBS Lett. 2008 Jul 9;582(16):2463-2466. Sung WS, Park SH, Lee DG. " Antimicrobial effect and membrane-active mechanism of Urechistachykinins, neuropeptides derived from Urechis unicinctus. " DRAMP04530 LRQSQFVGSR 10 Urechistachykinins I (UI) P40751 Not found Not found Urechis unicinctus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. Antifungal. Has no hemolytic activity. [Ref.18570895] Gram-negative bacteria: Escherichia coli O-157 (MIC=10.6μM), Pseudomonas aeruginosa (MIC=21.3μM), Vibrio vulnificus (MIC=42.5μM) ;##Gram-positive bacteria: Streptococcus mutans(MIC=21.3μM), Staphylococcus aureus (MIC=42.5μM),Enterococcus faecium (MIC=21.3μM) ;##Fungi: Candida albicans (MIC=42.5μM), Trichosporon beigelii (MIC=21.3μM), Malassezia furfur (MIC=42.5μM). [Ref.18570895] Has no hemolytic activities against human erythrocyte cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18570895 FEBS Lett. 2008 Jul 9;582(16):2463-2466. Sung WS, Park SH, Lee DG. " Antimicrobial effect and membrane-active mechanism of Urechistachykinins, neuropeptides derived from Urechis unicinctus. " DRAMP01224 GFISTVKNLATNVAGTVIDTIKCKVTGGC 29 Palustrin-2AR (Palustrin-2ARa; Ranatuerin-2SEa; Frogs, amphibians, animals) No entry found Not found Not found Rana areolata (North American crawfish frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative bacterium Escherichia coli. Has hemolytic activity. [Ref.12429503] Gram-negative bacterium: Escherichia coli (MIC=110 μM) [Ref.12429503] HC50>300 μM against human erythrocytes Cyclic Free Cyclization (Cys23 and Cys29) Disulfide bond between Cys23 and Cys29. L No cytotoxicity information found Not found 12429503 Biochim Biophys Acta. 2002 Nov 19;1601(1):55-63. Ali MF, Lips KR, Knoop FC, Fritzsch B, Miller C, Conlon JM. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. DRAMP03013 LNLTKWLGKLGVILSHLNK 19 Bombolitin-6 (Insects, animals) P0CD67 Belongs to the MCD family Bombolitin subfamily Not found Bombus lapidarius (Red-tailed bumblebee) (Apis lapidaria) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide. May also display antibacterial and antifungal activities (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16626777 Toxicon. 2006 May;47(6):676-687. Favreau P, Menin L, Michalet S, Perret F, Cheneval O, Stöcklin M, Bulet P, Stöcklin R. Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen. DRAMP03014 LKLKDILGKIKVILSHLNK 19 Bombolitin-7 (Insects, animals) P0CD68 Belongs to the MCD family Bombolitin subfamily Not found Bombus lapidarius (Red-tailed bumblebee) (Apis lapidaria) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide. May also display antibacterial and antifungal activities (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16626777 Toxicon. 2006 May;47(6):676-687. Favreau P, Menin L, Michalet S, Perret F, Cheneval O, Stöcklin M, Bulet P, Stöcklin R. Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen. DRAMP03015 LKLKSILGKLGVILSHLNK 19 Bombolitin-8 (Insects, animals) P0CD69 Belongs to the MCD family Bombolitin subfamily Not found Bombus lapidarius (Red-tailed bumblebee) (Apis lapidaria) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Mast cell degranulating peptide. May also display antibacterial and antifungal activities (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16626777 Toxicon. 2006 May;47(6):676-687. Favreau P, Menin L, Michalet S, Perret F, Cheneval O, Stöcklin M, Bulet P, Stöcklin R. Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen. DRAMP03016 VTCDLLSFKGQVNDSACAANCLSLGKAGGHCEKGVCICRKTSFKDLWDKRF 51 Defensin-1 (Insects, animals) Q5J8R1 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Apis mellifera carnica (Carniolan bee) Antimicrobial, Antibacterial Protein level Not found Not found Function: Found in royal jelly and in hemolymph, potent antibacterial protein against Gram-positive bacteria at low concentration (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15607651 Insect Biochem Mol Biol. 2005 Jan;35(1):11-22. Klaudiny J, Albert S, Bachanová K, Kopernický J, Simúth J. Two structurally different defensin genes, one of them encoding a novel defensin isoform, are expressed in honeybee Apis mellifera. DRAMP18418 FIGMIPGLIGGLISAFK 17 ToAP1 A0A1D3IXR7 Derived from NDBP subfamily 4 Not found Tityus obscurus Antimicrobial, Antifungal, Antibiofilm Transcript level Alpha helix The peptide adopts a structure with 64.71% alpha helix Function: Antibacterial activity against the all Candida spp. Has hemolytic activity. [Ref.27917162] Fungi:Candida albicans (SC5314)(MIC=50μM), Candida tropicalis (ATCC 750)(MIC=12.5μM), Candida parapsilosis (ATCC 22019)(MIC=200μM), Candida glabrata (ATCC 90030)(MIC>400μM), Candida neoformans (H99 serotype A)(MIC=25μM) [Ref.27917162] 20% hemolysis at 1.58 μM, 22% hemolysis at 3.16 μM, 23% hemolysis at 6.31 μM, 24% hemolysis at 12.59 μM, 28% hemolysis at 25.12 μM, 45% hemolysis at 50.11 μM , 50% hemolysis at 100μM against human red blood cell Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27917162 Front Microbiol. 2016 Nov 18;7:1844. eCollection 2016. Guilhelmelli F, Vilela N, Smidt KS, de Oliveira MA, da Cunha Morales ?lvares A, Rigonatto MC, da Silva Costa PH, Tavares AH, de Freitas SM, Nicola AM, Franco OL, Derengowski LD, Schwartz EF, Mortari MR, Bocca AL, Albuquerque P, Silva-Pereira I. Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms. DRAMP03023 INWKALLDAAKKVL 14 Mastoparan (Protonectarina-MP; Insects, animals) P0C1Q5 Not found Not found Protonectarina sylveirae (Brazilian wasp) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Shows potent antimicrobial action against both Gram-positive and Gram-negative bacteria By similarity. This peptide shows potent histamine releasing activities on rat peritoneal mast cells. Also Has hemolytic and cytolytic activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)." [Swiss_Prot Entry P0C1Q5]Potent antimicrobial peptide against both Gram-positive and Gram-negative bacteria (By similarity) [Ref.20108158]ED50 =3.4 × 10−5 M against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7513243##19857508##20108158 Nat Toxins. 1993;1(5):271-276.##Toxicon. 2010 Apr 1;55(4):711-718.##Amino Acids. 2011 Jan;40(1):77-90. Dohtsu K, Okumura K, Hagiwara K, Palma MS, Nakajima T.##Baek JH, Lee SH.##de Souza BM, Dos Santos Cabrera MP, Neto JR, Palma MS. Isolation and sequence analysis of peptides from the venom of Protonectarina sylveirae (Hymenoptera-Vespidae).##Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae).##Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities. DRAMP02842 RRWQWR 6 LfcinB(20-25) P24627 bovine LfcinB LTF bovine Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found 1LFC Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.29984236] Gram-positive bacterium: Staphylococcus aureus ATCC 33591 (MIC=100 μg/ml; MBC=199 μg/ml) [Ref.29984236] 3% hemolysis at 5 μM, 5% hemolysis at 12 μM, 5% hemolysis at 22 μM, 0% hemolysis at 50 μM, 2% hemolysis at 100 μM against human red blood cell.##[Ref.29551999] 7.1% hemolysis at 25μM, 50% hemolysis at >100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29984236##29551999##20844765 Biomed Res Int. 2018 Jun 10;2018:5252891##Front Microbiol. 2018 Mar 2;9:329.##PLoS One. 2010 Sep 10;5(9):e12684. doi: 10.1371/journal.pone.0012684 Sandra C. Vega Chaparro, J. Tatiana Valencia Salguero, Diana A. Mart##Nguyen LT, Chau JK, Perry NA, de Boer L, Zaat SA, Vogel HJ Effect of Polyvalence on the Antibacterial Activity of a Synthetic Peptide Derived from Bovine Lactoferricin against Healthcare-Associated Infectious Pathogens.##Design, Synthesis and Evaluation of Branched RRWQWR-Based Peptides as Antibacterial Agents against Clinically Relevant Gram-Positive and Gram-Negative Pathogens##Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs DRAMP03025 INLKAIAALAKKLL 14 Mastoparan M No entry found Not found Not found Vespa magnifica Antimicrobial, Antibacterial, Anti-gram+, Anti-gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=6.0 ± 3.5 mg/L, MBC=6.0 ± 3.5 mg/L), Enterococcus faecalis isolates(MIC=5.3 ± 2.3 mg/L, MBC=6.7 ± 2.3 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=4.0 ± 3.5 mg/L, MBC=4.7 ± 3.0 mg/L), Acinetobacter baumannii isolates(MIC=2.7 ± 1.2 mg/L, MBC=3.3 ± 1.2 mg/L) [Ref.27591703] 0% hemolysis at 64 μg/ml against human red blood cells; 0% hemolysis at 32 μg/ml , 6% hemolysis at 64 μg/ml against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15935330##27591703 Biochem Pharmacol. 2005 Jul 15;70(2):209-219. ##Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Yibin G, Jiang Z, Hong Z, Gengfa L, Liangxi W, Guo W, Yongling L.##Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K A synthesized cationic tetradecapeptide from hornet venom kills bacteria and neutralizes lipopolysaccharide in vivo and in vitro.##Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP03026 INWKKMAATALKMI 14 Parapolybia-MP (Insects, animals) No entry found Not found Not found Protonectarina sylveirae (Brazilian wasp) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20108158 Amino Acids. 2011 Jan;40(1):77-90. de Souza BM, Dos Santos Cabrera MP, Neto JR, Palma MS. Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities. DRAMP18227 LLDVLLE 7 Gageostatin B (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Asp-Val-Leu-Leu-Glu-3-beta-hydroxy-9, 11-dimethyltridecanoic acid surfactin like heptapeptides, cytotoxic. It is noteworthy that these compounds 1 Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85. Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis. DRAMP03029 INWKKIKSIIKAAMN 15 Mastoparan-V1 (Insects, animals) P0C1Q8 Not found Not found Vespula vulgaris (Yellow jacket) (Wasp) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Chemotactic peptide for polymorphonucleated leukocytes (PMNL), but causing no hemolysis to erythrocytes and no mast cell degranulation activity at physiological concentrations. Potent antimicrobial peptide against Gram-positive and Gram-negative bacteria. Expressed by the venom gland. PTM: C-terminal amidation (Asparagine amide: N15)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12759486 Int Arch Allergy Immunol. 2003 May;131(1):25-32. King T.P, Jim S.Y, Wittkowski K.M. Inflammatory role of two venom components of yellow jackets (Vespula vulgaris): a mast cell degranulating peptide mastoparan and phospholipase A1. DRAMP03030 INWKKIKSLIKAAMS 15 Mastoparan-V2 (Insects, animals) P0C1Q9 Not found Not found Vespula vulgaris (Yellow jacket) (Wasp) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Chemotactic peptide for polymorphonucleated leukocytes (PMNL), but causing no hemolysis to erythrocytes and no mast cell degranulation activity at physiological concentrations. Potent antimicrobial peptide against Gram-positive and Gram-negative bacteria. Expressed by the venom gland. PTM: C-terminal amidation (Serine amide: S15)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12759486 Int Arch Allergy Immunol. 2003 May;131(1):25-32. King T.P, Jim S.Y, Wittkowski K.M. Inflammatory role of two venom components of yellow jackets (Vespula vulgaris): a mast cell degranulating peptide mastoparan and phospholipase A1. DRAMP03031 INLKAIAAFAKKLL 14 Mastoparan-T (Insects, animals) P0C1Q7 Not found Not found Vespa tropica (Greater banded hornet) (Sphex tropica) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Chemotactic peptide for polymorphonucleated leukocytes (PMNL), but causing no hemolysis to rat erythrocytes and no mast cell degranulation activity at physiological concentrations. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12759486 Int Arch Allergy Immunol. 2003 May;131(1):25-32. King T.P, Jim S.Y, Wittkowski K.M. Inflammatory role of two venom components of yellow jackets (Vespula vulgaris): a mast cell degranulating peptide mastoparan and phospholipase A1. DRAMP03032 IKWKAILDAVKKVL 14 Mastoparan-A (Insects, animals) P0C1Q6 Not found Not found Vespa analis (Yellow-vented hornet) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Chemotactic peptide for polymorphonucleated leukocytes (PMNL), but causing no hemolysis to erythrocytes and no mast cell degranulation activity at physiological concentrations. Potent antimicrobial peptide against both Gram-positive and Gram-negative bacteria. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12759486 Int Arch Allergy Immunol. 2003 May;131(1):25-32. King T.P, Jim S.Y, Wittkowski K.M. Inflammatory role of two venom components of yellow jackets (Vespula vulgaris): a mast cell degranulating peptide mastoparan and phospholipase A1. DRAMP03048 KDLHTVVSAILQAL 14 Venom peptide 3 (OdVP3; Insects, animals) C7DT09 Belongs to the MCD family VP3 Orancistrocerus drewseni (Solitary wasp) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Exhibits strong antimicrobial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19857508 Toxicon. 2010 Apr 1;55(4):711-718. Baek JH, Lee SH. Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae). DRAMP03049 GRILSFIKGLAEHL 14 Eumenine mastoparan-OD (EMP-OD; Venom peptide 1, OdVP1; Insects, animals) P86146, C7DT07 Belongs to the MCD family (Mastoparan subfamily) VP1 Orancistrocerus drewseni (Solitary wasp) Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has hemolytic activity against ovine erythrocytes at micromolar concentrations. Also exhibits strong antimicrobial activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (Leucine amide: L14)." [Ref.19857508]Fungi: Candida albicans, Botrytis cinerea (++);##Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: S. aureus (+) [Ref.18695936]42% hemolytic activity at 50 μM against sheep blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen 19857508##18695936 Toxicon. 2010 Apr 1;55(4):711-718.##Amino Acids. 2009 Jul;37(2):389-394. Baek JH, Lee SH.##Murata K, Shinada T, Ohfune Y, Hisada M, Yasuda A, Naoki H, Nakajima T. Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae).##Novel mastoparan and protonectin analogs isolated from a solitary wasp, Orancistrocerus drewseni drewseni. DRAMP03058 ATCDLLSGTGINHSACAAHCLLRGNRGGYCNGKGVCVCRN 40 Phormia defensin A (insect defensin A, Ptdefensin A; Insects, animals) No entry found Not found Not found Phormia terranovae (Black blowfly) Antimicrobial, Antibacterial Not found Combine helix and strand structure Not found 1ICA resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2911573 Proc Natl Acad Sci U S A. 1989 Jan;86(1):262-266. Lambert J, Keppi E, Dimarcq JL, Wicker C, Reichhart JM, Dunbar B, Lepage P, Van Dorsselaer A, Hoffmann J, Fothergill J, et al. Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to Rabbit lung macrophage bactericidal peptides. DRAMP03059 ATCDLLSGTGINHSACAAHCLLRGNRGGYCNRKGVCVCRN 40 Phormia defensin B (insect defensin B; Insects, animals) No entry found Not found Not found Phormia terranovae (Black blowfly) Antimicrobial, Antibacterial Not found Not found Not found It contains three intramolecular disulfide bridges and differ from one another by only a single amino acid. This peptide is neither functionally nor structurally related to any known insect immune response peptides but show significant homology to microbicidal cationic peptides from mammalian granulocytes (defensins). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2911573 Proc Natl Acad Sci U S A. 1989 Jan;86(1):262-266. Lambert J, Keppi E, Dimarcq JL, Wicker C, Reichhart JM, Dunbar B, Lepage P, Van Dorsselaer A, Hoffmann J, Fothergill J, et al. Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. DRAMP03060 ATCDLLSMWNVNHSACAAHCLLLGKSGGRCNDDAVCVCRK 40 S.calcitrans defensin 2 (Smd2; defensins; Insects, animals) O16137 Belongs to the invertebrate defensin family (Type 1 subfamily) SMD2 Stomoxys calcitrans (Stable fly) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide active mostly against Gram-negative bacteria. Its activity is enhanced by lipopolysaccharide. Tissue specificity: Constitutively expressed in the anterior midgut and is up-regulated by blood feeding. Not expressed in the fat body or hemocytes. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9326639 Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11502-11507. Lehane MJ, Wu D, Lehane SM. Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans. DRAMP03061 AAKPMGITCDLLSLWKVGHAACAAHCLVLGDVGGYCTKEGLCVCKE 46 S.calcitrans defensin 1 (Smd1; defensins; Insects, animals) O16136 Belongs to the invertebrate defensin family (Type 1 subfamily) SMD1 Stomoxys calcitrans (Stable fly) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial peptide active mostly against Gram-negative bacteria. Its activity is enhanced by lipopolysaccharide (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9326639##11903625 Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11502-11507.##Insect Mol Biol. 2001 Dec;10(6):561-571. Lehane MJ, Wu D, Lehane SM.##Munks RJ, Hamilton JV, Lehane SM, Lehane MJ. Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans.##Regulation of midgut defensin production in the blood-sucking insect Stomoxys calcitrans. DRAMP03062 VTGELKRDKRVTCNIGEWVCVAHCNSKSKKSGYCSRGVCYCTN 43 Defensin-A (DefA; GmDefA; Insects, animals) Q8WTD4 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Glossina morsitans morsitans (Savannah tsetse fly) Antimicrobial, Antibacterial, Anti-Gram-, Antiprotozoal Protein level Not found Not found "Function: Antibacterial peptide mostly active against Gram-positive and Gram-negative bacteria. Tissue specificity: Hemolymph and fat body. Induction: By bacterial infection. PTM: Contains three disulfide bonds (By similarity)." Protozoan: Procyclic trypanosomes (IC50=10 µM).##Gram-negative bacteria: Sodalis (IC50=2 µM)，Escherichia coli DH5α (IC50=0.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11592981##11886771 Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12648-12653.##Insect Biochem Mol Biol. 2002 Apr;32(4):369-375. Hao Z, Kasumba I, Lehane MJ, Gibson WC, Kwon J, Aksoy S.##Boulanger N, Brun R, Ehret-Sabatier L, Kunz C, Bulet P. Tsetse immune responses and trypanosome transmission: implications for the development of tsetse-based strategies to reduce trypanosomiasis.##Immunopeptides in the defense reactions of Glossina morsitans to bacterial and Trypanosoma brucei brucei infections. DRAMP03064 HGVSGHGQHGVHG 13 Alloferon-1 (Insects, animals) P83412 Not found Not found Calliphora vicina (Blue blowfly) (Calliphora erythrocephala) Antimicrobial, Antiparasitic, Antiviral, Antitumor Protein level Not found Not found "Function: Antimicrobial peptide presumably with antiparasitic, antiviral and/or Antitumoral activities. Tissue specificity: Hemolymph. Induction: By bacterial infection. Miscellaneous: Stimulates antiviral and antitumoral resistance when injected in mice. Enhances natural cytotoxicity of blood and spleen lymphocytes. Induces interferon production in mouse and human." Human influenza viruses A and B. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12235362 Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12628-32. Chernysh S, Kim SI, Bekker G, Pleskach VA, Filatova NA, Anikin VB, Platonov VG, Bulet P. Antiviral and antitumor peptides from insects. DRAMP03065 GVSGHGQHGVHG 12 Alloferon-2 (Insects, animals) No entry found Not found Not found Calliphora vicina (Blue blowfly) (Calliphora erythrocephala) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Function: Alloferon can (i) stimulate natural cytotoxicity of human peripheral blood lymphocytes, (ii) induces IFN synthesis in mouse and human models, and (iii) enhances antiviral and antitumor resistance in mice. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12235362 Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12628-32. Chernysh S, Kim SI, Bekker G, Pleskach VA, Filatova NA, Anikin VB, Platonov VG, Bulet P. Antiviral and antitumor peptides from insects. DRAMP03066 ATCDLLSGTGIKHSACAAHCLLRGNRGGYCNGRAICVCRN 40 Lucifensin (Lucifensin II; Insects, animals) B3EWY5 Belongs to the invertebrate defensin family (Type 1 subfamil Not found Lucilia cuprina (Green bottle fly) (Australian sheep blowfly) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: May have antibacterial activity. Tissue specificity: Larval fat body, hemolymph and salivary glands (at protein level). PTM: Contains three disulfide bonds 3-30; 16-36; 20-38." Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2012) to UniProtKB El Shazely B, Veverka V, Fucik V, Voburka Z, Zdarek J, Cerovsky V. Lucifensin II, the defensin of medicinal maggots of the blowfly Lucilia cuprina. DRAMP03067 ATCDLLSGTGVKHSACAAHCLLRGNRGGYCNGRAICVCRN 40 Lucifensin (Lucilia defensin; Insects, animals) P86471 Belongs to the invertebrate defensin family (Type 1 subfamil Not found Lucilia sericata (Green bottle fly) (Phaenicia sericata) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Not found 2LLD resolved by NMR. "Function: May have antibacterial activity. Tissue specificity: Larval fat body, hemolymph and salivary glands (at protein level). PTM: Contains three disulfide bonds 3-30; 16-36; 20-38 (By similarity)." Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19921400##22322867 Cell Mol Life Sci. 2010 Feb;67(3):455-466.##J Biomol NMR. 2012 Mar;52(3):277-282. Cerovský V, Zdárek J, Fucík V, Monincová L, Voburka Z, Bém R.##Nygaard MK, Andersen AS, Kristensen HH, Krogfelt KA, Fojan P, Wimmer R. Lucifensin, the long-sought antimicrobial factor of medicinal maggots of the blowfly Lucilia sericata.##The insect defensin lucifensin from Lucilia sericata. DRAMP03068 ESAPAPEVSGDAVFSAIQNGXLKNLGNAFFW 31 Antifungal protein 1 (MAF-1; Insects, animals) P86696 Not found Not found Musca domestica (House fly) Antimicrobial Protein level Not found Not found Function: Antifungal activity against C.albicans ATCC 76615. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19728925 Cell Mol Immunol. 2009 Aug;6(4):245-251. Fu P, Wu J, Guo G. Purification and molecular identification of an antifungal peptide from the hemolymph of Musca domestica (housefly). DRAMP18226 LLDVLLE 7 Gageostatin A (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus subtilis Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Leu-Leu-Asp-Val-Leu-Leu-Glu-3-beta-hydroxy-11-methyltridecanoic acid Fuction: Surfactin like heptapeptides, cytotoxic. It is noteworthy that these compounds 1 Gram-positive, Gram-negative No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85. Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis. DRAMP03071 DEKPKLILPTPAPPNLPQLVGGGGGNRKDGFGVSVDAHQKVWTSDNGGHSIGVSPGYSQHLPGPYGNSRPDYRIGAGYSYNF 82 Diptericin-A (Insects, animals) P10836 Belongs to the attacin/sarcotoxin-2 family Not found Protophormia terraenovae (Northern blowfly) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has activity against E.coli. Miscellaneous: There seems to be a family of diptericin in protophormia. Diptericin A is the predominant member." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3276515 Eur J Biochem. 1988 Jan 15;171(1-2):17-22. Dimarcq JL, Keppi E, Dunbar B, Lambert J, Reichhart JM, Hoffmann D, Rankine SM, Fothergill JE, Hoffmann JA. Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A. DRAMP03072 DEKPKLILPTPAPPNLPQLVGGGGGNRKDGFGVSVDAHQKVWTSDNGRHSIGVTPGYSQHLGGPYGNSRPDYRIGAGYSYNF 82 Diptericin-D (Insects, animals) P18684 Belongs to the attacin/sarcotoxin-2 family Not found Protophormia terraenovae (Northern blowfly) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Has activity against E.coli. Induction: By bacterial infection. Miscellaneous: There seems to be a family of diptericin in protophormia. Diptericin A is the predominant member." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2544427 Eur J Biochem. 1989 Jun 15;182(2):423-437. Reichhart JM, Essrich M, Dimarcq JL, Hoffmann D, Hoffmann JA, Lagueux M. Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera). Transcriptional profiles during immunization. DRAMP03073 ATCDLLSGIGVQHSACALHCVFRGNRGGYCTGKGICVCRN 40 Sapecin-C (Sapecin C; defensins; Insects, animals) P31530 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Sapecins, which are potent bactericidal proteins, are produced in response to body injury. Thus, sapecin is probably a defense protein synthesized by Sarcophaga to prevent bacterial infection through the damaged body wall. This gene was also found to be activated in the embryonic and early pupal stages, suggesting that sapecin also plays a role in the ontogenetic processes of Sarcophaga. Gram-negative bacteria: Escherichia coli, Proteus mirabilis, Klebsiella Pneumoniae;##Gram-positive bacteria: Staphylococcus spps., Streptococcus spps, Bacillus megaterium, Bacillus circulans, Corynebacterium glutamicum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8471044 Biochem J. 1993 Apr 1;291 (Pt 1):275-279. Yamada K, Natori S. Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin. DRAMP03074 GWLKKIGKKIERVGQNTRDATVKGLEVAQQAANVAATVR 39 Cecropin (Insects, animals) P83403 Belongs to the cecropin family Not found Glossina morsitans morsitans (Savannah tsetse fly) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-negative bacteria. Tissue specificity: Hemolymph. Induction: By bacterial and parasitic infection. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11886771 Insect Biochem. Mol. Biol. 2002; 32:369-375. Boulanger N, Brun R, Ehret-Sabatier L, Kunz C, Bulet P. Immunopeptides in the defense reactions of Glossina morsitans to bacterial and Trypanosoma brucei brucei infections. DRAMP03076 GWLKKIGKKIERVGQHTRDATIQTIAVAQQAANVAATAR 39 Cecropin-1 (Cecropin 1; Insects, animals) Q06589 Belongs to the cecropin family CEC1 Ceratitis capitata (Mediterranean Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7916722 Gene. 1993 Dec 8;134(2):241-243. Rosetto M, Manetti AG, Marchini D, Dallai R, Telford JL, Baldari CT. Sequences of two cDNA clones from the medfly Ceratitis capitata encoding antibacterial peptides of the cecropin family. DRAMP03077 GWLKKIGKKIERVGQHTRDATIQTIGVAQQAANVAATLK 39 Cecropin-2 (Cecropin 2; Md-Cec, Mdc; Insects, animals) Q06590 Belongs to the cecropin family CEC2 Ceratitis capitata (Mediterranean fruit fly) (Musca domestica) Antimicrobial, Antibacterial, Antifungal Homology Alpha helix Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7916722 Gene. 1993 Dec 8;134(2):241-243. Rosetto M, Manetti AG, Marchini D, Dallai R, Telford JL, Baldari CT. Sequences of two cDNA clones from the medfly Ceratitis capitata encoding antibacterial peptides of the cecropin family. DRAMP03078 VFVALILAIAIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR 55 Cecropin-A2 (Insects, animals) O61281 Belongs to the cecropin family CecA2 Drosophila yakuba (Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9553148 Immunogenetics. 1998 May;47(6):417-429. Date A, Satta Y, Takahata N, Chigusa SI. Evolutionary history and mechanism of the Drosophila cecropin gene family. DRAMP03079 GWLKKIGKKIERVGQHTRDATIQGLGVAQQAANVAATAR 39 Cecropin-A1 (Insects, animals) P81685, P81688, B4HZP1 Belongs to the cecropin family CecA1 Drosophila mauritiana (Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9335607##9725836 Genetics. 1997 Oct;147(2):713-724.##Genetics. 1998 Sep;150(1):157-171. Clark AG, Wang L.##Ramos-Onsins S, Aguadé M. Molecular population genetics of Drosophila immune system genes.##Molecular evolution of the Cecropin multigene family in Drosophila. functional genes vs. pseudogenes. DRAMP03080 AGWLRKLGKKIERIGQHTRDASIQVLGIAQQAANVAATAR 40 Cecropin-B (Insects, animals) P67791, P67792, B4R1K3, O61273, P81689, P81686 Belongs to the cecropin family CecB Drosophila sechellia (Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9335607##9725836 Genetics. 1997 Oct;147(2):713-724.##Genetics. 1998 Sep;150(1):157-171. Clark AG, Wang L.##Ramos-Onsins S, Aguadé M. Molecular population genetics of Drosophila immune system genes.##Molecular evolution of the Cecropin multigene family in Drosophila. functional genes vs. pseudogenes. DRAMP03081 GWLKKLGKRIERIGQHTRDATIQGLGIAQQAANVAATAR 39 Cecropin-C (Insects, animals) P84222, P84223, P84224, P84225, P84226 Belongs to the cecropin family CecC Drosophila erecta (Drosophila orena) (Drosophila teissieri) (Drosophila takahashii) (Drosophila yaku Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Developmental stage: Expressed during metamorphosis in pupae." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J Mol Evol. 2002 May;54(5):665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP03082 GFGCPLDQMQCHRHCQTITGRSGGYCSGPLKLTCTCYR 38 Defensin (invertebrate defensin; Insects, animals) P80154 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Aeshna cyanea (Southern hawker dragonfly) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Mediates the inducible antibacterial activity in larvae of A. cyanea. Micrococcus luteus, A. viriduns, P. acidiluctici, R. meguterium, Streptococcus pyogenes, A. faecalis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1425705 Eur J Biochem. 1992 Nov 1;209(3):977-984. Bulet P, Cociancich S, Reuland M, Sauber F, Bischoff R, Hegy G, Van Dorsselaer A, Hetru C, Hoffmann JA. A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata). DRAMP03083 LTCEIDRSLCLLHCRLKGYLRAYCSQQKVCRCVQ 34 Sapecin-B (defensins; Insects, animals) P31529 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Sarcophaga peregrina (Flesh fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Sapecins, which are potent bactericidal proteins, are produced in response to body injury. Thus, sapecin is probably a defense protein synthesized by Sarcophaga to prevent bacterial infection through the damaged body wall. This gene was also found to be activated in the embryonic and early pupal stages, suggesting that sapecin also plays a role in the ontogenetic processes of Sarcophaga. Gram-negative bacteria: Escherichia coli, Proteus mirabilis, Klebsiella pneumoniae;##Gram-positive bacteria: Staphylococcus spps., Streptococcus spps, Bacillus megaterium, Bacillus circulans, Corynebacterium glutamicum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7635204##8471044 FEBS Lett. 1995 Jul 24;368(3):485-487.##Biochem J. 1993 Apr 1;291 (Pt 1):275-279. Lee SR, Kurata S, Natori S.##Yamada K, Natori S. Molecular cloning of cDNA for sapecin B, an antibacterial protein of Sarcophaga, and its detection in larval brain.##Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin. DRAMP03084 SIGSAFKKALPVAKKIGKAALPIAKAALP 29 Ceratotoxin-B (Insects, animals) P36191 Not found CTXB Ceratitis capitata (Mediterranean Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria. They have as well hemolytic activity. Temperature dependence: Thermostable. Still active at 100 degrees Celsius." [Swiss_Prot Entry P36191]Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria [Swiss_Prot Entry P36191]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8353519 Insect Biochem Mol Biol. 1993 Jul;23(5):591-598. Marchini D, Giordano PC, Amons R, Bernini LF, Dallai R. Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera). DRAMP03085 SIGSALKKALPVAKKIGKIALPIAKAALP 29 Ceratotoxin-A (Insects, animals) P36190, O17512 Not found CTXA1 Ceratitis capitata (Mediterranean Fruit fly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. Temperature dependence: Thermostable. Still active at 100 degrees Celsius." [Swiss_Prot Entry P36190]Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria [Swiss_Prot Entry P36190]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8353519##7890755 Insect Biochem Mol Biol. 1993 Jul;23(5):591-598.##J Biol Chem. 1995 Mar 17;270(11):6199-6204. Marchini D, Giordano PC, Amons R, Bernini LF, Dallai R.##Marchini D, Manetti AG, Rosetto M, Bernini LF, Telford JL, Baldari CT, Dallai R. Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera).##cDNA sequence and expression of the ceratotoxin gene encoding an antibacterial sex-specific peptide from the medfly Ceratitis capitata (diptera). DRAMP03086 SIGTAVKKAVPIAKKVGKVAIPIAKAVLSVVGQLVG 36 Ceratotoxin-D (Insects, animals) O17513 Not found CTXD Ceratitis capitata (Mediterranean Fruit fly) (Tephritis capitata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. Biophysicochemical properties: Temperature dependence (Thermostable. Still active at 100 degrees Celsius)." [Swiss_Prot Entry O17513]Female-specific peptides with potent activity against Gram-positive and Gram-negative bacteria [Swiss_Prot Entry O17513]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9569644 Insect Biochem Mol Biol. 1997 Dec;27(12):1039-1046. Rosetto M, De Filippis T, Manetti AG, Marchini D, Baldari CT, Dallai R. The genes encoding the antibacterial sex-specific peptides ceratotoxins are clustered in the genome of the medfly Ceratitis capitata. DRAMP03087 DDMTMKPTPPPQYPLNLQGGGGGGSGDGFGFAVQGHQKVWTSDNGRHEIGLNGGYGQHLGGPYGNSEPSWKVGSTYTYRFPNF 83 Drosophila diptericin (Insects, animals) No entry found Not found Not found Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2125051 J Biol Chem. 1990 Dec 25;265(36):22493-8. Wicker C, Reichhart JM, Hoffmann D, Hultmark D, Samakovlis C, Hoffmann JA. Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides. DRAMP03088 DDMTMKPTPPPQYPLNLQGGGGGQSGDGFGFAVQGHQKVWTSDNGRHEIGLNGGYGQHLGGPYGNSEPSWKVGSTYTYRFPNF 83 Diptericin (Insects, animals) P24492, O16838, O16839, O16840, O16841, O18669, Q9V8P5 Belongs to the attacin/sarcotoxin-2 family Dpt Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial Protein level Not found Not found Required to resist Gram-negative bacterial infections, regulated by Dredd. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2125051##11269502 J Biol Chem. 1990 Dec 25;265(36):22493-22498.##The Drosophila caspase Dredd is required to resist gram-negative bacterial infection. Wicker C, Reichhart JM, Hoffmann D, Hultmark D, Samakovlis C, Hoffmann JA.##Leulier F, Rodriguez A, Khush RS, Abrams JM, Lemaitre B. Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides.##The Drosophila caspase Dredd is required to resist Gram-negative bacterial infection. DRAMP18225 NKGCAICSIGAACLVDGPIPDFEIAGATGLFGLWG 35 Subtilosin A1 (Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Bacillus subtilis Antimicrobial, Antibacterial Not found A variant of Subtilosin A, where residue T6 in Subtilosin A has been mutated to isoleucine. Like Subtilosin A, it is an N- and C-circulated peptide with three rare cross-links between the sulfurs of Cys13, Cys7, and Cys 4 and the alpha-carbons of Phe22, THr28, and Phe31, respectively. Fuction: Active against B. anthracis, B. cereus, B. thuringiensis, E. faecalis, S. carnosus, L. monocytogenes, and S. pyogenes. In addition to the hemolytic activity, subtilosin A1 was found to exhibit enhanced antimicrobial activity against specific bacterial strains. [Ref.19633086]Gram-postive bacterium:Bacillus subtilis(MIC= 250μM), Bacillus anthracis(MIC= 16μM), Bacillus cereus(MIC= 40μM), Bacillus thuringiensis(MIC= 40μM), Enterococcus faecalis(MIC= 100μM), taphylococcus carnosus(MIC= 100μM), Listeria monocytogenes(MIC= 40μM), Streptococcus pyogenes (MIC= 100μM). [Ref.19633086] MLC=16 μM against rabbit blood agar Cyclic No specific N-terminal No specific C-terminal Thioether bridges between Cys4 and Phe31,Cys7 and Thr28,Cys13 and Phe22. Mixed(D-Thr28,D-Phe31) No cytotoxicity information found Not found 19633086 J Bacteriol. 2009 Sep;191(18):5690-6. Huang T, Geng H, Miyyapuram VR, Sit CS, Vederas JC, Nakano MM. Isolation of a variant of subtilosin A with hemolytic activity. DRAMP03092 ATCDLLSKWNWNHTACAGHCIAKGFKGGYCNDKAVCVCRN 40 Drosophila defensin (Insects, animals) P36192, Q4V3H2, Q867E6, Q867G6, Q86BV6, Q86BV7, Q9V5F5 Not found Def Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8168509 Eur J Biochem. 1994 Apr 1;221(1):201-219. Dimarcq JL, Hoffmann D, Meister M, Bulet P, Lanot R, Reichhart JM, Hoffmann JA. Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity. DRAMP03093 DCLSGRYKGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC 44 Drosomycin (Cys-rich; insect defensins; Insects, animals) P41964, Q2UYN5, Q9VZQ2 Not found Drs Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal Protein level Combine helix and strand structure Not found 1MYN resolved by NMR. "Function: Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi. It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology. Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway. Tissue specificity: Synthesized in the fat body and is secreted into the blood. In hemolymph 6 hours after immune challenge, levels of expression increase for first 24 hours and persist for the following three weeks. PTM: Contains four disulfide bonds 2-44; 11-33; 19-39; 23-41." Fungi: Neurospora crassa (IC50=0.6 µM), Botrytis cinerea (IC50=1.2 µM), Fusarium culmorum (IC50=1.0 µM), Alternaria brassicicola (IC50=0.9 µM), A. longipes (IC50=1.4 µM), Nectria haematococca (IC50=1.8 µM), Fusarium oxysporum(IC50=4.2 µM), A. pisi (IC50=3.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization (Cys2 and Cys44) Disulfide bonds between Cys2 and Cys44; Cys11 and Cys33; Cys19 and Cys39,Cys23 and Cys41. L No cytotoxicity information found Not found 7806546##8808632##9736738##12872120 J Biol Chem 1994; 269: 33159-33163.##Cell. 1996 Sep 20;86(6):973-983.##Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11342-11347.##Nat Immunol. 2003 Aug;4(8):794-800. Fehlbaum P et al Hoffmann JA.##Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA.##Uttenweiler-Joseph S, Moniatte M, Lagueux M, Van Dorsselaer A, Hoffmann JA, Bulet P.##Weber AN, Tauszig-Delamasure S, Hoffmann JA, Lelièvre E, Gascan H, Ray KP, Morse MA, Imler JL, Gay NJ. Insect immunity. Septic injury of drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides.##The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults.##Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study.##Binding of the Drosophila cytokine Spätzle to Toll is DRAMP03094 DCLSGKYKGPCAVWDNEMCRRICKEEGHISGHCSPSLKCWCEGC 44 Drosomycin-2 (Insects, animals) No entry found Not found Not found Drosophila melanogaster (Fruit fly) Antimicrobial, Antifungal, Antiparasitic Not found Not found Not found "Function: Drosomycin-2 is antiparasitic peptide which shows inhibitory effect on the ookinete development of the parasite Plasmodium berghei. Induction: Expressed in larva, pupa and adult." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18657321 Mol Immunol. 2008 Sep;45(15):3909-3916. Tian C, Gao B, Rodriguez Mdel C, Lanz-Mendoza H, Ma B, Zhu S. Gene expression, antiparasitic activity, and functional evolution of the drosomycin family. DRAMP03099 QRPYTQPLIYYPPPPTPPRIYRA 23 Attacin-C (Insects, animals) Q95NH6 Not found AttC Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Antifungal Protein level Rich Not found Comment: No comments found on DRAMP database Agrobacterium tumefaciens (MIC>200 µM), Enterobacter cloacae b12 (MIC>200 µM), Escherichia coli SBS 363 (MIC>200 µM), Escherichia coli D31 (MIC>=200 µM), Escherichia coli D22 (MIC>=200 µM), Erwinia carotovora carotovora (MIC>200 µM), Pseudomonas aeruginosa (MIC>200 µM), Salmonella typhimurium (MIC>200 µM), Serratia marcescens (MIC>200 µM), Bacillus megaterium (MIC>200 µM), Micrococcus luteus(MIC>200 µM), Staphylococcus aureus (MIC>200 µM), Streptococcus pyogenes (MIC>200 µM), Neurospora crassa (MIC>200 µM), Aspergillus fumigatus (MIC>200 µM), Candida albicans (MIC>200 µM), Candida glabrata (MIC>200 µM), Cryptococcus neoformans (MIC>200 µM), Saccharomyces cerevisiae (MIC>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14744858 J Biol Chem. 2004 Apr 9;279(15):14853-9. Epub 2004 Jan 26. Rabel D, Charlet M, Ehret-Sabatier L, Cavicchioli L, Cudic M, Otvos L Jr, Bulet P. Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain. DRAMP18224 EKYTEAPEYI 10 Ala-6-fenycin (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus sp. strain P34 Antimicrobial, Antibacterial, Anti-Gram+, Antiviral Not found An acyl chain (C15 to C17 carbons) is attached to E1, residue 2 is an ornithine (represented as K), and the carboxylic group of C-terminal I10 forms an ester bond with the side chain of Y3. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25477947 Braz J Microbiol. 2014 Oct 9;45(3):1089-94. eCollection 2014. Scopel e Silva D, de Castro CC, da Silva e Silva F, Sant'anna V, Vargas GD, de Lima M, Fischer G, Brandelli A, da Motta Ade S, H Antiviral activity of a Bacillus sp. P34 peptide against pathogenic viruses of domestic animals. DRAMP03101 GWLRKIGKKIERVGQHTRDATIQVLGIAQQAANVAATAR 39 Sarcotoxin-1C (Sarcotoxin IC; Insects, animals) P08377 Belongs to the cecropin family Not found Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Sarcotoxins, which are potent bactericidal proteins, are produced in response to injury. They are cytotoxic to both Gram-positive and Gram-negative bacteria. PTM: Problely Arginine amide at R39." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3888997 J Biol Chem. 1985 Jun 25;260(12):7174-7177. Okada M, Natori S. Primary structure of sarcotoxin I, an antibacterial protein induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae. DRAMP03102 GWLKKIGKKIERVGQHTRDATIQVIGVAQQAANVAATAR 39 Sarcotoxin-1B (Sarcotoxin IB; Insects, animals) P08376 Belongs to the cecropin family Not found Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Sarcotoxins, which are potent bactericidal proteins, are produced in response to injury. They are cytotoxic to both Gram-positive and Gram-negative bacteria. PTM: Problely Arginine amide at R39." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3888997##2689214 J Biol Chem. 1985 Jun 25;260(12):7174-7177.##FEBS Lett. 1989 Dec 4;258(2):199-202. Okada M, Natori S.##Kanai A, Natori S. Primary structure of sarcotoxin I, an antibacterial protein induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae.##Cloning of gene cluster for sarcotoxin I, antibacterial proteins of Sarcophaga peregrina. DRAMP03103 GWIRDFGKRIERVGQHTRDATIQTIAVAQQAANVAATLKG 40 Sarcotoxin-1D (Sarcotoxin ID; Insects, animals) P18312 Belongs to the cecropin family Not found Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Sarcotoxins, which are potent bactericidal proteins, are produced in response to injury. They are cytotoxic to both Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus FDA209P, Staphylococcus smith, Micrococcus luteus, Bacillus subtilis, Mycobacterium smegmatis, Corynebacterium bouis, Corynebacterium michiganense.##Gram-negagtive bacteria: Xantbmonas oryzae, Pseudomonas lachrymans, Escherichia coli, Shigella sonnei, Proteus vulgaris. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3182836 J Biol Chem. 1988 Nov 15;263(32):17112-17116. Matsuyama K, Natori S. Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina. DRAMP03105 QHGHGGQDQHGYGHGQQAVYGKGHEGHGVNNLGQDGHGQHGYAHGHSDQHGHGGQHGQHDGYKNRGY 67 Antifungal protein (AFP; Insects, animals) Q08617 Not found Not found Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) Antimicrobial, Antifungal Protein level Not found Not found Function: This protein inhibits the growth of a variety of fungal species. The antifungal activity of this protein is enhanced by the presence of sarcotoxin IA. Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8505329##8454635 J Biol Chem. 1993 Jun 5;268(16):12055-12061.##J Biol Chem. 1993 Mar 25;268(9):6641-6648. Iijima R, Kurata S, Natori S.##Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregrina (flesh fly) larvae.##Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP03106 VFIDILDKMENAIHKAAQAGIGIAKPIENMILPKLTK 37 Andropin (Insects, animals) Q8WSV4, Q8WSV5 Not found Anp Drosophila simulans (Fruit fly) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J Mol Evol. 2002 May;54(5):665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP03107 FINLLDKVEDALHTGAQAGFKLIRPVERGATPKKSEKPEK 40 Andropin (Insects, animals) Q8WSV1 Not found Anp Drosophila teissieri (Fruit fly) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J Mol Evol. 2002 May;54(5):665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP03108 IFVDVLDNVETALHNAAKAGFKLIKPIEKLIMPK 34 Andropin (Insects, animals) Q8WPA1, B4PLU4, Q8WP55, Q8WSU9 Not found Anp Drosophila yakuba (Fruit fly) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J Mol Evol. 2002 May;54(5):665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP03109 VFIDILDKMENAIHKAAQAGIGLAKPIENMILPK 34 Andropin (Insects, animals) Q8WSV2, B4HZP0, P81687 Not found Anp Drosophila sechellia (Fruit fly) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438## 9725836 J Mol Evol. 2002 May;54(5):665-670.##Genetics. 1998 Sep;150(1):157-171. Date-Ito A, Kasahara K, Sawai H, Chigusa SI.##Ramos-Onsins S, Aguade M. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila.##Molecular evolution of the Cecropin multigene family in Drosophila: functional genes vs pseudogenes. DRAMP03110 VFIDILDKMENAIHKAAQAGIGIAKPIEKMILPK 34 Andropin (Insects, animals) O16825, Q8WSV3 Not found Anp Drosophila mauritiana (Fruit fly) Antimicrobial, Antibacterial, Antiprotozoal Transcript level Not found Not found Andropin is constitutively expressed in the adult male ejaculatory duct in response to mating not bacterial infection. Leishmania panamensis (EC50=23.45 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J. Mol. Evol. 2002; 54:665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP03111 QSDALFVDIIDNVENAIHKAAKTGIGMVKPIENIFIPNQQKKSTEASN 48 Andropin (Insects, animals) Q8WSV0 Not found Anp Drosophila orena (Fruit fly) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11965438 J. Mol. Evol. 2002; 54:665-670. Date-Ito A, Kasahara K, Sawai H, Chigusa SI. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila. DRAMP18223 CWSCMGHSCWSCMGHSCWSCAGHSCWSCMGHSCWSCMGHSCWSCAGHCCGSCWHGGM 57 Sonorensin(Bacteriocin) X2CRH8 Belongs to the class I bacteriocin Not found Bacillus sonorensis MT93 Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found The Clustal W alignment of the N terminus of sonorensin revealed homology with the leader sequences of protoxins from various Bacillus strains. This indicated that sonorensin, produced initially as a protoxin, was posttransitionally modified to active bacteriocin. The purified sonorensin was also found to be heat stable, stable at low temperature, biologically active over a wide pH range, and not affected in the presence of organic solvents, surfactants, and reducing agents. However, sonoresin was protease-sensitive. Gram-positive, Gram-negative (broad spectrum) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24610839 Appl Environ Microbiol. 2014 May;80(10):2981-90. Chopra L, Singh G, Choudhary V, Sahoo DK. Sonorensin: an antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93. DRAMP03114 GWLKKIGKKIERIGQHTRDATIQGLGIAQQAANVAATAR 39 Cecropin-1/3 (Insects, animals) Q94557 Not found Not found Drosophila virilis (Fruit fly) Antimicrobial, Antibacterial Homology Not found Not found Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9060393##17994087 J Mol Evol. 1997 Mar;44(3):272-281.##Nature. 2007 Nov 8;450(7167):203-218. Zhou X, Nguyen T, Kimbrell D.A.##Drosophila 12 genomes consortium. Identification and characterization of the Cecropin antibacterial protein gene locus in Drosophila virilis.##Evolution of genes and genomes on the Drosophila phylogeny. DRAMP03118 RRFKKFLKKVEGAGRRVANAAQKGLPLAAGVKGLV 35 Cecropin-C (AgCecC; Insects, animals) Q8MUF3, B2FVD8, Q7QEE4 Belongs to the cecropin family CecC Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12421409 Insect Mol Biol. 2002 Dec;11(6):517-525. Zheng XL, Zheng AL. Genomic organization and regulation of three cecropin genes in Anopheles gambiae. DRAMP03119 ATCDLASFSSQWVTPNDSLCAAHCIARRYRGGYCNGKRVCVCR 43 Def-BAT (hybrid defensins; Insects, animals) Q17027 Not found Not found Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Alpha helix (1 helices; 7 residues) For Def-BAT, the two extended strands do not form an anti-parallel β-sheet. The helix is separated from the β-sheet by a turn (T1) and the two strands of the b-sheet by turn T2. 2E3F resolved by NMR. "Function: Responsible for the anti Gram-positive activity of immune hemolymph and proves to be efficient against sensitive strains as against resistant and multi-resistant strains." Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=6.25 µg/mL), Staphylococcus aureus strain 4 (IC90=6.25 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03120 ATCDLASFSSQWVTPNDSLCAAHCLVKGYRGGYCKNKICHCRDKF 45 Def-BBB (hybrid defensins; Insects, animals) Q17027 Not found Not found Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Global fold has a N-terminal loop L1, followed by a helix and a two-stranded antiparallel β-sheet forming the CSab motif. 2E3E resolved by NMR. "Function: Responsible for the anti Gram-positive activity of immune hemolymph and proves to be efficient against sensitive strains as against resistant and multi-resistant strains." Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=10 µg/mL), Staphylococcus aureus strain 4 (IC90>80 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03121 ATCDLASGFGVGSSLCAAHCLVKGYRGGYCKNKICHCRDKF 41 Def-ABB (hybrid defensins; Insects, animals) Q17027 Not found Not found Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Global fold has a N-terminal loop L1, followed by a helix and a two-stranded antiparallel β-sheet forming the CSab motif. 2NY9 resolved by NMR. "Function: Responsible for the anti Gram-positive activity of immune hemolymph and proves to be efficient against sensitive strains as against resistant and multi-resistant strains." Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90>25 µg/mL), Staphylococcus aureus strain 4 (IC90>80 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03122 ATCDLASGFGVGSSLCAAHCIARRYRGGYCNSKAVCVCRN 40 Anopheles gambiae defensin (DEF-AAA; Insects, animals) Q17027, O61721, Q38L95, Q38L99, Q38LA3, Q38LA4, Q38LA6, Q38LB0, Q38LB2 Belongs to the invertebrate defensin family (Type 1 subfamily) Def1 Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Global fold has a N-terminal loop L1, followed by a helix and a two-stranded antiparallel β-sheet forming the CSab motif. 2NY8 resolved by NMR. "Function: Responsible for the anti Gram-positive activity of immune hemolymph and proves to be efficient against sensitive strains as against resistant and multi-resistant strains. Developmental stage: In larvae, transcript is enhanced 4 hours after the bacterial infection, increases up to 12 hours post inoculation and declines by 24 hours and by 30 hours returns to background levels. In adult female, expression is evident by 18 hours after infection. Constitutively expressed in both early and late pupae. Induction: By bacterial infection. PTM: Contains three disulfide bonds 3-30; 16-36; 20-38." Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=6.25 µg/mL), Staphylococcus aureus strain 4 (IC90=6.25 µg/mL).##T1=100 mg/kg, T2>100 mg/kg.##T1, dose causing the first signs of toxicity on mice. T2, lethal dose. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8799739##18214975 Insect Mol Biol. 1996 Aug;5(3):203-210.##Proteins. 2008 Jul;72(1):229-239. Richman AM, Bulet P, Hetru C, Barillas-Mury C, Hoffmann JA, Kafalos FC.##Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Inducible immune factors of the vector mosquito Anopheles gambiae: biochemical purification of a defensin antibacterial peptide and molecular cloning of preprodefensin cDNA.##Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03123 APRWKFGKRLEKLGRNVFRAAKKALPVIAGYKAL 34 Cecropin-B (AgCecB; Insects, animals) Q8MUF4, Q7QEE2 Belongs to the cecropin family CecB Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12421409 Insect Mol Biol. 2002 Dec;11(6):517-525. Zheng XL, Zheng AL. Genomic organization and regulation of three cecropin genes in Anopheles gambiae. DRAMP03124 ATCDLASIFNVNHALCAAHCIARRYRGGYCNSKAVCVCRN 40 Def-AcAA (hybrid defensins; Insects, animals) Q17027 Not found Not found Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Global fold has a N-terminal loop L1, followed by a helix and a two-stranded antiparallel β-sheet forming the CSab motif. 2NZ3 resolved by NMR. Function: Among the five hybrid defensins tested, Def-AcAA appears to be more efficient than Def-AAA on the multi resistant and sensitive strains. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=1.56 µg/mL), Staphylococcus aureus strain 4 (IC90=3.125 µg/mL).##T1=100 mg/kg, T2>100 mg/kg.##T1, dose causing the first signs of toxicity on mice. T2, lethal dose. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03125 ATCDLASKWNWNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 Def-DAA (hybrid defensins; Insects, animals) Q17027 Not found Not found Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Combine helix and strand structure Global fold has a N-terminal loop L1, followed by a helix and a two-stranded antiparallel β-sheet forming the CSab motif. 2E3G resolved by NMR. Function: Among the five hybrid defensins tested, Def-DAA appears to be more efficient than Def-AAA on the multi resistant and sensitive strains. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=0.75 µg/mL), Staphylococcus aureus strain 4 (IC90=1.5 µg/mL).##T1=8 mg/kg, T2=30 mg/kg.##T1, dose causing the first signs of toxicity on mice. T2, lethal dose. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP03126 QLKNLACVTNEGPKWANTYCAAVCHMSGRGAGSCNAKDECVCSMT 45 Antimicrobial peptide defensin 3 (AgDef3; Insects, animals) Q5TWR9, Q2KM07 Not found Def3 Anopheles gambiae (African malaria mosquito) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial peptide mostly active against Gram-positive bacteria with atypical up-regulation of expression. Developmental stage: Basal levels of expression during all life stages, with higher levels during larval development peaking at larval instars 2/3. Induction: Not induced in 4th instar larvae following a blood meal, an infected blood meal, sterile injection or bacterial injection (E.coli K12 RM148 and M.luteus). PTM: Contains three disulfide bonds 7-34; 20-39; 24-42." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18353100##16835022 Insect Mol Biol. 2008 Apr;17(2):103-112.##Insect Biochem Mol Biol. 2006 Jul;36(7):570-575. Meredith JM, Hurd H, Lehane MJ, Eggleston P.##Calvo E, Pham VM, Lombardo F, Arcà B, Ribeiro JM. The malaria vector mosquito Anopheles gambiae expresses a suite of larval-specific defensin genes.##The sialotranscriptome of adult male Anopheles gambiae mosquitoes. DRAMP03127 GGLKKFGKKLEGVGKRVFKASEKALPVVTGFKAL 34 Cecropin-A (Insects, animals) Q86PR6 Not found CECA Culex pipiens pipiens (Northern house mosquito) Antimicrobial, Antibacterial Homology Not found Not found Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. Bartholomay L.C, Farid H.A, Ramzy R.M, Christensen B.M. Innate immunity in the Culex pipiens-Wuchereria bancrofti host-parasite relationship. DRAMP03128 GRLKKLGKKIEKAGKRVFNAVQKGLPVAAGVQAL 34 Cecropin-B1 (Insects, animals) Q86PR5 Not found CECB1 Culex pipiens pipiens (Northern house mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. Bartholomay L.C, Farid H.A, Ramzy R.M, Christensen B.M. Innate immunity in the Culex pipiens-Wuchereria bancrofti host-parasite relationship DRAMP03129 GRSKKLGKKIEKAGKRVFNAAQKGLPVAAGVQAL 34 Cecropin-B2 (Insects, animals) Q86PR4 Not found CECB2 Culex pipiens pipiens (Northern house mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. Bartholomay L.C, Farid H.A, Ramzy R.M, Christensen B.M. Innate immunity in the Culex pipiens-Wuchereria bancrofti host-parasite relationship DRAMP03130 GGLKKFGKKLEGVGKRVFKASEKALPVAVGIKALG 35 Cecropin-A2 (Insects, animals) Q963B0 Belongs to the cecropin family CECA2 Aedes albopictus (Asian tiger mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. Sun D, Fallon A.M. Characterization of genomic DNA encoding mosquito cecropins. DRAMP03131 GGLKKLGKKLEGVGKRVFKASEKALPVLTGYKAIG 35 Cecropin-B (Insects, animals) Q9Y0Y0, Q963A9 Belongs to the cecropin family CECB1 AND CECB2 Aedes albopictus (Asian tiger mosquito) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity) Developmental stage: Expressed within 2 hours after induction and continued to accumulate over 24 hours. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10413113 FEBS Lett. 1999; 454:147-151. Sun D, Eccleston ED, Fallon AM. Cloning and expression of three cecropin cDNAs from a mosquito cell line. DRAMP03132 GGLKKLGKKLEGAGKRVFNAAEKALPVVAGAKALG 35 Cecropin-C (Insects, animals) Q963A8, Q9Y0X9 Belongs to the cecropin family CECC1 AND CECC2 Aedes albopictus (Asian tiger mosquito) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087945 Biochim Biophys Acta. 2000 Nov 30;1543(1):95-105. sir YJ, Knoop FC, Dulka J, Conlon JM. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. DRAMP03133 GGLKKLGKKLEGVGKRVFKASEKALPVAVGIKALG 35 Cecropin-A1 (AalCecA; Cecropin-A; Insects, animals) P81417, Q963B1 Belongs to the cecropin family CECA1 Aedes albopictus (Asian tiger mosquito) Antimicrobial, Antibacterial Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10413113##9712710 FEBS Lett. 1999 Jul 2;454(1-2):147-151.##Biochem Biophys Res Commun. 1998 Aug 19;249(2):410-415. Sun D, Eccleston ED, Fallon AM.##Sun D, Eccleston ED, Fallon AM. Cloning and expression of three cecropin cDNAs from a mosquito cell line.##Peptide sequence of an antibiotic cecropin from the vector mosquito, Aedes albopictus. DRAMP03134 ATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCPI 40 Defensin-D (AaeDefD; Insects, animals) No entry found Not found Not found Aedes aegypti (Yellowfever mosquito) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli D31;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10469248 Insect Mol Biol. 1999 Aug;8(3):311-318. Gao Y, Hernandez VP, Fallon AM. Immunity proteins from mosquito cell lines include three defensin A isoforms from Aedes aegypti and a defensin D from Aedes albopictus. DRAMP03135 ATCDLLSGFGVGDSACAAHCIARGNRGGYCNSQKVCVCRN 40 Defensin-B (AaeDefB; Insects, animals) P81602, Q71U14, Q71U15 Belongs to the invertebrate defensin family (Type 1 subfamily) DEFB Aedes aegypti (Yellowfever mosquito) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Antibacterial peptide mostly active against Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Has three disulfide bonds L No cytotoxicity information found Not found 7633471 Insect Biochem Mol Biol. 1995 Jul;25(7):867-873. Lowenberger C, Bulet P, Charlet M, Hetru C, Hodgeman B, Christensen BM, Hoffmann JA. Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti. DRAMP03136 ATCDLLSGFGVGDSACAAHCIARRNRGGYCNAKKVCVCRN 40 Defensin-C (AaeDefC; Insects, animals) P81603, Q17EE4, Q9Y0F0, Q9Y0F1 Belongs to the invertebrate defensin family (Type 1 subfamily) DEFC Aedes aegypti (Yellowfever mosquito) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Antibacterial peptide mostly active against Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7633471 Insect Biochem Mol Biol. 1995 Jul;25(7):867-873. Lowenberger C, Bulet P, Charlet M, Hetru C, Hodgeman B, Christensen BM, Hoffmann JA. Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti. DRAMP03139 ISCDLLSGLGWGHSICAGHCLAISWRYRGGYCNDQGVCVCRT 42 AAEL003849-PA Q17EE5 Not found DEFE Aedes aegypti (Yellowfever mosquito) (Culex aegypti) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17510324 Science. 2007 Jun 22;316(5832):1718-1723. Nene V, Wortman JR, Lawson D, Haas B, Kodira C, Tu ZJ, et al. Genome sequence of Aedes aegypti, a major arbovirus vector. DRAMP03141 QTPCSSAKKVRCNVHCRGYTKLGSCYDDNCSCVDKPAAMKASFAA 45 Putative defensin 5 A9QVW3 Not found DEF5 Anopheles gambiae (African malaria mosquito) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19328852 Insect Biochem Mol Biol. 2009 May-Jun;39(5-6):382-394. Neira Oviedo M, Ribeiro JM, Heyland A, VanEkeris L, Moroz T, Linser PJ. The salivary transcriptome of Anopheles gambiae (Diptera: Culicidae) larvae: A microarray-based analysis. DRAMP03142 STCKLFTADVVSSITCKMYCVIKGKTGGYCNSEGLCTCRAEDLHFLLKPIINKD 54 AGAP004632-PA (Defensin) Q5TRV9, Q1X7M1, Q2EQ06 Not found DEF2 Anopheles gambiae (African malaria mosquito) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12364791 Science. 2002 Oct 4;298(5591):129-149. Holt RA, Subramanian GM, Halpern A, Sutton GG, Charlab R, et al, Collins FH, Hoffman SL. The genome sequence of the malaria mosquito Anopheles gambiae. DRAMP03143 MKQVCILLAVLLCTAAVADAMVFAYAPTCARCKSIGARYCGYGYLNRKGVSCDGQTTINSCEDCKRKFGRCSDGFITECFF 81 AGAP008645-PA (Putative infection responsive short peptide) Q9XZN6, Q7Q8G3 Not found irsp Anopheles gambiae (African malaria mosquito) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11606751 Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12630-5. Vizioli J, Bulet P, Hoffmann JA, Kafatos FC, Müller HM, Dimopoulos G. Gambicin: a novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae. DRAMP03144 ATCDLASGFGVGSSLCAAHCIARRYRGGYCNSQQVCVCRN 40 Salivary defensin A2TJI3 Not found Not found Anopheles stephensi (Indo-Pakistan malaria mosquito) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18275930 Acta Trop. 2008 Apr;106(1):75-79. Dixit R, Sharma A, Patole MS, Shouche YS. Molecular and phylogenetic analysis of a novel salivary defensin cDNA from malaria vector Anopheles stephensi. DRAMP03145 ATCDLLSGFGVGDSACAAHCIARRNRGGYCNAKTVCVC 38 Defensin Q9GYU6 Not found Not found Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Melinda PM, Kostas B, Scott OL. Wolbachia neither induces nor suppresses transcripts encoding antimicrobial peptides. DRAMP03146 ATCDLLSGFGVNDSACAAHCILRGNRGGYCNGKKVCVCRN 40 Defensin Q86PP9 Not found Not found Culex pipiens pipiens (Northern house mosquito) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14550895 Mol Biochem Parasitol. 2003 Aug 11;130(1):43-50. tholomay LC, Farid HA, Ramzy RM, Christensen BM. Culex pipiens pipiens: characterization of immune peptides and the influence of immune activation on development of Wuchereria bancrofti. DRAMP03147 ATCDLLSGLGVNDSACAAHCIARGNRGGYCNSKKVCVCRN 40 Defensin-A B0W2M6 Not found Not found Culex quinquefasciatus (Southern house mosquito) (Culex pungens) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases The Broad Institute Genome Sequencing Platform. Annotation of Culex pipiens quinquefasciatus. DRAMP03148 DELPEETYQAAVENYRRKRATCDLLSGFGVGDSACAAHCIARRNRGGYCNAKTVCVC 57 Defensin Q9GYU6 Not found Not found Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Melinda PM, Kostas B, Scott OL. Wolbachia neither induces nor suppresses transcripts encoding antimicrobial peptides. DRAMP03149 VPTVICFLAMCLVAITGAYPQEPVLADEAQSVANSLFDELPEESYQAAVENLRLKRATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCPI 96 Defensin D O77217 Not found DefD Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10469248 Insect Mol Biol. 1999 Aug;8(3):311-318. Gao Y, Hernandez VP, Fallon AM. Immunity proteins from mosquito cell lines include three defensin A isoforms from Aedes aegypti and a defensin D from Aedes albopictus. DRAMP03151 RWKVFKKIEKVGRNVRDGIIKAGPAIGVLGQAKALG 36 Spodoptera cecropins A (insects, invertebrates, animals) Q9XZG9 Not found CECA Spodoptera litura larvae (Common cutworm) Antimicrobial, Antibacterial Protein level Not found Not found Function: It retains antibacterial activities in all conditions tested (at pH 5.6-8.0 and in the presence of 50-150 mM NaCl) that was adapted to confirm the antibacterial properties of Spodoptera cecropins. Northern blot analysis with (32)P-labeled PCR product coding for Spodoptera cecropin A revealed that Spodoptera cecropin genes are expressed in immunized fat body, but not in normal fat body. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11790350 Comp Biochem Physiol C Toxicol Pharmacol. 2000 Mar;125(3):287-297. Choi CS, Lee IH, Kim E, Kim SI, Kim HR. Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura. DRAMP03152 RWKVFKKIEKMGRNIRDGIVKAGPAIEVLGSAKALGK 37 Spodoptera cecropins B (insects, invertebrates, animals) Q9XZH0 Belongs to the cecropin family CECB Spodoptera litura larvae (Common cutworm) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Induction: Induced as part of the humoral response to a bacterial invasion. Transcripts appear within the immunized fat body. Tissue specificity: Expressed in immunized fat body. NOTE: It retains antibacterial activities in all conditions tested (at pH 5.6-8.0 and in the presence of 50-150 mM NaCl) that was adapted to confirm the antibacterial properties of Spodoptera cecropins. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11790350 Comp Biochem Physiol C Toxicol Pharmacol. 2000 Mar;125(3):287-297. Choi CS, Lee IH, Kim E, Kim SI, Kim HR. Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura. DRAMP03154 GILDTIKSIASKVWNSKTVQDLKRKGINWVANKLGVSPQAA 41 Hadrurin (Non-disulfide-bridged peptide 3.1) P82656 Belongs to the antimicrobial peptide scorpion family Not found Hadrurus aztecus Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Has antimicrobial activity. Also shows cytolytic activity when tested in human erythrocytes. Gram-negative bacteria: Salmonella typhimurium, Klebsiella pneumoniae, Enterobacter cloacae, Pseudomonas aeruginosa, Escherichia coli, Serratia marcescens. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10931184 Eur J Biochem. 2000 Aug;267(16):5023-5031. Torres-Larios A, Gurrola GB, Zamudio FZ, Possani LD. Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus. DRAMP03155 ACLPNSCVSKGCCCGBSGYWCRQCGIKYTC 30 Sillucin P02885 Not found Not found Rhizomucor pusillus Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Sillucin is an antimicrobial agent produced by the thermophilic fungus Rhizomucor pusillus in liquid culture; it is effective against Gram-positive bacteria at the level of RNA metabolism. PTM: Contains four disulfide bonds 2-7; 12-24; 13-30; 14-21." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 761621##11294620 FEBS Lett. 1979 Jan 1;97(1):81-83.##Biochemistry. 2001 Apr 17;40(15):4531-4538. Bradley WA, Somkuti GA.##Qi J, Wu J, Somkuti GA, Watson JT. The primary structure of sillucin and antimicrobial peptide from Mucor pusillus.##Determination of the disulfide structure of sillucin, a highly knotted, cysteine-rich peptide, by cyanylation/cleavage mass mapping. DRAMP03156 RRLRPRRPRLPRPRPRPRPRPRSLPLPRPQPRRIPRPILLPWRPPRPIPRPQPQPIPRWL 60 Cathelicidin-3 (Bactenecin-7, Bac7; PR-59; mammals, animals) P50415 Belongs to the cathelicidin family CATHL3 Ovis aries (Sheep) Antimicrobial, Antibacterial Protein level Not found Not found Function: Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7498547 FEBS Lett. 1995 Dec 4;376(3):225-228. Bagella L, Scocchi M, Zanetti M. cDNA sequences of three sheep myeloid cathelicidins. DRAMP03157 ALLHHGLNCAKGVLA 15 Halocidin subunit B P83706 Not found Not found Halocynthia aurantium (Sea peach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antimicrobial activity, possibly by attacking the bacterial cell membrane. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12067731 FEBS Lett. 2002 Jun 19;521(1-3):81-86. Jang WS, Kim KN, Lee YS, Nam MH, Lee IH. Halocidin: a new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. DRAMP03158 WLNALLHHGLNCAKGVLA 18 Halocidin subunit A (invertebrates, animals; Preclinical) P83705 Not found Not found Halocynthia aurantium (Sea peach) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antimicrobial activity against S.aureus and P.aeruginosa, possibly by attacking the bacterial cell membrane. Mouse model: A single intravenous injection of the modified chain A by itself into mice resulted in an significant therapeutic effect (Jang et al. 2007;51: 4148-4156). Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12067731 FEBS Lett. 2002 Jun 19;521(1-3):81-86. Jang WS, Kim KN, Lee YS, Nam MH, Lee IH. Halocidin: a new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. DRAMP03159 VKKGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRP 67 WAP four-disulfide core domain protein 12 (mammals, animals) A4K2V4 Not found WFDC12 Pongo abelii (Sumatran orangutan) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 1 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP03160 VKVNIEKPGVCPADNIRCIKSDPPQCHTDQDCQGIRKCCYLHCGFKCVIPVKELEEGGNKDEDVSRPCPEPGWEAKPPGVFSTRCPQK 88 WAP four-disulfide core domain protein 12 (mammals, animals) A4K2U1 Not found WFDC12 Callithrix jacchus (white-tufted-ear-marmoset) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 4 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP03161 DHYNCVKGGGQCLYSACPIYTKVQGTCYGGKAKCCK 36 Beta-defensin 1 (BD-1; Defensin, beta 1; mammals, animals), Q95M66 Belongs to the beta-defensin family DEFB1 Saguinus oedipus (Cotton-top tamarin) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds 5-34; 12-27; 17-35." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11862391 Immunogenetics. 2002 Feb;53(10-11):907-913. Del Pero M, Boniotto M, Zuccon D, Cervella P, Spanò A, Amoroso A, Crovella S. Beta-defensin 1 gene variability among non-human primates. DRAMP03163 ATCDLFSFRSKWVTPNHAACAAHCLLRGNRGGRCKGTICHCRK 43 R. prolixus defensin A (RprDefA; insect defensin; Insects, animals) No entry found Not found Not found Rhodnius prolixus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Not found Combine helix and strand structure Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP03164 ATCDLLSFRSKWVTPNHAGCAAHCLLRGNRGGHCKGTICHCRK 43 R. prolixus defensin B (RprDefB; insect defensin; Insects, animals) No entry found Not found Not found Rhodnius prolixus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Not found Combine helix and strand structure Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP03165 ATCDLFSFRSKWVTPNHAGCAAHCIFLGNRGGRCVGTVCHCRK 43 R. prolixus defensin C (RprDefC; insect defensin; Insects, animals) No entry found Not found Not found Rhodnius prolixus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Not found Combine helix and strand structure Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP03167 RFIPPILRPPVRPPFRPPFRPPFRPPPIIRFFGG 34 P9 No entry found Not found Not found Cervus elaphus (New Zealand deer) Not found Not found Not found Not found Function: showes good antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16011891 Int J Antimicrob Agents. 2005 Aug;26(2):165-169. Treffers C, Chen L, Anderson RC, Yu PL. Isolation and characterisation of antimicrobial peptides from deer neutrophils. DRAMP03168 DDRRSPLEECFQQNDYEEFLEIAKNGLKKTXNPKHVXV 38 L-amino-acid oxidase (K-LAO; LAAO; LAO; reptilia, animals) P0C2D4 Belongs to the flavin monoamine oxidase family (FIG1 subfamily) Not found Naja naja kaouthia (Monocled cobra) Antimicrobial, Antibacterial Protein level Not found Not found Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L- Phe and L-Tyr, and moderately active against L-Trp, L-Met, L-Leu, and L-Arg), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities (By similarity). This protein inhibits both agonist- and shear stress-induced platelet aggregation (SIPA). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet FAD, Flavoprotein 1612186##11600144 Int J Biochem. 1992 Jun;24(6):967-973.##Toxicon. 2001 Dec;39(12):1827-1833. Tan NH, Swaminathan S.##Sakurai Y, Takatsuka H, Yoshioka A, Matsui T, Suzuki M, Titani K, Fujimura Y. Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom.##Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. DRAMP03170 MQKLAEAIAAAVQAGQDKDWGKMGTSIVGIVENGISVLGKIFGF 44 Antibacterial protein 1 homolog (Gram-positive bacteria) Q4L5M5 Belongs to the staphylococcal hemolytic protein family Not found Staphylococcus haemolyticus (strain JCSC1435) Antimicrobial, Antibacterial Homology Not found Not found Function: Has haemolytic activity and also inhibits the growth of gonococci (By similarity). Gonococci No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16237012 J Bacteriol. 2005 Nov;187(21):7292-7308. Takeuchi F, Watanabe S, Baba T, Yuzawa H, Ito T, Morimoto Y, Kuroda M, Cui L, Takahashi M, Ankai A, Baba S, Fukui S, Lee JC, Hiramatsu K. Whole-genome sequencing of staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species. DRAMP18222 GDCGGTCTWTKDCSICPSWSCWSWSC 26 PseA(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus pseudomycoides DSM 12442 Antimicrobial, Antibacterial, Anti-Gram+ Not found This antibiotic with four thioether rings and a disulfide bond. The leader sequence shows highest (37%) similarity to the leader sequence of mersacidin.The N terminus of the corepeptide contains the conserved lipid II binding motif of class II lantibiotics (TxS/TxE/DC) and, interestingly, the C terminus of the core peptide contains two SWSC motifs. Such motifs also are found in the heterocycloanthracins. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25769830 Appl Environ Microbiol. 2015 May 15;81(10):3419-29. Basi-Chipalu S, Dischinger J, Josten M, Szekat C, Zweynert A, Sahl HG, Bierbaum G. Pseudomycoicidin, a Class II Lantibiotic from Bacillus pseudomycoides. DRAMP03172 MSKLVQAISDAVQAGQNQDWAKLGTSIVGIVENGVGILGKLFGF 44 Antibacterial protein 3 homolog (Gram-positive bacteria) Q4L5M1 Belongs to the staphylococcal hemolytic protein family Not found Staphylococcus haemolyticus (strain JCSC1435) Antimicrobial, Antibacterial Homology Not found Not found Function: Has haemolytic activity and also inhibits the growth of gonococci (By similarity). Gonococci No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16237012 J Bacteriol. 2005 Nov;187(21):7292-7308. Takeuchi F, Watanabe S, Baba T, Yuzawa H, Ito T, Morimoto Y, Kuroda M, Cui L, Takahashi M, Ankai A, Baba S, Fukui S, Lee JC, Hiramatsu K. Whole-genome sequencing of staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species. DRAMP03174 RWCVYAYVRIRGVLVRYRRCW 21 Arenicin-2 (Ar-2; marine polychaeta, animals) Q5SC59, P84106 Not found Not found Arenicola marina (Lugworm) (Lumbricus marinus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand (2 strands; 16 residues) NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon 2JNI, 2L8X resolved by NMR. "Function: Has antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteriua as well as yeast C. albicans. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. PTM: Contains one disulfide bond 3-20. Domian: Contains 1 BRICHOS domain." Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacterium: Escherichia coli ML-35p.##Yeast: Candida albicans 820. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys3 and Cys20. L No cytotoxicity information found Anionic lipid vesicles 15527787##17935487##17585874 FEBS Lett. 2004 Nov 5;577(1-2):209-214.##Biochem J. 2008 Feb 15;410(1):113-122.##Biochem Biophys Res Commun. 2007 Aug 17;360(1):156-162. Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN.##Andrä J, Jakovkin I, Grötzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M.##Ovchinnikova TV, Shenkarev ZO, Nadezhdin KD, Balandin SV, Zhmak MN, Kudelina IA, Finkina EI, Kokryakov VN, Arseniev AS. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina.##Structure and mode of action of the antimicrobial peptide arenicin.##Recombinant expression, synthesis, purification, and solution structure of arenicin. DRAMP03175 FNKLKQGSSKRTCAKCFRKIMPSVHELDERRRGANRWAAGFRKCVSSICRY 51 Perinerin P84117, P83551 Not found Not found Nereis aibuhitensis (Clamworm) (Perinereis aibuhitensis) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antibacterial activity against both Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas aeruginosa, Escherichia coli K-12, Proteus vulgaris;##Gram-positive bacteria: Bacillus megaterium, Aerococcus viridans, Staphylococcus aureus, Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15113828 J Biochem. 2004 Mar;135(3):297-304. Pan W, Liu X, Ge F, Han J, Zheng T. Perinerin, a novel antimicrobial peptide purified from the clamworm Perinereis aibuhitensis grube and its partial characterization. DRAMP03177 SWLSKTYKKLENSAKKRISEGIAIAIQGGPR 31 Cecropin-P2 (CP2; nematodes, animals) Q5H7N6 Belongs to the cecropin family ASCEC-2 Ascaris suum (Pig roundworm) (Ascaris lumbricoides) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15850460 Biochem J. 2005 Aug 15;390(Pt 1):207-214. Pillai A, Ueno S, Zhang H, Lee JM, Kato Y. Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum. DRAMP03178 SWLSKTAKKLENSAKKRISEGIAIAIKGGSR 31 Cecropin-P3 (CP3; nematodes, animals) Q5H7N5 Belongs to the cecropin family ASCEC-3 Ascaris suum (Pig roundworm) (Ascaris lumbricoides) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15850460 Biochem J. 2005 Aug 15;390(Pt 1):207-214. Pillai A, Ueno S, Zhang H, Lee JM, Kato Y. Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum. DRAMP03179 SWLSKTYKKLENSAKKRISEGVAIAILGGLR 31 Cecropin-P4 (CP4; nematodes, animals) Q5H7N4 Belongs to the cecropin family ASCEC-4 Ascaris suum (Pig roundworm) (Ascaris lumbricoides) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism. Tissue specificity: Expressed in the body wall, intestine, uterus and ovary. Induction: Induced as part of the humoral response to a bacterial invasion. Transcripts appear within the immunized fat body." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15850460 Biochem J. 2005 Aug 15;390(Pt 1):207-214. Pillai A, Ueno S, Zhang H, Lee JM, Kato Y. Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum. DRAMP03180 AVDFSSCARMDVPGLSKVAQGLCISSCKFQNCGTGHCEKRGGRPTCVCDRCGRGGGEWPSVPMPKGRSSRGRRHS 75 ASABF-alpha (ASABF; nematodes, animals) P90683 Not found asabf-alpha Ascaris suum (Pig roundworm) (Ascaris lumbricoides) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Not found 2D56 resolved by NMR. Slight hemolytic activity against human erythrocytes. [Ref.10991847]Gram-negative bacteria: Escherichia coli JM109 (IC50=50 µg/ml), Proteus vulgaris ATCC 13315 (IC50=10 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC6538P (IC50=0.6 µg/ml), Bacillus subtilis ATCC6633 (IC50=1.2 µg/ml), Micrococcus luteus ATCC398 (IC50=0.8 µg/ml). [Ref.10991847]4.5% hemolytic activity at 1000 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8940016##10991847 J Biol Chem. 1996 Nov 29;271(48):30493-30498.##Antimicrob Agents Chemother. 2000 Oct;44(10):2701-2715. Kato Y, Komatsu S.##Zhang H, Yoshida S, Aizawa T, Murakami R, Suzuki M, Koganezawa N, Matsuura A, Miyazawa M, Kawano K, Nitta K, Kato Y. ASABF, a novel cysteine-rich antibacterial peptide isolated from the nematode Ascaris suum. Purification, primary structure, and molecular cloning of cDNA.##In vitro antimicrobial properties of recombinant ASABF, an antimicrobial peptide isolated from the nematode Ascaris suum. DRAMP03182 ACNFQSCWATCQAQHSIYFRRAFCDRSQCKCVFVRG 36 Termicin (Termite defensin; Insects, animals) P82321 Not found Not found Pseudacanthotermes spiniger Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Combine helix and strand structure Not found 1MM0 resolved by NMR. Function: Has antibacterial activity. Gram-positive bacteria: Bacillus megaterium, Micrococcus luteus, Streptococcus pyogenes(++).##Fungi: Fusarium culmorum, Fusarium oxysporum, Neurospora crassa, Nectria haematococca, Trichoderma viride(+); Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisiae(+++). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11053427##12592014 J Biol Chem. 2001 Feb 9;276(6):4085-4092.##Protein Sci. 2003 Mar;12(3):438-446. Lamberty M, Zachary D, Lanot R, Bordereau C, Robert A, Hoffmann JA, Bulet P.##Da Silva P, Jouvensal L, Lamberty M, Bulet P, Caille A, Vovelle F. Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect.##Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger. DRAMP03183 DAECEICKFVIQQVEAFIESNHSQAEIQKELNKL 34 Naegleriapore A Q95X03 Not found NP-A Naegleria fowleri (Brain eating amoeba) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiprotozoal, Cytotoxic Predicted Alpha helix It is characterized by a structure of amphipathic α-helices and an invariant framework of cysteine residues involved in disulfide bonds. Function: Posesses antibacterial, cytotoxicity and pore-forming activity. In concentrations up to 10 µm, naegleriapore A is inactive against the Gram-negative bacterium E. coli D31. The specific pore-forming activities of naegleriapore A and B are 3.1±1.7 units pmol−1 and 3.7±1.3 units pmol−1, respectively. Gram-negative bacterium: Escherichia coli K-12 D31;##Gram-positive bacterium: Bacillus subtilis strain 60015. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11948186 J Biol Chem. 2002 Jun 21;277(25):22353-22360. Herbst R, Ott C, Jacobs T, Marti T, Marciano-Cabral F, Leippe M. Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. DRAMP03184 SVIGCEICEWLVATAEGFVNKTKPQIEQELLQICAKLGPYEQICDQLVLMELPDIIDQIIAKEPPAIVCSQVKICNG 77 Naegleriapore B Q95X02 Not found NP-B Naegleria fowleri (Brain eating amoeba) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiprotozoal, Cytotoxic Predicted Alpha helix It is characterized by a structure of amphipathic α-helices and an invariant framework of cysteine residues involved in disulfide bonds. Function: Posesses antibacterial, cytotoxicity and pore-forming activity. Naegleriapore B does not exert any antibacterial activity in concentration up to 10 µm against the bacteria tested. The specific pore-forming activities of naegleriapore A and B are 3.1±1.7 units pmol−1 and 3.7±1.3 units pmol−1, respectively. Gram-negative bacterium: Escherichia coli K-12 D31;##Gram-positive bacterium: Bacillus subtilis strain 60015. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11948186 J Biol Chem. 2002 Jun 21;277(25):22353-22360. Herbst R, Ott C, Jacobs T, Marti T, Marciano-Cabral F, Leippe M. Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. DRAMP03185 SFGLCRLRRGFCAHGRCRFPSIPIGRCSRFVQCCRRVW 38 Spheniscin-1 (Sphe-1; penguin avian beta-defensin 103a; birds ,animals) P83429 Belongs to the beta-defensin family Not found Aptenodytes patagonicus (King penguin) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antifungal activity and antibacterial activity against Gram-positive and Gram-negative bacteria. Involved in the process of food preservation in the stomach during the incubation fast. May also be present during infection. PTM: Contains three disulfide bond: 5-33; 12-27; 17-34. Tissue specificity: Secreted into the stomach cavity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys5 and Cys33; Cys12 and Cys27; Cys17 and Cys34. L No cytotoxicity information found Not found 14525994 J Biol Chem. 2003 Dec 19;278(51):51053-8. Thouzeau C, Le Maho Y, Froget G, Sabatier L, Le Bohec C, Hoffmann JA, Bulet P. Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus. DRAMP03188 RLGGILRKAGEKIGGGLKKIGQKIKDFFGKLAPRTES 37 Antibacterial protein LL-37 (primates, mammals, animals) Q1KLX0 Belongs to the cathelicidin family CAMP Saguinus oedipus (Cotton-top tamarin) Antimicrobial, Antibacterial, Anti-Gram- Homology Bridge Not found Function: Has antibacterial activity (By similarity). Gram-negative bacteria: Escherichia coli ML-35, Pseudomonas aeruginosa ATCC 27853, Staphylococcus aureus 710A, Enterococcus faecalis A16.##Yeast: Candida albicans clinical isolate. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP03189 VARLGGILRKAGEKIGGGLKKIGQKIKDFFGKLAPRTES 39 Antibacterial protein LL-39 (primates, mammals, animals) Q1KLX0 Belongs to the cathelicidin family CAMP Saguinus oedipus (Cotton-top tamarin) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP18221 TVYTQA 6 Fusaricidin D (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus polymyxa KT-8 Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found The carboxylic end of Ala6 forms an ester bond with the hydroxyl group of T1. Val2, Gln5, Ala6 are D-amino acids and Thr4 is a D-allo-Thr. In addition, the N-terminus NH is lipidated with 15-guanidino-3-hydroxypentadecanoic acid (GHPD). Fusaricidin A was elucidated to be a cyclic depsipeptide containing a unique fatty acid, 15-guanidino-3-hydroxypentadecanoic acid. Fusaricidins B, C, and D are minor components from the culture broth of a bacterial strain Bacillus polymyxa KT-8. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9127193##23185515 J Antibiot (Tokyo). 1997 Mar;50(3):220-8.##PLoS One. 2012;7(11):e50003. Kajimura Y, Kaneda M.##Yu WB, Yin CY, Zhou Y, Ye BC. Fusaricidins B, C and D, new depsipeptide antibiotics produced by Bacillus polymyxa KT-8: isolation, structure elucidation and biological activity.##Prediction of the mechanism of action of fusaricidin on Bacillus subtilis. DRAMP03192 RLGGFLQKAREKIARGFKKIGQKINDFLGKLAPRTEA 37 Antibacterial protein LL-37 (cathelicidin; primates, mammals, animals) Q1KLY5 Belongs to the cathelicidin family CAMP Cebus capucinus (white-faced-sapajou) Antimicrobial, Antibacterial Homology Not found Not found Function: Has antibacterial activity. (By similarity) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16720578 J Biol Chem. 2006 Jul 21;281(29):19861-19871. Zelezetsky I, Pontillo A, Puzzi L, Antcheva N, Segat L, Pacor S, Crovella S, Tossi A. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. DRAMP03194 RCVCTRGFC 9 Theta defensin subunit A (primates, mammals, animals) P86722 Belongs to the alpha-defensin family (Theta subfamily) Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Forms a cyclic peptide with subunit A (PhTD-3) or with subunit B (PhTD-1). An additional intersubunit disulfide bond is formed. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20155756 Rapid Commun Mass Spectrom. 2010 Mar 15;24(5):599-604. Stegemann C, Tsvetkova EV, Aleshina GM, Lehrer RI, Kokryakov VN, Hoffmann R. De novo sequencing of two new cyclic theta-defensins from baboon (Papio hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass spectrometry. DRAMP03195 RCVCRRGVC 9 Theta defensin subunit B (primates, mammals, animals) P86723 Belongs to the alpha-defensin family (Theta subfamily) Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Forms a cyclic peptide with subunit A (PhTD-1). An additional intersubunit disulfide bond is formed. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20155756 Rapid Commun Mass Spectrom. 2010 Mar 15;24(5):599-604. Stegemann C, Tsvetkova EV, Aleshina GM, Lehrer RI, Kokryakov VN, Hoffmann R. De novo sequencing of two new cyclic theta-defensins from baboon (Papio hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass spectrometry. DRAMP03199 RRICRCRIGRCLGLEVYFGVCFLHGRLARRCCR 33 PhD1 (PhD-1; Defensin-1; primates, mammals, animals) P84757 Not found Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Listeria monocytogenes, Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16978151 Biochemistry (Mosc). 2006 Aug;71(8):879-883. Tsvetkova EV, Aleshina GM, Shamova OV, Leonova LE, Lehrer RI, Kokryakov VN. alpha-Defensins from blood leukocytes of the monkey Papio hamadryas. DRAMP03200 RICRCRIGRCLGLEVYFGVCFLHGRLARRCCR 32 PhD2 (PhD-2; Defensin-2; primates, mammals, animals) P84757 Belongs to the alpha-defensin family Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Listeria monocytogenes, Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16978151 Biochemistry (Mosc). 2006 Aug;71(8):879-83. Tsvetkova EV, Aleshina GM, Shamova OV, Leonova LE, Lehrer RI, Kokryakov VN. alpha-Defensins from blood leukocytes of the monkey Papio hamadryas. DRAMP03201 RTCRCRLGRCSRRESYSGSCNINGRIYSLCCR 32 PhD3 (PhD-3; Defensin-3; primates, mammals, animals) P84758 Belongs to the alpha-defensin family Not found Papio hamadryas (Hamadryas baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Listeria monocytogenes, Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16978151 Biochemistry (Mosc). 2006 Aug;71(8):879-883. Tsvetkova EV, Aleshina GM, Shamova OV, Leonova LE, Lehrer RI, Kokryakov VN. alpha-Defensins from blood leukocytes of the monkey Papio hamadryas. DRAMP03202 VKGGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGARKCCYLHCGFKCVIPVKKLEEGGNKDEDVSGPCPEPGWEAKSPGSSSTGCPQK 88 WAP four-disulfide core domain protein 12 (primates, mammals, animals) A4K2M6 Not found WFDC12 Papio anubis (Olive baboon) Antimicrobial, Antibacterial Homology Not found Not found "Function: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). Doamin: Contains 1 WAP domain" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17267810 Genome Res. 2007 Mar;17(3):276-286. Hurle B, Swanson W; NISC Comparative Sequencing Program, Green ED. Comparative sequence analyses reveal rapid and divergent evolutionary changes of the WFDC locus in the primate lineage. DRAMP18220 TVYTNA 6 Fusaricidin C (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus polymyxa KT-8 Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found The carboxylic end of Ala6 forms an ester bond with the hydroxyl group of T1. Val2, Asn5, Ala6 are D-amino acids and Thr4 is a D-allo-Thr. In addition, the N-terminus NH is lipidated with 15-guanidino-3-hydroxypentadecanoic acid (GHPD). Fusaricidin A was elucidated to be a cyclic depsipeptide containing a unique fatty acid, 15-guanidino-3-hydroxypentadecanoic acid. Fusaricidins B, C, and D are minor components from the culture broth of a bacterial strain Bacillus polymyxa KT-8. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9127193##23185515 J Antibiot (Tokyo). 1997 Mar;50(3):220-8.##PLoS One. 2012;7(11):e50003. Kajimura Y, Kaneda M.##Yu WB, Yin CY, Zhou Y, Ye BC. Fusaricidins B, C and D, new depsipeptide antibiotics produced by Bacillus polymyxa KT-8: isolation, structure elucidation and biological activity.##Prediction of the mechanism of action of fusaricidin on Bacillus subtilis. DRAMP18219 TVVTQA 6 Fusaricidin B (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus polymyxa KT-8 Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found The carboxylic end of Ala6 forms an ester bond with the hydroxyl group of T1. Val2, Gln5, Ala6 are D-amino acids and Thr4 is a D-allo-Thr. In addition, the N-terminus NH is lipidated with 15-guanidino-3-hydroxypentadecanoic acid (GHPD). Fusaricidin A was elucidated to be a cyclic depsipeptide containing a unique fatty acid, 15-guanidino-3-hydroxypentadecanoic acid. Fusaricidins B, C, and D are minor components from the culture broth of a bacterial strain Bacillus polymyxa KT-8. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9127193##23185515 J Antibiot (Tokyo). 1997 Mar;50(3):220-8.##PLoS One. 2012;7(11):e50003. Kajimura Y, Kaneda M.##Yu WB, Yin CY, Zhou Y, Ye BC. Fusaricidins B, C and D, new depsipeptide antibiotics produced by Bacillus polymyxa KT-8: isolation, structure elucidation and biological activity.##Prediction of the mechanism of action of fusaricidin on Bacillus subtilis. DRAMP03206 RCICLLGIC 9 Theta defensin subunit C (BTD-c; BTD-4 subunit 2; primates, mammals, animals) B6ULW6, P86033 Belongs to the alpha-defensin family (Theta subfamily) BTDC Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Forms a cyclic peptide with subunit A (BTD-4). An additional intersubunit disulfide bond is formed. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP03207 RCFCRRGVC 9 Theta defensin subunit D (BTD-d; BTD-7 subunit 2; primates, mammals, animals) B6ULW7, P86034 Belongs to the alpha-defensin family (Theta subfamily) BTDD Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Forms a cyclic peptide with subunit A (BTD-7). An additional intersubunit disulfide bond is formed. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP03208 RCVCTRGFCRCVCRRGVC 18 BTD-1 (theta-defensin; primates, mammals, animals) B6ULW4, P86031, B6ULW5, P86032 Not found Not found Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: BTD-1 has antimicrobial activity against the Gram-negative bacterium E. coli ML35 and the Gram-positive bacterium S. aureus 502a, and the fungus C. albicans 16820. Gram-positive bacterium: Staphylococcus aureus 502a;##Gram-negative bacterium: Escherichia coli ML35.##Fungi: Candida albicans 16820. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP03209 RCVCRRGVCRCVCRRGVC 18 BTD-2 (theta-defensin; primates, mammals, animals) B6ULW5, P86032 Not found Not found Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: BTD-2 has antimicrobial activity against the Gram-negative bacterium E. coli ML35 and the Gram-positive bacterium S. aureus 502a, and the fungus C. albicans 16820. Among the five BTDs detected, the most potent peptide is BTD-2. BTD-2 is more effective against E. coli than BTD-1. Gram-positive bacterium: Staphylococcus aureus 502a;##Gram-negative bacterium: Escherichia coli ML35.##Fungi: Candida albicans 16820. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP18218 TVVTNA 6 Fusaricidin A (Bacteriocin) No entry found Belongs to the lipopeptides family Not found Bacillus polymyxa KT-8 Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Not found The carboxylic end of Ala6 forms an ester bond with the hydroxyl group of T1. Val2, Asn5, Ala6 are D-amino acids and Thr4 is a D-allo-Thr. In addition, the N-terminus NH is lipidated with 15-guanidino-3-hydroxypentadecanoic acid (GHPD). Fusaricidin A was elucidated to be a cyclic depsipeptide containing a unique fatty acid, 15-guanidino-3-hydroxypentadecanoic acid. Fusaricidins B, C, and D are minor components from the culture broth of a bacterial strain Bacillus polymyxa KT-8. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8621351##23185515 J Antibiot (Tokyo). 1996 Feb;49(2):129-35.##PLoS One. 2012;7(11):e50003. Kajimura Y, Kaneda M.##Yu WB, Yin CY, Zhou Y, Ye BC. Fusaricidin A, a new depsipeptide antibiotic produced by Bacillus polymyxa KT-8. Taxonomy, fermentation, isolation, structure elucidation and biological activity.##Prediction of the mechanism of action of fusaricidin on Bacillus subtilis. DRAMP03211 RCVCTRGFCRCICLLGIC 18 BTD-4 (theta-defensin; primates, mammals, animals) B6ULW4, B6ULW6 Not found Not found Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: BTD-4 has antimicrobial activity against the Gram-negative bacterium E. coli ML35 and the Gram-positive bacterium S. aureus 502a, and the fungus C. albicans 16820. Among the five BTD detected, BTD-4 is least positively charged (net charge +2). This may be responsible for its weaker antimicrobial activity observed in vitro. It disrupts E. coli membranes. Gram-positive bacterium: Staphylococcus aureus 502a;##Gram-negative bacterium: Escherichia coli ML35.##Fungi: Candida albicans 16820. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP03212 RCVCTRGFCRCFCRRGVC 18 BTD-7 (theta-defensin; primates, mammals, animals) B6ULW4, B6ULW7 Not found Not found Papio anubis (Olive baboon) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: BTD-7 has antimicrobial activity against the Gram-negative bacterium E. coli ML35 and the Gram-positive bacterium S. aureus 502a, and the fungus C. albicans 16820. Gram-positive bacterium: Staphylococcus aureus 502a;##Gram-negative bacterium: Escherichia coli ML35.##Fungi: Candida albicans 16820. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 18852242 Infect Immun. 2008 Dec;76(12):5883-5891. Garcia AE, Osapay G, Tran PA, Yuan J, Selsted ME. Isolation, synthesis, and antimicrobial activities of naturally occurring theta-defensin isoforms from baboon leukocytes. DRAMP18217 WEEYNIIXQLGNKGQ 15 Licheniocin 50.2(Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Bacillus licheniformis VPS50.2 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Fuction: The bacteriocin activity was insensitive to lysozyme and proteinase K, heat stable after incubation at 100 Celsius degree for 30 min and over wide range of pH (2 Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2423832 Laryngol Rhinol Otol (Stuttg). Maier H, Adler D. Treatment of chronic recurring parotitis with the protease inhibitor aprotinin (trasylol). DRAMP18216 GWGDVLCVAGTIGGAGTGGLGGAAAGSAVPVIGTGIGGAIGGVSGGLTGAATFC 54 Cerein 7A(Bacteriocin) No entry found Belongs to the class IId bacteriocin Not found Bacillus cereus Bc7 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found When the purified cerein 7A and 7B were combined at a 1 : 1 ratio, no synergistic activity was observed between the two bacteriocins. Gram-positive (wide range) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 16451187##10971770 FEMS Microbiol Lett.##J Appl Microbiol. Osc Purification and sequencing of cerein 7B, a novel bacteriocin produced by Bacillus cereus Bc7.##Characterization and mechanism of action of cerein 7, a bacteriocin produced by Bacillus cereus Bc7. DRAMP03218 GKFSVFGKILRSIAKVFKGVGKVRKQFKTASDLDKNQ 37 M-oxotoxin-Ot2a (Oxyopinin-2a, Oxki2a; spiders, Arthropods, animals) P83248 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) Antimicrobial, Antibacterial, Insecticidal Protein level Alpha helix Not found Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides. No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. DRAMP03219 GKFSGFAKILKSIAKFFKGVGKVRKQFKEASDLDKNQ 37 M-oxotoxin-OtIIb (Oxyopinin-IIb, OxkiIIb; spiders, Arthropods, animals) P83249 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) Antimicrobial, Antibacterial, Insecticidal Protein level Not found Not found Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides. No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. DRAMP03220 GKLSGISKVLRAIAKFFKGVGKARKQFKEASDLDKNQ 37 M-oxotoxin-Ot2c (Oxyopinin-2c, Oxki2c; spiders, Arthropods, animals) P83250 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) Antimicrobial, Antibacterial, Insecticidal Protein level Alpha helix Not found Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides. No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. DRAMP03221 GKFSVFSKILRSIAKVFKGVGKVRKQFKTASDLDKNQ 37 M-oxotoxin-Ot2d (Oxyopinin-2d, Oxki2d; spiders, Arthropods, animals) P83251 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) Antimicrobial, Antibacterial, Insecticidal Protein level Not found Not found Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides. No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. DRAMP03223 GFGSLFKFLAKKVAKTVAKQAAKQGAKYIANKQME 35 M-ctenitoxin-Cs1b (M-CNTX-Cs1b; Cupiennin-1b; spiders, Arthropods, animals) P83620 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) Antimicrobial, Antibacterial, Insecticidal Protein level Not found Not found Function: Has antimicrobial activity. Has insecticidal activity. Probably acts by disturbing membrane Function: with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. LD50 is 5.9 pmol/mg on Drosophila. No MICs found in DRAMP database [Ref.11792701]Not determined Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11792701 J Biol Chem. 2002 Mar 29;277(13):11208-11216. Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). DRAMP03224 GFGSLFKFLAKKVAKTVAKQAAKQGAKYIANKQTE 35 M-ctenitoxin-Cs1c (M-CNTX-Cs1c; Cupiennin-1c; spiders, Arthropods, animals) P83621 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has antimicrobial activity. Probably acts by disturbing membrane Function: with its amphipathic structure. Gram-negative bacteria: Escherichia coli ATCC 25922, Pseudomonas aeruginosa ATCC 27853;##Gram-positive bacteria: Staphylococcus aureus ATCC 29213, Enterococcus faecalis ATCC 29212. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11792701 J Biol Chem. 2002 Mar 29;277(13):11208-11216. Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). DRAMP03228 GLFGKLIKKFGRKAISYAVKKARGKN 26 M-zodatoxin-Lt2b (M-ZDTX-Lt2b; Latarcin-2b, Ltc-2b; spiders, Arthropods, animals) Q1ELU0 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against both Gram-positive and Gram-negative bacteria, and the yeasts. Also has a strong hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (Musca domestica) larvae. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database [Swiss_Prot Entry Q1ELU0]has a strong hemolytic activity against rabbit erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-209892. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03234 QAFQTFKPDWNKIRYDAMKMQTSLGQMKKRFNL 33 M-zodatoxin-Lt6a (M-ZDTX-Lt6a; Latarcin 6a, Ltc-6a; spiders, Arthropods, animals) Q1ELU8 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Not found Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-20992. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP03235 QAFKTFTPDWNKIRNDAKRMQDNLEQMKKRFNLNL 35 M-zodatoxin-Lt6b (M-ZDTX-Lt6b; Latarcin 6b, Ltc-6b; spiders, Arthropods, animals) Q1ELU8 Belongs to the latarcin family Not found Lachesana tarabaevi (Spider) Antibacterial, Antimicrobial, Antifungal, Antiviral Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16735513 J Biol Chem. 2006 Jul 28;281(30):20983-20992. Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. DRAMP18215 TTPLCVGVIIGITASIKICK 20 Cerecidin A7(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus cereus Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Fuction: Active against Gram-positive bacteria B. cereus As 1.348, B. cereus As 1.352, B. thuringiensis 1.1013, B. thuringiensis 1.1014, B. subtilis 1.107, B. subtilis DB104, B. pumilus 1.1165, E. faecalis 1.14, E. faecalis V583, E. durans 1.2023, E. pernyi 1.1010, L. coprophilus 1.214, L. acidophilus 100-33, L. casei 1.575, L. rhamnosus 1.104, L. plantarum 1.551, L. brevis 1.2028, L. brevis 1.7, L. buchneri 1.40, L. lactis LM0230, L. lactis MG1363, L. curvatus LTH1.174, L. dextranicum 181 (zone inhibition 7-11 mm), M. flavus NCIB8166 (zone inhibition 18 mm), S. aureus 1-1, S. bovis LG42, S. gordonii 1.2496, S. salivarius 1.2498, S. thermophilus 1.1864 (Zone inhibition 7-11 mm), including resistant superbugs (MRSA and VRE). Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24532070 Appl Environ Microbiol. 2014 Apr;80(8):2633-43. Wang J, Zhang L, Teng K, Sun S, Sun Z, Zhong J. Cerecidins, novel lantibiotics from Bacillus cereus with potent antimicrobial activity. DRAMP03238 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKYYGKKALQKASEKL 69 M-zodatoxin-Lt8c (M-ZDTX-Lt8c; Cytoinsectotoxin-1c, CIT-1c; spiders, Arthropods, animals) P85255, B3W6I1 Belongs to the cytoinsectotoxin family cit 1-3 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal Protein level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis(By similarity). Tissue specificity: Expressed by the venom gland." Gram-positive bacteria: Micrococcus luteus VKM Ac-2230, Staphylococcus aureus 209P, Arthrobacter globiformis VKM Ac-1112, Bacillus subtilis VKM B-501;##Gram-negative bacteria: Escherichia coli C600, E. coli DH5α, E. coli MH1, Pseudomonas aeruginosa PAO1, Pseudomonas fluorescens VKM B-894, Serratia marcescens VKM B-1248. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03239 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGITKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 M-zodatoxin-Lt8d (M-ZDTX-Lt8d; Cytoinsectotoxin-1d, CIT-1d; spiders, Arthropods, animals) P85256, B3W6I2 Belongs to the cytoinsectotoxin family cit 1-4 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Protein level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03240 GFFGNTWKKIKGKSDKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 M-zodatoxin-Lt8e (M-ZDTX-Lt8e; Cytoinsectotoxin-1e, CIT-1e; spiders, Arthropods, animals) P85256, B3W6I3 Belongs to the cytoinsectotoxin family cit 1-5 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Protein level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03241 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKALQKASEKL 69 M-zodatoxin-Lt8f (M-ZDTX-Lt8f; Cytoinsectotoxin-1f, CIT-1f; spiders, Arthropods, animals) P85258, B3W6I4 Belongs to the cytoinsectotoxin family cit 1-7 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal Protein level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S. carnaria. Has antibacterial activity against the Gram-negative bacteria E.coli. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03242 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKALQKASEKL 69 M-zodatoxin-Lt8g (M-ZDTX-Lt8g; Cytoinsectotoxin-1g, CIT-1g; spiders, Arthropods, animals) P85259, B3W6I5 Belongs to the cytoinsectotoxin family cit 1-8 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal Protein level Not found Not found "Function: Has insecticidal activity against the flesh fly S. carnaria. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03243 GFFGNAWKKIKGKAEKFFRKKAAKIIAKKEGITKEEAEAKVDTMSKKQIKVYLLKHYGKKALQKASEKL 69 M-zodatoxin-Lt8h (M-ZDTX-Lt8h; Cytoinsectotoxin-1h, CIT-1h; spiders, Arthropods, animals) P85247, B3W6I6 Belongs to the cytoinsectotoxin family cit 1-11 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal Protein level Not found Not found "Function: Has insecticidal activity against the flesh fly S. carnaria. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03244 GFFGNTWKKIKGKTDKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKALQKASEKL 69 M-zodatoxin-Lt8j (M-ZDTX-Lt8j; Cytoinsectotoxin 1-9; spiders, Arthropods, animals) P0CAZ3 Belongs to the cytoinsectotoxin family cit 1-9 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski AA, Kozlov SA, Samsonova OV, Egorova NS, Karpunin DV, Pluzhnikov KA, Feofanov AV, Grishin EV. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03245 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKALQKVSEKL 69 M-zodatoxin-Lt8k (M-ZDTX-Lt8k; Cytoinsectotoxin 1-10; spiders, Arthropods, animals) P0CAZ4 Belongs to the cytoinsectotoxin family cit 1-10 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03246 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGIFKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 M-zodatoxin-Lt8i (M-ZDTX-Lt8i; Cytoinsectotoxin 1-6; spiders, Arthropods, animals) P0CAZ2 Belongs to the cytoinsectotoxin family cit 1-6 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski AA, Kozlov SA, Samsonova OV, Egorova NS, Karpunin DV, Pluzhnikov KA, Feofanov AV, Grishin EV. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03247 GFFGNAWKKIKGKAEKFFRKKAAKIIAKKEGITKEEAEAKVDPMSKKQIKVYLLKHYGKKALQKASEKL 69 M-zodatoxin-Lt8l (M-ZDTX-Lt8l; Cytoinsectotoxin 1-12; spiders, Arthropods, animals) P0CAZ5 Belongs to the cytoinsectotoxin family cit 1-12 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03248 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKLFKKRPKNCDQ 71 M-zodatoxin-Lt8m (M-ZDTX-Lt8m; Cytoinsectotoxin 1-13; spiders, Arthropods, animals) P0CAZ6 Belongs to the cytoinsectotoxin family cit 1-13 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03249 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKLFKKRPKNCDQ 71 M-zodatoxin-Lt8o (M-ZDTX-Lt8o; Cytoinsectotoxin 1-14; spiders, Arthropods, animals) P0CAZ7 Belongs to the cytoinsectotoxin family cit 1-14 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03250 GFFGNTWKKIKGKADKIMLKKAVKLMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKSSSKSVRKIVISKSF 75 M-zodatoxin-Lt8p (M-ZDTX-Lt8p; Cytoinsectotoxin 1-15; spiders, Arthropods, animals) P0CAZ8 Belongs to the cytoinsectotoxin family cit 1-15 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03251 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKSSSKSFRKIVISKSF 75 M-zodatoxin-Lt8q (M-ZDTX-Lt8q; Cytoinsectotoxin 1-16; spiders, Arthropods, animals) P0CAZ9 Belongs to the cytoinsectotoxin family cit 1-16 Lachesana tarabaevi (Spider) Antimicrobial, Antibacterial, Insecticidal Transcript level Not found Not found "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V. Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom. DRAMP03252 KIKWFKTMKSLAKFLAKEQMKKHLGE 26 M-lycotoxin-Ls2a (M-LCTX-Ls2a; Lycocitin-3; spiders, Arthropods, animals) P0C2U8 Not found Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane. Potently inhibits the growth of bacteria and yeast. May Function: both in the prey capture strategy as well as protection from infectious organisms arising from prey ingestion. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 14991689 J Mass Spectrom. 2004 Feb;39(2):193-201. Budnik BA, Olsen JV, Egorov TA, Anisimova VE, Galkina TG, Musolyamov AK, Grishin EV, Zubarev RA. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. DRAMP03255 MIASHLAFEKLSKLGSKHTML 21 M-lycotoxin-Ls4a (M-LCTX-Ls4a; Peptide 2340; spiders, Arthropods, animals) P0C2V0 Not found Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May inhibit growth of bacteria. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14991689 J Mass Spectrom. 2004 Feb;39(2):193-201. Budnik B.A, Olsen J.V, Egorov T.A, Anisimova V.E, Galkina T.G, Musolyamov A.K, Grishin E.V, Zubarev R.A. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. DRAMP03256 AGIGKIGDFIKKAIAKYKN 19 U1-lycotoxin-Ls1a (U1-LCTX-Ls1a; Peptide 2034; spiders, Arthropods, animals) P0C2U9 Not found Not found Lycosa singoriensis (Wolf spider) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May inhibit growth of bacteria. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14991689 J Mass Spectrom. 2004 Feb;39(2):193-201. Budnik B.A, Olsen J.V, Egorov T.A, Anisimova V.E, Galkina T.G, Musolyamov A.K, Grishin E.V, Zubarev R.A. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. DRAMP03257 QPFSLERW 8 Oligoventin (spiders, Arthropods, animals) B3EWR9 Not found Not found Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has antibacterial activity against Gram-positive bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2012) to UniProtKB Ferreira I.L.C, Sayegh R.S.R, Batista I.F.C, Silva P.I. Jr. Isolation and characterization a novel ultrashort antibacterial peptide from the eggs of the spider Phoneutria nigriventer (Ctenidae). DRAMP03258 IIIQYEGHKH 10 Rondonin (spiders, Arthropods, animals) B3EWP8 Not found Not found Acanthoscurria rondoniae (Spider) Antimicrobial, Antifungal Protein level Not found Not found Function: Exhibits antifungal activity against Candida sp. No hemolytic activity No MICs found in DRAMP database [Swiss_Prot Entry B3EWP8]Non-hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Results Immunol. 2012;2:66-71. Riciluca K.C.T, Sayegh R.S.R, Melo R.L, Silva P.I. Jr. Rondonin an antifungal peptide from spider (Acanthoscurria rondoniae) haemolymph. DRAMP03259 RTCMIKKEGWGKCLIDTTCAHSCKNRGYIGGDCKGMTRTCYCLVNC 46 VrCRP (Cyst-rich; Plant defensin) No entry found Not found Not found V. radiata (a bruchid-resistant mungbean) Insecticidal Not found Not found Not found Function: VrCRP exhibits insecticidal activity in vitro against C. chinensis. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12452641 J Agric Food Chem. 2002 Dec 4;50(25):7258-7263. Chen KC, Lin CY, Kuan CC, Sung HY, Chen CS. A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid. DRAMP03260 EKYCPTPRNTSCKKMNIRNNCCRDSDCTSNAFCCAEPCGNFCHKASDKPGGRRVDPNASCQTGYVYW 67 U14-lycotoxin-Ls1a (Toxin-like structure LSTX-N1; spiders, Arthropods, animals) B6DD34 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03262 EKYCPTPRNTSCKKMNIRNNCCRDSDCTSNAFCCAEPCGNFCHKASDKPGGRRVDPNASCKTGYVYW 67 U14-lycotoxin-Ls1b (Toxin-like structure LSTX-N3; spiders, Arthropods, animals) B6DD36 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP18214 TTPLCVGVIIGLTTSIKICK 20 Cerecidin A1(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Bacillus cereus Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Fuction: Active against multiple Gram-positive strains, B. cereus As 1.348, B. cereus As 1.352, B. thuringiensis 1.1013, B. thuringiensis 1.1014, B. subtilis 1.107, B. subtilis DB104, B. pumilus 1.1165, E. faecalis 1.14, E. faecalis V583, E. durans 1.2023, E. pernyi 1.1010, L. coprophilus 1.214, L. acidophilus 100-33, L. casei 1.575, L. rhamnosus 1.104, L. plantarum 1.551, L. brevis 1.2028, L. brevis 1.7, L. buchneri 1.40, L. lactis LM0230, L. lactis MG1363, L. curvatus LTH1.174, L. dextranicum 181 (zone inhibition 6-10 mm, M. flavus NCIB8166 (zone inhibition 15 mm), S. bovis LG42, S. gordonii 1.2496, S. salivarius 1.2498, and S. thermophilus 1.1864 (Zone inhibition 7-9 mm), including resistant superbugs (MRSA and VRE). Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24532070 Appl Environ Microbiol. 2014 Apr;80(8):2633-43. Wang J, Zhang L, Teng K, Sun S, Sun Z, Zhong J. Cerecidins, novel lantibiotics from Bacillus cereus with potent antimicrobial activity. DRAMP03265 EKYCPTPRNTSCKKMNIKNNCCRDSDCTSNAFCCAEPCGNFCHKASDKPGGRRVDPNASCQTGYVYW 67 U14-lycotoxin-Ls1c (Toxin-like structure LSTX-N6; spiders, Arthropods, animals) B6DD39 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03266 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPTDRPGGKRAAGGKSCKTGYVYY 67 U15-lycotoxin-Ls1f (Toxin-like structure LSTX-N7; spiders, Arthropods, animals) B6DD40 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03267 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPTDRPGGKRAAGGKSCKTGYVY 66 U15-lycotoxin-Ls1d (Toxin-like structure LSTX-N8; spiders, Arthropods, animals) B6DD41 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP18213 VKLFPVKLFP 10 Gramicidin S(Bacteriocin) No entry found Not found Not found Bacillus brevis Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Beta sheet The second and seventh residues of this cyclic peptide are Ornithines, an analog of lysine (one CH2 shorter). They are represented here with lysines. In addition, residue F is a D-amino acid. Function: This is the first cyclic peptide antibiotic used clinically. For gram-negative bacteria, however, activity was strongly dependent on whether the assay was carried out in solution or in agar. It was found that GS was active against gram-negative microorganisms in the solution-based assay, but inactive against these using an agar-based assay. GS was also found to have antifungal activity when measured using a liquid-broth assay. Gram-positive, Gram-negative (broad-spectrum) It exhibits hemolytic activity at 25 μM and 45 μM against human red cells and sheep red cells. Cyclic No specific N-terminal No specific C-terminal The 'O' in sequence is Ornithine Mixed(D-Phe) No cytotoxicity information found Cell membrane 8836773##24388950 Int J Pept Protein Res. 1996 Jun;47(6):460-6.##Biochim Biophys Acta. 2014 May;1838(5):1420-9. Kondejewski LH, Farmer SW, Wishart DS, Hancock RE, Hodges RS.##Abraham T, Prenner EJ, Lewis RN, Mant CT, Keller S, Hodges RS, McElhaney RN. Gramicidin S is active against both gram-positive and gram-negative bacteria.##Structure-activity relationships of the antimicrobial peptide gramicidin S and its analogs: aqueous solubility, self-association, conformation, antimicrobial activity and interaction with model lipid membranes. DRAMP03269 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPTDRPGGKRAAGGKSCKTSYVY 66 U15-lycotoxin-Ls1a (Toxin-like structure LSTX-N10; spiders, Arthropods, animals) B6DD43 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03270 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWYCATPCGNFCKYPTDRPGGKRAAGGKSCKTGYVY 66 U15-lycotoxin-Ls1b (Toxin-like structure LSTX-N11; spiders, Arthropods, animals) B6DD44 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03271 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNICKYPTDRPGGKRAAGGKSCKTGYVY 66 U15-lycotoxin-Ls1c (Toxin-like structure LSTX-N12; spiders, Arthropods, animals) B6DD45 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP18211 TSQTWGSPVP 10 Anacyclamide A10(Bacteriocin) No entry found Belongs to the class I bacteriocin Not found Anabaena sp. 90 Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available APPLIED AND ENVIRONMENTAL MICROBIOLOGY. 2010 Feb;76(3):701-709. Leikoski N,Fewer DP,Jokela J,Wahlsten M,Rouhiainen L,Sivonen K. Highly Diverse Cyanobactins in Strains of the Genus Anabaena. DRAMP18212 LASTLGISTAAAKKAIDIIDAASTIASIISLIGIVTGAGAISYAIVATAKTMIKKYGKKYAAAW 64 Amylocyclicin(Bacteriocin) No entry found Belongs to the class IIc bacteriocin acnA Bacillus amyloliquefaciens FZB42 Antimicrobial, Antibacterial, Anti-Gram+ Not found Most similar to circular Uberolysin (45.9%). Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 24610713 J Bacteriol. 2014 May;196(10):1842-52. Scholz R, Vater J, Budiharjo A, Wang Z, He Y, Dietel K, Schwecke T, Herfort S, Lasch P, Borriss R. Amylocyclicin, a Novel Circular Bacteriocin Produced by Bacillus amyloliquefaciens FZB42. DRAMP03273 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPTDRPGGRRAAGGKSCKTGYVY 66 U15-lycotoxin-Ls1e (Toxin-like structure LSTX-N14; spiders, Arthropods, animals) B6DD47 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP18210 SCNCVCGVCCSC 12 Amythiamicin C/D(Bacteriocin) P0C912 Belongs to the class I bacteriocin Not found Amycolatopsis sp. (strain MI481-42F4 / FERM P-12739) Antimicrobial, Antibacterial, Anti-Gram+, Antiparasitic Not found The main frame from C-1 to C-41 of these antibiotics was the same as that of amythiamicin D. Amino acid autoanalyses of amythiamicins A, B and C showed that these have another one mole of serine and proline in comparison with amythiamicin D. Stereochemistries of both amino acids were determined to be L by chiral HPLC. These seryl-prolyl residues in amythiamicins A, B and C are attached at C-41 through an oxazoline ring, amide and ester Sequence uncertainty (position 4): C or T. Function: Has bacteriocidal activity against Gram-positive bacteria: including multi-drug resistant strains such as Staphylococcus aureus MS9610 and Methicillin-resistant S.aureus, but is not active against most Gram-negative bacteria and fungi. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Elongation Factor Tu (EF-Tu) 8040071##7961166##16262432 J Antibiot (Tokyo). 1994 Jun;47(6):668-74.##J Antibiot (Tokyo). 1994 Oct;47(10):1153-9.##J Am Chem Soc. 2005 Nov 9;127(44):15644-51. Shimanaka K, Kinoshita N, Iinuma H, Hamada M, Takeuchi T.##Shimanaka K, Takahashi Y, Iinuma H, Naganawa H, Takeuchi T.##Hughes RA, Thompson SP, Alcaraz L, Moody CJ. Novel antibiotics, amythiamicins. I. Taxonomy, fermentation, isolation, physico-chemical properties, and antimicrobial activity.##Novel antibiotics, amythiamicins. III. Structure elucidations of amythiamicins A, B and C.##Total synthesis of the thiopeptide antibiotic amythiamicin D. DRAMP03276 DQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPADRPGGKRAAGGKSCKTGYVY 66 U15-lycotoxin-Ls1g (Toxin-like structure LSTX-N17; spiders, Arthropods, animals) B6DD50 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03277 DQYCPKSSITACKKMNTRNDCCKDDDCTGGSWCCATPCGNFCKYPTDRPGGKRAAGGKSCKTGYVYY 67 U15-lycotoxin-Ls1h (Toxin-like structure LSTX-N18; spiders, Arthropods, animals) B6DD51 "Spider wap-1 family (Contains 1 WAP domain)" Not found Lycosa singoriensis (Wolf spider) (Aranea singoriensis) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19875276 Zoology (Jena). 2010 Jan;113(1):10-18. hang Y, Chen J, Tang X, Wang F, Jiang L, Xiong X, Wang M, Rong M, Liu Z, Liang S. Transcriptome analysis of the venom glands of the Chinese wolf spider Lycosa singoriensis. DRAMP03281 LSCKRGTCHFGRCPSHLIKGSCSGG 25 Turkey Heterophil Peptide 3 (Antimicrobial peptide THP3; Birds, animals) P80393 Belongs to the beta-defensin family Not found Meleagris gallopavo (Common turkey) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7964174 J Leukoc Biol. 1994 Nov;56(5):661-665. Evans EW, Beach GG, Wunderlich J, Harmon BG. Isolation of antimicrobial peptides from avian heterophils. DRAMP03282 GKREKCLRRNGFCAFLKCPTLSVISGTCSRFQVCC 35 Turkey Heterophil Peptide 1 (Antimicrobial peptide THP1; Birds, animals) P80391 Belongs to the beta-defensin family Not found Meleagris gallopavo (Common turkey) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found PTM: Contains two disulfide bonds Gram-negative bacterium: Escherichia coli ATCC 25922;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7964174 J Leukoc Biol. 1994 Nov;56(5):661-665. Evans EW, Beach GG, Wunderlich J, Harmon BG. Isolation of antimicrobial peptides from avian heterophils. DRAMP03283 LFCKRGTCHFGRCPSHLIKVGSCFGFRSCCKWPWDA 36 Turkey Heterophil Peptide 2 (Antimicrobial peptide THP2, THP2; Birds, animals) P80392 Belongs to the beta-defensin family Not found Meleagris gallopavo (Common turkey) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Tissue specificity: Expressed in circulating heterophil granulocytes and bone marrow (at protein level). PTM: Contains three disulfide bonds 3-29; 8-23; 13-30." Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7964174##19151352 J Leukoc Biol. 1994 Nov;56(5):661-665.##Poult Sci. 2009 Feb;88(2):372-379. Evans EW, Beach GG, Wunderlich J, Harmon BG.##Kannan L, Rath NC, Liyanage R, Lay JO Jr. Isolation of antimicrobial peptides from avian heterophils.##Direct screening identifies mature beta-defensin 2 in avian heterophils. DRAMP03284 LPRHTLHCVAYHGYCFHSKV 20 Beta-defensin (Birds, animals) P86385 Belongs to the beta-defensin family Not found Dromaius novaehollandiae (Emu) Antimicrobial, Antibacterial Protein level Not found Not found Function: Has bactericidal activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22044478 Gene. 2012 Jan 15;492(1):244-249. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. DRAMP03289 FFLLFLQGAAGNSVLCRIRGGRCHVGSCHFPERHIGRCSGFQACCIRTWG 50 Apl-AvBD16 (Beta defensins; Ducks, birds, animals) No entry found Not found Not found Anas platyrhynchos (Peking duck) Antimicrobial, Antibacterial, Antiviral Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23112840 PLoS One. 2012;7(10):e47743. Ma D, Zhang K, Zhang M, Xin S, Liu X, Han Z, Shao Y, Liu S. Ma D, Zhang K, Zhang M, Xin S, Liu X, Han Z, Shao Y, Liu S. DRAMP03290 MRILYLLFSVLFLVLQVSPGLSLPQRDMFLCRIGSCHFGRCPIHLVRVGSCFGFRSCCKSPWDV 64 Anas platyrhynchos avian beta-defensin 2 (Apl_AvBD2; Ducks, birds, animals) Q4VSK2 Belongs to the beta-defensin family BD2 Anas platyrhynchos (Domestic duck) Antimicrobial, Antibacterial Predicted Bridge Not found The widespread tissue distribution and the potent bactericidal and chemotactic activity make Apl_AvBD2 an important molecule in the innate immune response in ducks. It may play a vital role in the immune response of these birds against bacterial and viral pathogens. Micrococcus luteusNCIM 2871 (MBC=3.7 µM), Escherichia coli NCIM 2685, Riemerella anatipestifer (MBC=2.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19362739 Mol Immunol. 2009 Jun;46(10):2029-2038. Soman SS, Arathy DS, Sreekumar E. Discovery of Anas platyrhynchos avian beta-defensin 2 (Apl_AvBD2) with antibacterial and chemotactic functions DRAMP03291 DTLACRQSHGSCSFVACRAPSVDIGTCRGGKLKCCK 36 Beta defensin-6-like antimicrobial peptide (Ducks, birds, animals; Predicted) A3FPG7 Not found Not found Anas platyrhynchos (Domestic duck) (Anas boschas) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19996700 J Microbiol Biotechnol. 2009 Nov;19(11):1447-1455. Ma D, Liao W, Wang R, Han Z, Liu S. Two novel duck antibacterial peptides, avian beta-defensins 9 and 10, with antimicrobial activity. DRAMP03292 GMKEKCVTMGGYCRKQCRVQDALSGYCRNENPCCV 35 Defensin-B1 (DefB1; OaDefB1; mammals, animals) P0C8A5 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Expressed at low levels in kidney, lung, and spleen. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03293 GLNNKCAYFRGQCRRKCPQRDIFFGFCRNHDQCCLSSLHTRH 42 Defensin-B2 (DefB2; OaDefB2; mammals, animals) P0C8A6 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Lowly expressed in spleen, and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03294 GISRVRICREKGGHCDADCHLEERHLGGCRAAYLTFCC 38 Defensin-B3 (DefB3; OaDefB3; mammals, animals) P0C8A7 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Lowly expressed in spleen, and expressed at lower levels in kidney, lung and testis. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03295 CKGKLGYCRSKCQSKQVELGKCSTKAICCGISTGTSSSQGSHEVPVINSEPALESKPEPQDTQEEEATMVSE 72 Defensin-B4 (DefB4; OaDefB4; mammals, animals) P0C8A8 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in kidney, lowly expressed in spleen, and expressed at lower levels in lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03296 KKCRERGGQCHSGVCSWNEKFIGFCSFARPCC 32 Defensin-B5 (DefB5; OaDefB5; mammals, animals) P0C8A9 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in kidney, and expressed at lower levels in testis. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03297 KMEILLGSNGGARCDINKKSFDCYHRNGRCRFNCRKREYNNGDCSQYQSCCLPTRNL 57 Defensin-B6 (DefB6; OaDefB6; mammals, animals) P0C8B0 Belongs to the beta-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Lowly expressed in spleen, kidney and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03298 DTTFCRCRVSCNILEKYSGKCELSGRTARICC 32 Defensin-A1 (DefA1; OaDefA1; mammals, animals) P0C8A1 Belongs to the alpha-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in intestine, expressed at lower levels in spleen, and at very low levels in kidney and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03299 STITCYCRSRCRMLEKNSGTCRSSNCTYTLCC 32 Defensin-A2 (DefA2; OaDefA2; mammals, animals) P0C8A2 Belongs to the alpha-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in intestine, expressed at lower levels in spleen, and at very low levels in kidney and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03300 RIITCSCRTFCFLGERISGRCYQSVFIYRLCCRG 34 Defensin-A3 (DefA3; OaDefA3; mammals, animals) P0C8A3 Belongs to the alpha-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in spleen, and expressed at lower levels in intestin and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03301 HSCVCRRICAARQVRKGRCSRRRRICCLY 29 Defensin-A4 (DefA4; OaDefA4; mammals, animals) P0C8A4 Belongs to the alpha-defensin family Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found "Function: Has antimicrobial activity (By similarity). Tissue specificity: Lowly expressed in spleen, and expressed at lower levels in kidney and lung. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03302 EVRRRRRRPPCEDVNGQCQPRGNPCLRLRGACPRGSRCCMPTVAAH 46 Defensin-BvL (DefB-vL; OaDefB-vL; mammals, animals) P0C8B1 Not found Not found Ornithorhynchus anatinus (Duckbill platypus) Antimicrobial Transcript level Not found Not found 2MN3 resolved by NMR. "Function: Has antimicrobial activity (By similarity). Tissue specificity: Highly expressed in intestine, liver and spleen and expressed at lower levels in brain, kidney, lung, testis and venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18463304##18662710 Genome Res. 2008 Jun;18(6):986-994.##Toxicon. 2008 Sep 15;52(4):559-565. Whittington CM, Papenfuss AT, Bansal P, Torres AM, Wong ES, Deakin JE, Graves T, Alsop A, Schatzkamer K, Kremitzki C, Ponting CP, Temple-Smith P, Warren WC, Kuchel PW, Belov K.##Whittington CM, Papenfuss AT, Kuchel PW, Belov K. Defensins and the convergent evolution of platypus and reptile venom genes.##Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. DRAMP03303 DHHHDHGHDDHEHEELTLEKIKEKIKDYADKTPVDQLTERVQAGRDYLLGKGARPSHLPARVDRHLSKLTAAEKQELADYLLTFLH 86 Theromyzin (Frogs, amphibians, animals) Q6T6C1 Not found Not found Theromyzon tessulatum (Duck leech) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15102860 J Biol Chem. 2004 Jul 23;279(30):30973-30982. Tasiemski A, Vandenbulcke F, Mitta G, Lemoine J, Lefebvre C, Sautière PE, Salzet M. Molecular characterization of two novel antibacterial peptides inducible upon bacterial challenge in an annelid, the leech Theromyzon tessulatum. DRAMP03304 QIVDCWETWSRCTKWSQGGTGTLWKSCNDRCKELGRKRGQCEEKPSRCPLSKKAWTCICY 60 Hydramacin-1 (Hm-1; annelida, animals) B3RFR8 Belongs to the macin family Not found Hydra vulgaris (Hydra) (Hydra attenuata) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure The molecule possesses two short α-helices (residues 10-14 and 27-33) at the N terminus which are separated by a long flexible loop. The C-terminal region contains two β-strands (residues 38-42 and 56-60) in an antiparallel arrangement separated by a long flexible loop. 2K35 resolved by NMR. "Function: Hydramacin-1 is potently active against Gram-positive and Gram-negative bacteria including multi-resistant human pathogenic strains. Is not active against the Gram-positive Coccus species, Gram-negative non-fermentation species and against the fungus C.albicans. It leads to aggregation of bacteria as an initial step of its bactericidal mechanism. Aggregated cells are connected via electron-dense contacts and adopt a thorn apple-like morphology. Hydramycin contains a belt of positively charged residues that separate two hydrophobic areas. This structure may explain the observed aggregation of bacteria, since each of these areas can immerse into the outer leaflets of the membranes of two individual bacteria. Is able to permeabilize membranes of viable bacteria at low and neutral pH values, but no pore-forming activity is not detected. Tissue specificity: Expressed in the endodermal epithelium. Induction: By bacterial lipopolysaccharides (LPS). PTM: Contains four disulfide bonds." Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MBC=7.1 µM), Burkholderia cepacia ATCC 25416 (MBC>14.3 μM),Burkholderia cepacia ATCC 17759 (MBC>14.3 μM), B. cepacia LMG 16654 (MBC>14.3 μM), Citrobacter freundii NCTC 9750 (MBC=7.1 μM), C. freundii C7 (MBC=0.9 μM), Enterobacter cloacae Va11263/03 (MBC>14.3 μM), E. cloacae Va12270/03 (MBC=0.9 μM), Escherichia coli ATCC 25922 (MBC=0.9 μM), Klebsiella pneumoniae ATCC 13883 (MBC=0.9 μM), Klebsiella oxytoca ATCC 13182 (MBC=0.9 μM), Proteus mirabilis ATCC 21100 (MBC=14.3 μM), P. vulgaris ATCC 13315 (MBC>14.3 μM), Providencia rettgeri NCTC 7475 (MBC>14.3 μM), Pseudomonas aeruginosa NCTC 11446 (MBC>14.3 μM), Salmonella typhimurium 10003442 (MBC=0.9 μM), S. typhimurium 10003630 (MBC=0.9 μM), Serratia marcescens Mero060/148 (MBC>14.3 µM), S. marcescens Mero103/013 (MBC>14.3 μM), S. marcescens NCTC 10211 (MBC>14.3 μM), Yersinia enterocolitica NCTC 11176 (MBC=0.9 µM).##Multi-resistant Gram-negative bacteria: Escherichia coli Co 86 ESBL (MBC=3.6 μM), Klebsiella oxytoca ESBL 33 (MBC=7.1 µM), K. oxytoca ESBL 37 (MBC=3.6 μM), Klebsiella pneumoniae ATCC 700603 (MBC=3.6 μM).##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MBC>14.3 μM), Staphylococcus haemolyticus ATCC 29970 (MBC=1.8 μM), Streptococcus pyogenes ATCC 12344 (MBC>14.3 μM).##Multi-resistant Gram-positive bacteria: Staphylococcus aureus ATCC 33593 (MRSA) (MBC>14.3 μM), Enterococcus faecalis ATCC 51299 (MBC>14.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrane 19013190##19019828 Dev Comp Immunol. 2009 Apr;33(4):559-569.##J Biol Chem. 2009 Jan 16;284(3):1896-1905. Bosch TC, Augustin R, Anton-Erxleben F, Fraune S, Hemmrich G, Zill H, Rosenstiel P, Jacobs G, Schreiber S, Leippe M, Stanisak M, Grötzinger J, Jung S, Podschun R, Bartels J, Harder J, Schröder JM.##Jung S, Dingley AJ, Augustin R, Anton-Erxleben F, Stanisak M, Gelhaus C, Gutsmann T, Hammer MU, Podschun R, Bonvin AM, Leippe M, Bosch TC, Grötzinger J. Uncovering the evolutionary history of innate immunity: the simple metazoan Hydra uses epithelial cells for host defence.##Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra. DRAMP03305 DCYEDWSRCTPGTSFLTGILWKDCHSRCKELGHRGGRCVDSPSKHCPGVLKNNKQCHCY 59 Neuromacin (Annelida, animals) A8V0B3 Belongs to the macin family Not found Hirudo medicinalis (Medicinal leech) Antimicrobial Homology Not found Not found "Function: May have antimicrobial activity. PTM: Contains four disulfide bonds By similarity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18606660 J Immunol. 2008 Jul 15;181(2):1083-1095. Schikorski D, Cuvillier-Hot V, Leippe M, Boidin-Wichlacz C, Slomianny C, Macagno E, Salzet M, Tasiemski A. Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia. DRAMP03306 GCFEDWSRCSPSTSRGTGVLWRDCDSYCKVCFKADRGECFDSPSLNCPQRLPNNKQCRCINARTAKDNRNPTCWA 75 Theromacin (Annelida, animals) Q6T6C2 Belongs to the macin family Not found Theromyzon tessulatum (Duck leech) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Function: Has a bactericidal activity. Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15102860 J Biol Chem. 2004 Jul 23;279(30):30973-82. Tasiemski A, Vandenbulcke F, Mitta G, Lemoine J, Lefebvre C, Sautière PE, Salzet M. Molecular characterization of two novel antibacterial peptides inducible upon bacterial challenge in an annelid, the leech Theromyzon tessulatum. DRAMP03307 ADTLACRQSHQSCSFVACRAPSVDIGTCRGGKLKCCKWAPSS 42 Duck AvBD9 (avian beta defensin 9; Birds, animals) No entry found Not found Not found Anas platyrhynchos (Peking duck) Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database Escherichia coli, Staphylococcus aureus, Pasteurella multocida, Salmonella choleraesuis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19996700 J Microbiol Biotechnol. 2009 Nov;19(11):1447-1455. Ma D, Liao W, Wang R, Han Z, Liu S. Two novel duck antibacterial peptides, avian beta-defensins 9 and 10, with antimicrobial activity. DRAMP03308 VLLFLFQAAPGSADAPFADTAACRSQGNFCRAGACPPTFAASGSCHGGLLNCCAK 55 Duck AvBD10 (avian beta defensin 10; Birds, animals) No entry found Not found Not found Anas platyrhynchos (Domestic duck) Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database Escherichia coli, Staphylococcus aureus, Pasteurella multocida, Salmonella choleraesuis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19996700 J Microbiol Biotechnol. 2009 Nov;19(11):1447-1455. Ma D, Liao W, Wang R, Han Z, Liu S. Two novel duck antibacterial peptides, avian beta-defensins 9 and 10, with antimicrobial activity. DRAMP18209 ASSGWVCTLTIECGTVICACR 21 NAI-802 (Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Actinoplanes strains ID104802 and ID104771 Antimicrobial, Antibacterial, Anti-Gram+ Not found This peptide shares 19 residues with class II lantibiotic actagardine. In addition, it contains one extra Ala at the N-terminus and an extra Arg at the C-terminus. Actagardine, Ala(0)-actagardine, actagardine B, michiganin A, NAI-802 and Ala(0)-NAI-802 share three conserved thioether bridges within a core 19-aa peptide consisting of 14 invariant residues. As expected from the overall higher positive charge, NAI-802 was slightly more active than actagardine against staphylococci and streptococci. Further improvement of its antibacterial activity was achieved by adding one additional positive charge through conversion of the C-terminal carboxylate into the corresponding basic amide. Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 23168402 J Antibiot (Tokyo). 2013 Feb;66(2):73-8. Simone M, Monciardini P, Gaspari E, Donadio S, Maffioli SI. Isolation and characterization of NAI-802, a new lantibiotic produced by two different Actinoplanes strains. DRAMP03313 VDKPDYRPRPWPRPN 15 Metalnikowin-2A (Metalnikowin IIA; Insects, animals) P80409 Not found Not found Palomena prasina (Green shield bug) (Cimex prasinus) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide active against Gram-negative bacteria. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Insect Physiol. 1996; 42: 81-89. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin. DRAMP03314 VDKPDYRPRPWPRNMI 16 Metalnikowin-2B (Metalnikowin IIB; Insects, animals) P80410 Not found Not found Palomena prasina (Green shield bug) (Cimex prasinus) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide active against Gram-negative bacteria. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Insect Physiol. 1996; 42: 81-89. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin. DRAMP03315 VDKPDYRPRPWPRPNM 16 Metalnikowin-3 (Metalnikowin III; Insects, animals) P80411 Not found Not found Palomena prasina (Green shield bug) (Cimex prasinus) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial peptide active against Gram-negative bacteria. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Insect Physiol. 1996; 42: 81-89. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin. DRAMP03316 ATCDALSFSSKWLTVNHSACAIHCLTKGYKGGRCVNTICNCRN 43 Defensin (Insects, animals) P80407 Belongs to the invertebrate defensin family (Type 1 subfamily) Not found Palomena prasina (Green shield bug) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Antibacterial peptide active against Gram-negative bacteria. Induction: By bacterial infection. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J. Insect Physiol. 1996;42:81-89. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin DRAMP03317 AKRGGFWRKVGRKLGKGIRKIGKTIKSQLGKFRPRLQYRYQF 42 Cathelicidin-related antimicrobial peptide (AMPs) Q0R5P1 Not found CRAMP Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: Escherichia coli, Moraxella catarrhalis 1857;##Gram-positive bacterium: Streptococcus pneumoniae serotype 14. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17113647 Mol Immunol. 2007 Mar;44(9):2446-2458. McGillivary G, Ray WC, Bevins CL, Munson RS Jr, Bakaletz LO. A member of the cathelicidin family of antimicrobial peptides is produced in the upper airway of the chinchilla and its mRNA expression is altered by common viral and bacterial co-pathogens of otitis media. DRAMP03318 GAILCNLCKDTVKLVENLLTVDGAQAVRQYIDNLCGKASGFLGTLCEKILSFGVDELVKLIENHVDPVVVCEKIHAC 77 Pore-forming peptide ameobapore B (EH-APP; saposin-like protein) Q24824 Not found Not found Entamoeba histolytica (protozoan parasite) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Forms pores in the cytoplasmic membrane of host cells. Implicated in the cytolytic activity of the parasite. Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7715451 Mol Microbiol. 1994 Dec;14(5):895-904. Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. DRAMP03319 IPVLCPVCTSLVGKLIDLVLGGAVDKVTDYLETLCAKADGLVETLCTKIVSYGIDKLIEKILEGGSAKLICGLIHAC 77 Pore-forming peptide ameobapore C (EH-APP; saposin-like protein) Q24825 Not found Not found Entamoeba histolytica (protozoan parasite) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found Forms pores in the cytoplasmic membrane of host cells. Implicated in the cytolytic activity of the parasite. Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7715451 Mol Microbiol. 1994 Dec;14(5):895-904. Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. DRAMP03322 HPLKQYWWRPSI 12 PW2 No entry found Not found Not found Phage display peptide library Antimicrobial, Antifungal Not found Non helix or strand structure In the absence of an interface, PW2 is in random coil conformation. In micelles, structural calculation shows that Trp-7 forms the hydrophobic core that is important for the peptide folding. Lys-4, Tyr-6, Trp-8, and Arg-9 are in the same surface, possibly facing the micelle interface. (Ref.2) 1M02 resolved by NMR. Function: Synthetic PW2 shows anticoccidial activity against E. acervulina and Eimeria tenella with very low hemolytic activity. It also displays antifungal activity but no activity against bacteria.(Ref.2) Fungi: Eimeria acervulina sporozoites, E. tenella sporozoites, Toxoplasma gondii tachyzoites (low activity). [Ref.11849705]1.60% hemolytic activity at 100 μM against human erythrocytes,1.57% hemolytic activity at 100 μM against rabbit erythrocytes,1.42% hemolytic activity at 100 μM against chicken erythrocytes, Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11849705##12130641 Mol Biochem Parasitol. 2002 Mar;120(1):53-60.## Biol Chem. 2002 Sep 27;277(39):36351-6. da Silva A Jr, Kawazoe U, Freitas FF, Gatti MS, Dolder H, Schumacher RI, Juliano MA, da Silva MJ, Leite A.##co LW, Da Silva A Jr, Leite A, Valente AP, Almeida FC. Avian anticoccidial activity of a novel membrane-interactive peptide selected from phage display libraries.##NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display libraries. DRAMP03323 MKTLVLLSPSSCWPSRSRLILSKTQMKRLKLRSSQRKRTR 40 Testis defensin P70438 Not found Not found Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9369178 Biol Reprod. 1997 Nov;57(5):1115-1122. Grandjean V, Vincent S, Martin L, Rassoulzadegan M, Cuzin F. Antimicrobial protection of the mouse testis: synthesis of defensins of the cryptdin family. DRAMP03324 MKTLVLLSALFLLAFQVQADPIQNTDEETNTEVQPQEEDQA 41 Testis defensin P70439 Not found Defa26 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9369178 Biol Reprod. 1997 Nov;57(5):1115-1122. Grandjean V, Vincent S, Martin L, Rassoulzadegan M, Cuzin F. Antimicrobial protection of the mouse testis: synthesis of defensins of the cryptdin family. DRAMP03325 QMRQTTELQPLHGEESRADIAIPMQKRRKRDINFPICRFCCQCCNKPSCGICCE 54 Hepcidin antimicrobial peptide 2 Q5M9M1 Not found Hamp2 Mus musculus (Mouse) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19468303 PLoS Biol. 2009 May 5;7(5):e1000112. Lineage-specific biology revealed by a finished genome assembly of the mouse. Lineage-specific biology revealed by a finished genome assembly of the mouse. DRAMP18204 SNASVWECCSTGSWVPFTCC 20 Labyrinthopeptin A1(Bacteriocin) C0MP59 Belongs to the lantibiotics family (Class I bacteriocin) labA1 Actinomadura namibiensis DSM 6313 Antimicrobial, Antiviral, Anti-HIV, Anti-HSV Not found LabyA1 contains a special amino acid labionin at positions 1, 4, 8, 10, 13, and 19. Labs 1,4 and labs 10, 13 are connected via a carbon-carbon bond, while labs 4, 8 and labs 13, 19 form normal thioether bonds. In addition, a disulfide bond occurs between C9 and C20. Function: LabyA1 also demonstrated additive to synergistic effects in its anti-HIV-1 and anti-HSV-2 activity with anti(retro)viral drugs in dual combinations such as tenofovir, acyclovir, saquinavir, raltegravir and enfuvirtide. HSV(EC50: 0.29 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23724015 PLoS One. 2013 May 28;8(5):e64010. F The Lantibiotic Peptide Labyrinthopeptin A1 Demonstrates Broad Anti-HIV and Anti-HSV Activity with Potential for Microbicidal Applications DRAMP03327 PSELEKALSNLIDVYHNYSNIQGNHHALYKNDFKKMVTTECPQFVQNINIENLFRELDINSDNAINFEEFLAMVIKVGVASHKDSHKE 88 Protein S100-A8 (Calgranulin-A; MRP-8; Rodents, mammals, animals) P27005, P31724 Belongs to the S-100 family S100a8 Mus musculus (Mouse) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn2+ which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect. Disruption phenotype: Death at an early embryonic stage due to embryo resorption, starting about 8 days after fertilization. Miscellaneous: Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 1373330##17767165##18403730 Blood. 1992 Apr 15;79(8):1907-15.##Nat Med. 2007 Sep;13(9):1042-9.##Circ Res. 2008 May 23;102(10):1239-46. Lagasse E, Weissman IL.##Vogl T, Tenbrock K, Ludwig S, Leukert N, Ehrhardt C, van Zoelen MA, Nacken W, Foell D, van der Poll T, Sorg C, Roth J.##Boyd JH, Kan B, Roberts H, Wang Y, Walley KR. Mouse MRP8 and MRP14, two intracellular calcium-binding proteins associated with the development of the myeloid lineage.##Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock.##S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products. DRAMP18206 ASGWVCTLTIECGTLVCAC 19 Deoxyactagardine B(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) ligA Actinoplanes liguriae NCIMB41362 Antimicrobial, Antibacterial, Anti-Gram+ Not found Actagardine, Ala(0)-actagardine, actagardine B, michiganin A, NAI-802 and Ala(0)-NAI-802 share three conserved thioether bridges within a core 19-aa peptide consisting of 14 invariant residues. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 23168402 J Antibiot (Tokyo). 2013 Feb;66(2):73-8. Simone M, Monciardini P, Gaspari E, Donadio S, Maffioli SI. Isolation and characterization of NAI-802, a new lantibiotic produced by two different Actinoplanes strains. DRAMP18205 SDWSLWECCSTGSLFACC 18 Labyrinthopeptin A2 (Bacteriocin) C0MP60 Belongs to the lantibiotics family (Class I bacteriocin) labA2 Actinomadura namibiensis DSM 6313 Antimicrobial, Antiviral Not found This peptide contains a special amino acid labionin at positions 1, 4, 8, 10, 13, and 17. Labs 1,4 and labs 10, 13 are connected via a carbon-carbon bond, while labs 4, 8 and labs 13, 17 form normal thioether bonds. In addition, a disulfide bond occurs between C9 and C18. Comment: No comments found on DRAMP database HSV No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20191635 Angew Chem Int Ed Engl. 2010 Mar 22;49(13):2436-40. M In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification. DRAMP03329 LRDLVCYCRSRGCKGRERMNGTCRKGHLLYTLCCR 35 Alpha-defensin cryptdin-1 (Crp1; Rodents, mammals, animals) P11477, Q61448 Belongs to the alpha-defensin family Defa1 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Has antibacterial activity against attenuated mutants of S. typhimurium. Tissue specificity: Paneth cells of the small bowel. Developmental stage: Accumulates to high levels in mouse intestinal crypt epithelium during postnatal development. PTM: Contains three disulfide bonds (By similarity). " Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 1500431 J Cell Biol. 1992 Aug;118(4):929-936. Selsted ME, Miller SI, Henschen AH, Ouellette AJ. Enteric defensins: antibiotic peptide components of intestinal host defense. DRAMP03330 LRDLVCYCRTRGCKRRERMNGTCRKGHLMYTLCCR 35 Alpha-defensin cryptdin-2 (Defensin-related cryptdin-2; Rodents, mammals, animals) P28309, P82293, Q60616, Q62537 Belongs to the alpha-defensin family Defa2 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has broad-spectrum antibacterial activity. Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds 6-34; 8-23; 13-33 (By similarity)." Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 1500431##1500163 J Cell Biol. 1992 Aug;118(4):929-936.##Infect Immun. 1992 Sep;60(9):3556-3565. Selsted ME, Miller SI, Henschen AH, Ouellette AJ.##Eisenhauer PB, Harwig SS, Lehrer RI. Enteric defensins: antibiotic peptide components of intestinal host defense.##Cryptdins: antimicrobial defensins of the murine small intestine. DRAMP03331 LRDLVCYCRKRGCKRRERMNGTCRKGHLMYTLCCR 35 Alpha-defensin cryptdin-3 (Defensin-related cryptdin-3; Rodents, mammals, animals) P28310, Q499K7 Belongs to the alpha-defensin family Defa3 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds (By similarity). " Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 1500431 J Cell Biol. 1992 Aug;118(4):929-936. Selsted ME, Miller SI, Henschen AH, Ouellette AJ. Enteric defensins: antibiotic peptide components of intestinal host defense. DRAMP03332 LRGLLCYCRKGHCKRGERVRGTCGIRFLYCCPRR 34 Alpha-defensin cryptdin-4 (Defensin-related cryptdin4; Rodents, mammals, animals) P28311, A3KPC1, Q9QZL4 Belongs to the alpha-defensin family Defa4 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand (3 strands; 18 residues) Not found 2GW9, 1TV0, 2GWP, 2LEW, 2LEY resolved by NMR. "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds. " Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys31,Cys8 and Cys23,Cys13 and Cys30. L No cytotoxicity information found Phospholipid 15595831##7927786##16857681 Biochemistry. 2004 Dec 21;43(50):15759-15766.##Infect Immun. 1994 Nov;62(11):5040-5047.##J Biol Chem. 2006 Sep 22;281(38):28068-78. Jing W, Hunter HN, Tanabe H, Ouellette AJ, Vogel HJ.##Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Rosengren KJ, Daly NL, Fornander LM, Jönsson LM, Shirafuji Y, Qu X, Vogel HJ, Ouellette AJ, Craik DJ. Solution structure of cryptdin-4, a mouse paneth cell alpha-defensin.##Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structural and functional characterization of the conserved salt bridge in mammalian paneth cell alpha-defensins: solution structures of mouse CRYPTDIN-4 and (E15D)-CRYPTDIN-4. DRAMP03333 SKKLICYCRIRGCKRRERVFGTCRNLFLTFVFCCS 35 Alpha-defensin cryptdin-5 (Defensin-related cryptdin5; Rodents, mammals, animals) P28312, Q64382 Belongs to the alpha-defensin family Defa5 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. PTM: Contains three disulfide bonds." Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 1500431 J Cell Biol. 1992 Aug;118(4):929-936. Selsted ME, Miller SI, Henschen AH, Ouellette AJ. Enteric defensins: antibiotic peptide components of intestinal host defense. DRAMP03334 DLVCYCRARGCKGRERMNGTCRKGHLLYMLCCR 33 Alpha-defensin cryptdin-6/12 (Defensin-related cryptdin-6/12; Rodents, mammals, animals) P50704, P50710, P82294 Belongs to the alpha-defensin family Defa6 AND Defa12 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found "Function: Has broad-spectrum antibacterial activity. Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bondss 4-32; 6-21; 11-31. Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa." Gram-positive bacterium: Listeria monocytogenes EGD;##Gram-negative bacteria: Escherichia coli ML-35p, mouse-avirulent Salmonella typhimurium 7953. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys4 and Cys32,Cys6 and Cys21,Cys11 and Cys31. L No cytotoxicity information found Not found 7927786##1500163 Infect. Immun. 1994;62:5040-5047.##Infect. Immun. 1992;60:3556-3565. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Eisenhauer P.B, Harwig S.S.S.L, Lehrer R.I. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Cryptdins: antimicrobial defensins of the murine small intestine. DRAMP03335 LRDLVCYCRTRGCKRREHMNGTCRKGHLMYTLCCR 35 Alpha-defensin cryptdin-7 (Defensin-related cryptdin-7; Rodents, mammals, animals) P50705 Belongs to the alpha-defensin family Defa7 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds 6-34; 8-23; 13-33 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03336 LRDLVCYCRKRGCKRREHMNGTCRKGHLMYTLCCR 35 Alpha-defensin cryptdin-8 (Defensin-related cryptdin-8; Rodents, mammals, animals) P50706 Belongs to the alpha-defensin family Defa8 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds 6-34; 8-23; 13-33 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03337 LRDLVCYCRKRGCKRREHMNGTCRKGHLLYMLCCR 35 Alpha-defensin cryptdin-9 (Defensin-related cryptdin-9; Rodents, mammals, animals) P50707 Belongs to the alpha-defensin family Defa9 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03338 LRDLVCYCRKRGCKGRERMNGTCRKGHLLYTMCCR 35 Alpha-defensin cryptdin-10 (Defensin-related cryptdin-10; Rodents, mammals, animals) P50708 Belongs to the alpha-defensin family Defa10 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03339 LRDLVCYCRSRGCKGRERMNGTCRKGHLLYMLCCR 35 Alpha-defensin cryptdin-11 (Defensin-related cryptdin-11; Rodents, mammals, animals) P50709 Belongs to the alpha-defensin family Defa11 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03340 LRDLVCYCRKRGCKRREHMNGTCRRGHLMYTLCCR 35 Alpha-defensin cryptdin-13 (Defensin-related cryptdin-13; Rodents, mammals, animals) P50711 Belongs to the alpha-defensin family Defa13 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03341 LRDLVCYCRTRGCKRRERMNGTCRKGHLMHTLCCR 35 Alpha-defensin cryptdin-14 (Defensin-related cryptdin-14; Rodents, mammals, animals) P50712 Belongs to the alpha-defensin family Defa14 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found 7YOA "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03342 LRDLVCYCRKRGCKRREHINGTCRKGHLLYMLCCR 35 Alpha-defensin cryptdin-15 (Defensin-related cryptdin-15; Rodents, mammals, animals) P50713 Belongs to the alpha-defensin family Defa15 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03343 LRDLVCYCRSRGCKGRERMNGTCRKGHLMYTLCCR 35 Alpha-defensin cryptdin-16 (Defensin-related cryptdin-16; Rodents, mammals, animals) P50714 Belongs to the alpha-defensin family Defa16 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. Tissue specificity: Paneth cells of the small bowel. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786##8188287 Genomics. 1994;19:448-453.##Infect Immun. 1994 Nov;62(11):5040-5047. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME.##Huttner KM, Selsted ME, Ouellette AJ. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.##Structure and diversity of the murine cryptdin gene family. DRAMP03344 LRDLVCYCRKRGCKRREHMNGTCRKGHLLYTLCCR 35 Alpha-defensin cryptdin-17 (CRYP17; Rodents, mammals, animals) Q64016 Belongs to the alpha-defensin family Defa17 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found Function: Probably contributes to the antimicrobial barrier Function: of the small bowel mucosa. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys6 and Cys34,Cys8 and Cys23,Cys13 and Cys33. L No cytotoxicity information found Not found 7927786 Genomics. 1994;19:448-453. Ouellette AJ, Hsieh MM, Nosek MT, Cano-Gauci DF, Huttner KM, Buick RN, Selsted ME. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms. DRAMP03345 SRDLICYCRKGGCNRGEQVYGTCSGRLLYCCPRR 34 Alpha-defensin cryptdin-20 (Defensin-related cryptdin-20; Rodents, mammals, animals) Q45VN2 Belongs to the alpha-defensin family Defa20 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: May have microbicidal activities (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Chen B, Zha Y, Xu X, Deng X. Unknown DRAMP03346 SRDLICLCRNRRCNRGELFYGTCAGPFLRCCRRRR 35 Alpha-defensin cryptdin-21 (Defensin-related cryptdin-21; Rodents, mammals, animals) Q8C1P2 Belongs to the alpha-defensin family Defa21 Mus musculus (Mouse) Antimicrobial Homology Not found Not found "Function: May have microbicidal activities (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP03347 SRDLICLCRKRRCNRGELFYGTCAGPFLRCCRRRR 35 Alpha-defensin cryptdin-22 (Defensin-related cryptdin-22; Rodents, mammals, animals) Q8C1N8 Belongs to the alpha-defensin family Defa22 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: May have microbicidal activities (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP03348 LRDLVCYCRTRGCKRRERMNGTCRKGHLIYTLCC 34 Alpha-defensin cryptdin-23 (Defensin-related cryptdin-23; Rodents, mammals, animals) Q5G866, Q059S0 Belongs to the alpha-defensin family Defa23 Mus musculus (Mouse) Antimicrobial Homology Not found Not found Function: May have microbicidal activities (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476##15489334 Physiol Genomics. 2004 Dec 15;20(1):1-11.##Genome Res. 2004 Oct;14(10B):2121-2127. Patil A, Hughes AL, Zhang G.##The MGC Project Team. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03349 LRDLVCYCRARGCKGRERMNGTCSKGHLLYMLCC 34 Alpha-defensin cryptdin-24 (Defensin-related cryptdin-24; Rodents, mammals, animals) Q5G865 Belongs to the alpha-defensin family Defa24 Mus musculus (Mouse) Antimicrobial Homology Not found Not found Function: May have microbicidal activities (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP03350 CEDLICYCRTRGCKRRERLNGTCRKGHLMYMLWCC 35 Alpha-defensin cryptdin-25 (Defensin-related cryptdin-25; Rodents, mammals, animals) Q5G864 Belongs to the alpha-defensin family Defa25 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found Function: May have microbicidal activities (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP03351 LRDLGCYCRKRGCTRRERINGTCRKGHLMYTLCCL 35 Alpha-defensin cryptdin-26 (Defensin-related cryptdin-26; Rodents, mammals, animals) Q3L180 Belongs to the alpha-defensin family Defa26 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found Function: May have microbicidal activities (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15494476 Physiol Genomics. 2004 Dec 15;20(1):1-11. Patil A, Hughes AL, Zhang G. Rapid evolution and diversification of mammalian alpha-defensins as revealed by comparative analysis of rodent and primate genes. DRAMP03352 RFPWCRKCRVCQKCQVCQKCPVCPTCPQCPKQPLCEERQNKTAITTQAPNTQHKGC 56 Alpha-defensin-related sequence 1 (Defensin-related cryptdin 1; Rodents, mammals, animals) P17533, Q9QVW7 Belongs to the alpha-defensin family Defa-rs1 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activit. Developmental stage: Accumulates to high levels in intestinal crypt epithelium during postnatal development." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2351676##8034619 J Biol Chem. 1990 Jun 15;265(17):9831-9837.##J Biol Chem. 1994 Jul 15;269(28):18702. Ouellette AJ, Lualdi JC.##Ouellette AJ, Lauldi J. A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin.##A novel gene family coding for cationic, cysteine-rich peptides. Regulation in mouse small intestine and cells of myeloid origin. DRAMP03353 LGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK 33 Alpha-defensin-related sequence 2 (Defensin-related cryptdin 2; Rodents, mammals, animals) P17534, Q64111 Belongs to the alpha-defensin family Defa-rs2 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activit. Developmental stage: Accumulates to high levels in intestinal crypt epithelium during postnatal development. Tissue specificity: Small bowel, spleen, colon, kidney, liver, stomach and femur marrow." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2351676##8034619##7896294 J. Biol. Chem. 1990;265:9831-9837.##J Biol Chem. 1994 Jul 15;269(28):18702.##Genomics 1994;24:99-109. Ouellette A.J, Lauldi J.C.## A novel mouse gene family coding for cationic, cysteine-richpeptides. Regulation in small intestine and cells of myeloid origin.##A novel gene family coding for cationic, cysteine-rich peptides. Regulation in mouse small intestine and cells of myeloid origin.##A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells. DRAMP03354 PRCPPCPRCSWCPRCPTCPRCNCNPK 26 Alpha-defensin-related sequence 7 (Defensin-related cryptdin 3; Rodents, mammals, animals) P50715, Q64109, Q68VH1 Belongs to the alpha-defensin family Defa-rs7 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activit. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7896294##15235601 Genomics. 1994 Nov 1;24(1):99-109.##Nat. Immunol. 2004;5:836-843. Huttner K.M, Ouellette A.J.##Hornef M.W, Putsep K, Karlsson J, Refai E, Andersson M. A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells.##Increased diversity of intestinal antimicrobial peptides by covalentdimer formation. DRAMP03355 PPCPSCPSCPWCPMCPRCPSCKCNPK 26 Alpha-defensin-related sequence 10 (CRS4C-4; Cryptdin-related protein 4C-4; Rodents, mammals, ani Q64263, Q0VDL7 Belongs to the alpha-defensin family Defa-rs10 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7896294##15489334 Genomics. 1994 Nov 1;24(1):99-109.##Genome Res. 2004 Oct;14(10B):2121-2127. Huttner KM, Ouellette AJ.##Feingold EA, et al, Malek J. A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03356 PPCPSCLSCPWCPRCLRCPMCKCNPK 26 Alpha-defensin-related sequence 12 (Defensin-related cryptdin 12; Rodents, mammals, animals) P50716, Q64110 Belongs to the alpha-defensin family Defa-rs12 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities. Tissue specificity: Paneth cells of the small bowel." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7896294 Genomics. 1994 Nov 1;24(1):99-109. Huttner KM, Ouellette AJ. A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells. DRAMP03357 LQDAALGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK 38 Cryptdin related sequence peptide (CRS4C-1a; Rodents, mammals, animals) Q70LV2, Q70LV8, Q70LV7, Q70LV6, Q70LV4 Not found Defa-rs2 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found "Function: Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium. MOA: CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation." Gram-positive bacteria: Enterococcus faecalis (LC=1.9 µM), Lactobacillus fermentum DSM 20052 (LC=1.1 µM), Strepococcus pyogenes clinical isolate (LC=0.4 µM), Listeria monocytogenes type 1 clinical isolate (LC=1.4 µM);##Gram-negative bacteria: Escherichia coli strain D21 (LC=2.4 µM), Salmonella typhimurium ATCC 14028 (LC=1.7 µM).##NOTE: Dimerized peptide was two- to fourfold more potent than monomeric peptide. LC, Lethal concentrations. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef MW, Pütsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03358 LQDAAVGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK 38 Cryptdin related sequence peptide (CRS4C-1d; Rodents, mammals, animals) Q70LV9, Q70LV5, Q70LV3 Not found Defa-rs4 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found "Function: Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium. MOA: CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation." Gram-negative bacterium: Salmonella typhimurium ATCC 14028;##Gram-positive bacteria: Enterococcus faecalis, Listeria monocytogenes type 1 clinical isolate, Streptococcus pyogenes clinical isolate. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef MW, Pütsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03359 LQDAALGWGRRCPRCPPCPRCSWCPRCPTCPRCNCNPK 38 Cryptdin related sequence peptide (CRS4C-2; Rodents, mammals, animals) Q70LV0, Q70LU3 Not found Defa-rs7 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found "Function: Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium. MOA: CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation." Gram-negative bacterium: Salmonella typhimurium ATCC 14028;##Gram-positive bacteria: Enterococcus faecalis, Listeria monocytogenes type 1 clinical isolate, Streptococcus pyogenes clinical isolate. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef MW, Pütsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03360 LQDAALGWGRRCPRCPPCPRCSWCPRCPTCPGCNCNPK 38 Cryptdin related sequence peptide (CRS4C-2b; Rodents, mammals, animals) Q70LV1 Not found Defa-rs7 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Predicted Not found Not found "Function: Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium. MOA: CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation." Gram-negative bacterium: Salmonella typhimurium ATCC 14028;##Gram-positive bacteria: Enterococcus faecalis, Listeria monocytogenes type 1 clinical isolate, Streptococcus pyogenes clinical isolate. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef MW, Pütsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03361 LQDAALGWGRRCPRCPRCPNCRRCPRCPTCPSCNCNPK 38 CRS4C-3a (Cryptdin related sequence peptide; Rodents, mammals, animals) No entry found Not found Not found Mus musculus (Mouse) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef M.W, Putsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03362 LQDAALGWSRRCPRCPPCPNCRRCPRCPTCPSCNCNPK 38 CRS4C-3c (Cryptdin related sequence peptide; Rodents, mammals, animals) No entry found Not found Not found Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found "Function: Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium. MOA: CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation." Gram-negative bacterium: Salmonella typhimurium ATCC 14028;##Gram-positive bacteria: Enterococcus faecalis, Listeria monocytogenes type 1 clinical isolate, Streptococcus pyogenes clinical isolate. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef M.W, Putsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03363 LQDAALGWGRRCPRCPRCPNCKRCPRCPTCPRCNCNPK 38 CRS4C-3d (Cryptdin related sequence peptide; Rodents, mammals, animals) No entry found Not found Not found Mus musculus (Mouse) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15235601 Nat Immunol. 2004 Aug;5(8):836-843. Hornef M.W, Putsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. DRAMP03364 DTNFPICIFCCKCCNNSQCGICCKT 25 Hepcidin (mammals, rodents, animals) Q9EQ21 Not found Hamp Mus musculus (Mouse) Antimicrobial Protein level Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. Tissue specificity: Highly expressed in the liver and to a much lesser extent in the heart. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11113132##11447267 J Biol Chem. 2001 Mar 16;276(11):7811-7819.##Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8780-8785. Pigeon C, Ilyin G, Courselaud B, Leroyer P, Turlin B, Brissot P, Loréal O.##Nicolas G, Bennoun M, Devaux I, Beaumont C, Grandchamp B, Kahn A, Vaulont S. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload.##Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. DRAMP03365 DINFPICRFCCQCCNKPSCGICCEE 25 Hepcidin-2 (mammals, rodents, animals) Q80T19, Q8BFW2 Not found Hamp2 Mus musculus (Mouse) Antimicrobial Transcript level Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Tissue specificity: Highly expressed in the liver and to a much lesser extent in the heart. Also expressed in pancreas. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12729891##16141072 FEBS Lett. 2003 May 8;542(1-3):22-26.##Science. 2005 Sep 2;309(5740):1559-1563. Ilyin G, Courselaud B, Troadec MB, Pigeon C, Alizadeh M, Leroyer P, Brissot P, Loréal O.##Carninci P, Kasukawa T, Katayama S, et al. Comparative analysis of mouse hepcidin 1 and 2 genes: evidence for different patterns of expression and co-inducibility during iron overload.##The transcriptional landscape of the mammalian genome. DRAMP03366 DQYKCLQHGGFCLRSSCPSNTKLQGTCKPDKPNCCKS 37 Beta-defensin 1 (BD-1; mBD-1; Defensin, beta 1; Rodents, mammals, animals) P56386 Belongs to the beta-defensin family Not found Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Bridge Not found PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9287114 FEBS Lett. 1997 Aug 11;413(1):45-49. Huttner KM, Kozak CA, Bevins CL. The mouse genome encodes a single homolog of the antimicrobial peptide human beta-defensin 1. DRAMP03367 AVGSLKSIGYEAELDHCHTNGGYCVRAICPPSARRPGSCFPEKNPCCKYMK 51 Beta-defensin 2 (BD-2, mBD-2; Defensin, beta 2; Defb2; Rodents, mammals, animals) P82020 Belongs to the beta-defensin family Defb2 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 17-46; 24-39; 29-47. Tissue specificity: Kidney, uterus and to a lesser extent in heart. Induction: In tracheal epithelium, by lipopolysaccharide or inflammation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9923615 FEBS Lett. 1999 Jan 8;442(1):112-116. Morrison GM, Davidson DJ, Dorin JR. A novel mouse beta defensin, Defb2, which is upregulated in the airways by lipopolysaccharide. DRAMP03368 KKINNPVSCLRKGGRCWNRCIGNTRQIGSCGVPFLKCCKRK 41 Beta-defensin 3 (BD-3, mBD-3; Defensin, beta 3; Rodents, mammals, animals) Q9WTL0, Q29R78 Belongs to the beta-defensin family Defb3 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found PTM: Contains three disulfide bonds 9-37; 17-30; 20-38. Highest expression in salivary glands, epididymis, ovary and pancreas and to a lesser extent in lung, liver and brain. Low or no expression in skeletal muscle and tongue. By bacterial infection. Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys9 and Cys37,Cys17 and Cys30,Cys20 and Cys38. L No cytotoxicity information found Not found 10377137 Infect Immun. 1999 Jul;67(7):3542-3547. Bals R, Wang X, Meegalla R.L, Wattler S, Weiner D.J, Nehls M.C, Wilson J.M. Mouse beta-defensin 3 is an inducible antimicrobial peptide expressed in the epithelia of multiple organs. DRAMP03369 QIINNPITCMTNGAICWGPCPTAFRQIGNCGHFKVRCCKIR 41 Beta-defensin 4 (BD-4, mBD-4; Defensin, beta 4; Rodents, mammals, animals) P82019 Belongs to the beta-defensin family Defb4 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Bridge Not found PTM: Contains three disulfide bonds 9-37; 16-30; 20-38. When expressed as a fusion protein, mBD-4 showed activity against both E. coli and S. aureus at 1ug/ml as well as chemotactic activity via CCR6-expressing cells (Rohrl J et al. J Biol Chem. 2010 Mar 5;285(10):7028-34). Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys9 and Cys37,Cys16 and Cys30,Cys20 and Cys38. L No cytotoxicity information found Not found 10922379 J Biol Chem. 2000 Oct 27;275(43):33314-33320. Jia HP, Wowk SA, Schutte BC, Lee SK, Vivado A, Tack BF, Bevins CL, McCray PB Jr. A novel murine beta-defensin expressed in tongue, esophagus, and trachea. DRAMP03371 KTINNPVSCCMIGGICRYLCKGNILQNGNCGVTSLNCCKRK 41 Beta-defensin 5 (BD-5, mBD-5; Defensin, beta 5; Rodents, mammals, animals) Q9EPV9 Belongs to the beta-defensin family Defb5 Mus musculus (Mouse) Antimicrobial, Antibacterial, Antifungal Transcript level Bridge Not found PTM: Contains three disulfide bonds 9-37; 16-30; 20-38. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Adler D.A, Holloway J.L, Haldeman B.E, Rixon M, Jaspers S, Fox B, Gosink J, Sheppard P, Presnell S, Gao Z, Whitmore T, Stamm M, Laube D, Diamond G. EST and genomic database mining yield novel human and mouse beta-defensins DRAMP03372 NSKRACYREGGECLQRCIGLFHKIGTCNFRFKCCKFQIPEKKTKIL 46 Beta-defensin 7 (BD-7, mBD-7; Defensin, beta 7; Rodents, mammals, animals) Q91V70 Belongs to the beta-defensin family Defb7 Mus musculus (Mouse) Antimicrobial, Antibacterial Protein level Combine helix and strand structure Not found 1E4T resolved by NMR. PTM: Contains three disulfide bonds 6-33; 13-27; 17-34. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##11714914 Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.##Protein Sci. 2001 Dec;10(12):2470-2479. Conejo-Garcia JR, Nehls MC, Wattler S, Bals R, Heitland A, Kluever E, Liepke C, Adermann K, Forssmann WG.##Bauer F, Schweimer K, Klüver E, Conejo-Garcia JR, Forssmann WG, Rösch P, Adermann K, Sticht H. Cloning and characterization of mBD-7 and mBD-8, two novel mouse beta-defensins.##Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. DRAMP03373 NEPVSCIRNGGICQYRCIGLRHKIGTCGSPFKCCK 35 Beta-defensin 8 (BD-8, mBD-8; Defensin, beta 8; Rodents, mammals, animals) Q91V82, Q8R556 Belongs to the beta-defensin family Defb8 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine helix and strand structure Not found 1E4R resolved by NMR. "PTM: Contains three disulfide bonds 6-33; 13-27; 17-34. Function: The antimicrobial activity against S. aureus, E. coli and B.cepacia is reduced in raised concentration of NaCl, but its action against Pseudomonas aeruginosa is independent of NaCl concentration." Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Pseudomonas aeruginosa, Escherichia coli, Burkholderia cepacia. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##11714914 Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.##Protein Sci. 2001 Dec;10(12):2470-2479. Conejo-Garcia JR, Nehls MC, Wattler S, Bals R, Heitland A, Kluever E, Liepke C, Adermann K, Forssmann WG.##Bauer F, Schweimer K, Klüver E, Conejo-Garcia JR, Forssmann WG, Rösch P, Adermann K, Sticht H. Cloning and characterization of mBD-7 and mBD-8, two novel mouse beta-defensins.##Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. DRAMP03374 IIGVSEMERCHKKGGYCYFYCFSSHKKIGSCFPEWPRCCKNIK 43 Beta-defensin 9 (BD-9, mBD-9; Defensin, beta 9; Rodents, mammals, animals) Q8R2I6 Belongs to the beta-defensin family Defb9 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 10-38; 17-31; 21-39. Tissue specificity: Expressed in both adult and neonate brain, and very weakly in kidneys, epididymis, and testis." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567 Mol Biol Evol. 2003 Mar;20(3):460-470. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family. DRAMP03375 DLKHLILKAQLTRCYKFGGFCHYNICPGNSRFMSNCHPENLRCCKNIKQF 50 Beta-defensin 10 (BD-10, mBD-10; Defensin, beta 10; Rodents, mammals, animals) Q8R2I8, A2A4E8 Belongs to the beta-defensin family Defb10 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 14-43; 21-36; 26-44. Tissue specificity: Expressed in both adult and neonate brain, and very weakly in kidneys, epididymis, and testis. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567##19468303 Mol Biol Evol. 2003 Mar;20(3):460-470.##PLoS Biol. 2009 May 5;7(5):e1000112. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R.##Church D.M, Goodstadt L, Hillier L.W, Zody M.C, Goldstein S, et al, Ponting C.P. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family.##Lineage-specific biology revealed by a finished genome assembly of the mouse. DRAMP03376 DLKHLILKAQLARCYKFGGFCYNSMCPPHTKFIGNCHPDHLHCCINMKELEGST 54 Beta-defensin 11 (BD-11, mBD-11; Defensin, beta 11; Rodents, mammals, animals) Q8R2I7, Q499L3 Belongs to the beta-defensin family Defb11 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 14-43; 21-36; 26-44. Tissue specificity: Expressed in both adult and neonate brain, and very weakly in kidneys, epididymis, and testis. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567##19468303 Mol Biol Evol. 2003 Mar;20(3):460-470.##PLoS Biol. 2009 May 5;7(5):e1000112. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R.##Church D.M, Goodstadt L, Hillier L.W, Zody M.C, Goldstein S, et al, Ponting C.P. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family.##Lineage-specific biology revealed by a finished genome assembly of the mouse. DRAMP03377 GLEYSQSFPGGEIAVCETCRLGRGKCRRTCIESEKIAGWCKLNFFCCRERI 51 Beta-defensin 12 (BD-12, mBD-12; Defensin, beta 12; Rodents, mammals, animals) Q8K4N3 Belongs to the beta-defensin family Defb12 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 19-46; 26-40; 30-47. Tissue specificity: Only expressed in epididymis (caput, corpus and cauda). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12193721##16141072##14718547 J Immunol. 2002 Sep 1;169(5):2516-2523.##Science. 2005 Sep 2;309(5740):1559-1563.##J Biol Chem. 2004 Mar 26;279(13):12421-12426. Yamaguchi Y, Nagase T, Makita R, Fukuhara S, Tomita T, Tominaga T, Kurihara H, Ouchi Y.##Carninci P, Kasukawa T, Katayama S, et al.##Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification of multiple novel epididymis-specific beta-defensin isoforms in humans and mice.##The transcriptional landscape of the mammalian genome.##Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03378 TLYRRFLCKKMNGQCEAECFTFEQKIGTCQANFLCCRKRKEH 42 Beta-defensin 13 (BD-13, mBD-13; Defensin, beta 13; Rodents, mammals, animals) Q8R2I4, A2A4E3 Belongs to the beta-defensin family Defb13 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 8-35; 15-29; 19-36. Tissue specificity: Expressed in testis and to a lesser extent in epididymis (caput, corpus and cauda). Also weakly expressed in kidneys." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567##19468303##14718547 Mol Biol Evol. 2003 Mar;20(3):460-470.##PLoS Biol. 2009 May 5;7(5):e1000112.##J Biol Chem. 2004 Mar 26;279(13):12421-6. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R.##Church D.M, Goodstadt L, Hillier L.W, Zody M.C, Goldstein S. et al, Ponting C.P.##Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family.##Lineage-specific biology revealed by a finished genome assembly of the mouse.##Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03379 FLPKTLRKFFCRIRGGRCAVLNCLGKEEQIGRCSNSGRKCCRKKK 45 Beta-defensin 14 (BD-14, mBD-14; Defensin, beta 14; Rodents, mammals, animals) Q7TNV9, Q14BD1 Belongs to the beta-defensin family Not found Mus musculus (Mouse) Antimicrobial, Antibacterial, Antifungal Transcript level Bridge Not found PTM: Contains three disulfide bonds 11-40; 18-33; 23-41. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15489334##18167348 Genome Res. 2004 Oct;14(10B):2121-2127.##J Biol Chem. 2008 Feb 29;283(9):5414-5419. Gerhard DS, Wagner L, et al.##Röhrl J, Yang D, Oppenheim JJ, Hehlgans T. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).##Identification and Biological Characterization of Mouse beta-defensin 14, the orthologue of human beta-defensin 3. DRAMP03380 FFDEKCSRVNGRCTASCLKNEELVALCQKNLKCCVTVQPCGKSKSNQSDEGSGHMGTWG 59 Beta-defensin 15 (BD-15, mBD-15; Defensin, beta 15; Rodents, mammals, animals) Q8R2I5, A2A4E5 Belongs to the beta-defensin family Defb15 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found "PTM: Contains three disulfide bonds 6-33; 13-27; 17-34. Tissue specificity: Expressed in testis and to a lesser extent in epididymis (caput, corpus and cauda). Also weakly expressed in kidneys and colon." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567##19468303##14718547 Mol Biol Evol. 2003 Mar;20(3):460-470.##PLoS Biol. 2009 May 5;7(5):e1000112.##J Biol Chem. 2004 Mar 26;279(13):12421-6. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R.##Church D.M, Goodstadt L, Hillier L.W, Zody M.C, Goldstein S. et al, Ponting C.P.##Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family.##Lineage-specific biology revealed by a finished genome assembly of the mouse.##Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03381 KKSYPEYGSLDLRKECKMRRGHCKLQCSEKELRISFCIRPGTHCCM 46 Beta-defensin 17 (BD-17, mBD-17; Defensin, beta 17; Rodents, mammals, animals) Q30KP6 Belongs to the beta-defensin family Defb17 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 16-44; 23-37; 27-45. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03382 APQMKTREVAERTHKCSLVRGTCKSECNSWEYKYNYCHTEPCCVVREYKRMEKLLSTPKYTT 62 Beta-defensin 18 (BD-18, mBD-18; Defensin, beta 18; Rodents, mammals, animals) Q30KP5 Belongs to the beta-defensin family Defb18 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03383 GKNPILQCMGNRGFCRSSCKKSEQAYFYCRTFQMCCLQSYVRISLTGVDDNTNWSYEKHWPRIP 64 Beta-defensin 19 (BD-19, mBD-19; Defensin, beta 19; Rodents, mammals, animals) Q8K3I8, Q3V0L7 Belongs to the beta-defensin family Defb19 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found Specifically expressed in male gonads (Sertoli cells). Not detected at 11.5 dpc. Specific signals are observed within seminiferous cords in male gonads at 12.5, 13.5, 14.5, and 16.5 dpc and in newborn testes. In 16.5 and newborn testes, its expression is also found in epididymis. No specific signal is found in female gonads. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12128228 Mech Dev. 2002 Aug;116(1-2):217-221. Yamamoto M, Matsui Y. Testis-specific expression of a novel mouse defensin-like gene, Tdl. DRAMP03384 KRCFSNVEGYCRKKCRLVEISEMGCLHGKYCCVNELENKKHKKHSVVEETVKLQDKSKVQDYMILPTVTYYTISI 75 Beta-defensin 20 (BD-20, mBD-20; Defensin, beta 20; Rodents, mammals, animals) Q30KP3, Q8C5A7 Belongs to the beta-defensin family Defb20 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03385 EFKRCWNGQGACRTFCTRQETFMHLCPDASLCCLSYSFKPSRPSRVGDV 49 Beta-defensin 25 (BD-25, mBD-25; Defensin, beta 25; Rodents, mammals, animals) Q30KN8 Belongs to the beta-defensin family Defb25 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains three disulfide bonds 5-32; 12-26; 16-33. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03386 GLFGFRSSKRQEPWIACELYQGLCRNACQKYEIQYLSCPKTRKCCLKYPRKITSF 55 Beta-defensin 29 (BD-29, mBD-29; Defensin, beta 29; Rodents, mammals, animals) Q8BGW9 Belongs to the beta-defensin family Defb29 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 17-44; 24-38; 28-45. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16141072 Science. 2005 Sep 2;309(5740):1559-1563. Carninci P, Kasukawa T, Katayama S, Gough J, Frith M.C, et al, Hayashizaki Y. The transcriptional landscape of the mammalian genome. DRAMP03387 GVNMYIKRIYDTCWKLKGICRNTCQKEEIYHIFCGIQSLCCLEKKEMPVLFVK 53 Beta-defensin 30 (BD-30, mBD-30; Defensin, beta 30; Rodents, mammals, animals) Q30KN4 Belongs to the beta-defensin family Defb30 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains three disulfide bonds 13-40; 20-34; 24-41. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15489334 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Genome Res. 2004 Oct;14(10B):2121-2127. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Gerhard DS, Wagner L, et al. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03388 RKRNSKFRPCEKMGGICKSQKTHGCSILPAECKSRYKHCCRL 42 Beta-defensin 33 (BD-33, mBD-33; Defensin, beta 33; Rodents, mammals, animals) Q30KN3 Belongs to the beta-defensin family Defb33 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains three disulfide bonds 12-39; 17-32; 25-40. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15489334 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Genome Res. 2004 Oct;14(10B):2121-2127. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Gerhard DS, Wagner L, et al. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03389 FFFFDEKCSRINGRCTASCLKNEELVALCWKNLKCCVTVQSCGRSKGNQSDEGSGHMGTRG 61 Beta-defensin 34 (BD-34, mBD-34; Defensin, beta 34; Rodents, mammals, animals) Q7TNV8 Belongs to the beta-defensin family Defb34 Mus musculus (House mouse) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Only expressed in epididymis (caput, corpus and cauda). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14718547 J Biol Chem. 2004 Mar 26;279(13):12421-6. Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03390 EIAVCETCRLGRGKCRRACIESEKIVGWCKLNFFCCRERI 40 Beta-defensin 35 (BD-35, mBD-35; Defensin, beta 35; Rodents, mammals, animals) Q8R2I3 Belongs to the beta-defensin family Defb35 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 8-35; 15-29; 19-36. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12644567##14718547 J Biol Chem. 2004 Mar 26;279(13):12421-12426.##J Biol Chem. 2004 Mar 26;279(13):12421-12426. Morrison G.M, Semple C.A.M, Kilanowski F.M, Hill R.E, Dorin J.R.##Zaballos A, Villares R, Albar J.P, Martinez-A C, Marquez G. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family.##Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03391 QKCWNLHGKCRHRCSRKESVYVYCTNGKMCCVKPKYQPKPKPWMF 45 Beta-defensin 36 (BD-36, mBD-36; Defensin, beta 36; Rodents, mammals, animals) Q8K3U4, A3KGR4, Q3V491 Belongs to the beta-defensin family Defb36 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 3-30; 10-24; 14-31. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##16141072 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Science. 2005 Sep 2;309(5740):1559-1563. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Carninci P, Kasukawa T, Katayama S, Gough J, Frith M.C, et al, Hayashizaki Y. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The transcriptional landscape of the mammalian genome. DRAMP03392 QNNPVAMLDTIACIENKDTCRLKNCPRLHNVVGTCYEGKGKCCHKN 46 Beta-defensin 37 (BD-37, mBD-37; Defensin, beta 37; Rodents, mammals, animals) Q7TMD2 Belongs to the beta-defensin family Defb37 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 13-42; 20-35; 25-43. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14718547 J Biol Chem. 2004 Mar 26;279(13):12421-12426. Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03393 IGPDTKKCVQRKNACHYFECPWLYYSVGTCYKGKGKCCQKRY 42 Beta-defensin 38 (BD-38, mBD-38; Defensin, beta 38; Rodents, mammals, animals) Q7TNV7 Belongs to the beta-defensin family Defb38 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found PTM: Contains three disulfide bonds 8-37; 15-30; 20-38. Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa, Enterococcus faecium. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14718547 J Biol Chem. 2004 Mar 26;279(13):12421-12426. Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03394 DDSIQCFQKNNTCHTNQCPYFQDEIGTCYDKRGKCCQKRLLHIRVPRKKKV 51 Beta-defensin 39 (BD-39, mBD-39; Defensin, beta 39; Rodents, mammals, animals) Q70KL3, Q7TNV6 Belongs to the beta-defensin family Defb39 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14718547 J Biol Chem. 2004 Mar 26;279(13):12421-12426. Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03395 LDTIKCLQGNNNCHIQKCPWFLLQVSTCYKGKGRCCQKRRWFARSHVYHV 50 Beta-defensin 40 (BD-40, mBD-40; Defensin, beta 40; Rodents, mammals, animals) Q70KL2, Q7TNV5 Belongs to the beta-defensin family Defb40 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14718547 J Biol Chem. 2004 Mar 26;279(13):12421-12426. Zaballos A, Villares R, Albar JP, Martínez-A C, Márquez G. Identification on mouse chromosome 8 of new beta-defensin genes with regionally specific expression in the male reproductive organ. DRAMP03396 RSHIDIKNGIERCEKVRGMCKTVCDIDEYDYGYCIRWRNQCCI 43 Beta-defensin 41 (BD-41, mBD-41; Defensin, beta 41; Rodents, mammals, animals) Q8C1G4, Q4FZ55 Belongs to the beta-defensin family Defb41 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains three disulfide bonds 13-41; 20-34; 24-42. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##16023745 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Biochim. Biophys. 2005 Acta 1730:22-30. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Jalkanen J, Huhtaniemi I, Poutanen M. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Discovery and characterization of new epididymis-specific beta-defensins in mice. DRAMP03397 FLENQDCSKHRHCRMKCKANEYAVRYCEDWTICCRVKKKESKKKKMW 47 Beta-defensin 43 (BD-43, mBD-43; Defensin, beta 43; Rodents, mammals, animals) Q30KM9 Belongs to the beta-defensin family Defb43 Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Bridge Not found PTM: Contains two disulfide bonds: 7-34; 13-27. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15489334 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Genome Res. 2004 Oct;14(10B):2121-2127. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Gerhard DS, Wagner L, et al. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03398 HPGTFHVRIKCMPKMTAVFGDNCSFYSSMGDLCNNTKSVCCMVPVRMDNI 50 Beta-defensin 50 (BD-50, mBD-50; Defensin, beta 50; Prostate beta-defensin 1; Rodents, mammals, a Q6TU36, Q30KM7 Belongs to the beta-defensin family Defb50 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Bridge Not found PTM: Contains two disulfide bonds 11-40; 23-41. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14659016 Genome Biol. 2003;4(12):R79. Abbott D.E, Pritchard C, Clegg N.J, Ferguson C, Dumpit R, Sikes R.A, Nelson P.S. Expressed sequence tag profiling identifies developmental and anatomic partitioning of gene expression in the mouse prostate. DRAMP03399 PGDIPPGIRNTVCLMQQGHCRLFMCRSGERKGDICSDPWNRCCVPYSVKDRR 52 Sperm-associated antigen 11 (Rodents, mammals, animals) Q8K4N2, Q2HPE4, Q30KM3 Belongs to the beta-defensin family Spag11 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram- Homology Not found Not found Is also responsible for sperm maturation, storage, and protection. Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##12193721 Physiol Genomics. 2005 Sep 21;23(1):5-17.##J Immunol. 2002 Sep 1;169(5):2516-2523. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G.##Yamaguchi Y, Nagase T, Makita R, Fukuhara S, Tomita T, Tominaga T, Kurihara H, Ouchi Y. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Identification of multiple novel epididymis-specific beta-defensin isoforms in humans and mice. DRAMP03400 GGVKGEEKRVCPPDYVRCIRQDDPQCYSDNDCGDQEICCFWQCGFKCVLPVKDNSEEQIPQSKV 64 WAP four-disulfide core domain protein 12 (Rodents, mammals, animals) Q9JHY3 Not found Wfdc12 Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (IC90=10 µM);##Gram-positive bacterium: Staphylococcus aureus (IC90=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12574366 J Immunol. 2003 Feb 15;170(4):1973-1979. Hagiwara K, Kikuchi T, Endo Y, Huqun, Usui K, Takahashi M, Shibata N, Kusakabe T, Xin H, Hoshi S, Miki M, Inooka N, Tokue Y, Nukiwa T. Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. DRAMP03401 QPRATRKGVTPKQGYCPEFLLDCPFVLLPVCSRDKGCKGTKKCCFYYCQMRCVEPWTTLT 60 WAP four-disulfide core domain protein 15A (Rodents, mammals, animals) Q8BH89 Not found Wfdc15a Mus musculus (Mouse) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16141072 Science. 2005 Sep 2;309(5740):1559-1563. Carninci P, Kasukawa T, Katayama S, et al. The transcriptional landscape of the mammalian genome. DRAMP03402 RPEIKKKNVFSKPGYCPEYRVPCPFVLIPKCRRDKGCKDALKCCFFYCQMRCVDPWESPE 60 WAP four-disulfide core domain protein 15B (Elafin-like protein I; Rodents, mammals, animals) Q9JHY4, A2A5M6, Q8BVC0 Not found Wfdc15b Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli (IC90=10 µM);##Gram-positive bacterium: Staphylococcus aureus (IC90=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12574366 J Immunol. 2003 Feb 15;170(4):1973-1979. Hagiwara K, Kikuchi T, Endo Y, Huqun, Usui K, Takahashi M, Shibata N, Kusakabe T, Xin H, Hoshi S, Miki M, Inooka N, Tokue Y, Nukiwa T. Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. DRAMP03403 AGANDLCQECEDIVHLLTKMTKEDAFQDTIRKFLEQECDILPLKLLVPRCRQVLDVYLPLVIDYFQGQIKPKAICSHVGLC 81 SP-BN (N-terminal region of Surfactant Protein B; SAPLIP; Rodents, mammals, animals) No entry found Not found Not found Mus musculus (Mouse) Antimicrobial, Antibacterial Not found Not found Not found Transgenic mice overexpressing SP-BN has significantly decreased bacterial burden and increased survival following intranasal inoculation with bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20007532 J Immunol. 2010 Jan 15;184(2):975-983. Yang L, Johansson J, Ridsdale R, Willander H, Fitzen M, Akinbi HT, Weaver TE. Surfactant protein B propeptide contains a saposin-like protein domain with antimicrobial activity at low pH. DRAMP03404 GEKLKKIGQKIKNFFQKL 18 Cramp 18 (CRAMP analogue) No entry found Not found Not found Mus musculus (Mouse) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10973820 Biochem Biophys Res Commun. 2000 Sep 7;275(3):904-909. Shin SY, Kang SW, Lee DG, Eom SH, Song WK, Kim JI. CRAMP Analogues Having Potent Antibiotic Activity against Bacterial, Fungal, and Tumor Cells without Hemolytic Activity. DRAMP03407 DPVTYIRNGGICQYRCIGLRHKIGTCGSPFKCCK 34 Defr1 (Murine beta-defensin related peptide; Rodents, mammals, animals) No entry found Belongs to the beta-defensin family Not found Mus musculus (Mouse) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found The antimicrobial activity of Defr1 against S. aureus, E. coli, and B. cepacia was found to be reduced in raised concentration of NaCl, but its action against P. aeruginosa was independent of NaCl concentration. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Pseudomonas aeruginosa, Escherichia coli, Burkholderia cepacia. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12226710 Mamm Genome. 2002 Aug;13(8):445-451. Morrison GM, Rolfe M, Kilanowski FM, Cross SH, Dorin JR. Identification and characterization of a novel murine beta-defensin-related gene. DRAMP03408 VTCFCRRRGCASRERHIGYCRFGNTIYRLCCRR 33 Neutrophil defensin 1 (HANP-1; alpha-defensin; Rodents, mammals, animals) P81465 Belongs to the alpha-defensin family Not found Mesocricetus auratus (Golden hamster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Function: Anti-fungal and bactericidal activity, greater against Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus, Streptococcus pyogenes, Enterococcus faecalis;##Gram-negative bacteria: Escherichia coli, Salmonella serotype krefeld, Klebsiella oxytoca, Pseudomonas aeruginosa.##Fungi: Candida albicans, Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L No cytotoxicity information found Not found 8890190 Infect Immun. 1996 Nov;64(11):4444-4449. Mak P, Wójcik K, Thogersen IB, Dubin A. Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins. DRAMP03409 CFCKRPVCDSGETQIGYCRLGNTFYRLCCRQ 31 Neutrophil defensin 2 (HANP-2; alpha-defensin; Rodents, mammals, animals) P81466 Belongs to the alpha-defensin family Not found Mesocricetus auratus (Golden hamster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Function: Bactericidal activity, greater against Gram-positive bacteria. Low anti-fungi activity Gram-positive bacteria: Staphylococcus aureus, Streptococcus pyogenes, Enterococcus faecalis;##Gram-negative bacteria: Escherichia coli, Salmonella serotype krefeld, Klebsiella oxytoca, Pseudomonas aeruginosa.##Fungi: Candida albicans, Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization(Cys1 and Cys29). Free Disulfide bonds between Cys1 and Cys29,Cys3 and Cys18,Cys8 and Cys28. L No cytotoxicity information found Not found 8890190 Infect Immun. 1996 Nov;64(11):4444-4449. Mak P, Wójcik K, Thogersen IB, Dubin A. Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins. DRAMP03410 VTCFCRRRGCASRERLIGYCRFGNTIYGLCCRR 33 Neutrophil defensin 3 (HANP-3; alpha-defensin; Rodents, mammals, animals) P81467 Belongs to the alpha-defensin family Not found Mesocricetus auratus (Golden hamster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Function: Anti-fungal and bactericidal activity, greater against Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus, Streptococcus pyogenes, Enterococcus faecalis;##Gram-negative bacteria: Escherichia coli, Salmonella serotype krefeld, Klebsiella oxytoca, Pseudomonas aeruginosa.##Fungi: Candida albicans, Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L No cytotoxicity information found Not found 8890190 Infect Immun. 1996 Nov;64(11):4444-4449. Mak P, Wójcik K, Thogersen IB, Dubin A. Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins. DRAMP03411 VTCFCKRPVCDSGETQIGYCRLGNTFYRLCCRQ 33 Neutrophil defensin 4 (HANP-4; alpha-defensin; Rodents, mammals, animals) P81468 Belongs to the alpha-defensin family Not found Mesocricetus auratus (Golden hamster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Function: Bactericidal activity, greater against Gram-positive bacteria. Low anti-fungi activity. Gram-positive bacteria: Staphylococcus aureus, Streptococcus pyogenes, Enterococcus faecalis;##Gram-negative bacteria: Escherichia coli, Salmonella serotype krefeld, Klebsiella oxytoca, Pseudomonas aeruginosa.##Fungi: Candida albicans, Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L No cytotoxicity information found Not found 8890190 Infect Immun. 1996 Nov;64(11):4444-4449. Mak P, Wójcik K, Thogersen IB, Dubin A. Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins. DRAMP03412 MRTLCSLLLIGCLLFSYATPVAGILGPLRIQTDYHRCLREKGFCLNAVCPRSTLFVGTCFPYKFYCCKFKR 71 Beta-defensin 2 Q32ZI5 Not found Defb2 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil A.A, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03413 MKTLVLLSALVLLALQVQAEPTPKTDEGTKTDEQPGKEDQVVSVSIEGQGDPAFQDGVLRDLKCFCRAKSCNWGEGIMGICNKRYGMLILCCR 93 Defensin 7 Q6B328 Not found Defa24 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Infect. Immun. 2004,0:0-0. Viera A., Kurland A.R., Condon M.R., Diamond G. Identification and expression of alpha-defensin genes in the rat small intestine. DRAMP03414 MKTLVLLSALVLVAYQVQADPIQGAEEETKTEEQPSDEDQDVSVSFEGPEASALQDFEIGRPVRRCRCRANCGPKEYATAFCAQGPFKQFKFCCT 95 Defensin alpha 6 (Protein Defa6) Q4JEI8 Not found Defa6 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Patil A, Zhang G. Rapid duplication and diversification of mammalian alpha-defensins as evidenced by comparative analysis of rodent and human defensin genes. DRAMP03415 MRTLTLLTTLLLLALHTQAESPQGSRSTEEALDQEQLVMEDQDISISFGGDKGTALQDADVKSGVTCYCRLLSCQFGERLAGSCRSGGVTYPLCCH 96 Defensin alpha 7 (Defensin) Q4JEI7 Not found Defa7 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Patil A, Zhang G. Rapid duplication and diversification of mammalian alpha-defensins as evidenced by comparative analysis of rodent and human defensin genes. DRAMP03416 MRTLTLLTALLLLALHTQAESPQGSPKEAPDQEQLDMEDQDISVFFGGDKGTALQDAAGSTCSCRIGTCVSGEWLSWVCRINGRIYRLCCR 91 Defensin alpha 10 (Defensin) Q4JEI4 Not found Defa10 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Patil A, Zhang G. Rapid duplication and diversification of mammalian alpha-defensins as evidenced by comparative analysis of rodent and human defensin genes. DRAMP03417 MKTLILLSALVLLALQVQADPIQEAEEETKTEEQPADEDQDVSVSFEGPEASAVQDLRVRRTLQCSCRRVCRNTCSCIRLSRSTYAS 87 Defensin alpha-related sequence 1 (Protein Defa-rs1) Q4JEI2 Not found Defa-rs1 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found 5GWG Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Patil A, Zhang G. Rapid duplication and diversification of mammalian alpha-defensins as evidenced by comparative analysis of rodent and human defensin genes. DRAMP03418 DTNFPICLFCCKCCKNSSCGLCCIT 25 Hepcidin (mammals, rodents, animals) Q99MH3 Not found Hamp Rattus norvegicus (Rat) Antimicrobial Homology Not found Not found "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity. PTM: Contains four disulfide bonds 7-23; 10-13; 11-19; 14-22." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11113132 J Biol Chem. 2001 Mar 16;276(11):7811-7819. Pigeon C, Ilyin G, Courselaud B, Leroyer P, Turlin B, Brissot P, Loréal O. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. DRAMP03420 VTCYCRSTRCGFRERLSGACGYRGRIYRLCCR 32 Neutrophil antibiotic peptide NP-2 (RatNP-2; Rodents, mammals, animals) Q62715 Belongs to the alpha-defensin family Defa Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Active in vitro against S. aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Salmonella typhimurium. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L No cytotoxicity information found Not found 2254017##7594610 Infect. Immun. 1990;58:3899-3902.##J. Immunol. 1995;155:4476-4484. Eisenhauer P.B, Harwig S.S.S.L, Szklarek D, Ganz T, Lehrer R.I.##Yount N.Y, Wang MS.C, Yuan J, Banaiee N, Ouellette A.J, Selsted M.E. Polymorphic expression of defensins in neutrophils from outbred rats.##Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis. DRAMP03421 CSCRTSSCRFGERLSGACRLNGRIYRLCC 29 Neutrophil antibiotic peptide NP-3 (RatNP-3a, RatNP-3b; Rodents, mammals, animals) Q62713, Q9Z1F1 Belongs to the alpha-defensin family Not found Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Bridge Not found Active in vitro against S. aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus. Gram-positive bacterium: Staphylococcus aureus 502A;##Gram-negative bacterium: Escherichia coli ML-35.##Fungi: Candida albicans 820, Cryptococcus neoformans A-383. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization(Cys1 and Cys29). Cyclization(Cys1 and Cys29). Disulfide bonds between Cys1 and Cys29,Cys3 and Cys18,Cys8 and Cys28. L No cytotoxicity information found Not found 2254017##7594610 Infect. Immun. 1990;58:3899-3902.##J. Immunol. 1995;155:4476-4484. Eisenhauer P.B, Harwig S.S.S.L, Szklarek D, Ganz T, Lehrer R.I.##Yount N.Y, Wang MS.C, Yuan J, Banaiee N, Ouellette A.J, Selsted M.E. Polymorphic expression of defensins in neutrophils from outbred rats.##Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis. DRAMP03423 DIPPGIRNTVCFMQRGHCRLFMCRSGERKGDICSDPWNRCCVSSSIKNR 49 BIN1b (Sperm-associated antigen 11; Antimicrobial-like protein Bin-1b; Rodents, mammals, animals) Q8VBV2 Belongs to the beta-defensin family Spag11 Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Not found Not found "Function: Antimicrobial peptide against E.coli. Is also responsible for sperm maturation, storage, and protection. Tissue specificity: Only expressed in epididymis (middle part of the caput). Developmental stage: Its expression starts at 30 days of age, reaches a maximum during the sexually mature period, and then decreased in old rats. PTM: Contains three disulfide bonds 11-40; 18-33; 23-41." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11230693 J Biotechnol. 2009 Jan 1;139(1):33-37##Science. 2001 Mar 2;291(5509):1783-1785. Guo C, Diao H, Lian Y, Yu H, Gao H, Zhang Y, Lin D.##Li P, Chan HC, He B, So SC, Chung YW, Shang Q, Zhang YD, Zhang YL. Recombinant expression and characterization of an epididymis-specific antimicrobial peptide BIN1b/SPAG11E.##An antimicrobial peptide gene found in the male reproductive system of rats. DRAMP03424 DQYRCLQNGGFCLRSSCPSHTKLQGTCKPDKPNCCRS 37 Beta-defensin 1 (BD-1, RBD-1; Defensin, beta 1; Rodents, mammals, animals) O89117 Belongs to the beta-defensin family Defb1 Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 5-34; 12-27; 17-35." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##10456937 Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.##Infect Immun. 1999 Sep;67(9):4827-4833. Page R.A, Malik A.N.##Jia HP, Mills JN, Barahmand-Pour F, Nishimura D, Mallampali RK, Wang G, Wiles K, Tack BF, Bevins CL, McCray PB Jr. Rat beta defensin-1 peptide: candidate marker for diabetic nephropathy.##Molecular cloning and characterization of rat genes encoding homologues of human beta-defensins. DRAMP03425 KKVYNAVSCMTNGGICWLKCSGTFREIGSCGTRQLKCCKKK 41 Beta-defensin 3 (BD-3, RBD-3; Defensin, beta 3; Rodents, mammals, animals) Q32ZI4 Belongs to the beta-defensin family Defb3 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 9-37; 16-30; 20-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03426 QSINNPITCLTKGGVCWGPCTGGFRQIGTCGLPRVRCCKKK 41 Beta-defensin 4 (BD-4, RBD-4; Defensin, beta 4; RBD-2; Rodents, mammals, animals) O88514, Q32ZE9 Belongs to the beta-defensin family Defb4 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 9-37; 16-30; 20-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03427 QSINNPVSCVTHGGICWGRCPGSFRQIGTCGLGKVRCCKKK 41 Beta-defensin 5 (BD-5, RBD-5; Defensin, beta 5; Rodents, mammals, animals) Q32ZI3 Belongs to the beta-defensin family Defb5 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 9-37; 16-30; 20-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03428 ELKHLGLKTEFEQCQRIRGYCLNTYCRFPTSHVGSCYPEKRYCCKNIR 48 Beta-defensin 9 (BD-9, RBD-9; Defensin, beta 9; Rodents, mammals, animals) Q32ZI2 Belongs to the beta-defensin family Defb9 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 14-43; 21-36; 26-44." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03429 ELKHLGMTAETEWCRLFEGFCHDKNCPPPTSHVGSCHPEKRSCCKDRR 48 Beta-defensin 10 (BD-10, RBD-10; Defensin, beta 10; Rodents, mammals, animals) Q32ZI1 Belongs to the beta-defensin family Defb10 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 14-43; 21-36; 26-44." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03430 FLRRSVSGFQECHSKGGYCYRYYCPRPHRRLGSCYPYAANCCRRRR 46 Beta-defensin 11 (BD-11, RBD-11; Defensin, beta 11; Rodents, mammals, animals) Q32ZI0 Belongs to the beta-defensin family Defb11 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 12-41; 19-34; 24-42." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03431 GLEYSQSFPGGEFAVCETCRLGRGKCRRTCLDSEKIAGKCKLNFFCCRERI 51 Beta-defensin 12 (BD-12, RBD-12; Defensin, beta 12; Rodents, mammals, animals) Q32ZH9 Belongs to the beta-defensin family Defb12 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 19-46; 26-39; 30-47." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03432 TLYRRFLCKKMKGRCETACLSFEKKIGTCRADLTPLCCKEKKKH 44 Beta-defensin 13 (BD-13, RBD-13; Defensin, beta 13; Rodents, mammals, animals) Q32ZH8 Belongs to the beta-defensin family Defb13 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 8-37; 15-29; 19-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03433 FIPKSLRRFFCRVRGGRCAILNCLGKEEQIGRCSNRGQKCCRKKK 45 Beta-defensin 14 (BD-14, RBD-14; Defensin, beta 14; Rodents, mammals, animals) Q32ZH7 Belongs to the beta-defensin family Defb14 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 11-40; 18-33; 23-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03434 FFDEKCSRINGRCTESCLKNEELIALCQKNLKCCVTVQPCGRDKGDELDEDSGYNRTRG 59 Beta-defensin 15 (BD-15, RBD-15; Defensin, beta 15; Rodents, mammals, animals) Q32ZH6 Belongs to the beta-defensin family Defb15 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 6-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03435 KRSYPEYGSLDLRKECRMSKGHCKLQCSENEIRIAFCIRPGTHCCI 46 Beta-defensin 17 (BD-17, RBD-17; Defensin, beta 17; Rodents, mammals, animals) Q32ZH5 Belongs to the beta-defensin family Defb17 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 16-44; 23-37; 27-45." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03436 APQMKTRDVLERTHKCFLVGGECKSECSSWEYEYVFCYTGPCCVMREYKRVEKFSNTPKYTT 62 Beta-defensin 18 (BD-18, RBD-18; Defensin, beta 18; Rodents, mammals, animals) Q32ZH4 Belongs to the beta-defensin family Defb18 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03437 CRKSCWVIRGHCRKHCRSGERVKKPCSNGDYCCIAKKINTVPQAPKNAFSRNFRVHSRTAPVAVLKNST 69 Beta-defensin 19 (Rodents, mammals, animals) Q32ZH3 Belongs to the beta-defensin family Defb19 Rattus norvegicus (Rat) Antimicrobial Transcript level Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03438 KRCFSNVAGYCRKRCRLVEISEMGCLHGKYCCVNELENKRHKKDTVVEQPMEPRDKSKVQDYMVLPTITYYTITI 75 Beta-defensin 20 (BD-20, RBD-20; Defensin, beta 20; Rodents, mammals, animals) Q32ZH2 Belongs to the beta-defensin family Defb20 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03439 MRLLLMALPLLALLPQVIPDYSAEKRCLNRLGHCKRKCKAGEMVMETCKYFQVCCVLDDNDYKQKASITRTMEKTSTIEYNLS 83 Beta-defensin 21 (DEFB21; Protein Defb21; rodents, mammals, animals) Q32ZH1 Belongs to the beta-defensin family Defb21 Rattus norvegicus (Rat) Antimicrobial Homology Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03440 MKLVLLLLAIFVTTELVMSGKNPTLQCMGNRGFCRPSCKKGEQAYFYCRTYQICCLQSHVRISLTGVEDNTNWSYEKHWPRIP 83 Beta-defensin 24 (DEFB24; Protein Defb24; rodents, mammals, animals) Q32ZG8 Belongs to the beta-defensin family Defb24 Rattus norvegicus (Rat) Antimicrobial Homology Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03441 EFKRCWNGQGACRTYCTRQEKFIHLCPDASLCCLSYSLKASPHSRAGGV 49 Beta-defensin 25 (BD-25, RBD-25; Defensin, beta 25; Rodents, mammals, animals) Q32ZG7 Belongs to the beta-defensin family Defb25 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 5-32; 12-26; 16-33." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03442 MKTAVLTMVLLLLLSQVIPGSPEKCWKSFGICREECLRKEKFYIFCWDGSLCCVKPKNVPQWSQSSE 67 Beta-defensin 27 (DEFB27; Protein Defb27; rodents, mammals, animals) Q32ZG5 Belongs to the beta-defensin family Defb27 Rattus norvegicus (Rat) Antimicrobial Homology Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03443 MLLTRSSTLSGHIKLWFLTLAVLVVLAQTSPEGWFRTCFYGMGKCRHVCRANEKKKERCGENSFCCLGETKSKLSNIPTNKGRKKD 86 Beta-defensin 28 (Rodents, mammals, animals) Q32ZG4 Belongs to the beta-defensin family Defb28 Rattus norvegicus (Rat) Antimicrobial Transcript level Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03444 GLFGLRSGKRREPWVSCELYQGSCRNACQKYEIQYLTCPKKRKCCLKFPMKITRV 55 Beta-defensin 29 (BD-29, RBD-29; Defensin, beta 29; Rodents, mammals, animals) Q32ZG3 Belongs to the beta-defensin family Defb29 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 17-44; 24-38; 28-45." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03445 GVNMYIRQIYDTCWKLKGHCRNVCGKKEIFHIFCGTQFLCCIERKEMPVLFVK 53 Beta-defensin 30 (BD-30, RBD-30; Defensin, beta 30; Rodents, mammals, animals) Q32ZG2 Belongs to the beta-defensin family Defb30 Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Anti-Gram- Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 13-40; 20-34; 24-41." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03446 RKRNTKFRQCEKMGGICKYQKTHGCSILPAECKSRYKHCCRL 42 Beta-defensin 33 (BD-33, RBD-33; Defensin, beta 33; Rodents, mammals, animals) Q32ZG1 Belongs to the beta-defensin family Defb33 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 10-39; 17-32; 25-40." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03447 MKISCFLLLVLSLSCFQINPFAVLDTRVCIEKRNTCHILQCPLFRDVVGTCFEGIGKCCHKYF 63 Beta-defensin 37 (Rodents, mammals, animals) Q32ZF9 Belongs to the beta-defensin family Defb37 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03448 TDQDTAKCVQKKNVCYYFECPWLSISVSTCYKGKAKCCQKRY 42 Beta-defensin 38 (BD-38, RBD-38; Defensin, beta 38; Rodents, mammals, animals) Q32ZF8 Belongs to the beta-defensin family Defb38 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 8-37; 15-30; 20-38." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03449 IDSVKCFQKNNTCHTIRCPYFQDEVGTCYEGRGKCCQKRLLSIRVPKKKV 50 Beta-defensin 39 (BD-39, RBD-39; Defensin, beta 39; Rodents, mammals, animals) Q32ZF7 Belongs to the beta-defensin family Defb39 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds 6-35; 13-28; 18-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03450 MKISCFLMLVLFLSCFQMNSGAGLDTMKCVRGKNNCHMHRCPWFFVLISTCYSGKGSCCQKRRWFTRSHVNNV 73 Beta-defensin 40 (Protein Defb40; rodents, mammals, animals) Q32ZF6 Belongs to the beta-defensin family Defb40 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03451 MRSHSFLSALFLLVMMMPRGKAGVVPGEKQCILLKGVCKDVSCTSTDDTIGVCNDEKKCCRRWWVFDPYPTPVPKGKSP 79 Beta-defensin 41 (Protein Defb41; rodents, mammals, animals) Q32ZF5 Belongs to the beta-defensin family Defb41 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03452 MRLYLLLSTLLFLLGLLPRVRSGLGAAETHCVNLQGICRRDICKLIEDEIGACRRRWKCCRLWWVLLPIPTPVIFSDYQEPLQTKMK 87 Beta-defensin 42 (Protein Defb42; rodents, mammals, animals) Q32ZF4 Belongs to the beta-defensin family Defb42 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03453 FLANQECFSEYRHCRMKCKANEYAIRYCADWTICCRVKKREAKKKIMW 48 Beta-defensin 43 (BD-43, RBD-43; Defensin, beta 43; Rodents, mammals, animals) Q32ZF3 Belongs to the beta-defensin family Defb43 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains two disulfide bonds 7-35; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03454 MDLHLLCLLLFLVTSLPEGYCVIGNSGVSFKPCTSEGGYCFFGCKLGWIWITYCNNIMSCCKKDTKHSLPQTKGV 75 Beta-defensin 44 (Protein Defb44; rodents, mammals, animals) Q32ZF2 Belongs to the beta-defensin family Defb44 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03455 MKLPVLFLLFCFLDLLKTVKAEMKDTLFCFLKKGKCRHVCMNVEKRVGPCTKLNANCCIFVRDMRAIIPEDQRTVSIKIRNKQN 84 Beta-defensin 49 (Protein Defb49; rodents, mammals, animals) Q32ZF1 Belongs to the beta-defensin family Defb49 Rattus norvegicus (Rat) Antimicrobial Homology Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03456 HPGTVHVRFKCIPKIAAVFGDNCPFYGNVDGLCNDKKSVCCMVPVRLDNI 50 Beta-defensin 50 (BD-50, RBD-50; Defensin, beta 50; Rodents, mammals, animals) Q30KJ2 Belongs to the beta-defensin family Defb50 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Bridge Not found "Function Has antibacterial activity (By similarity). PTM: Contains two disulfide bonds 11-40; 23-41." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15489334 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Genome Res. 2004 Oct;14(10B):2121-2127. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G.##Gerhard DS, Wagner L, et al. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03457 MRIHAFLALLAIFQVLHAITSALNFQRPCYLRGGICLKQGTPNCEPFRGPCRAFTVCCKIRS 62 Beta-defensin 51 (Protein Defb51; rodents, mammals, animals) Q32ZF0 Belongs to the beta-defensin family Defb51 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03458 MKLLYLLISVVLLISQVMAAPEGCKQEGQTEWKDFVRTKGAFIHFFNNDYGHHYCDSPTSVCLRRRTNCTRMPGLCPGRSFCCVRT 86 Beta-defensin 52 (Protein Defb52; rodents, mammals, animals) Q30KJ1 Belongs to the beta-defensin family Defb52 Rattus norvegicus (Rat) Antimicrobial Predicted Not found Not found Function Has antibacterial activity (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03459 GKNPTLQCMGNRGFCRPSCKKGEQAYFYCRTYQICCLQSHVRISLTGVEDNTNWSYEKHWPRIP 64 DEFB24 (defensin; Rodents, mammals, animals) No entry found Not found Not found Rattus norvegicus (Rat) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16457734 Reprod Biol Endocrinol. 2006 Feb 4;4:7. Yenugu S, Chintalgattu V, Wingard CJ, Radhakrishnan Y, French FS, Hall SH. Identification, cloning and functional characterization of novel beta-defensins in the rat (Rattus norvegicus). DRAMP03460 GGVKGAEKGVCPPDNVRCIRGEDPQCHNDNDCKDQKICCYWHCGFKCVQPVKDSWEQ 57 WAP four-disulfide core domain protein 12 (mammals, rodents, animals) Q6IE40 Not found Wfdc12 Rattus norvegicus (Rat) Antimicrobial, Antibacterial Homology Not found Not found PTM: Contains four disulfide bonds 11-39; 18-43; 26-38; 32-47 and one WAP Domain: (residue 4-51). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15057822##15060002 Genome sequence of the Brown Norway rat yields insights into mammalian evolution.##Genome Res. 2004 Apr;14(4):609-622. Gibbs R.A, Weinstock G.M, Metzker M.L, Muzny D.M, Sodergren E.J, et al, Collins F.S.##Puente XS, López-Otín C. Genome sequence of the Brown Norway rat yields insights into mammalian evolution.##A genomic analysis of rat proteases and protease inhibitors. DRAMP03461 LRDLKCFCRRKSCNWGEGIMGICKKRYGSPILCCR 35 Defensin 5 (Enteric defensin; RD-5; Rodents, mammals, animals) P82106 Belongs to the alpha-defensin family Not found Rattus norvegicus (Rat) Antimicrobial Transcript level Not found Not found "Function: Probably contributes to the antimicrobial barrier Function: of the small intestine. Tissue specificity: Small intestine. Not present in heart, liver, spleen, kidney, large intestine and colon. Induction: By hemorrhagic shock. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10456932 Infect Immun. 1999 Sep;67(9):4787-4793. Condon MR, Viera A, D'Alessio M, Diamond G. Induction of a rat enteric defensin gene by hemorrhagic shock. DRAMP03462 ATELEKALSNVIEVYHNYSGIKGNHHALYRDDFRKMVTTECPQFVQNKNTESLFKELDVNSDNAINFEEFLVLVIRVGVAAHKDSHKE 88 Protein S100-A8 (Calgranulin-A; MRP-8; Rodents, mammals, animals) P50115 Belongs to the S-100 family S100a8 Rattus norvegicus (Rat) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn2+ which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect. Miscellaneous: Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 21487906 Inflammation. 2012 Apr;35(2):409-419. Koike A, Arai S, Yamada S, Nagae A, Saita N, Itoh H, Uemoto S, Totani M, Ikemoto M. Dynamic mobility of immunological cells expressing S100A8 and S100A9 in vivo: a variety of functional roles of the two proteins as regulators in acute inflammatory reaction. DRAMP03466 PRGSPRTEYEAARR 14 Ribosome-inactivating protein luffacylin (rRNA N-glycosidase; Plants) P84073 Not found Not found Luffa cylindrica (Smooth loofah) (Sponge gourd) Antimicrobial, Antifungal Protein level Not found Not found "Function: Has antifungal activity against F. oxysporum and M. arachidicola. Inhibits cell-free translation in rabbit reticulocyte lysate system. Has some N-glycosidase activity. Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA." Fungi: Mycosphaerella arachidicola, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12126727 Peptides. 2002 Jun;23(6):1019-10124. Parkash A, Ng TB, Tso WW. Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds. DRAMP03468 GVCDMADLA 9 Alveolarin (Fungus) P84760 Not found Not found Polyporus alveolaris (Hexagonal-pored polypore) (Favolus alveolaris) Antimicrobial, Antifungal Protein level Not found Not found Function: Antifungal activity. Inhibits mycelial growth of F. cinera, F. oxysporum, M. arachidicola and P. piricola. Lacks protease, ribonuclease, deoxyribonuclease and hemagglutinating activity. Fungi: Botrytis cinerea, Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15165727 Peptides. 2004 Apr;25(4):693-696. Wang H, Ng TB, Liu Q. Alveolarin, a novel antifungal polypeptide from the wild mushroom Polyporus alveolaris. DRAMP03469 MDVVRTLILCVCLFGLTFA 19 Serine protease inhibitor Cvsi-1 (molluscs, animals) Q30HU9, P84574 Not found Not found Crassostrea virginica (Eastern oyster) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found "Function: Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A, perkinsin and trypsin with dissociation constants of 0.29 nM, 13.7 nM and 17.7 nM respectively. Not active against thermolysin, papain or pepsin. Has antiparasitic activity against the protozoan P. marinus. Tissue specificity: Detected in hemolymph (at protein level). In oysters collected in the summer the expression level is highest in the digestive gland with low levels of expression in gill, mantle, labial palp, style-sac midgut, gonad, heart, and hemocyte. In winter expression levels are higher in all tissues with highest expression levels observed in the digestive gland. Within the digestive gland expression is limited to the basophil cells of the digestive diverticula." Subtilisin A and Prochlorococcus marinus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16872855##19720077 Comp Biochem Physiol B Biochem Mol Biol. 2006 Sep;145(1):16-26.##Dev Comp Immunol. 2010 Jan;34(1):84-92. Xue QG, Waldrop GL, Schey KL, Itoh N, Ogawa M, Cooper RK, Losso JN, La Peyre JF.##La Peyre JF, Xue QG, Itoh N, Li Y, Cooper RK. A novel slow-tight binding serine protease inhibitor from eastern oyster (Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus.##Serine protease inhibitor cvSI-1 potential role in the eastern oyster host defense against the protozoan parasite Perkinsus marinus. DRAMP03470 GFGCPWNRYQCHSHCRSIGRLGGYCAGSLRLTCTCYRS 38 Defensin-1 (American oyster defensin, AOD; molluscs, animals) P85008 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Crassostrea virginica (American oyster) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found PTM: Contains three disulfide bond: 4-25; 11-33; 15-35. Gram-positive bacteria: Lactococcus lactis subsp. lactis (MECs=2.4 µg/ml), Staphylococcus aureus (MECs=3 µg/ml);##Gram-negative bacteria: Escherichia coli D31 (MECs=7.6 µg/ml), Vibrio parahaemolyticus (MECs=15 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16297885 Biochem Biophys Res Commun. 2005 Dec 30;338(4):1998-2004. Seo JK, Crawford JM, Stone KL, Noga EJ. Purification of a novel arthropod defensin from the American oyster, Crassostrea virginica. DRAMP03473 DNGEAGRAAR 10 Antimicrobial ribonuclease (Fungus) P84528 Not found Not found Pleurotus sajor-caju (Oyster mushroom) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has ribonuclease activity towards yeast tRNA and polyuracil and weak ribonuclease activity towards other polyhomoribonucleotides. Has weak deoxyribonuclease activity. Displays antimitogenic activity towards murine splenocytes and antiproliferative activity towards HepG2 hepatoma cells and L1210 leukemia cells. Biophysicochemical properties: pH dependence (Optimum pH is from 5.5 to 6.0); Temperature dependence (Optimum temperature below 60 degrees Celsius. Active from 0 to 100 degrees Celsius)." Bacteria: Pseudomonas aeruginosa, Pseudomonas fluorescens, Staphylococcus aureus.##Fungi: Fusarium oxysporum (IC50=95 µM), Mycosphaerella arachidicola (IC50=72 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15003351 Peptides. 2004 Jan;25(1):11-17. Ngai PH, Ng TB. A ribonuclease with antimicrobial, antimitogenic and antiproliferative activities from the edible mushroom Pleurotus sajor-caju. DRAMP03475 QCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQE 35 Vicilin-like Antimicrobial peptide 2a (MiAMP2a; Plant defensin) Q9SPL3 Belongs to the vicilin-like family AMP2-3 Macadamia integrifolia (Macadamia nut) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: (- Ca2+, + Ca2+): Clavibacter michiganensis (IC50=50, >50 µg/ml).##Fungi (- Ca2+, + Ca2+): Alternaria helianthi (IC50=5-10, ND µg/ml), Ceratocystis paradoxa (IC50=20-50, >50 µg/ml), Cercospora nicotianae (IC50=5-10, 5-10 µg/ml), Chalara elegans (IC50=2-5, 10-20 µg/ml), Fusarium oxysporum (IC50=10, 20-50 µg/ml), Leptosphaeria maculans (IC50=25, >50 µg/ml), Sclerotinia sclerotiorum (IC50=20-50, >50 µg/ml), Verticillium dahliae (IC50=5-10, >50 µg/ml), Saccharomyces cerevisiae (IC50=20-50, >50 µg/ml), Phytophthora cryptogea (IC50=5-10, 10-25 µg/ml), Phytophthora parasitica nicotianae (IC50=10-20, >50 µg/ml).##[NOTE:, Ca2+ = Medium with low content of CaCl2 (50 µM); + Ca2+ = Medium supplemented with high concentration of CaCl2 (1 mM)] No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10571855 Plant J. 1999 Sep;19(6):699-710. Marcus JP, Green JL, Goulter KC, Manners JM. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. DRAMP03476 ATRVVYCNRRSGSVVGGDDTVYYEG 25 Eryngin (mushroom, fungi) P84525 Not found Not found Pleurotus eryngii Antimicrobial, Antifungal Protein level Not found Not found Comment: No comments found on DRAMP database Fungi: Fusarium oxysporum, Mycosphaerella arachidicola. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15003349 Peptides. 2004 Jan;25(1):1-5. Wang H, Ng TB. Eryngin, a novel antifungal peptide from fruiting bodies of the edible mushroom Pleurotus eryngii. DRAMP03478 AGETHTVMINHAGRGAPKLVVGGKKLS 27 Ganodermin (Fungus) P84995 Not found Not found Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus) Antimicrobial, Antifungal Protein level Not found Not found Function: Has antifungal activity. Lacks hemagglutinating activity towards rabbit erythrocytes. Lacks deoxyribonuclease, ribonuclease and protease inhibitory activities. Fungi: Botrytis cinerea (IC50=15.2 µM), Fusarium oxysporum (IC50=12.4 µM), Physalospora piricola (IC50=18.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16039755 Peptides. 2006 Jan;27(1):27-30. Epub 2005 Jul 21. Wang H, Ng TB. Ganodermin, an antifungal protein from fruiting bodies of the medicinal mushroom Ganoderma lucidum DRAMP03479 WNPFKELERAGQRVRDAVISAAPAVATVGQAAAIARG 37 Bactericidin B-2 (Cecropin-like peptide B-2; Insects, animals) P14662 Belongs to the cecropin family Not found Manduca sexta (Tobacco hornworm) Antimicrobial, Antibacterial Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3143727 J Biol Chem. 1988 Dec 25;263(36):19424-19429. Dickinson L, Russell V, Dunn PE. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. DRAMP03480 WNPFKELERAGQRVRDAIISAGPAVATVGQAAAIARG 37 Bactericidin B-3 (Cecropin-like peptide B-3; Insects, animals) P14663 Belongs to the cecropin family Not found Manduca sexta (Tobacco hornworm) Antimicrobial, Antibacterial Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3143727 J Biol Chem. 1988 Dec 25;263(36):19424-19429. Dickinson L, Russell V, Dunn PE. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. DRAMP03481 WNPFKELERAGQRVRDAIISAAPAVATVGQAAAIARG 37 Bactericidin B-4 (Cecropin-like peptide B-4; Insects, animals) P14664 Belongs to the cecropin family Not found Manduca sexta (Tobacco hornworm) Antimicrobial, Antibacterial Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3143727 J Biol Chem. 1988 Dec 25;263(36):19424-19429. Dickinson L, Russell V, Dunn PE. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. DRAMP03482 MGSKVYYVLMLALSFYVVQLCAFPRNSVAFEKQHESLPHADYIVTQKTESHEKTTAEPKLPGRIWCQYEEVTEDAICQEHCIPKGYSYGLCISNTCSCI 99 Defensin-like protein 1 (Predicted; Insects, animals; Predicted) D1KRL1 Not found Def1 Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19909380 Insect Mol Biol. 2010 Feb;19(1):61-75. Pauchet Y, Wilkinson P, Vogel H, Nelson DR, Reynolds SE, Heckel DG, ffrench-Constant RH. Pyrosequencing the Manduca sexta larval midgut transcriptome: messages for digestion, detoxification and defence. DRAMP03483 MKSSMLLLVCVTFLVIVSSPQNGVLADKLIGSCVWGAVDYTSNCNAECVRRGLR 54 Defensin-like protein 2 (Predicted; Insects, animals) D1KRL2 Not found Def2 Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19909380 Insect Mol Biol. 2010 Feb;19(1):61-75. Pauchet Y, Wilkinson P, Vogel H, Nelson DR, Reynolds SE, Heckel DG, ffrench-Constant RH. Pyrosequencing the Manduca sexta larval midgut transcriptome: messages for digestion, detoxification and defence. DRAMP03484 MNTKLIIFLATLVILTDAYVVKSPKDLSSADSNALEKNSQSLLHATYDESLYIPMRVSSCSDGICDLGCKILGYPHGRCISANTCQCY 88 Defensin-like protein 3 (Predicted; Insects, animals; Predicted) D1KRL3 Not found Def3 Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19909380 Insect Mol Biol. 2010 Feb;19(1):61-75. Pauchet Y, Wilkinson P, Vogel H, Nelson DR, Reynolds SE, Heckel DG, ffrench-Constant RH. Pyrosequencing the Manduca sexta larval midgut transcriptome: messages for digestion, detoxification and defence. DRAMP03485 WNPFKELERAGQRVRDAVISAAAVATVGQAAAIARGG 37 Bactericidin B-5P (Cecropin-like peptide B-5; Insects, animals) P14665 Belongs to the cecropin family Not found Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) Antimicrobial, Antibacterial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3143727 J Biol Chem. 1988 Dec 25;263(36):19424-19429. Dickinson L, Russell V, Dunn PE. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. DRAMP03487 QRFSQPTFKLPQGRLTLSRKF 21 Lebocin Peptide 1A (LP1A; Insects, animals) No entry found Belongs to the cecropin family Not found Manduca sexta Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dev Comp Immunol. 2010 Jun;34(6):638-647. Rayaprolu S, Wang Y, Kanost MR, Hartson S, Jiang H. Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta. DRAMP03488 WDFLKELEGVGQRVRDSIISAGPAIDVLKKSQGPRRWSRP 40 Defense protein 4 (DFP-4; Insects, animals) Q5MGD8 Belongs to the cecropin family Not found Lonomia obliqua (Moth) Antimicrobial Homology Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16023793 Gene. 2005 Aug 1;355:11-27. Veiga AB, Ribeiro JM, Guimarães JA, Francischetti IM. A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome. DRAMP03489 LTVRAAQSFGRCNQKQCDADCVKKGYFGGLCTLTSCFCTGSRS 43 Defense protein 6 (DFP-6; Insects, animals) Q5MGC9 Belongs to the invertebrate defensin family Not found Lonomia obliqua (Moth) Antimicrobial Homology Not found Not found "Function: Has antibacterial activity (By similarity). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16023793 Gene. 2005 Aug 1;355:11-27. Veiga AB, Ribeiro JM, Guimarães JA, Francischetti IM. A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome. DRAMP03490 VFGTLGSTDDSLFGRYKQDIFNDHRGHLQGQAYGSR 36 Gloverin (Insects, animals) P86358 Not found Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial Protein level Not found Not found Function: Antibacterial protein (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2009) to UniProtKB Shelby KS. Unknown DRAMP03491 YDNVNLDEILANDRLLVPYIKCLLDEGKKAPDAKELKEHIRXAL 44 Viresin (Insects, animals) P86354 Not found Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found Function: Has antibacterial activity against the Gram-negative bacteria E. coli and E. cloacae, but not against the Gram-negative bacteria P. aeruginosa, P. vulgaris, K. pneumoniae and S. enteritidis or the Gram-positive bacteria S. aureus, S. epidermidis and S. salivarius. Gram-negative bacteria: E. coli K12 D31, E. coli and E. cloacae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651803 Eur J Biochem. 2000 Feb;267(3):677-683. Viresin. A novel antibacterial protein from immune hemolymph of Heliothis virescens pupae. Viresin. A novel antibacterial protein from immune hemolymph of Heliothis virescens pupae. DRAMP03492 DKLIGSCVWGAVNYTSDCNGECLLRGYKGGHCGSFANVNCWCET 44 Defensin heliomicin (Mutation: K23L, R24L) P81544 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Heliothis virescens (tobacco budworm) Antimicrobial, Antibacterial, Antifungal Protein level Combine helix and strand structure Not found 1I2V resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11580275 Biochemistry. 2001 Oct 9;40(40):11995-12003. Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. DRAMP03494 WKPFKKIEKAVRRVRDGVAKAGPAVAVVGQAT 32 Cecropin (Insects, animals) P83420 Not found Not found Oiketicus kirbyi (Bagworm moth) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Has also activity against fungi No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P. Unknown DRAMP03495 INNWVRVPPCDQVCSRTNPEKDECCRAHGHAFHATCSGGMQCYRR 45 Psychimicin (Insects, animals) P83421 Not found Not found Oiketicus kirbyi (Bagworm moth) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity. Is particularly active against fungi, and to a lesser extent against Gram-positive and Gram-negative bacteria. Tissue specificity: Hemolymph. PTM: Contains three disulfide bonds 10-24; 14-36; 25-42." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P. Unknown DRAMP03496 RWKVFKKIEKVGRNIRDGVIKAAPAIEVLGQAKAL 35 Cecropin-A (Insects, animals) P83413 Not found Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Has also activity against fungi. Tissue specificity: Hemolymph. Induction: By bacterial infection. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted JUL-2002 to the SWISS-PROT data bank. Bulet P, Lamberty M, Brookhart G, Bushey D. Unknown DRAMP03497 KWKVFKKIEKVGRNIRDGIVKAGPAIAVLGQAN 33 Cecropin-B (Insects, animals) P83414 Belongs to the cecropin family Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Has also activity against fungi. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB. Bulet P, Lamberty M, Brookhart G, Bushey D. Unknown DRAMP03498 RWKVFKKIEKMGRNIRDGVIKAAPAIEVLGQAK 33 Cecropin-C (Insects, animals) P83415 Belongs to the cecropin family Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Has also activity against fungi. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB. Bulet P, Lamberty M, Brookhart G, Bushey D. Unknown DRAMP03499 QRFIHPTYRPPPQPRRPVIMRA 22 Heliocin (Pro-rich; Insects, animals) P83427 Belongs to the lebocin family Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity, preferentially against Gram-negative bacteria. Tissue specificity: Hemolymph. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB. Bulet P, Lamberty M, Charlet M, Sabatier L, Rabel D. Unknown DRAMP03500 GKIPIGAIKKAGKAIGKGLRAVNIASTAHDVYTFFKPKKRH 41 Virescein (Insects, animals) P83416 Belongs to the moricin family Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has antibacterial activity against Gram-positive and Gram-negative bacteria. Tissue specificity: Hemolymph. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB. Bulet P, Lamberty M, Charlet M, Sabatier L, Rabel D. Unknown DRAMP03501 AIGCNTVASKMAPCLPYVTGKGPLGGCCGGVKGLIDAARTTPDRQAVCNCLKTLAKSYSGINLGNAAGLPGKCGVSIPYQISPNTDCSKVH 91 La-LTP (LJAFP; Insects, animals) Q52RN7 Not found Afp Leonurus japonicus (Chinese motherwort) (Leonurus artemisia) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). Gram-positive Bacteria: Bacillus subtilis (IC50>15 µM). ##Gram-negative Bacteria: Pseudomonas solanacearum (IC50=7.5-15 µM), Ralstonia solanacearum (IC50=15 µM).##Fungi: Alternaria alternate (IC50<7.5 µM), Alternaria brassicae (IC50<7.5 µM), Aspergillus niger (IC50<7.5 µM), Bipolaris maydis (IC50<7.5 µM), Botrytis cinerea (IC50=7.5-15 µM), Cerospora personata (IC50=7.5-15 µM), Colletotrichum gloeosporiodes (IC50<7.5 µM), Fusarium graminearum (IC50=7.5-15 µM), Fusarium oxysporum (IC50=7.5-15 µM), Penicillium digitatum (IC50>15 µM), Pyricularia grisea (IC50=7.5-15 µM), Rhizoctonia solani (IC50<7.5 µM), Rhizoctonia cerealis (IC50=7.5-15 µM), Saccharomyces cerevisiae (IC50>15 µM), Sclerotinia sclerotiorum (IC50>15 µM), Trichoderma harzianum (IC50=7.5-15 µM), Verticillium dahliae (IC50=7.5-15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding PubMed ID is not available Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Yang X, Xiao Y, Pei Y, Zhen C. LJAFP, a novel non-specific lipid transfer protein-like antimicrobial protein from motherwort (Leonurus japonicus) confers disease resistance against phytopathogenic fungi and bacterium in transgenic tobacco. DRAMP03502 RWKIFKKIERVGQNVRDGIIKAGPAIQVLGTAKAL 35 Hyphancin-3D (Hyphancin IIID; Cecropin-A; Insects, animals) P50720 Not found Not found Hyphantria cunea (Fall webworm moth) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted MAR-1995 to the EMBL GenBank DDBJ databases. Park SS, Shin SW, Kim MK, Park DS, Oh HW, Park HY. Differences in the skin peptides of the male and female Australian tree frog Litoria splendida. The discovery of the aquatic male sex pheromone splendipherin, together with Phe8 caerulein and the antibiotic peptide caerin 1.10. DRAMP03503 RWKFFKKIERVGQNVRDGLIKAGPAIQVLGAAKAL 35 Hyphancin-3E (Hyphancin IIIE; Cecropin-A1; Insects, animals) P50721 Not found Not found Hyphantria cunea (Fall webworm moth) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted MAR-1995 to the EMBL GenBank DDBJ databases. Park SS, Shin SW, Kim MK, Park DS, Oh HW, Park HY. Differences in the skin peptides of the male and female Australian tree frog Litoria splendida. The discovery of the aquatic male sex pheromone splendipherin, together with Phe8 caerulein and the antibiotic peptide caerin 1.10. DRAMP03504 RWKVFKKIEKVGRNIRDGVIKAGPAIAVVGQAKAL 35 Hyphancin-3F (Hyphancin IIIF; Cecropin-A2; Insects, animals) P50722 Not found Not found Hyphantria cunea (Fall webworm moth) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted MAR-1995 to the EMBL GenBank DDBJ databases. Park SS, Shin SW, Kim MK, Park DS, Oh HW, Park HY. Differences in the skin peptides of the male and female Australian tree frog Litoria splendida. The discovery of the aquatic male sex pheromone splendipherin, together with Phe8 caerulein and the antibiotic peptide caerin 1.10. DRAMP03505 RWKVFKKIEKVGRHIRDGVIKAGPAITVVGQATAL 35 Hyphancin-3G (Hyphancin IIIG; Cecropin-A3; Insects, animals) P50723 Not found Not found Hyphantria cunea (Fall webworm moth) Antimicrobial, Antibacterial Homology Not found Not found "Function: Has antibacterial activity. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted MAR-1995 to the EMBL GenBank DDBJ databases. Park SS, Shin SW, Kim MK, Park DS, Oh HW, Park HY. Differences in the skin peptides of the male and female Australian tree frog Litoria splendida. The discovery of the aquatic male sex pheromone splendipherin, together with Phe8 caerulein and the antibiotic peptide caerin 1.10. DRAMP03506 TPDHREVPSFSSRWEPNFGLTFSK 24 Attacin (Insects, animals) P86359 Belongs to the attacin/sarcotoxin-2 family Not found Heliothis virescens (Tobacco budworm moth) Antimicrobial, Antibacterial Protein level Not found Not found Function: Hemolymph antibacterial protein (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2009) to UniProtKB Shelby KS. Unknown DRAMP03508 DILRG 5 Yamamarin (Growth-suppressing pentapeptide; Plant defensin; Insects, animals) P84863 Not found Not found Antheraea yamamai (Japanese oak silkmoth) Unknown Protein level Not found Not found "Function: Suppresses growth in rat hepatoma cells and maintains diapause in insects. Developmental stage: Diapause. PTM: Diapausing first instar larvae contain both amidated and non-amidated forms." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not availbale##PubMed ID is not availbale J. Insect Biotechnol. Sericology. 2004;73:7-13.##J. Insect Biotechnol. Sericology. 2007;76:63-69. Yang P, Abe S, Zhao Y, An Y, Suzuki K.##Yang P, Abe S, Sato Y, Yamashita T, Matsuda F, Hamayasu T, Imai K, Suzuki K. Growth suppression of rat heptatoma cells by a pentapeptide from Antheraea yamamai.##A palmitonyl conjugate of an insect pentapeptide causes growth arrest in mammalian cells and mimics the action of diapause hormone. DRAMP03509 RWKFFKKIEKVGQNIRDGIIKAGPAVAVVGQAASIT 36 Cecropin-A (Insects, animals) P50724 Belongs to the cecropin family Not found Trichoplusia ni (Cabbage looper) Antimicrobial, Antibacterial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8882660 Insect Biochem Mol Biol. 1996 Feb;26(2):177-184. Kang D, Liu G, Gunne H, Steiner H. PCR differential display of immune gene expression in Trichoplusia ni. DRAMP02962 GRFRRLRKKTRKRLKKIGKVLKWIPPIVGSIPLGCG 36 PMAP-36 P49931 Belongs to the cathelicidin family PMAP36 Sus scrofa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix PMAP-36 contains a typical Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. Has hemolytic activity. [Ref.27251456] Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=2 μM, MBC=4 μM), Staphylococcus aureus 25923 (MIC=2 μM, MBC=4 μM), Staphylococcus epidermidis 12228 (MIC=2 μM, MBC=4 μM), Bacillus subtilis 63501 (MIC=1 μM, MBC=1 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=1 μM, MBC=4 μM), Escherichia coli EC183 (MIC=1 μM, MBC=1 μM), Escherichia coli 1005 (MIC=2 μM, MBC=2 μM), Salmonella typhimurium C77-31 (MIC=1 μM, MBC=2 μM);##Fungi: Candida albicans 2.2086 (MIC=128 μM, MFC=128 μM), Candida albicans CA276 (MIC=128 μM, MFC=128 μM), Candida tropicalis 2.1975 (MIC=1 μM, MFC=2 μM), Candida krusei 2.1857 (MIC=8 μM, MFC=8 μM). [Ref.27251456] 5% hemolysis at 4 µM, MHC=4 µM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27251456 Sci Rep. 2016 Jun 2;6:27258. Lyu Y, Yang Y, Lyu X, Dong N, Shan A. Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. DRAMP03511 KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL 35 Cecropin-B (Immune protein P9; Insects, animals) P01508 Belongs to the cecropin family Not found Hyalophora cecropia (Cecropia moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli D21 (MLC=0.32 µM), Escherichia coli D31 (MLC=0.32 µM), Serratia marcescens Db11 (MLC=4.5 µM), Serratia marcescens Db1108 (MLC=2.4 µM), Serratia marcescens Db1121 (MLC=2.2 µM), Serratia marcescens Strain 122 (MLC=2.9 µM), Pseudomonas aeruginosa OT97 (MLC=1.9 µM), Xenorhabdus nematophilus Xn21 (MLC=1.6 µM);##Gram-positive bacteria: Bacillus megaterium Bmll (MLC=0.44 µM), Bacillus subtilis Bs11 (MLC=18 µM), B.thuringiensis Bt11 (MLC>133 µM), Streptococcus fecalis AD-4 (MLC=7.3 µM), Streptococcus fecalis DS16 (MLC>24 µM), Micrococcus luteus M111 (MLC=1.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7140755 Eur J Biochem. 1982 Sep;127(1):207-217. Hultmark D, Engström A, Bennich H, Kapur R, Boman HG. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. DRAMP03512 WNPFKELEKVGQRVRDAVISAGPAVATVAQATALAK 36 Cecropin-D (Cecropin D; Insects, animals) P01510 Belongs to the cecropin family Not found Hyalophora cecropia (Cecropia moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli D21 (LC=0.43 µM), Escherichia coli D31 (LC=0.40 µM), Serratia marcescens Db11 (LC=14 µM), Serratia marcescens Db1108 (LC=12 µM), Serratia marcescens Db1121 (LC=12 µM), Strain 122 (LC=19 µM), Pseudomonas aeruginosa OT97 (LC=100 µM), Xenorhabdus nematophilus Xn21 (LC=19 µM);##Gram-positive bacteria: Bacillus megaterium Bmll (LC=41 µM), Bacillus subtilis Bs11 (LC>95 µM), B.thuringiensis Bt11 (LC>95 µM), Streptococcus fecalis AD-4 (LC>95 µM), Streptococcus fecalis DS16 (LC=88 µM), Micrococcus luteus M111 (LC=21 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7140755##1711035 Eur J Biochem. 1982 Sep;127(1):207-217.##J Biol Chem. 1991 Jun 25;266(18):11510-11517. Hultmark D, Engström A, Bennich H, Kapur R, Boman HG.##Gudmundsson GH, Lidholm DA, Asling B, Gan R, Boman HG. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae.##The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia. DRAMP03522 MKIAFIVAISLAFLAVTSCIEFEKSTESHDIQKRGVTITVKPPFPGCVFYECIANCRSRGYKNGGYCTINGCQCLR 76 Gallerimycin (defensins; Insects, animals) Q8MVY9 Not found Not found Galleria mellonella (Greater wax moth) Antimicrobial, Antifungal Predicted Not found Not found Comment: No comments found on DRAMP database Metarhizium anisopliae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12811766 Arch Insect Biochem Physiol. 2003 Jul;53(3):125-133. Schuhmann B, Seitz V, Vilcinskas A, Podsiadlowski L. Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response of greater wax moth larvae, Galleria mellonella. DRAMP03529 RWKLFKKIEKVGRNVRDGLIKAGPAIAVIGQAKSL 35 Cecropin-A (Insects, animals) Q27239 Belongs to the cecropin family CECA Bombyx mori (Silk moth) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Tissue specificity: Highest expression in fat body and hemocytes. Is also expressed in Malpighian tubules and to a much lesser extent in midgut. Not present in silk gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7765280 Biosci Biotechnol Biochem. 1994 Aug;58(8):1476-1478. Yamano Y, Matsumoto M, Inoue K, Kawabata T, Morishima I. Cloning of cDNAs for cecropins A and B, and expression of the genes in the silkworm, Bombyx mori. DRAMP03530 RWKIFKKIEKMGRNIRDGIVKAGPAIEVLGSAKAI 35 Cecropin-B (Lepidopteran-A/B; Insects, animals) P04142 Belongs to the cecropin family CECB1 and CECB2 Bombyx mori (Silk moth) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Tissue specificity: Highest expression in fat body and hemocytes. Is also expressed in Malpighian tubules and to a much lesser extent in midgut. Not present in silk gland. PTM: Lepidopteran-B differs from lepidopteran-A by its hydroxylated residue." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2184991##7765280 Comp. Biochem. Physiol. 1990; 95:551-554.##Biosci Biotechnol Biochem. 1994 Aug;58(8):1476-1478. Morishima I, Suginaka S, Ueno T, Hirano H.##Yamano Y, Matsumoto M, Inoue K, Kawabata T, Morishima I. Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori.##Cloning of cDNAs for cecropins A and B, and expression of the genes in the silkworm, Bombyx mori. DRAMP03531 GNFFKDLEKMGQRVRDAVISAAPAVDTLAKAKALGQ 36 Cecropin-D (Insects, animals) O76146 Belongs to the cecropin family CECD Bombyx mori (Silk moth) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10392453 Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):409-414. Yang J, Furukawa S, Sagisaka A, Ishibashi J, Taniai K, Shono T, Yamakawa M. cDNA cloning and gene expression of cecropin D, an antibacterial protein in the silkworm, Bombyx mori. DRAMP18208 VSTLSVSSPCPGWPSSFTWSNC 22 NAI-112(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Actinoplanes sp. Antimicrobial, Antibacterial, Antinociceptive, Antiallodynic, Anti-Gram+ Not found The structural data indicate that NAI-112 is a 22-aa, neutrally charged, glycosylated lanthipeptide containing N-terminal Lab and C-terminal MeLab residues separated by a 4-aa linker. It carries a 6-deoxyhexose moiety N-linked to a tryptophan residue. NAI-112 represents the ?rst occurrence of a lanthipeptide containing a MeLab and an N-glycosylation. NAI-112 and labyrinthopeptin A2 share a similar ring topology. Comment: No comments found on DRAMP database Gram-positive (modest) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24191663 ACS Chem Biol. 2014 Feb 21;9(2):398-404. Iorio M, Sasso O, Maffioli SI, Bertorelli R, Monciardini P, Sosio M, Bonezzi F, Summa M, Brunati C, Bordoni R, Corti G, Tarozzo G, Piomelli D, Reggiani A, Donadio S. A glycosylated, labionin-containing lanthipeptide with marked antinociceptive activity. DRAMP18207 ASGWVCTLTIECGTLVCAC 19 Actagardine B(Bacteriocin) No entry found Belongs to the lantibiotics family (Class I bacteriocin) Not found Actinoplanes liguriae NCIMB41362 Antimicrobial, Antibacterial, Anti-Gram+ Not found Actagardine, Ala(0)-actagardine, actagardine B, michiganin A, NAI-802 and Ala(0)-NAI-802 share three conserved thioether bridges within a core 19-aa peptide consisting of 14 invariant residues. Comment: No comments found on DRAMP database Gram-positive No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid II 23168402 J Antibiot (Tokyo). 2013 Feb;66(2):73-8. Simone M, Monciardini P, Gaspari E, Donadio S, Maffioli SI. Isolation and characterization of NAI-802, a new lantibiotic produced by two different Actinoplanes strains. DRAMP03534 PWNIFKEIERAVARTRDAVISAGPAVRTVAAATSVAS 37 Antibacterial peptide enbocin (Moricin; Insects, animals) P48821 Belongs to the cecropin family Not found Bombyx mori (Silk moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Homology Not found Not found Function: Has antibacterial activity against Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Bacillus subtilis, Bacillus thuringiensis, Staphyllococcus aureus;##Gram-negative bacteria: Psedomonas solanacearum, Salmonellar typhimurium, Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9610369 Biochem Biophys Res Commun. 1998 May 19;246(2):388-392. Kim SH, Park BS, Yun EY, Je YH, Woo SD, Kang SW, Kim KY, Kang SK. Cloning and expression of a novel gene encoding a new antibacterial peptide from silkworm, Bombyx mori. DRAMP03535 DLRFLYPRGKLPVPTPPPFNPKPIYIDMGNRY 32 Lebocin-1/2 (Pro-rich; Insects, animals) P54684 Belongs to the lebocin family Not found Bombyx mori (Silk moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Rich Not found "Function: Antibacterial peptide. Tissue specificity: Hemolymph. Produced in fat body. Induction: By bacterial infection. PTM: O-glycosylation is important for the antibacterial activity of lebocin, O-linked glycan structure is a disaccharide (Gal-GalNAc) in case of lebocin 1 and a monosaccharide (GalNAc) in case of lebocin 2." Gram-negative bacteria: Acinetobacter sp. NISL B-4653, Escherichia coli HB1ll, Pseudomonas fluorescens IAM1179;##Gram-positive bacterium: Staphylococcus aureus ATCC6538P. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7654207##7545395 Biochem J. 1995 Sep 1;310 (Pt 2):651-656.##Biochem Biophys Res Commun. 1995 Sep 5;214(1):271-278. Hara S, Yamakawa M.##Chowdhury S, Taniai K, Hara S, Kadono-Okuda K, Kato Y, Yamamoto M, Xu J, Choi SK, Debnath NC, Choi HK, et al. A novel antibacterial peptide family isolated from the silkworm, Bombyx mori.##cDNA cloning and gene expression of lebocin, a novel member of antibacterial peptides from the silkworm, Bombyx mori. DRAMP03536 DLRFLYPRGKLPVPTLPPFNPKPIYIDMGNRY 32 Lebocin-3 (LEB 3; Insects, animals) P55796 Belongs to the lebocin family LEB3 Bombyx mori (Silk moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found A unique threonine residue in each peptide was O-glycosylated and the modification seemed to be important for expression of antibacterial activity. Function: Antibacterial peptide. Gram-negative bacteria: Acinetobacter sp. NISL B-4653, Escherichia coli HB1ll, Pseudomonas fluorescens IAM1179;##Gram-positive bacterium: Staphylococcus aureus ATCC 6538P. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 7654207##9325165 Biochem J. 1995 Sep 1;310 (Pt 2):651-656.##Biochem Biophys Res Commun. 1997 Sep 29;238(3):769-774. Hara S, Yamakawa M.##Furukawa S, Taniai K, Ishibashi J, Hara S, Shono T, Yamakawa M. A novel antibacterial peptide family isolated from the silkworm, Bombyx mori.##A novel member of lebocin gene family from the silkworm, Bombyx mori. DRAMP03537 DLRFWNPREKLPLPTLPPFNPKPIYIDMGNRY 32 Lebocin-4 (Leb 4; Insects, animals) O15946 Belongs to the lebocin family LEB4 Bombyx mori (Silk moth) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial peptide. Tissue specificity: Hemolymph. Produced in fat body. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9325165 Biochem. Biophys. Res. Commun. 1997; 238:769-774 Furukawa S, Taniai K, Ishibashi J, Hara S, Shono T, Yamakawa M. A novel member of lebocin gene family from the silkworm, Bombyx mori. DRAMP03538 RWKIFKKIEKVGQNIRDGIVKAGPAVAVVGQAATI 35 Cecropin (Antibacterial peptide CM-IV; Insects, animals) P14666 Belongs to the cecropin family Not found Bombyx mori (Silk moth) Antimicrobial, Antibacterial Protein level Not found Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3318666 Annu Rev Microbiol. 1987;41:103-126. Boman HG, Hultmark D. Cell-free immunity in insects. DRAMP03541 KSKEKIGKEFKRIVQRIKDFLRNLVPR 27 Human KS-27 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17012259 FASEB J. 2006 Oct;20(12):2068-2080. Yamasaki K, Schauber J, Coda A, Lin H, Dorschner RA, Schechter NM, Bonnart C, Descargues P, Hovnanian A, Gallo RL. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. DRAMP03543 HSDAVFTDNYTRLRKQMAVKKYLNSILN 28 Vasoactive intestinal polypeptide (VIP; Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found 2RRH Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18603306 J Neuroimmunol. 2008 Aug 30;200(1-2):11-16. El Karim IA, Linden GJ, Orr DF, Lundy FT. Antimicrobial activity of neuropeptides against a range of micro-organisms from skin, oral, respiratory and gastrointestinal tract sites. DRAMP03544 ACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAF 37 Calcitonin gene-related peptide (CGRP; Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18603306 J Neuroimmunol. 2008 Aug 30;200(1-2):11-16. El Karim IA, Linden GJ, Orr DF, Lundy FT. Antimicrobial activity of neuropeptides against a range of micro-organisms from skin, oral, respiratory and gastrointestinal tract sites. DRAMP03545 RVIEVVQGACRAIRHIPRRIRQGLERIL 28 LLP Lentivirus lytic peptide (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9371339 Antimicrob Agents Chemother. 1997 Nov;41(11):2394-2398. Tencza SB, Douglass JP, Creighton DJ Jr, Montelaro RC, Mietzner TA. Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins. DRAMP03546 KQEGRDHDKSKGHFHMIVIHHKGGQAHHG 29 SgII peptide A (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18714013 J Immunol. 2008 Sep 1;181(5):3413-3421. Edström AM, Malm J, Frohm B, Martellini JA, Giwercman A, Mörgelin M, Cole AM, Sørensen OE. The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins. DRAMP03547 HNKQEGRDHDKSKGHFHRVVIHHKGGKAH 29 SgI-29 (85-113) (SgI-derived peptide; Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18314226 Peptides. 2008 Apr;29(4):505-511. Zhao H, Lee WH, Shen JH, Li H, Zhang Y. Identification of novel semenogelin I-derived antimicrobial peptide from liquefied human seminal plasma. DRAMP03548 RIAGYGLRGLAVIIRICIRGLNLIFEIIR 29 ELP (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9371339 Antimicrob Agents Chemother. 1997 Nov;41(11):2394-2398. Tencza SB, Douglass JP, Creighton DJ Jr, Montelaro RC, Mietzner TA. Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins. DRAMP03549 ALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 38 ALL-38 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found 2K6O Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12759353 J Biol Chem. 2003 Aug 1;278(31):28540-6. Sørensen OE, Gram L, Johnsen AH, Andersson E, Bangsbøll S, Tjabringa GS, Hiemstra PS, Malm J, Egesten A, Borregaard N. Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina. DRAMP03550 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA 42 Beta-amyloid peptide 42 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found 1IYT Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20209079 PLoS One. 2010 Mar 3;5(3):e9505. Soscia SJ, Kirby JE, Washicosky KJ, Tucker SM, Ingelsson M, Hyman B, Burton MA, Goldstein LE, Duong S, Tanzi RE, Moir RD. The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide. DRAMP03551 YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY 52 Adrenomedullin (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found 2L7S Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10225288 FEMS Immunol Med Microbiol. 1999 Apr;23(4):289-293. Allaker RP, Zihni C, Kapas S. An investigation into the antimicrobial effects of adrenomedullin on members of the skin, oral, respiratory tract and gut microflora. DRAMP03552 DIPEVVVSLAWDESLAPKHPGSRKNMDCYCRIPACIAGERRYGTCIYQGRLWAFCC 56 HP 3-56 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15616305 Antimicrob Agents Chemother. 2005 Jan;49(1):269-275. Ericksen B, Wu Z, Lu W, Lehrer RI. Antibacterial activity and specificity of the six human {alpha}-defensins. DRAMP03553 DIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC 56 HP 1-56 (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15616305 Antimicrob Agents Chemother. 2005 Jan;49(1):269-275. Ericksen B, Wu Z, Lu W, Lehrer RI. Antibacterial activity and specificity of the six human {alpha}-defensins. DRAMP03554 ASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKV 67 CCL20(1-67) (Human, mammals, animals) P78556 Belongs to the intercrine beta (chemokine CC) family CCL20 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge (2 disulfide bonds) Not found Function: Chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Possesses antibacterial activity E. coli ATCC 25922 and S. aureus ATCC 29213. Gram-negative bacterium: Escherichia coli ATCC 25922,##Gram-positive bacterium: Staphylococcus aureus ATCC 29213. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12149255 J Biol Chem. 2002 Oct 4;277(40):37647-54. Hoover DM, Boulegue C, Yang D, Oppenheim JJ, Tucker K, Lu W, Lubkowski J. The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins. DRAMP03555 SNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM 69 CCL20(2-70) (Human, mammals, animals) P78556 Belongs to the intercrine beta (chemokine CC) family CCL20 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge (2 disulfide bonds) Not found Function: Chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Possesses antibacterial activity E. coli ATCC 25922 and S. aureus ATCC 29213. Gram-negative bacterium: Escherichia coli ATCC 25922,##Gram-positive bacterium: Staphylococcus aureus ATCC 29213. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12149255 J Biol Chem. 2002 Oct 4;277(40):37647-54. Hoover DM, Boulegue C, Yang D, Oppenheim JJ, Tucker K, Lu W, Lubkowski J. The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins. DRAMP03556 ASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM 70 C-C motif chemokine 20 (Human, mammals, animals) P78556 Belongs to the intercrine beta (chemokine CC) family CCL20 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Possesses antibacterial activity E. coli ATCC 25922 and S. aureus ATCC 29213. Gram-negative bacterium: Escherichia coli ATCC 25922,##Gram-positive bacterium: Staphylococcus aureus ATCC 29213. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12149255 J Biol Chem. 2002 Oct 4;277(40):37647-54. Hoover DM, Boulegue C, Yang D, Oppenheim JJ, Tucker K, Lu W, Lubkowski J. The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins. DRAMP03557 GRDYRTCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPSTGPL 83 Granulysin (Lymphokine LAG-2; Human, mammals, animals) P22749 Not found GNLY Homo sapiens (Human) Antimicrobial, Antibacterial, Antifungal, Antiparasitic Protein level Alpha helix Not found 1L9L resolved by X-ray. "Function: Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis. Tissue specificity: Expressed in natural killer and T-cells. Induction: By T-cell growth factor and IL2/interleukin-2." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9756476##12488100 Science. 1998 Oct 2;282(5386):121-125.##J Mol Biol. 2003 Jan 10;325(2):355-365. Stenger S, Hanson DA, Teitelbaum R, Dewan P, Niazi KR, Froelich CJ, Ganz T, Thoma-Uszynski S, Melián A, Bogdan C, Porcelli SA, Bloom BR, Krensky AM, Modlin RL.##Anderson DH, Sawaya MR, Cascio D, Ernst W, Modlin R, Krensky A, Eisenberg D. An antimicrobial activity of cytolytic T cells mediated by granulysin.##Granulysin crystal structure and a structure-derived lytic mechanism. DRAMP03558 EAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES 70 human platelet factor 4 (hPF4; Human, mammals, animals) No entry found Belongs to the intercrine alpha (chemokine CxC) family Not found Homo sapiens (Human) Antiparasitic Not found Not found Not found Function: human platelet factor 4 (hPF4) kills malaria parasites inside erythrocytes by selectively lysing the parasite digestive vacuole (DV). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23245326 Cell Host Microbe. 2012 Dec 13;12(6):815-823. Love MS, Millholland MG, Mishra S, Kulkarni S, Freeman KB, Pan W, Kavash RW, Costanzo MJ, Jo H, Daly TM, Williams DR, Kowalska MA, Bergman LW, Poncz M, DeGrado WF, Sinnis P, Scott RW, Greenbaum DC. Platelet factor 4 activity against P. falciparum and its translation to nonpeptidic mimics as antimalarials. DRAMP03559 VPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKAIKNLLKAVSKERSKRSP 77 CXCL10 (Human, mammals, animals) P02778, Q96QJ5 Belongs to the intercrine alpha (chemokine CxC) family CXCL10 Homo sapiens (Human) Antimicrobial, Antibacterial, Antiparasitic Protein level Combine helix and beta structure Not found 1O80,1O7Z,1O7Y resolved by X-ray.##1LV9 resolved by NMR. Function: Chemotactic for monocytes and T-lymphocytes. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binds to CXCR3 12949249##12737818 J Leukoc Biol. 2003 Sep;74(3):448-455.##Structure. 2003 May;11(5):521-32. Yang D, Chen Q, Hoover DM, Staley P, Tucker KD, Lubkowski J, Oppenheim JJ.##Swaminathan GJ, Holloway DE, Colvin RA, Campanella GK, Papageorgiou AC, Luster AD, Acharya KR. Many chemokines including CCL20/MIP-3alpha display antimicrobial activity.##Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine. DRAMP03560 TELRCQCLQTLQGIHLKNIQSVKVKSPGPHCAQTEVIATLKNGQKACLNPASPMVKKIIEKMLKNGKSN 69 CXC chemokine GRObeta [5-73] (Human, mammals, animals) P19875 Belongs to the intercrine alpha (chemokine CxC) family CXCL2 Homo sapiens (Human) Antimicrobial, Antibacterial, Antiparasitic, Chemotactic Protein level Combine helix and beta structure GRObeta [5-73] forms a dimer in solution that is architectured by a six-stranded antiparallel beta-sheet (residues 25 to 29, 39 to 44, 49 to 52) and a pair of helices (residues 58 to 68) with 2-fold symmetry, while the C terminus of the protein is disordered.(Ref.2) 1QNK resolved by NMR. "Function: Produced by activated monocytes and neutrophils and expressed at sites of inflammation. Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. GRO-beta(5-73) shows a highly enhanced hematopoietic activity. PTM: The N-terminal processed form GRO-beta(5-73) is produced by proteolytic cleavage after secretion from bone marrow stromal cells. Pharmaceutical use: GRO-beta(5-73) is available under the name Garnocestim as immunomodulator. It is used prior to hematopoietic transplantation for peripheral blood stem cell mobilization and reduction of incidence, duration, and/or severity of chemotherapy induced cytopenias." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12949249##10600366 J Leukoc Biol. 2003 Sep;74(3):448-455.##J Mol Biol. 1999 Dec 17;294(5):1065-1072. Yang D, Chen Q, Hoover DM, Staley P, Tucker KD, Lubkowski J, Oppenheim JJ.##Qian YQ, Johanson KO, McDevitt P. Many chemokines including CCL20/MIP-3alpha display antimicrobial activity.##Nuclear magnetic resonance solution structure of truncated human GRObeta [5-73] and its structural comparison with CXC chemokine family members GROalpha and IL-8. DRAMP03561 GPVSAVLTELRCTCLRVTLRVNPKTIGKLQVFPAGPQCSKVEVVASLKNGKQVCLDPEAPFLKKVIQKILDSGNKKN 77 CXCL6 (C-X-C motif chemokine 6; Human, mammals, animals) P80162 Belongs to the intercrine alpha (chemokine CxC) family CXCL6 Homo sapiens (Human) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found Function: Chemotactic for neutrophil granulocytes. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Heparin-binding 18443119 Antimicrob Agents Chemother. 2008 Jul;52(7):2599-2607. Linge HM, Collin M, Nordenfelt P, Mörgelin M, Malmsten M, Egesten A. The human CXC chemokine granulocyte chemotactic protein 2 (GCP-2)/CXCL6 possesses membrane-disrupting properties and is antibacterial. DRAMP03564 ICIFCCGCCHRSKCGMCCKT 20 Human hepcidin-20 (Hepc20; one chain of Hepcidin; Human, mammals, animals) P81172, Q1HE14, Q9BY68 Not found HAMP Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand Not found 1M4E resolved by NMR. "Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa. Tissue specificity: Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine. PTM: Contains four disulfide bonds 2-18; 5-17; 6-14; 8-9." Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Staphylococcus aureus, S. epidermidis, group B Streptococcus.##Fungi: Candida albicans, Aspergillus fumigatus, Aspergillus niger. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11113131##12138110##11034317 J Biol Chem. 2001 Mar 16;276(11):7806-7810.##J Biol Chem. 2002 Oct 4;277(40):37597-37603.##FEBS Lett. 2000 Sep 1;480(2-3):147-150. Park CH, Valore EV, Waring AJ, Ganz T.##Hunter HN, Fulton DB, Ganz T, Vogel HJ.##Krause A et al Adermann K. Hepcidin, a urinary antimicrobial peptide synthesized in the liver.##The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.##LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. ref2) Hepcidin, a rinary antimicrobial peptide synthesized in the liver. DRAMP03565 DTHFPICIFCCGCCHRSKCGMCCKT 25 Human hepcidin-25 (Hepc25; one chain of Hepcidin; Human, mammals, animals) P81172, Q1HE14, Q9BY68 Not found HAMP Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Beta strand N-terminus is a metal-binding site. disulfide bonds are essential for antibacterial activity by probably binding to DNA. 1M4F, 2KEF resolved by NMR.##3H0T resolved by X-ray. "PTM: Contains four disulfide bonds 7-22; 10-13; 11-19; 14-22. Tissue specificity: Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine. Function: It showed antimicrobial activities in vitro, this peptide might be the long-sought hormone that regulates iron homeostasis in humans. A pathogen will survive if it can figure out a way to steal iron from the host." Gram-negative bacterium: Escherichia coli;##Gram-positive bacteria: Staphylococcus aureus, S. epidermidis, group B Streptococcus.##Fungi: Candida albicans, Aspergillus fumigatus, Aspergillus niger. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet DNA 11034317##11113131##12138110##19553669 FEBS Lett. 2000 Sep 1;480(2-3):147-150.##J Biol Chem. 2001 Mar 16;276(11):7806-7810.##J Biol Chem. 2002 Oct 4;277(40):37597-37603.##J Biol Chem. 2009 Sep 4;284(36):24155-24167. Krause A et al Adermann K.##Park CH, Valore EV, Waring AJ, Ganz T.##Hunter HN, Fulton DB, Ganz T, Vogel HJ.##Jordan JB, Poppe L, Haniu M, Arvedson T, Syed R, Li V, Kohno H, Kim H, Schnier PD, Harvey TS, Miranda LP, Cheetham J, Sasu BJ. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. ref2) Hepcidin, a rinary antimicrobial peptide synthesized in the liver.##Hepcidin, a urinary antimicrobial peptide synthesized in the liver.##The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.##Hepcidin revisited, disulfide connectivity, dynamics, and structure. DRAMP03566 MHDFWVLWVLLEYIYNSACSVLSATSSVSSRVLNRSLQVKVVKITN 46 Salvic (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J Hard Tissue Biol 2005; 14: 258-260. Kim YS et al Chung SI. Cloning and identification of a new antimicrobial peptide, salvic, from human salivary gland. DRAMP03572 FALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 39 Antibacterial protein FALL-39 (one chain of hCAP-18; Human, mammals, animals) P49913, Q71SN9 Belongs to the cathelicidin family CAMP Homo sapiens (Human) Antimicrobial, Antibacterial Protein level Alpha helix Not found 2K6O "Function: Has antibacterial activity. Tissue specificity: Expressed in bone marrow and testis and neutrophils. PTM: The N-terminus is blocked." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 7529412##8681941 Proc Natl Acad Sci U S A. 1995 Jan 3;92(1):195-199.##Eur J Biochem. 1996 Jun 1;238(2):325-332. Agerberth B, Gunne H, Odeberg J, Kogner P, Boman HG, Gudmundsson GH.##Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.##The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. DRAMP03576 DSHEKRHHGYRRKFHEKHHSHREFPFYGDYGSNYLYDN 38 Histatin-1 (His-rich; Human, mammals, animals) P15515 Not found HTN1 Homo sapiens (Human) Antimicrobial, Antifungal Protein level Rich Not found PTM: Phosphoserine at position 2; And Sulfotyrosine at position 27,30,34,36. Yeast: Candida albicans (99.5±0.5 % inhibition at 54 nmol). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3286634 J Biol Chem. 1988 Jun 5;263(16):7472-7477 Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, Troxler RF. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. DRAMP03577 RKFHEKHHSHREFPFYGDYGSNYLYDN 27 Histatin-2 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found HTN3 Homo sapiens (Human) Antimicrobial, Antifungal Protein level Rich Not found An autoproteolytic product from Histatin 1 but not phosphorylated (Lal et al. 1992 Arch Oral Bio 37: 7-13). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1528633 Oral Microbiol Immunol 1992; 7: 127-128. Xu L, Lal K, Pollock JJ. Histatins 2 and 4 are autoproteolytic degradation products of human parotid saliva. DRAMP03578 DSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN 32 Histatin-3 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Antifungal Protein level Rich Not found Comment: No comments found on DRAMP database Yeast: Candida albicans (98.5±0.5 % inhibition at 54 nmol) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3286634 J Biol Chem. 1988 Jun 5;263(16):7472-7477 Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, Troxler RF1988 Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. DRAMP03579 RKFHEKHHSHRGYRSNYLYDN 21 Histatin-4 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Protein level Rich Not found An autoproteolytic product from Histatin 3. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1528633 Oral Microbiol Immunol 1992; 7: 127-128. Xu L, Lal K, Pollock JJ. Histatins 2 and 4 are autoproteolytic degradation products of human parotid saliva. DRAMP03580 DSHAKRHHGYKRKFHEKHHSHRGY 24 His3-(20-43)-peptide (Histatin 5; derivatives: Dh-5; Clinical) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Antifungal Protein level Alpha helix Not found Histatin 5 is a proteolytic product of histatin 3. The active Domain: of histitin 5 (Dh-5) corresponding to residues 11-24 showed HIV inhibitory effects. However,the results with the Dh-5 mutants are mixed (Groot et al. 2006 J. Virol. 80: 9236-9243). The sequence of Dhvar4 is KRLFKKLLFSLRKY, a helical peptide which is active against bacteria and fungi. Dhvar5 has a sequence LLLFLLKKRKKRKY, which is active against bacteria and fungi (Ruissen AL et al 2002 Peptides 23:1391-9). P-113 is a 12-residue active peptide corresponding to residues 4-15 of histatin 5 (Rothstein DM et al. 2001 AAC 45: 1367). The His-His sequence is a good ligand for Cu2+ (Kulon K et al. 2008 J Inorg Biochem 102: 960-72). Derivatives were subjected to clinical trials. Yeast: Candida albicans (100% inhibition at 54 nmol), Cryptococcus neoformans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding (Zinc) 3286634 J Biol Chem. 1988 Jun 5;263(16):7472-7477. Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, Troxler RF. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. DRAMP03581 DSHAKRHHGYKRKFHEKHHSHRGYR 25 Histatin 6 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Protein level Rich Not found An autoproteolytic product from Histatin 3. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J Dent Res 1990; 69: 2-6. Troxler RF et al Oppenheim FG. Structural relation between human salivary histatins. DRAMP03582 RKFHEKHHSHRGY 13 Histatin 7 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Protein level Rich Not found An autoproteolytic product from Histatin 3 (residues 12-24). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available J Dent Res 1990; 69: 2-6. Troxler RF et al Oppenheim FG. Structural relation between human salivary histatins. DRAMP03583 KFHEKHHSHRGY 12 Histatin 8 (His-rich; Human, mammals, animals) P15516, Q16243, Q502Z1 Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Antifungal Protein level Rich Not found It is the fragment of histatin 5. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12711380 Arch Oral Biol 2003 May;48(5):361-368. Yin A, Margolis HC, Grogan J, Yao Y, Troxler RF, Oppenheim FG. Physical parameters of hydroxyapatite adsorption and effect on candidacidal activity of histatins. DRAMP03584 RKFHEKHHSHRGYR 14 Histatin 9 (His-rich; Also detected are Histatin 10; Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antifungal Not found Rich Not found An autoproteolytic product from Histatin 3 (residues 12-25). Histatin 12=residues 5-10; histatin 11=residues 5-11; Histatin 10=residues 13-25. Antimicrobial activities of Histatins 10-12 are Comment: No comments found on DRAMP databasen. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Oral Microbiol Immunol 1992; 7: 127-128. Xu L, Lal K, Pollock JJ. Histatins 2 and 4 are autoproteolytic degradation products of human parotid saliva. DRAMP03585 AELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDES 68 Human TC-1 (Chain of Platelet basic protein; Human, mammals, animals) P02775, B2R5F3, Q6IBJ8 Not found PPBP Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Not found 1TVX resolved by X-ray. PTM: Contains two disulfide bonds 5-31; 7-46. Gram-positive bacteria: Bacillus subtilis (MBC=0.4 µM), Staphylococcus aureus (MBC=6.8 µM);##Gram-negative bacterium: Escherichia coli (MBC=3.4 µM).##Fungi: Cryptococcus neoformans (MFC=1.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10877842##8034022 J Biol Chem. 2000 Jul 7;275(27):20374-20381.##FEBS Lett. 1994 Jun 27;347(2-3):300-303. Krijgsveld J, Zaat SA, Meeldijk J, van Veelen PA, Fang G, Poolman B, Brandt E, Ehlert JE, Kuijpers AJ, Engbers GH, Feijen J, Dankert J.##Kungl AJ, Machius M, Huber R, Schwer C, Lam C, Aschauer H, Ehn G, Lindley IJ, Auer M. Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines.##Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2). DRAMP03586 NLAKGKEESLDSDLYAELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDES 83 Human TC-2 (Chain of Platelet basic protein; Human, mammals, animals) P02775, B2R5F3, Q6IBJ8 Not found PPBP Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine helix and strand structure Not found 1F9P resolved by X-ray. PTM: Contains two disulfide bonds 19-46; 22-62. Gram-positive bacteria: Bacillus subtilis ATCC6633 (MBC=0.7 µM), Staphylococcus aureus 42D (MBC=11 µM);##Gram-negative bacterium: Escherichia coli ML35 (MBC=2.7 µM).##Fungi: Cryptococcus neoformans (MFC=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10877842##8034022 J Biol Chem. 2000 Jul 7;275(27):20374-20381.##FEBS Lett. 1994 Jun 27;347(2-3):300-303. Krijgsveld J, Zaat SA, Meeldijk J, van Veelen PA, Fang G, Poolman B, Brandt E, Ehlert JE, Kuijpers AJ, Engbers GH, Feijen J, Dankert J.##Kungl AJ, Machius M, Huber R, Schwer C, Lam C, Aschauer H, Ehn G, Lindley IJ, Auer M. Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines.##Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2). DRAMP03587 SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSV 47 DCD-1 (chain of Dermcidin; Human, mammals, animals) P81605, A5JHP2, A5JHP3, P58461, Q53YJ2 Not found DCD Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Proteolytic Protein level Alpha helix Structural analysis of dermcidin-1L in 50% TFE using an N15-labeled recombinant peptide reveals a long helix-hinge-helix motif, allowing it to associate with bacterial membranes (Jung et al. 2010 BMB Rep. 43: 362-8). 2KSG resolved by NMR.##2YMK resolved by X-ray. "Function: DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity. Survival-promoting peptide promotes survival of neurons and displays phosphatase activity. Catalytic activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. Cofactor: Manganese. Required for survival-promoting peptide. Tissue specificity: Specifically and constitutively expressed in eccrine sweat gland cells. Secreted into the sweat at a concentration of 1-10 micrograms/ml." Gram-negative bacteria: Escherichia coli, Enterococcus faecalis;##Gram-positive bacterium: Staphylococcus aureus.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet May bind IgG 11694882##17448443##20510021 Nat Immunol. 2001 Dec;2(12):1133-1137.##Biochem Biophys Res Commun. 2007 Jun 15;357(4):828-833.##BMB Rep. 2010 May;43(5):362-368. Schittek B, Hipfel R, Sauer B, Bauer J, Kalbacher H, Stevanovic S, Schirle M, Schroeder K, Blin N, Meier F, Rassner G, Garbe C.##Lee Motoyama JP, Kim-Motoyama H, Kim P, Nakagama H, Miyagawa K, Suzuki K.##Jung HH, Yang ST, Sim JY, Lee S, Lee JY, Kim HH, Shin SY, Kim JI. Dermcidin: a novel human antibiotic peptide secreted by sweat glands.##Identification of dermcidin in human gestational tissue and characterization of its proteolytic activity.##Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles. DRAMP03588 LAHQKPFIRKSYKCLHKRCR 20 Human MUC7 20-Mer (Human, mammals, animals) No entry found Not found Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Function: MUC7 20-mer showes potent activity against a variety of fungi, including C. albicans, C. glabrata, C. krusei, C. neoformans, and S. cerevisae. In addition, it is also active against several drug-resistant strains, including azole-resistant C. albicans, fluconazole-resistant C. glabrata, and amphotericin B-resistant C. neoformans. Gram-positive bacteria: Streptococcus mutans (EC50=1.39 µM), Streptococcus gordonii (EC50=2.43 µM);##Gram-negative bacteria: Escherichia coli (EC50=1.61 µM), Pseudomonas aeruginosa (EC50=4.41 µM), Porphyromonas gingivalis (EC50<1 µM).##Fungi: Candida albicans (DIS) (EC50=5.85 µM), C. albicans (azole resistant) (EC50=2.40 µM), Candida glabrata (EC50=5.02 µM), C. glabrata (fluconazole resistant) (EC50=12.3 µM), Candida krusei (EC50=5.16 µM), Cryptococcus neoformans (EC50=4.05 µM), Cryptococcus neoformans (amphotericin B resistant) (EC50=4.29 µM), Saccharomyces cerevisiae (EC50=5.23 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12543672 Antimicrob Agents Chemother 2003 Feb;47(2):643-652. Bobek LA, Situ H. MUC7 20-Mer: Investigation of Antimicrobial Activity, Secondary Structure, and Possible Mechanism of Antifungal Action. DRAMP03589 VKEGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRPYPEPGWEAKCPGSSSTRCPQK 88 WAP four-disulfide core domain protein 12 (Putative protease inhibitor WAP12; Human, mammals, ani Q8WWY7, Q5H980, Q9BR31 Not found WFDC12 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11779191 Biochem Biophys Res Commun. 2002 Jan 11;290(1):452-456. Lundwall A, Clauss A. Identification of a novel protease inhibitor gene that is highly expressed in the prostate. DRAMP03590 VAIALKAAHYHTHKE 15 Calcitermin (Human, mammals, animals) P80511, P83219, Q5SY66 Belongs to the S-101 family S100A12 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Alpha helix Not found "Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Possesses antifungal activity against C. albicans and is also active against E. coli and P. aeruginosa but not L. monocytogenes and S. aureus. Tissue specificity: Predominantly expressed by neutrophils, monocytes and activated macrophages. Expressed by eosinophils and macrophages in asthmatic airways in regions where mast cells accumulate. Found in high concentrations in the serum of patients suffering from various inflammatory disorders, such as rheumatoid arthritis, psoriatic arthritis, Crohn's disease, ulcerative colitis, and Kawasaki disease. Domain: The hinge Domain: contributes significantly to its chemotactic properties." Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa.##Yeast: Candida albicans at pH 5.4. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11522286 FEBS Lett. 2001 Aug 24;504(1-2):5-10. Cole AM, Kim YH, Tahk S, Hong T, Weis P, Waring AJ, Ganz T. Calcitermin, a novel antimicrobial peptide isolated from human airway secretions. DRAMP03591 ACYCRIPACIAGERRYGTCIYQGRLWAFCC 30 Neutrophil defensin 1 (Defensin, alpha 1; HNP-1, HP-1; Human, mammals, animals) P59665, P11479, Q14125, Q6EZF6 Belongs to the alpha-defensin family DEFA1, DEFA1B Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand Compared to HNP-2, HNP-1 contains one additional residue (Ala) at the N-terminus. It contains a long stretch of a double-stranded antiparallel beta-sheet in a hairpin conformation that contains a beta-bulge, a short region of triple-stranded beta-sheet, and several tight turns. 2KHT resolved by NMR "Function: Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. PTM: ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production. Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-rybosylation." [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM));SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(67% inbibition at 50 μg/mL);SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(58% inbibition at 50 μg/mL).##[Ref.15616305] Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=3.6±0.3 μg/ml), E. coli ATCC 25922 (vLD50=3.7±0.4 μg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=10±0.5 μg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=4.2±1.0 μg/ml), Staphylococcus aureus ATCC 29213 (vLD50=2.1±0.3 μg/ml), Bacillus cereus ATCC 10876 (vLD50=0.22±0.03 μg/ml).##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s).##[Ref.15118082]Gram-positive bacteria: Bacillus subtilis (Inhibition zone=24 mm in PH5.5, Inhibition zone=20 mm in PH7.5 completely inhibit at 10 μg/well), Staphylococcus aureus (Inhibition zone=1 mm in PH5.5, Inhibition zone=7 mm incompletely inhibit and Inhibition zone=2 mm completely inhibit in PH7.5 at 10 μg/well);##Gram-negative bacteria: Escherichia coli (Inhibition zone=5 mm incompletely inhibit and Inhibition zone=2 mm completely inhibit in PH7.5 at 10 μg/well);##Fungi: Candida albicans (Inhibition zone=13 mm in PH5.5, Inhibition zone=10 mm in PH7.5 completely inhibit at 10 μg/well). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys2 and Cys30). Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29. L [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL. Not found 34206990##19253295##15616305##15118082 Viruses. 2021 Jun 26;13(7):1246.##Proteomics. 2009 Mar;9(5):1364-1373.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275.##Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Stegemann C, Kolobov A Jr, Leonova YF, Knappe D, Shamova O, Ovchinnikova TV, Kokryakov VN, Hoffmann R.##Ericksen B, Wu Z, Lu W, Lehrer RI.##Yount NY, Yeaman MR. Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Isolation, purification and de novo sequencing of TBD-1, the first beta-defensin from leukocytes of reptiles.##Antibacterial activity and specificity of the six human {alpha}-defensins.##Multidimensional signatures in antimicrobial peptides. DRAMP03592 CYCRIPACIAGERRYGTCIYQGRLWAFCC 29 Neutrophil defensin 2 (HNP-2, HP-2, HP2; Human, mammals, animals) P59665, P11479, Q14125, Q6EZF6, P59666, P11479, Q14125 Belongs to the alpha-defensin family DEFA1 AND DEFA1B Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand Not found 1ZMH, 1ZMI, 1ZMK resolved by X-ray. "Function: Defensin 2 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. PTM: Contains three disulfide bonds 1-29; 3-18; 8-28." [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM)).##Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=3.5±0.79 µg/ml), E. coli ATCC 25922 (vLD50=3.5±0.6 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=16±4.0 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=4.2±0.9 µg/ml), S. aureus ATCC 29213 (vLD50=2.4±0.3 µg/ml), Bacillus cereus ATCC 10876 (vLD50=0.22±0.04 µg/ml).(Ref.2)##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys1 and Cys29,Cys3 and Cys18,Cys8 and Cys28. L No cytotoxicity information found in the reference(s) presented Not found 34206990##15616305##15894545 Viruses. 2021 Jun 26;13(7):1246.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275.##J Biol Chem. 2005 Sep 23;280(38):32921-9. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Ericksen B, Wu Z, Lu W, Lehrer RI.##Xie C, Prahl A, Ericksen B, Wu Z, Zeng P, Li X, Lu WY, Lubkowski J, Lu W. Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Antibacterial activity and specificity of the six human {alpha}-defensins.##Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. DRAMP03593 DCYCRIPACIAGERRYGTCIYQGRLWAFCC 30 Neutrophil defensin 3 (Defensin, alpha 3; HNP-3, HP-3, HP3; Human, mammals, animals) P59666, P11479, Q14125 Belongs to the alpha-defensin family DEFA3 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand Compared to HNP-2, HNP-3 contains one additional residue (Asp) at the N-terminus. The 3D structures remain the same. 1DFN, 2PM4, 2PM5 resolved by X-ray. "Function: Defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. PTM: Contains three disulfide bonds 2-30; 4-19; 9-29." [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(approximately 50% inbibition at 1 μg/mL (290 nM)).##Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=6.2±0.9 µg/ml), E. coli ATCC 25922 (vLD50=5.9±2.1 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=41±9.2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=13±2.1 µg/ml), S. aureus ATCC 29213 (vLD50=2.2±0.4 µg/ml), Bacillus cereus ATCC 10876 (vLD50=0.37±0.08 µg/ml).(Ref.2)##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys2 and Cys30). Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29. L No cytotoxicity information found in the reference(s) presented Not found 34206990##4056036##15616305 Viruses. 2021 Jun 26;13(7):1246.##J Clin Invest. 1985 Oct;76(4):1436-1439.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Selsted ME, Harwig SS, Ganz T, Schilling JW, Lehrer RI.##Ericksen B, Wu Z, Lu W, Lehrer RI. Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Primary structures of three human neutrophil defensins.##Antibacterial activity and specificity of the six human {alpha}-defensins. DRAMP03594 VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV 33 Neutrophil defensin 4 (Defensin, alpha 4; HNP-4, HP-4; Human, mammals, animals) P12838 Belongs to the alpha-defensin family DEFA4 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand Compared to HNP-2, HNP-1 contains one additional residue (Ala) at the N-terminus. It contains a long stretch of a double-stranded antiparallel beta-sheet in a hairpin conformation that contains a beta-bulge, a short region of triple-stranded beta-sheet, and several tight turns. 1ZMM resolved by X-ray. "Function: Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). In comparison with HNP1-3, inhibition of both strains of HIV-1 by HNP4 was noticeably stronger as evidenced by lower IC50 values (2-5 µM) and steeper and more complete inhibition curves. PTM: Contains three disulfide bonds 2-30; 4-19; 9-29." [Ref.34206990]Virus:showed inhibition against SARS-CoV-2.Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=3.3±0.4 µg/ml), E. coli ATCC 25922 (vLD50=3.0±0.7 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=6.6±0.2 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=7.3±1.4 µg/ml), S. aureus ATCC 29213 (vLD50=7.2±0.2 µg/ml), Bacillus cereus ATCC 10876 (vLD50=0.87±0.08 µg/ml).(Ref.4)##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s).##Yeast: Candida albicans ATCC 99788 amphotericin B resistant (IC90>100 µg/ml).(Ref.2) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29. L No cytotoxicity information found in the reference(s) presented Not found 34206990##17088326##15620707##15616305 Viruses. 2021 Jun 26;13(7):1246.##Protein Sci. 2006 Dec;15(12):2749-2760.##FEBS Lett. 2005 Jan 3;579(1):162-166.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Szyk A, Wu Z, Tucker K, Yang D, Lu W, Lubkowski J.##Wu Z, Cocchi F, Gentles D, Ericksen B, Lubkowski J, Devico A, Lehrer RI, Lu W.##Ericksen B, Wu Z, Lu W, Lehrer RI. Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Crystal structures of human alpha-defensins HNP4, HD5, and HD6.##Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro.##Antibacterial activity and specificity of the six human {alpha}-defensins. DRAMP03595 ATCYCRTGRCATRESLSGVCEISGRLYRLCCR 32 Human defensin-5 (HD-5; Defensin, alpha 5; Human, mammals, animals) Q01523, A0JDY6, Q3KNV2 Belongs to the alpha-defensin family DEFA5 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand The L- and D-forms of HD-5 are equally active than E.coli but not S. aureus (Wei G et al 2009 JBC 284: 29180-92). 1ZMP resolved by X-ray. "Function: Antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing. Tissue specificity: Paneth cells of the small intestine (at protein level). PTM: Contains three disulfide bonds." [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(60% inhibition at 12.5 μg/mL (3.45 μM));SARS-CoV-2 variant P.1:inhibition of infection in HeLa-hACE2 cells(72% inbibition at 50 μg/mL);SARS-CoV-2 variant B.1.1.7:inhibition of infection in HeLa-hACE2 cells(32% inbibition at 50 μg/mL).##Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=2.5±0.3 µg/ml), E. coli ATCC 25922 (vLD50=2.1±0.9 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=5.5±0.5 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=6.3±0.5 µg/ml), S. aureus ATCC 29213 (vLD50=3.2±0.3 µg/ml), Bacillus cereus ATCC 10876 (vLD50<0.31 µg/ml).(Ref.2)##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s). [Ref.26206286] It has 0% hemolysis at 100μM against human red blood cells. Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL. Not found 34206990##12021776##15616305##26206286 Viruses. 2021 Jun 26;13(7):1246.##Nat Immunol. 2002 Jun;3(6):583-590.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275.##Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Ghosh D, Porter E, Shen B, Lee SK, Wilk D, Drazba J, Yadav SP, Crabb JW, Ganz T, Bevins CL.##Ericksen B, Wu Z, Lu W, Lehrer RI.##Basil Mathew Ramakrishnan Nagaraj Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Paneth cell trypsin is the processing enzyme for human defensin-5.##Antibacterial activity and specificity of the six human {alpha}-defensins.##Antimicrobial activity of human -defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP03596 AFTCHCRRSCYSTEYSYGTCTVMGINHRFCCL 32 Human defensin-6 (HD-6; Defensin, alpha 6; Human, mammals, animals) Q01524 Belongs to the alpha-defensin family DEFA6 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2) Protein level Beta strand (3 strands; 19 residues) Not found 1ZMQ, 3QTE resolved by X-ray. "Function: Has very low antimicrobial activity against Gram-negative and Gram-positive bacteria. May protect cells against infection with HIV-1. Subunit structure: Homodimer. Tissue specificity: Paneth cells of the small intestine. PTM: Contains three disulfide bonds." [Ref.34206990]Virus:SARS-CoV-2:inhibition of infection in HEK293T-hACE2 cells(HD6 only blocked SARS-CoV-2 infection at the highest concentration tested (50 μg/mL, 13 μM)).##Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50>256 µg/ml), E. coli ATCC 25922 (vLD50=103±14 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=156±11 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50>256 µg/ml), S. aureus ATCC 29213 (vLD50>256 µg/ml), Bacillus cereus ATCC 10876 (vLD50=25±13 µg/ml).(Ref.3)##NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys4 and Cys31,Cys6 and Cys20,Cys10 and Cys30. L [Ref.34206990]No cytotoxicity on HEK293T cells up to 50 μg/mL. Not found 34206990##8417977##17088326##15616305 Viruses. 2021 Jun 26;13(7):1246.##FEBS Lett. 1993; 315:187-192.##Protein Sci. 2006 Dec;15(12):2749-2760.##Antimicrob Agents Chemother. 2005 Jan;49(1):269-275. Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.##Jones DE, Bevins CL.##Szyk A, Wu Z, Tucker K, Yang D, Lu W, Lubkowski J.##Ericksen B, Wu Z, Lu W, Lehrer RI. Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.##Defensin-6 mRNA in human Paneth cells: implications for antimicrobial peptides in host defense of the human bowel.##Crystal structures of human alpha-defensins HNP4, HD5, and HD6.##Antibacterial activity and specificity of the six human {alpha}-defensins. DRAMP03601 WYVKKCLNDVGICKKKCKPEEMHVKNGWAMCGKGRDCCVPAD 42 Human beta-defensin 26 (hBD-26; hBD26; Human, mammals, animals) No entry found Belongs to the beta-defensin family Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram- Not found Bridge Not found Function: Both hBD26 and hBD27 showe salt-sensitive antimicrobial activity against gram-negative E. coli but not against gram-positive S. aureus and S. cerevisiae. Gram-negative bacterium: Escherichia coli K12. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19373462 Appl Microbiol Biotechnol. 2009 Aug;84(2):301-308. Huang L, Leong SS, Jiang R. Soluble fusion expression and characterization of bioactive human beta-defensin 26 and 27. DRAMP03602 QLKKCWNNYVQGHCRKICRVNEVPEALCENGRYCCLNIKELEAC 44 Human beta-defensin 27 (hBD-27; hBD27; Human, mammals, animals) No entry found Belongs to the beta-defensin family Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram- Not found Bridge Not found Function: Both hBD26 and hBD27 showe salt-sensitive antimicrobial activity against gram-negative E. coli but not against gram-positive S. aureus and S. cerevisiae. Gram-negative bacterium: Escherichia coli K12. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19373462 Appl Microbiol Biotechnol. 2009 Aug;84(2):301-308. Huang L, Leong SS, Jiang R. Soluble fusion expression and characterization of bioactive human beta-defensin 26 and 27. DRAMP18202 LIGSLFRGAKAIFRGARQGWRSHKAVSRYRARYVRRPVIYYHRVYP 46 WB Piscidin 5 (fish, animals) E3UVF7(Precursor) Belongs to the defensin family Not found Morone chrysops Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic Not found Not found No more comments Staphylococcus aureus ATCC 29213(MIC 4.52uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 27552222 PLoS One. 11(8):e0159423(2016) Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes. DRAMP18203 SYVGDCGSNGGSCVSSYCPYGNRLNYFCPLGRTCCRRSY 39 Panusin (beta defensins; crustaceans, arthropods, invertebrates, animals) A0A0S2XGP2(Precursor) Belongs to the beta-defensin family Not found the Caribbean spiny lobster, Panulirus genus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Function: Active against E. coli, K. pneumonia, S. aureus, B. subtilisspizizenii, and C. albicans. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 27616720 Dev Comp Immunol. pii: S0145-305X(16)30274-9(2016) Montero-Alejo V, Corzo G, Porro-Suard Panusin represents a new family of beta-defensin-like peptides in invertebrates. DRAMP18200 FFGRLKSMWRGARGGLKAYKYQKDMAKMNKRYGPNWQQGGGQEPPADAQANDQPP 55 SB Piscidin 6 (fish, animals) No entry found Belongs to the defensin family Not found Morone saxatilis Antimicrobial, Antibacterial, Anti-Gram+, Antiparasitic Not found Not found No more comments Staphylococcus aureus ATCC 29213(MIC >32.11uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 27552222 PLoS One. 11(8):e0159423(2016) Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes. DRAMP18201 LFGSVKAWFKGAKKGFQDYRYQKDMAKMNKRYGPNWQQRGGQEPPADAQANDQPP 55 WB Piscidin 6 (fish, animals) No entry found Belongs to the defensin family Not found Morone chrysops Antimicrobial, Antibacterial, Anti-Gram+, Antiparasitic Not found Not found No more comments Staphylococcus aureus ATCC 29213(MIC >31.59uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 27552222 PLoS One. 11(8):e0159423(2016) Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes. DRAMP03606 AIHRALISKRMEGHCEAECLTFEVKIGGCRAELAPFCCKNRKKH 44 Beta-defensin 107 (Defensin, beta 107; Beta-defensin 7, BD-7; Human, mammals, animals) Q8IZN7, B2RPM1, Q30E75, Q8NET2 Belongs to the beta-defensin family DEFB107A AND DEFB107 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. Tissue specificity: Specifically expressed in testis. PTM: Problely contains two disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16421571##12734011##11854508 Nature. 2006 Jan 19;439(7074):331-335.##Genome Biol. 2003;4(5):R31.##Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-2133. Nusbaum C, Mikkelsen TS, Zody MC, et al, Lander ES.##Semple CA, Rolfe M, Dorin JR.##Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr. DNA sequence and analysis of human chromosome 8.##Duplication and selection in the evolution of primate beta-defensin genes.##Discovery of five conserved beta-defensin gene clusters using a computational search strategy. DRAMP03607 KFKEICERPNGSCRDFCLETEIHVGRCLNSRPCCLPLGHQPRIESTTPKKD 51 Putative beta-defensin 108A (Defensin, beta 108A; Human, mammals, animals) A8MXU0 Belongs to the beta-defensin family DEFB108P1 AND DEFB10 Homo sapiens (Human) Antimicrobial, Antibacterial Not found Bridge Not found "Function: Has antibacterial activity. PTM: Problely contains three disulfide bonds 6-33; 13-27; 17-34." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16421571##12734011 Nature. 2006 Jan 19;439(7074):331-335.##Genome Biol. 2003;4(5):R31. Nusbaum C, Mikkelsen TS, Zody MC, et al, Lander ES.##Semple CA, Rolfe M, Dorin JR. DNA sequence and analysis of human chromosome 8.##Duplication and selection in the evolution of primate beta-defensin genes. DRAMP03608 KFKEICERPNGSCRDFCLETEIHVGRCLNSQPCCLPLGHQPRIESTTPKKD 51 Beta-defensin 108B (Beta-defensin 8; hBD-8; Defensin, beta 108B; Human, mammals, animals) Q8NET1 Belongs to the beta-defensin family DEFB108B Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11854508 Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-2133. Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr. Discovery of five conserved beta-defensin gene clusters using a computational search strategy. DRAMP03610 GLGPAEGHCLNLFGVCRTDVCNIVEDQIGACRRRMKCCRAWWILMPIPTPLIMSDYQEPLKPNLK 65 Beta-defensin 109 (Defensin, beta 109; Defensin, beta 109; Human, mammals, animals) Q30KR1 Belongs to the beta-defensin family DEFB109P1 AND DEFB10 Homo sapiens (Human) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03611 KKKYPEYGSLDLRRECRIGNGQCKNQCHENEIRIAYCIRPGTHCCLQQ 48 Beta-defensin 110 (Beta-defensin 10, DEFB-10; Defensin, beta 110; Human, mammals, animals) Q30KQ9, Q30KR0 Belongs to the beta-defensin family DEFB110 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Antiparasitic Transcript level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03612 GPSVPQKKTREVAERKRECQLVRGACKPECNSWEYVYYYCNVNPCCAVWEYQKPIINKITSKLHQK 66 Beta-defensin 113 (Beta-defensin 13, DEFB-13; Defensin, beta 113; Human, mammals, animals) Q30KQ7 Belongs to the beta-defensin family DEFB113 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03613 DRCTKRYGRCKRDCLESEKQIDICSLPRKICCTEKLYEEDDMF 43 Beta-defensin 114 (Beta-defensin 14, DEFB-14; Defensin, beta 114; Human, mammals, animals) Q30KQ6, Q8NES9 Belongs to the beta-defensin family DEFB114 Homo sapiens (Human) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##11854508 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-33. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G.##Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Discovery of five conserved beta-defensin gene clusters using a computational search strategy. DRAMP03614 QTAPDGWIRRCYYGTGRCRKSCKEIERKKEKCGEKHICCVPKEKDKLSHIHDQKETSELYI 61 Beta-defensin 115 (Beta-defensin 15, DEFB-15; Defensin, beta 115; Human, mammals, animals) Q30KQ5 Belongs to the beta-defensin family DEFB115 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##11780052 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Nature. 2001 Dec 20-27;414(6866):865-871. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G.##Deloukas P, Matthews LH, Ashurst J, Burton J, et al, Rogers J. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The DNA sequence and comparative analysis of human chromosome 20. DRAMP18199 CEWYNISCQLGNKGQWCTLTKECQRSCK 28 Formicin (Bacteriocin;lantibiotic;Gram-positive bacteria, prokaryotes; U No entry found Belongs to the lantibiotic family (Class I bacteriocin) Not found Bacillus paralicheniformis APC 1576 Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Function: Active against a broad spectrum of Gram+ bacteria (e.g., L. s delbrueckii subsp. bulgaricus; L. amylophilus; L. lactis; M. luteus; S. smutans), including clinical strains S. aureus, C. difficile, and L. monocytogenes. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27450592 Microbiology. 162(9):1662-1671(2016) Collins FW, O'Connor PM, O'Sullivan O, Rea MC, Hill C, Ross RP Formicin - a novel broad-spectrum two-component lantibiotic produced by Bacillus paralicheniformis APC 1576. DRAMP03616 AYSGEKKCWNRSGHCRKQCKDGEAVKDTCKNLRACCIPSNEDH 43 Beta-defensin 118 (Beta-defensin 18, DEFB-18; Defensin, beta 118; Human, mammals, animals) Q96PH6, Q17RC4, Q8N691, Q9NUH0 Belongs to the beta-defensin family DEFB118 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. Tissue specificity: High-level and epididymis-specific expression. Most abundant in the epithelium of the caput and is also present in the lumen and bound to sperm. Expressed also in pancreas. PTM: Contains three disulfide bonds 8-35; 15-29; 19-36." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11564719##12600824 Endocrinology. 2001 Oct;142(10):4529-4539.##Am J Respir Cell Mol Biol. 2003 Jul;29(1):71-80. Liu Q, Hamil KG, Sivashanmugam P, Grossman G, Soundararajan R, Rao AJ, Richardson RT, Zhang YL, O'Rand MG, Petrusz P, French FS, Hall SH.##Kao CY, Chen Y, Zhao YH, Wu R. Primate epididymis-specific proteins: characterization of ESC42, a novel protein containing a trefoil-like motif in monkey and human.##ORFeome-based search of airway epithelial cell-specific novel human [beta]-defensin genes. DRAMP03617 KRHILRCMGNSGICRASCKKNEQPYLYCRNCQSCCLQSYMRISISGKEENTDWSYEKQWPRLP 63 Beta-defensin 119 (Beta-defensin 19, DEFB-19; Defensin, beta 119; Human, mammals, animals) Q8N690, Q5GRG1, Q5JWP1, Q5TH42, Q8N689 Belongs to the beta-defensin family DEFB119 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11854508 Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-2133. Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr. Discovery of five conserved beta-defensin gene clusters using a computational search strategy. DRAMP03618 QVTPVMKCWGKSGRCRTTCKESEVYYILCKTEAKCCVDPKYVPVKPKLTDTNTSLESTSAV 61 Beta-defensin 121 (Beta-defensin 21, DEFB-21; Defensin, beta 121; Human, mammals, animals) Q5J5C9, A1L4N1 Belongs to the beta-defensin family DEFB121 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11780052##15489334 Nature. 2001 Dec 20-27;414(6866):865-871.##Genome Res. 2004 Oct;14(10B):2121-2127. Deloukas P, Matthews LH, Ashurst J, Burton J, et al, Rogers J.##Gerhard DS, Wagner L, Feingold EA, Shenmen CM, et al, Malek J. The DNA sequence and comparative analysis of human chromosome 20.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP18120 PPTQNPSMAPPTQNPYGQPMTPPTQNPYGQPMAPP 35 BnPRP1 (Plant defensin) No entry found BnPRP1 Brassica napus Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Not found Not found BnPRP1 has 40.5% identity with a known proline-rich antimicrobial peptide SP-B from the pig. BnPRP1 isolated from B. napus was the first PR-AMP member that was characterized in plants, and its homology sequences were found in some other Brassicaceae plants by the genome sequences analysis. Gram-positive: M. luteus (MIC= 16.9 ± 2.7 uM );##Gram-negative: E. coli (MIC= 8.4 ± 1.4 uM);## Fungi:Sclerotinia sclerotiorum, Mucor sp., Magnaporthe oryzae and Botrytis cinerea No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26383098 PLoS One. 2015 Sep 18;10(9):e0137414. Cao H, Ke T, Liu R, et al. Identification of a Novel Proline-Rich Antimicrobial Peptide from Brassica napus. DRAMP18198 GFGSKPLDSFGLNFF 15 Chaxapeptin A0A0F7VRL1 Not found ls3A sle2_130 Streptomyces leeuwenhoekii Strain C58 Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Not found Not found 2N5C resolved by NMR Function: Active against Gram-positive strains, S. aureus and B. subtilis (MIC 30-35 ug/mL), and no activity against the Gram-negative bacteria. It also showed dose dependent inhibition of A549 cancer cells. S. aureus and B. subtilis (MIC 30-35 ug/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26402731 J Org Chem.80(20):10252-60(2015) Elsayed SS, Trusch F, Deng H, Raab A, Prokes I, Busarakam K, Asenjo JA, Andrews BA, van West P, Bull AT, Goodfellow M, Yi Y, Ebel R, Jaspars M, Rateb ME. Chaxapeptin, a Lasso Peptide from Extremotolerant Streptomyces leeuwenhoekii Strain C58 from the Hyperarid Atacama Desert. DRAMP03620 EFKRCWKGQGACQTYCTRQETYMHLCPDASLCCLSYALKPPPVPKHEYE 49 Beta-defensin 124 (Beta-defensin 24, DEFB-24; Defensin, beta 124; Human, mammals, animals) Q8NES8, Q30E74 Belongs to the beta-defensin family DEFB124 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##11854508##11780052 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-2133.##Nature. 2001 Dec 20-27;414(6866):865-871. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G.##Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr.##Deloukas P, Matthews LH, Ashurst J, Burton J, et al, Rogers J. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##Discovery of five conserved beta-defensin gene clusters using a computational search strategy.##The DNA sequence and comparative analysis of human chromosome 20. DRAMP03621 SFEPQKCWKNNVGHCRRRCLDTERYILLCRNKLSCCISIISHEYTRR 47 Beta-defensin 125 (Beta-defensin 25, DEFB-25; Defensin, beta 125; Human, mammals, animals) Q8N687, A1A502, Q7Z7B9 Belongs to the beta-defensin family DEFB125 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11854508##11780052##12975309 Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2129-2133.##Nature. 2001 Dec 20-27;414(6866):865-871.##Genome Res. 2003 Oct;13(10):2265-2270. Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB Jr.##Deloukas P, Matthews LH, Ashurst J, Burton J, et al, Rogers J.##Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, et al, Gray A. Discovery of five conserved beta-defensin gene clusters using a computational search strategy.##The DNA sequence and comparative analysis of human chromosome 20.##The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. DRAMP03624 ARLKKCFNKVTGYCRKKCKVGERYEIGCLSGKLCCANDEEEKKHVSFKKPHQHSGEKLSVLQDYIILPTITIFTV 75 Beta-defensin 128 (Beta-defensin 28, DEFB-28; Defensin, beta 128; Human, mammals, animals) Q7Z7B8, B2RU29 Belongs to the beta-defensin family DEFB128 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11780052##15489334 Nature. 2001 Dec 20-27;414(6866):865-871.##Genome Res. 2004 Oct;14(10B):2121-2127. Deloukas P, Matthews LH, Ashurst J, Burton J, et al, Rogers J.##Gerhard DS, Wagner L, Feingold EA, Shenmen CM, et al, Malek J. The DNA sequence and comparative analysis of human chromosome 20.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03626 FISNDECPSEYYHCRLKCNADEHAIRYCADFSICCKLKIIEIDGQKKW 48 Beta-defensin 131 (Beta-defensin 31, DEFB-31; Defensin, beta 131; Human, mammals, animals) P59861 Belongs to the beta-defensin family DEFB131 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). Tissue specificity: Highly expressed in testis. Is moderately expressed in the prostate and small intestine. PTM: Contains three disulfide bonds 7-34; 14-28; 18-35 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12600824##15815621 Am J Respir Cell Mol Biol. 2003 Jul;29(1):71-80.##Nature. 2005 Apr 7;434(7034):724-731. Kao CY, Chen Y, Zhao YH, Wu R.##Kremitzki C, Oddy L, Du H, et al, Wilson R.K. ORFeome-based search of airway epithelial cell-specific novel human [beta]-defensin genes.##Generation and annotation of the DNA sequences of human chromosomes 2 and 4. DRAMP03627 GGSKCVSNTPGYCRTCCHWGETALFMCNASRKCCISYSFLPKPDLPQLIGNHWQSRRRNTQRKDKKQQTTVTS 73 Beta-defensin 132 (Defensin, beta 132; Beta-defensin 32, BD-32; Human, mammals, animals) Q7Z7B7, B2RP72, Q4QY40 Belongs to the beta-defensin family DEFB132 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12620395 Genomics. 2003 Feb;81(2):175-183. Rodriguez-Jimenez FJ, Krause A, Schulz S, Forssmann WG, Conejo-Garcia JR, Schreeb R, Motzkus D. Distribution of new human beta-defensin genes clustered on chromosome 20 in functionally different segments of epididymis. DRAMP03628 AVKDTYSCFIMRGKCRHECHDFEKPIGFCTKLNANCYM 38 Beta-defensin 133 (Defensin, beta 133; Human, mammals, animals) Q30KQ1, Q4QY39 Belongs to the beta-defensin family DEFB133 Homo sapiens (Human) Antimicrobial, Antibacterial Transcript level Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains two disulfide bonds 8-36; 15-29." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03629 GINSLSSEMHKKCYKNGICRLECYESEMLVAYCMFQLECCVKGNPAP 47 Beta-defensin 134 (Defensin, beta 134; Human, mammals, animals) Q4QY38, A1L4A4 Belongs to the beta-defensin family DEFB134 Homo sapiens (Human) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##15489334 Physiol Genomics. 2005 Sep 21;23(1):5-17.##Genome Res. 2004 Oct;14(10B):2121-7. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G.##Gerhard DS, Wagner L, Feingold EA, Shenmen CM, et al, Malek J. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract.##The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). DRAMP03630 GPNVYIQKIFASCWRLQGTCRPKCLKNEQYRILCDTIHLCCVNPKYLPILTGK 53 Beta-defensin 135 (Defensin, beta 135; Human, mammals, animals) Q30KP9, Q4QY37 Belongs to the beta-defensin family DEFB135 Homo sapiens (Human) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP03631 MFGNDGVKVRTCTSQKAVCFFGCPPGYRWIAFCHNILSCCKNMTRFQPPQAKDPWVH 57 Beta-defensin 136 (Defensin, beta 136; Human, mammals, animals) Q30KP8, Q4QY36 Belongs to the beta-defensin family DEFB136 Homo sapiens (Human) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has antibacterial activity (Potential). PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865 Physiol Genomics. 2005 Sep 21;23(1):5-17. Patil AA, Cai Y, Sang Y, Blecha F, Zhang G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. DRAMP18140 VARGWKRKCPLFGKGG 16 VG16KRKP No entry found Synthetic construct Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram- Synthetic The solution-NMR structure of VG16KRKP in lipopolysaccharide features a folded conformation with a centrally located turn-type structure stabilized by aromatic-aromatic packing interactions with extended N- and C-termini. 2MXG,2MXH resolved by NMR VG16KRKP is capable of inhibiting bacterial disease progression in plants. Gram-negative: E. coli (MIC=8 uM), X. campestris (MIC=10 uM), X. oryzae (MIC=15 uM);##Gram-positive: B. subtilis (MIC=50 uM);##Fungi: Candida albicans (MIC=2 uM), Cryptococcus grubii (MIC=5 uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrane 26144972 Sci Rep. 2015 Jul 6;5:11951. Datta A, Ghosh A, Airoldi C, etal. Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control DRAMP18195 MKTILRFVAGYDIASHKKKTGGYPWERGKA 30 LsbB (Bacteriocin) Q7X2B5 Not found lsbB Lactococcus lactis subsp. lactis (Streptococcus lactis) Antimicrobial, Antibacterial alpha helical Structure determination by NMR spectroscopy showed that LsbB has an N-terminal alpha helix, whereas the C-terminal of the molecule remains unstructured. 2MLU, 2MLV resolved by NMR The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain. Alanine substitution revealed that the tryptophan in position 25 (Trp25) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin.  targeting primarily lactococcal cells No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12801935##24993828 J. Biol. Chem. 278:34291-34298(2003).##J. Biol. Chem. 289:23838-23845(2014) Gajic O., Buist G., Kojic M., Topisirovic L., Kuipers O.P., Kok J.##Ovchinnikov K.V., Kristiansen P.E., Uzelac G., Topisirovic L.,Kojic M., Nissen-Meyer J., Nes I.F., Diep D.B. Novel mechanism of bacteriocin secretion and immunity carried out bylactococcal multidrug resistance proteins.##Defining the structure and receptor binding domain of the leaderlessbacteriocin LsbB. DRAMP03633 MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE 93 Protein S100-A8 (Calgranulin-A; MRP-8; Human, mammals, animals) P05109, A8K5L3, D3DV37, Q5SY70, Q9UC84, Q9UC92, Q9UCJ0, Q9UCM6 Belongs to the S-100 family S100A8 Homo sapiens (Human) Antimicrobial, Antibacterial, Antifungal Protein level Combine helix and strand structure The dimeric form of MRP8 is stabilized by hydrophobic interactions between mutually wrapped helices. There are two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) is stronger than that of the N-terminal EF-hand (EF-1)]. 1MR8 resolved by X-ray. "Function: Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn2+ which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect. Tissue specificity: Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Miscellaneous: Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Metal-binding 3313057##10771424 Nature. 1987 Nov 5-11;330(6143):80-82.##Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):559-566. Odink K, Cerletti N, Brüggen J, Clerc RG, Tarcsay L, Zwadlo G, Gerhards G, Schlegel R, Sorg C.##Ishikawa K, Nakagawa A, Tanaka I, Suzuki M, Nishihira J. Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis.##The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution. DRAMP18194 GGLKKLGKKLEGAGKRVFKASEKALPVVVGIKAIGK 36 AAEL000598-PA Q17NR1 Not found CECD Aedes aegypti (Yellowfever mosquito) (Culex aegypti) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- alpha helical (N-terminal) The structure of Aedesin is depicted as a helix-bent-helix structure with good RMSD statistics for the N-terminal helix (helix 1) and for the C-terminal helix (helix 2) taken separately.The helical wheel diagram of Aedesin shows the amphipathic character of the first and second aloha helices, as well as the opposite localization of their hydrophobic and positively charged residues, respectively. 2MMM resolved by NMR. The anti-bacterial activity of Aedesin was found to be salt-resistant, indicating that it is active under physiological conditions encountered in body fluids characterized by ionic salt concentrations. Gram-negative (including drug-resistent): E. coli (MIC 2-4 ug/mL), P. aeruginosa (MIC 1-4 ug/mL), A. baumannii (MIC 1-2 ug/mL), K. pneunomiae (MIC 1-2 ug/mL).##No antibacterial effects of the peptide were observed against different isolates of Gram-positive S. aureus, E. faecalis and E. faecium strains showing MIC values over 32. (Pubmed:25162372) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17510324##25162372 Science 316:1718-1723(2007).##PLoS ONE 9:e105441-e105441(2014). Nene V., Wortman J.R., Lawson D., et al.##Godreuil S., Leban N., Padilla A., et al. Genome sequence of Aedes aegypti, a major arbovirus vector.##Aedesin: structure and antimicrobial activity against multidrugresistant bacterial strains. DRAMP03635 GRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA 48 Human lactoferricin (LfcinH; one chain of Lactotransferrin; Human, mammals, animals) P02788, B7Z4X2, E7EQH5, O00756, Q16780, Q16785, Q16786, Q16789, Q8IU92 Belongs to the transferrin family LTF Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix LfcinH shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. 1Z6V, 1Z6W resolved by NMR. "Function: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. Tissue specificity: High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine." Gram-negative bacterium: Escherichia coli serotype O111. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15155221##16048952 Antimicrob Agents Chemother. 2004 Jun;48(6):2190-2198.##Antimicrob Agents Chemother. 2005 Aug;49(8):3387-3395. Chapple DS, Hussain R, Joannou CL, Hancock RE, Odell E, Evans RW, Siligardi G.##Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ. Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide.##Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. DRAMP03636 FFSASCVPGADKGQFPNLCRLCAGTGENKCA 31 Kaliocin-1 (one chain of Lactotransferrin; Human, mammals, animals) P02788, B7Z4X2, E7EQH5, O00756, Q16780, Q16785, Q16786, Q16789, Q8IU92 Belongs to the transferrin family LTF Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes without causing extensive damage to the outer and inner bacterial membranes. Tissue specificity: High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine." Gram-negative bacterium: Escherichia coli serotype O111. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12693969 Biochemistry (Mosc). 2003 Feb;68(2):217-227. Viejo-Díaz M, Andrés MT, Pérez-Gil J, Sánchez M, Fierro JF. Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. DRAMP03637 ATFNFINNCPFTVWAAAVPG 20 Thaumatin-like protein (Actc2) P83958 Belongs to the thaumatin family tlp Actinidia chinensis (Kiwi) (Yangtao) Antimicrobial, Antifungal, Antiviral Protein level Not found Not found Function: Has antifungal activity. Inhibits HIV-1 reverse transcriptase. Botrytis cinerea, Coprinus comatus, Mycosphaerella arachidicola, Physalospora piricola, Candida albicans, Saccharomyces carlsbergensis, HIV-1 reverse transcriptase. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12165295##12417892##15536427 Phytochemistry. 2002 Sep;61(1):1-6.##J Allergy Clin Immunol. 2002 Nov;110(5):805-810.##J Allergy Clin Immunol. 2004 Nov;114(5):1169-1175. Wang H, Ng TB.##Gavrović-Jankulović M, ćIrković T, Vucković O, Atanasković-Marković M, Petersen A, Gojgić G, Burazer L, Jankov RM.##Bublin M, Mari A, Ebner C, Knulst A, Scheiner O, Hoffmann-Sommergruber K, Breiteneder H, Radauer C. Isolation of an antifungal thaumatin-like protein from kiwi fruits.##Isolation and biochemical characterization of a thaumatin-like kiwi allergen.##IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries. DRAMP03639 GLSQGVEPDIGQTYFEESRINQD 23 Astexin-1 (lasso peptide) No entry found Not found Not found Asticcacaulis excentricus CB 48 (Gram-negative bacteria) Antimicrobial, Antibacterial, Anti-Gram- Not found Beta strand (2 strands; 3 residues) The solution structure of astexin-1 was determined and found to have a nine-membered macrolactam ring followed by an 8-aa loop and a 6-aa tail. The extended length of the loop and tail regions allow for hydrogen-bonding interactions between the backbone and polar side chains of these regions of the peptide. 2LTI resolved by NMR. "Function: Astexin-1 has weak antimicrobial activity against Caulobacter crescentus. No growth inhibition is observed for any other strains of bacteria tested, and the growth inhibition of C. crescentus is quite modest." Gram-negative bacterium: Caulobacter crescentus CB15. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22949633 Proc Natl Acad Sci U S A. 2012 Sep 4. Maksimov MO, Pelczer I, Link AJ. Precursor-centric genome-mining approach for lasso peptide discovery. DRAMP03640 DSHEKRHHEHRRKFHEKHHSHRGY 24 Hcl-hst 5 (N.leucogenys histatin 5) No entry found Not found Not found Nomascus leucogenys Antimicrobial, Antifungal Not found Alpha helix (CD) Not found Rich in histidines. Partial helical in 50% TFE. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20423320 Protein Pept Lett. 2010 Jul;17(7):909-918. Padovan L, Segat L, Pontillo A, Antcheva N, Tossi A, Crovella S. Histatins In Non-Human Primates: Gene Variations and Functional Effects. DRAMP03641 DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG 47 Longicornsin (defensin-like; Arthropods, invertebrates, animals) B2MW54 Not found sGDLP Haemaphysalis longicornis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has antibacterial activity. Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa, Helicobacter pylori.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20027626 Protein Sci. 2010 Mar;19(3):392-327. Lu X, Che Q, Lv Y, Wang M, Lu Z, Feng F, Liu J, Yu H. A novel defensin-like peptide from salivary glands of the hard tick, Haemaphysalis longicorn. DRAMP03643 RLKRMTPFWRGVSLRPVGASCRDNSECITMLCRKNRCFLRTASE 44 Liver-expressed antimicrobial peptide 2 (LEAP-2; Birds, animals) Q6QLQ6 Not found Not found Gallus gallus (Chicken) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15148642 Immunogenetics. 2004 Jun;56(3):170-177. Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C. Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken. DRAMP03644 RVKRVWPLVIRTVIAGYNLYRAIKKK 26 Cathelicidin-1 (CATH-1; Fowlicidin-1; Birds, animals) Q6QLQ5, Q2IAM1 Not found CATHL1 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytolytic Protein level Alpha helix (2 helices; 13 residues) Fowlicidin-1 mainly adopts an alpha-helical conformation with a slight kink induced by glycine close to the center, in addition to a short flexible unstructured region near the N terminus. The short C-terminal helical segment after the kink, consisting of a stretch of eight amino acids (residues 16-23), may be required for the peptide to interact with LPS and lipid membranes and to permeabilize both prokaryotic and eukaryotic cells. 2AMN resolved by NMR. "Function: Has potent antimicrobial activity against Gram-positive and Gram-negative bacteria (in vitro). Has hemolytic activity (in vitro). May play a role in the innate immune response. Animal model (mouse): It increased mice survival by 50% from a lethal dose of S. aureus (MRSA). This truncated peptide also reduced TNF-alpha and NO production in macrophage by 77% and 96%, respectively." [Ref.16326712]Gram-negative bacteria: [No NaCl]Escherichia coli 25922 (MIC=1.59 µM), Escherichia coli O157:H7 700728 (MIC=0.80 µM), Salmonella typhimurium 14028 (MIC=0.80 µM), Salmonella typhimurium DT104 700408 (MIC=0.40 µM), Klebsiella pneumoniae 13883 (MIC=0.40 µM), Pseudomonas aeruginosa 27853 (MIC=3.18 µM);##[100mM NaCl]Escherichia coli 25922 (MIC=1.59 µM), Escherichia coli O157:H7 700728 (MIC=0.80 µM), Salmonella typhimurium 14028 (MIC=1.59 µM), Salmonella typhimurium DT104 700408 (MIC=1.59 µM), Klebsiella pneumoniae 13883 (MIC=0.80 µM), Pseudomonas aeruginosa 27853 (MIC=3.18 µM);##Gram-positive bacteria: Listeria monocytogenes 19115 (MIC=0.80 µM), Staphylococcus aureus 25923 (MIC=0.80 µM), Staphylococcus aureus (MRSA) BAA-39 (MIC=0.40 µM), Staphylococcus aureus (MRSA) 43300 (MIC=0.40 µM);##[100mM NaCl]Listeria monocytogenes 19115 (MIC=1.59 µM), Staphylococcus aureus 25923 (MIC=0.80 µM), Staphylococcus aureus (MRSA) BAA-39 (MIC=0.80 µM), Staphylococcus aureus (MRSA) 43300 (MIC=0.40 µM) [Ref.16326712]80% hemolytic activity at 10 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 16326712##16817888 Biol Chem. 2006 Feb 3;281(5):2858-2867.##FEBS J. 2006 Jun;273(12):2581-2593. Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE, Zhang G.##Xiao Y, Dai H, Bommineni YR, Soulages JL, Gong YX, Prakash O, Zhang G. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity.##Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken. DRAMP03648 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCKRIWG 40 Gallinacin-1 (Gal-1; Beta-defensin 1; Birds, animals) P46156, Q09MK1, Q6B9W7, Q6GXJ4 Belongs to the beta-defensin family GAL1 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Tissue specificity: Strong expression in the bone marrow, lung, testis. Moderate expression in the bursa and intestine. Low expression in the cloaca, gall bladder, brain and pancreas. Expressed in the vagina, ovarian stroma and the theca and granulosa layers of the ovarian follicle. Developmental stage: Detected in the theca layer of the ovarian follicle in the white follicle (WF) stage, but decreases throughout the F1, F3, F5, and postovulatory follicle stages. Detected in the granulosa layer of the ovarian follicle in the white follicle (WF) stage, F1, F3, F5, and postovulatory follicle stages. In the vagina expression is higher in laying hens than in non-laying hens, and is higher in older laying hens than in young laying hens. Induction: Induced in the theca layer of the F3 stage ovarian follicle by intravenous injection of LPS. Repressed in the granulosa layer of the F3 stage ovarian follicle by intravenous injection of LPS. Expression in cultured vaginal cells is increased by LPS and S.enteritidis. Expression in the kidney and liver is not affected by intravenous injection of LPS. PTM: Contains three disulfide bonds 6-34; 13-28; 18-35." Gram-negative bacterium: Escherichia coli ML-35;##Gram-positive bacterium: Listeria monocytogenes.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8150085##16394622##17244739 FEBS Lett. 1994 Apr 11;342(3):281-285.##J Reprod Dev. 2006 Apr;52(2):211-218.##Reproduction. 2007 Jan;133(1):127-133. Harwig SS, Swiderek KM, Kokryakov VN, Tan L, Lee TD, Panyutich EA, Aleshina GM, Shamova OV, Lehrer RI.##Yoshimura Y, Ohashi H, Subedi K, Nishibori M, Isobe N.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes.##Effects of age, egg-laying activity, and Salmonella-inoculation on the expressions of gallinacin mRNA in the vagina of the hen oviduct.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus). DRAMP03649 GRKSDCFRKNGFCAFLKCPYLTLISGKCSRFHLCCKRIW 39 Gallinacin-1 alpha (Gal-1 alpha; Antimicrobial peptide CHP2; Birds, animals) P46157, P80390, Q09MR8, Q9DG59 Belongs to the beta-defensin family Not found Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found PTM: Contains three disulfide bonds 6-34; 13-28; 18-35. Gram-negative bacterium: Escherichia coli ML-35;##Gram-positive bacteria: Staphylococcus aureus, Listeria monocytogenes.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7964174##8150085 J Leukoc Biol. 1994 Nov;56(5):661-665.##FEBS Lett. 1994 Apr 11;342(3):281-285. Evans EW, Beach GG, Wunderlich J, Harmon BG.##Harwig SS, Swiderek KM, Kokryakov VN, Tan L, Lee TD, Panyutich EA, Aleshina GM, Shamova OV, Lehrer RI. Isolation of antimicrobial peptides from avian heterophils.##Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes. DRAMP03650 LFCKGGSCHFGGCPSHLIKVGSCFGFRSCCKWPWNA 36 Gallinacin-2 (Gal-2; Beta-defensin 2; Birds, animals) P46158, Q09MT0, Q0PWH3, Q6B9W8, Q6GXJ3 Belongs to the beta-defensin family GAL2 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Beta strand (3 strands; 11 residues) The three-dimensional NMR structure of chicken AvBD2 defensin displays the structural three-stranded antiparallel β-sheet characteristic of β-defensins. The surface of the molecule does not display any amphipathic character. 2LG5, 2LG6 resolved by NMR. "Tissue specificity: Expressed in circulating heterophil granulocytes and bone marrow (at protein level). Strong expression in the bone marrow, lung and testis. Moderate expression in the bursa and intestine. Low expression in the cloaca, gall bladder, brain, pancreas, trachea, air sacs and spleen. Expressed in the vagina, ovarian stroma and the theca layer of the ovarian follicle, but not in the granulosa layer of the ovarian follicle. Developmental stage: Detected in the theca layer of the ovarian follicle in the white follicle (WF), F1, F3, F5, and postovulatory follicle stages. In the vagina expression is higher in laying hens than in non-laying hens, and is higher in older laying hens than in young laying hens. Induction: Not induced in the ovarian follicle by intravenous injection of LPS. Expression in cultured vaginal cells is increased by LPS and S.enteritidis. PTM: Contains three disulfide bonds 3-29, 8-23, 13-30." Gram-negative bacteria: Escherichia coli ML-35, Salmonella enteritidis;##Gram-positive bacteria: Bacillus cereus, Listeria monocytogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 8150085##19151352##15148642##17244739##16394622##22205 FEBS Lett. 1994 Apr 11;342(3):281-285.##Poult Sci. 2009 Feb;88(2):372-379.##Immunogenetics. 2004 Jun;56(3):170-177.##Reproduction. 2007 Jan;133(1):127-133.##J Reprod Dev. 2006 Apr;52(2):211-218.##J Biol Chem. Harwig SS, Swiderek KM, Kokryakov VN, Tan L, Lee TD, Panyutich EA, Aleshina GM, Shamova OV, Lehrer RI.##Kannan L, Rath NC, Liyanage R, Lay JO Jr.##Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Yoshimura Y, Ohashi H, Subedi K, Nishibori M, Isobe N.##Derache C, Meudal H, Aucagne V, Mark KJ, Cadène M, Delmas AF, Lalmanach AC, Landon C. Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes.##Direct screening identifies mature beta-defensin 2 in avian heterophils.##Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##Effects of age, egg-laying activity, and Salmonella-i DRAMP03651 IATQCRIRGGFCRVGSCRFPHIAIGKCATFISCCGRAY 38 Gallinacin-3 (Gal-3; Beta-defensin 3; Birds, animals) Q9DG58, Q0PWH2, Q6GXJ2 Belongs to the beta-defensin family GAL3 Gallus gallus (Chicken) Antimicrobial, Antibacterial Transcript level Not found Not found "Tissue specificity: Strongly expressed in the tongue, bone marrow, bursa of Fabricius and trachea. Also expressed in skin, esophagus and air sacs. Weak expression in the large intestine, kidney and ovary. Expressed in the vagina and ovarian stroma, but not in the ovarian follicle. Developmental stage: In the vagina expression is higher in laying hens than in non-laying hens, and is higher in older laying hens than in young laying hens. Induction: Expression in cultured vaginal cells is increased by LPS and S. enteritidis. PTM: contains three disulfide bonds 3-31; 10-25; 15-33. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11254635##15148642##16394622 Infect Immun. 2001 Apr;69(4):2684-2691.##Immunogenetics. 2004 Jun;56(3):170-177.##J Reprod Dev. 2006 Apr;52(2):211-218. Zhao C, Nguyen T, Liu L, Sacco RE, Brogden KA, Lehrer RI.##Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Yoshimura Y, Ohashi H, Subedi K, Nishibori M, Isobe N. Gallinacin-3, an inducible epithelial beta-defensin in the chicken.##Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##Effects of age, egg-laying activity, and Salmonella-inoculation on the expressions of gallinacin mRNA in the vagina of the hen oviduct. DRAMP03652 RYHMQCGYRGTFCTPGKCPHGNAYLGLCRPKYSCCRWL 38 Gallinacin-4 (Gal-4; Beta-defensin 4; Birds, animals) Q6GXJ1, Q0PXU4, Q6QLR0 Belongs to the beta-defensin family GAL4 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found Tissue specificity: Strong expression in the bone marrow and testis. Widely expressed. Weak expression in the ovarian stroma, but not expressed in the ovarian follicles. PTM: Contains three disulfide bonds 6-34; 13-28; 18-35. Gram-negative bacteria: Salmonella typhimurium, Salmonella entiriditis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17346671##15310403##15148642##17244739 Biochem Biophys Res Commun. 2007 Apr 27;356(1):169-174.##BMC Genomics. 2004 Aug 13;5(1):56.##Immunogenetics. 2004 Jun;56(3):170-177.##Reproduction. 2007 Jan;133(1):127-133. Milona P, Townes CL, Bevan RM, Hall J.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. The chicken host peptides, gallinacins 4, 7, and 9 have antimicrobial activity against Salmonella serovars.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response DRAMP03653 GLPQDCERRGGFCSHKSCPPGIGRIGLCSKEDFCCRSRWYS 41 Gallinacin-5 (Gal-5; Beta-defensin 5; Birds, animals) Q6IV26, Q09MS7, Q0PWH0, Q6QLQ8 Belongs to the beta-defensin family GAL5 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Not found Not found Tissue specificity: Strong expression in the tongue and bone marrow. Low expression in the esophagus, trachea, lung, brain and ovary. Expressed in the ovarian stroma, but not in the ovarian follicles. PTM: contains three disulfide bonds 6-34; 13-28; 18-35. Gram-negative bacteria: Salmonella typhimurium, Salmonella entiriditis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17346671##15310403##15148642##17244739 Biochem Biophys Res Commun. 2007 Apr 27;356(1):169-174.##BMC Genomics. 2004 Aug 13;5(1):56.##Immunogenetics. 2004 Jun;56(3):170-177.##Reproduction. 2007 Jan;133(1):127-133. Milona P, Townes CL, Bevan RM, Hall J.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. The chicken host peptides, gallinacins 4, 7, and 9 have antimicrobial activity against Salmonella serovars.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response DRAMP03654 SPIHACRYQRGVCIPGPCRWPYYRVGSCGSGLKSCCVRNRWA 42 Gallinacin-6 (Gal 6; Beta-defensin 6; Birds, animals) Q6QLR3 Belongs to the beta-defensin family GAL6 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found Tissue specificity: Expressed in bone marrow, testis, ovary, lung and trachea. Expressed in the ovarian stroma, but not in the ovarian follicles. PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. Gram-negative bacteria: Salmonella typhimurium, Salmonella entiriditis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17346671##15310403##15148642##17244739 Biochem Biophys Res Commun. 2007 Apr 27;356(1):169-174.##BMC Genomics. 2004 Aug 13;5(1):56.##Immunogenetics. 2004 Jun;56(3):170-177.##Reproduction. 2007 Jan;133(1):127-133. Milona P, Townes CL, Bevan RM, Hall J.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Lynn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. The chicken host peptides, gallinacins 4, 7, and 9 have antimicrobial activity against Salmonella serovars.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response DRAMP03655 RPIDTCRLRNGICFPGICRRPYYWIGTCNNGIGSCCARGWRS 42 Gallinacin-7 (Gal 7; Beta-defensin 7; Birds, animals) Q6QLR2, Q09MR1, Q09MV1 Belongs to the beta-defensin family GAL7 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Transcript level Bridge Not found 5LCS "Tissue specificity: Strong expression in the bone marrow and testis. Expressed in the ovarian stroma and the theca layer of the ovarian follicles. Not expressed in the granulosa layer of the ovarian follicles. Developmental stage: Detected in the theca and granulosa layers of the ovarian follicle in the white follicle (WF), F1, F3, F5, and postovulatory follicle stages. Induction: Induced in the theca layer of the F3 stage ovarian follicle by intravenous injection of LPS. Expression in the kidney and liver is not affected by intravenous injection of LPS. PTM: Contains three disulfide bonds 6-35; 13-28; 18-36." Gram-negative bacterium: Salmonella enteriditis. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15148642##15310403##17244739 Immunogenetics. 2004 Jun;56(3):170-177.##BMC Genomics. 2004 Aug 13;5(1):56.##Reproduction. 2007 Jan;133(1):127-133. nn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus). DRAMP03656 NNEAQCEQAGGICSKDHCFHLHTRAFGHCQRGVPCCRTVYD 41 Gallinacin-8 (Gal-8; Beta-defensin 8; Birds, animals) Q6IV23, Q6GXI7 Belongs to the beta-defensin family GAL8 Gallus gallus (Chicken) Antimicrobial, Antibacterial Transcript level Bridge Not found Tissue specificity: Expressed in the liver, kidney, gall bladder, testis, ovary and male and femae reproductive tracts. Expressed in the ovarian stroma and the theca and granulosa layers of the ovarian follicle. Detected in the theca and granulosa layers of the ovarian follicle in the white follicle (WF), F1, F3, F5, and postovulatory follicle stages. Induction: Induced in the theca layer of the F3 stage ovarian follicle by intravenous injection of LPS. Expression in the granulosa layer of the ovarian follicle is not affected by intravenous injection of LPS. PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. Escherichia coli, Listeria monocytogenes, Salmonella typhimurium, Streptococcus pyogenes No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17244739##15310403##15744537 Reproduction. 2007 Jan;133(1):127-133.##BMC Genomics. 2004 Aug 13;5(1):56.##Immunogenetics. 2005 Apr;57(1-2):90-98. Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Higgs R, Lynn DJ, Gaines S, McMahon J, Tierney J, James T, Lloyd AT, Mulcahy G, O'Farrelly C. Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##The synthetic form of a novel chicken beta-defensin identified in silico is predominantly active against intestinal pathogens. DRAMP03657 ADTLACRQSHGSCSFVACRAPSVDIGTCRGGKLKCCKWAPSS 42 Gallinacin-9 (Gal-9; Beta-defensin 9; Gallinacin-6, Gal-6; Birds, animals) Q6QLR1, Q09MS3 Belongs to the beta-defensin family GAL9 Gallus gallus (Chicken) Antimicrobial, Antibacterial Transcript level Bridge Not found Tissue specificity: Strong expression in the testis, liver, gall bladder, kidney, esophagus and crop. Also expressed in the glandular stomach, ovary and male and female reproductive tracts. Low expression in the intestinal tract. Expressed in the ovarian stroma, but not in the ovarian follicles. PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. C.jejuni, C.perfringens, Staphylococcus aureus, Candida albicans and Saccharomyces cerevisiae. Less potent against Salmonella typhimurium and Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15148642##15310403##17244739##17194828 Immunogenetics. 2004 Jun;56(3):170-177.##BMC Genomics. 2004 Aug 13;5(1):56.##Reproduction. 2007 Jan;133(1):127-133.##Antimicrob Agents Chemother. 2007 Mar;51(3):912-922. nn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Subedi K, Isobe N, Nishibori M, Yoshimura Y.##van Dijk A, Veldhuizen EJ, Kalkhove SI, Tjeerdsma-van Bokhoven JL, Romijn RA, Haagsman HP. Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##The beta-defensin gallinacin-6 is expressed in the DRAMP03658 FPDTVACRTQGNFCRAGACPPTFTISGQCHGGLLNCCAKIPAQ 43 Gallinacin-10 (Gal-10; Beta-defensin 10; Birds, animals) Q6QLQ9 Belongs to the beta-defensin family GAL10 Gallus gallus (Chicken) Antimicrobial, Antibacterial Transcript level Bridge Not found Tissue specificity: Strong expression in the testis, liver, gall bladder and kidney. Also expressed in the ovary and male and female reproductive tracts. Expressed in the ovarian stroma and the theca and granulosa layers of the ovarian follicle. Developmental stage: Detected in the theca and granulosa layers of the ovarian follicle in the white follicle (WF), F1, F3, F5, and postovulatory follicle stages. Induction: Expression in the theca and granulosa layers of the F3 stage ovarian follicle is not affected by intravenous injection of LPS. PTM: Contains three disulfide bonds 7-36; 14-29; 19-37. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15148642##15310403##17244739 Immunogenetics. 2004 Jun;56(3):170-177.##BMC Genomics. 2004 Aug 13;5(1):56.##Reproduction. 2007 Jan;133(1):127-133. nn DJ, Higgs R, Gaines S, Tierney J, James T, Lloyd AT, Fares MA, Mulcahy G, O'Farrelly C.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Subedi K, Isobe N, Nishibori M, Yoshimura Y. Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken.##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus). DRAMP03660 HGPDSCNHDRGLCRVGNCNPGEYLAKYCFEPVILCCKPLSPTPTKT 46 Gallinacin-12 (Gal-12; Beta-defensin 12; Birds, animals) Q6QLQ7, A0MV42, Q0PWG3, Q6IV19 Belongs to the beta-defensin family GAL12 Gallus gallus (Chicken) Antimicrobial, Antibacterial Transcript level Bridge Not found Tissue specificity: Expressed in the large intestine, kidney liver, gall bladder, testis, ovary and male and female reproductive tracts. Expressed in the ovarian stroma and the theca and granulosa layers of the ovarian follicle. Developmental stage: Detected in the theca and granulosa layers of the ovarian follicle in the white follicle (WF), F1, F3, F5, and postovulatory follicle stages. Induction: Induced in the theca layer of the F3 stage ovarian follicle by intravenous injection of LPS. Repressed in the granulosa layer of the F3 stage ovarian follicle by intravenous injection of LPS. PTM: Contains three disulfide bonds 6-35; 13-28; 18-36. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17244739##15310403 Reproduction. 2007 Jan;133(1):127-33. Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G. Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins. DRAMP03661 FSDSQLCRNNHGHCRRLCFHMESWAGSCMNGRLRCCRFSTKQPFSNPKHSVLHTAEQDPSPSLGGT 66 Gallinacin-13 (Gal-13; Beta-defensin 13; Birds, animals) Q6IV18, Q66VU2 Belongs to the beta-defensin family GAL13 Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Tissue specificity: Expressed in the liver, gall bladder, kidney, small intestine, spleen, testis, ovary and male and female reproductive tracts. Not detected in the ovarian stroma and the theca and granulosa layers of the ovarian follicle. PTM: Contains three disulfide bonds 7-35; 14-28; 18-36. Gram-negative bacteria: Escherichia coli, Salmonella typhimurium;##Gram-positive bacteria: Listeria monocytogenes, Streptococcus pyogenes. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17244739##15310403##15744537 Reproduction. 2007 Jan;133(1):127-133.##BMC Genomics. 2004 Aug 13;5(1):56.##Immunogenetics. 2005 Apr;57(1-2):90-98. Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Xiao Y, Hughes AL, Ando J, Matsuda Y, Cheng JF, Skinner-Noble D, Zhang G.##Higgs R, Lynn DJ, Gaines S, McMahon J, Tierney J, James T, Lloyd AT, Mulcahy G, O'Farrelly C. Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins.##The synthetic form of a novel chicken beta-defensin identified in silico is predominantly active against intestinal pathogens. DRAMP03662 ESDTVTCRKMKGKCSFLLCPFFKRSSGTCYNGLAKCCRPFW 41 Gallinacin-14 (Gal-14; Beta-defensin 14; Birds, animals) Q0E4V3 Belongs to the beta-defensin family GAL14 Gallus gallus (Chicken) Antimicrobial, Antibacterial Homology Not found Not found PTM: Contains three disulfide bonds 7-36; 14-29; 19-37. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17244739##PubMed ID is not available Reproduction. 2007 Jan;133(1):127-133.##Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. Subedi K, Isobe N, Nishibori M, Yoshimura Y.##Soulier A.J, Rothwell L, Lovell M.A, Bumstead N, Barrow P.A, Kaiser P. Changes in the expression of gallinacins, antimicrobial peptides, in ovarian follicles during follicular growth and in response to lipopolysaccharide in laying hens (Gallus domesticus).##A novel chicken beta-defensin, gallinacin 14. DRAMP03663 MTPFWRGVSLRPVGASCRDNSECITMLCRKNRCFLRTASE 40 cLEAP-2 (Chicken LEAP-2; Birds, animals) No entry found Not found Not found Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: S. enterica serovar Typhimurium strain SL1344, mutant S. enterica serovar Typhimurium strain phoP. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrane 15557621 Infect Immun. 2004 Dec;72(12):6987-6893. wnes CL, Michailidis G, Nile CJ, Hall J. Induction of cationic chicken liver-expressed antimicrobial peptide 2 in response to Salmonella enterica infection. DRAMP03664 ADNKNPLEECFRETNYEEFLEIAR 24 L-amino-acid oxidase (LAAO, LAO, TM-LAO; reptilia, animals) P0C2D6 Not found Not found Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops mucrosquamatus) Antimicrobial, Antibacterial, Anti-Gram- Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis, and antiparasitic activities By similarity. This protein has antibacterial activity abd cytotoxic activity, as well as an ability to induce platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Tissue specificity: Expressed by the venom gland. PTM: Contains one disulfide bond." Gram-negative bacterium: E. coli;##S. aureus, B. dysenteriae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12621545 Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Mar;35(3):219-224. Wei JF, Wei Q, Lu QM, Tai H, Jin Y, Wang WY, Xiong YL. Purification, characterization and biological activity of an L-amino acid oxidase from Trimeresurus mucrosquamatus venom. DRAMP03665 IAIQGGXGYLXQPGDGYKYA 20 Lysozyme P85152 Not found Not found Lysobacter sp. (strain XL1) Antimicrobial, Antibacterial Protein level Not found Not found "Biophysicochemical properties: Optimum pH is 8.0; Optimum temperature is 60 degrees Celsius. Also has Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2007) to UniProtKB. Muranova T.A, Stepnaya O.A, Tsfasman I.M, Kulaev I.S. Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1. DRAMP03666 XNVVFLNXPXPQW 13 N-acetylmuramoyl-L-alanine amidase L2 P85143 Not found Not found Lysobacter sp. Antimicrobial, Antibacterial Protein level Not found Not found "Biophysicochemical properties: Optimum pH is 8.0; Optimum temperature is 65 degrees Celsius. Also has Catalytic activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2007) to UniProtKB. Muranova T.A, Stepnaya O.A, Tsfasman I.M, Kulaev I.S. Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1. DRAMP03667 ATVQGGIXYRMP 12 Proteinase L5 P85158 Not found Not found Lysobacter sp. strain XL1 (Gram-negative bacteria) Antimicrobial, Antibacterial Protein level Not found Not found Biophysicochemical properties: Optimum pH is 7.5; Optimum temperature is 80 degrees Celsius. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-2007) to UniProtKB. Muranova T.A, Stepnaya O.A, Tsfasman I.M, Kulaev I.S. Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1. DRAMP03668 YLDVKQLANYLLCIGNGQVFNGRKTCQIGCRAVCQQPGCSGYKECEQIPNIRLHKYRCHCNEA 63 Megourin-1 (arthropod; animals) P83417 Not found Not found Megoura viciae (Vetch aphid) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria and fungi. Induction: By bacterial infection. PTM: Contains four disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P, Charlet M, Chernish S, Hetru C. Unknown DRAMP03669 YLDVNQIASYLLCLGQGAVFNGRKTCQIGCRAACQQPGCGGYKECEQIPNIRLHKYRCHCNSG 63 Megourin-2 (arthropod; animals) P83418 Not found Not found Megoura viciae (Vetch aphid) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria and fungi. Induction: By bacterial infection. PTM: Contains four disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P, Charlet M, Chernish S, Hetru C. Unknown DRAMP03670 YLDVNQIASYLLCLGEGAVFNGRKTCQIGCRAACQQPGCGGYKECEQIPNIRLHKYRCHCISG 63 Megourin-3 (arthropod; animals) P83419 Not found Not found Megoura viciae (Vetch aphid) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found "Function: Has antimicrobial activity against Gram-positive bacteria and fungi. Induction: By bacterial infection. PTM: Contains four disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P, Charlet M, Chernish S, Hetru C. Unknown DRAMP03671 ATTGCSCPQCIIFDPICASSYKNGRRGFSSGCHMRCYNRCHGTDYFQISKGSKCI 55 Locustin (Insects, animals) P83428 Not found Not found Locusta migratoria (Migratory locust) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Stored in hemocyte granules and secreted into the hemolymph." Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2002) to UniProtKB Bulet P, Charlet M, Sabatier-Ehret L. Unknown DRAMP03672 VHVGPCDQVCSRIDPEKDECCRAHGYRGHSSCYYGRMECY 40 Spodomicin (Insects, animals) P83411 Belongs to the diapausin family Not found Spodoptera littoralis Antimicrobial, Antifungal Protein level Not found Not found "Function: Fungicide. Tissue specificity: Hemolymph. Induction: By bacterial infection. PTM: Contains three disulfide bonds." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2003) to UniProtKB Bulet P, Lamberty M, Brookhart G, Bushey D. Unknown DRAMP03673 FFHHIFRGIVHVGKSIHKLVTG 22 Dicentracin (Dicentracine) P59906 Belongs to the pleurocidin family Not found Dicentrarchus labrax (European seabass) (Morone labrax) Antimicrobial Homology Not found Not found Function: May have antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Salerno G, Roch P, Sri Widada J. Dicentracine, first antimicrobial peptide isolated from the fish Dicentrarchus labrax. DRAMP03674 DTHISEKIIDCNDIG 15 Cystatin-1 (Cystatin-I) P84911 Belongs to the caerin subfamily Not found Capra hircus (Goat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Inhibits papain, ficin and bromelain with an IC50 of 0.09 µM, 0.115 µM and 0.113 µM respectively. Has antibacterial activity against Gram-positive bacteria and against the Gram-negative bacteria. Reduced antibacterial activity against Gram-positive bacterium B.subtilis. No antibacterial activity against the Gram-negative bacterium P.fluorescens. Miscellaneous: Stable in the pH range 5.0-9.0 at 37 degrees Celsius. Stable when incubated in the temperature range 25-75 degrees Celsius and pH 7.5. Sequence uncertainty: K or Y at position 7." [Swiss_Prot Entry P84911]has antibacterial activity against Gram-positive bacteria S.aureus and S.hemolyticus, and against the Gram-negative bacterium E.coli. Reduced antibacterial activity against Gram-positive bacterium B.subtilis. No antibacterial activity against the Gram-negative bacterium P.fluorescens [Swiss_Prot Entry P84911]Not found Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16257555 Comp Biochem Physiol B Biochem Mol Biol. 2005 Dec;142(4):361-368. Sadaf Z, Shahid PB, Bilqees B. Isolation, characterization and kinetics of goat cystatins. DRAMP18192 FLFSLIPNAISGLLSAFK 18 Antimicrobial peptide AcrAP2 A0A0A1I6N9 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an Not found Androctonus crassicauda (Arabian fat-tailed scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Has antimicrobial activity against the Gram-positive bacteria S.aureus and the yeast C.albicans. Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Gram-positive bacteria: S.aureus (MIC=8 uM, MBC=32 uM);##Yeast: C.albicans (MIC=16 uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 25332684 Int. J. Biol. Sci. 10:1097-1107(2014) Du Q., Hou X., Ge L., Li R., Zhou M., Wang H., Wang L., Wei M.,Chen T., Shaw C. Cationicity-enhanced analogues of the antimicrobial peptides, AcrAP1and AcrAP2, from the venom of the scorpion, Androctonus crassicauda,display potent growth modulation effects on human cancer cell lines. DRAMP03678 SRRSCHRNKGVCALTRCPRNMRQIGTCFGPPVKCCRKK 38 Beta-defensin 1 (GBD-1; Defensin, beta 1; ruminant, animals) O97946 Belongs to the beta-defensin family DEFB1 Capra hircus (Goat) Antimicrobial, Antibacterial Homology Bridge Not found "Function: Has bactericidal activity (By similarity). PTM: Contains three disulfide bonds 5-34; 12-27; 17-35. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531296 Infect Immun. 1999 Nov;67(11):6221-6224. Zhao C, Nguyen T, Liu L, Shamova O, Brogden K, Lehrer RI. Differential expression of caprine beta-defensins in digestive and respiratory tissues. DRAMP03680 RFRLPFRRPPIRIHPPPFYPPFRRFL 26 Cathelicidin-3.4 (Bactenecin-3.4, Bac3.4; ChBac3.4; ruminant, animals) P85170 Belongs to the cathelicidin family Not found Capra hircus (Goat) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Has low hemolytic activity towards human red blood cells. [Swiss_Prot Entry P85170]Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa;##Gram-positive bacteria: Staphylococcus aureus, Listeria monocytogenes [Swiss_Prot Entry P85170]Low hemolytic activity against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAY-2007) to UniProtKB. Shamova O, Orlov D, Stegemann C, Lehrer RI, Brogden KA, Kolodkin N, Hoffmann R, Kokryakov VN. Unknown DRAMP03681 ADDRNPLEECFRETDYEEFLEIARNGLKKT 30 L-amino-acid oxidase (LAAO; OHAP-1) P0C2D5 Not found Not found Trimeresurus flavoviridis (Habu) (Protobothrops flavoviridis) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. This protein has an ability to induce hemolysis and apoptosis. Tissue specificity: Expressed by the venom gland. PTM: Contains one disulfide bond and N-glycosylated." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Glycyrrhizin (GL) 12650671##9781840 Toxicol In Vitro. 2003 Apr;17(2):169-177.##Biol Pharm Bull. 1998 Sep;21(9):924-927. Sun LK, Yoshii Y, Hyodo A, Tsurushima H, Saito A, Harakuni T, Li YP, Kariya K, Nozaki M, Morine N.##Abe Y, Shimoyama Y, Munakata H, Ito J, Nagata N, Ohtsuki K. Apoptotic effect in the glioma cells induced by specific protein extracted from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to oxidative stress.##Characterization of an apoptosis-inducing factor in Habu snake venom as a glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro. DRAMP03689 GWINEEKIQKKIDEP 15 Scorpine-like (Arthropods, animals) P86121 Belongs to the Belongs to the long chain scorpion toxin famiy Not found Opisthacanthus cayaporum (South American scorpion) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Has antimicrobial activity against S. aureus (78% growth inhibition at 1.8 µM). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds." Gram-positive bacterium: Staphylococcus aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18502464 Toxicon. 2008 Jun 15;51(8):1499-1508. Schwartz EF, Camargos TS, Zamudio FZ, Silva LP, Bloch C Jr, Caixeta F, Schwartz CA, Possani LD. Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03690 FWSFLVKAASKILPSLIGGGDDNKSSS 27 Probable antimicrobial peptide Con10 (Arthropods, animals) C5J897 Not found Not found Opisthacanthus cayaporum (South American scorpion) Antimicrobial Transcript level Not found Not found "Function: Probable antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19379768 Toxicon. 2009 Sep 1;54(3):252-261. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03692 ACQFWSCNSSCISRGYRQGYCWGIQYKYCQCQ 32 Defensin-1 (Cll-dlp; Arthropods, animals) Q6GU94, P83738 Belongs to the invertebrate defensin family Not found Centruroides limpidus limpidus (Mexican scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 6B9W "Function: Antibacterial protein involved in the immune response to septic injury. When combined with 14.026 kDa and 14.059 kDa hemolymph antimicrobial peptides, it has a strong cooperative activity against bacteria. No detectable antibacterial activity when present alone. Has no hemolytic activity against human erythrocytes. Induction: By septic injury. PTM: Contains three disulfide bonds 2-21; 7-29; 11-31." [Ref.15197474]Gram-positive bacteria: Bacillus subtilis (MIC>50 µg/ml), Staphylococcus aureus ATCC 25923 (MIC>50 µg/ml);##Gram-negative bacteria: Escherichia coli DH5a (MIC>50 µg/ml), Klebsiella pneumoniae ATCC 13883 (MIC>50 µg/ml).##NOTE: Liquid growth inhibition assay. [Swiss_Prot Entry Q6GU94]Non-hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15197474 Cell Mol Life Sci. 2004 Jun;61(12):1507-1519. Rodríguez de la Vega RC, García BI, D'Ambrosio C, Diego-García E, Scaloni A, Possani LD. Antimicrobial peptide induction in the haemolymph of the Mexican scorpion Centruroides limpidus limpidus in response to septic injury. DRAMP03695 GFWSKIKDFAKKAWNSPLANELKSKALNAAKNFVSEKIGATPS 43 Probable antimicrobial peptide Con13 (Arthropods, animals) C7C1L2 Belongs to the antimicrobial peptide scorpion family Not found Opisthacanthus cayaporum (South American scorpion) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Hemolytic and antibacterial and antifungal peptide (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database [Swiss_Prot Entry C7C1L2]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrane 19379768 Toxicon. 2009 Sep 1;54(3):252-261. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03696 GWWNAFKSIGKKLLKSKLAKDITKMAKQRAKEYVVKKLNGPPEEEVAAIDALMNSLDY 58 Bradykinin-potentiating peptide-like (BPP; Non-disulfide-bridged peptide 3.7; Arthropods, animals P0C8L3 Belongs to the scorpion BPP family Not found Hadrurus gertschi (Scorpion) Unknown Transcript level Not found Not found "Function: defense response to bacterium. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17506894 BMC Genomics. 2007 May 16;8:119. Schwartz EF, Diego-Garcia E, Rodríguez de la Vega RC, Possani LD. Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). DRAMP03697 ARDAYIANDRNCVYTCALNPYCDSECKKNGADSGYCQWFGRFGNACWCKNLPDKVPIRIPGECR 64 Neurotoxin MeuNaTx-2 (Arthropods, animals) P86403 Belongs to the Sodium channel inhibitor family (Alpha subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Inhibits Nav1.4 and DmNav1 sodium channels. Has antibacterial activity. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity). " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2009) to UniProtKB Zhu S.Y, Gao B. Characterization of a sodium channel toxin from the scorpion Mesobuthus eupeus venom. DRAMP03698 ARDAYIAKPHNCVYECFDAFSSYCNGVCTKNGAKSGYCQILGTYGNGCWCIALPDNVPIRIPGKCH 66 Neurotoxin MeuNaTx-5 (Arthropods, animals) P86405 Belongs to the Sodium channel inhibitor family (Alpha subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial Protein level Combine helix and strand structure Not found 2LKB resolved by NMR. "Function: Inhibits sodium channels (Nav). Has antimicrobial activity. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##21969612 Submitted (NOV-2009) to UniProtKB##Mol Cell Proteomics. 2012 Jan;11(1):M111.012054. Zhu SY, Gao B.##Zhu S, Peigneur S, Gao B, Lu X, Cao C, Tytgat J. Characterization of a sodium channel toxin from the scorpion Mesobuthus eupeus venom.##Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels. DRAMP03699 DNGYLLDKYTGCKVWCVINNESCNSECKIRRGNYGYCYFWKLACYCEGAPKSELWHYETNKCNGRM 66 Neurotoxin MeuNaTx-6 (Arthropods, animals) P86406 Belongs to the Sodium channel inhibitor family (Alpha subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial Protein level Not found Not found "Function: Inhibits sodium channels (Nav). Has antimicrobial activity. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2009) to UniProtKB Zhu S.Y, Gao B. Characterization of a sodium channel toxin from the scorpion Mesobuthus eupeus venom. DRAMP03701 QLEARFEPKQRNFRKRELDFEKLFANMPDY 30 Imcroporin (Arthropods, animals) C7B247 Belongs to the short cationic antimicrobial peptide family Not found Isometrus maculatus (Lesser brown scorpion) Antimicrobial, Antibacterial, Anti-Gram+ Transcript level Not found Not found "Function: Has potent antibacterial activity against Gram-positive bacteria, but not Gram-negative bacteria. Shows a weak cytotoxicity effect against mammalian cell lines and hemolytic activity against human erythrocytes. Tissue specificity: Expressed by the venom gland." [Ref.19451300]Gram-positive bacteria: Micrococcus luteus(MIC=20μg/ml), Bacillus thuringiensis(MIC=50μg/ml), Staphylococcus aureus(MIC=20μg/ml), Bacillus subtilis(MIC=50μg/ml). [Ref.19451300]5% hemolytic activity at 40 μg/mL, 20% hemolytic at 50 μg/mL, 70% hemolytic aactivity at 100 μg/mL against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 19451300 Antimicrob Agents Chemother. 2009 Aug;53(8):3472-7. Zhao Z, Ma Y, Dai C, Zhao R, Li S, Wu Y, Cao Z, Li W. Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates. DRAMP03703 LFFLPSLIGGLISAFK 16 Mucroporin-like peptide (NDBP13; Arthropods, animals) D9U2B8 Belongs to the short cationic antimicrobial peptide family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cationic host defense peptide that have antibacterial activity by breaking membranes. Is more effective on Gram-positive than on Gram-negative bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 20663230 BMC Genomics. 2010 Jul 28;11:452. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03704 LFGLIPSMMGGLVSAFK 17 Antimicrobial peptide 36.4 (Arthropods, animals) P0CI89 Belongs to the short cationic antimicrobial peptide family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cationic host defense peptide that have antibacterial activity by breaking membranes. Is more effective on Gram-positive than on Gram-negative bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 20663230 BMC Genomics. 2010 Jul 28;11:452. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03705 LFFLPSLIGGLISAIK 16 Antimicrobial peptide 143 (Arthropods, animals) P0CI90 Belongs to the short cationic antimicrobial peptide family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Cationic host defense peptide that have antibacterial activity by breaking membranes. Is more effective on Gram-positive than on Gram-negative bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 20663230 BMC Genomics. 2010 Jul 28;11:452. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03708 RYCPRNPEACYNYCLRTGRPGGYCGGRSRITCFCFR 36 Tddefensin (Arthropods, animals) P0CF77 Belongs to the invertebrate defensin family Not found Tityus discrepans (Venezuelan scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial peptide mostly active against Gram-positive bacteria (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19470401 Biochimie. 2009 Aug;91(8):1010-1019. D'Suze G, Schwartz EF, García-Gómez BI, Sevcik C, Possani LD. Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans. DRAMP03709 GFREKHFQRFVKYAVPESTLRTVLQTVVHKVGKTQFGCPAYQGYCDDHCQDIEKKEGFCHGFKCKCGIPMGF 72 Potassium channel toxin MeuTXK-beta-1 (MeuTXKbeta1; Arthropods, animals) A9XE60 Belongs to the long chain scorpion toxin family (Class 1 subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Has a low affinity binding to potassium channels of rat brain synaptosomes. Displays weak antibacterial activity against Stenotrophomonas sp. Strongly inhibits the development of the Plasmodium berghei ookinetes. Displays hemolytic effect on mouse erythrocytes. Induces cytolysis on Xenopus oocytes at high concentrations. Is not toxic on mice and on the insect Tenebrio molitor. Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database [Ref.20045493]10.3% hemolytic activity at 10 μM, 14.8% hemolytic activity at 20 μM against mouse erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20045493 Biochim Biophys Acta. 2010 Apr;1804(4):872-883. Zhu S, Gao B, Aumelas A, del Carmen Rodríguez M, Lanz-Mendoza H, Peigneur S, Diego-Garcia E, Martin-Eauclaire MF, Tytgat J, Possani LD. MeuTXKbeta1, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity. DRAMP03710 GFREKHFQRFVKYAVPESTLRTVLQTVVHKVGKTQFGCSAYQGYCDDHCQDIEKKEGFCHGFKCKCGIPMGF 72 Potassium channel toxin MeuTXK-beta-2 (MeuTXKbeta2; Arthropods, animals) A9XE59 Belongs to the long chain scorpion toxin family (Class 1 subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has a low affinity binding to potassium channels of rat brain synaptosomes. Displays weak antibacterial activity against Stenotrophomonas sp. Strongly inhibits the development of the Plasmodium berghei ookinetes. Displays slight hemolytic effect on mouse erythrocytes. Induces cytolysis on Xenopus oocytes at high concentrations. Is not toxic on mice and on the insect Tenebrio molitor. Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database [Ref.20045493]Slight hemolytic activity against mouse erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20045493 Biochim Biophys Acta. 2010 Apr;1804(4):872-883. Zhu S, Gao B, Aumelas A, del Carmen Rodríguez M, Lanz-Mendoza H, Peigneur S, Diego-Garcia E, Martin-Eauclaire MF, Tytgat J, Possani LD. MeuTXKbeta1, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity. DRAMP03711 GLIHKVTKVQQLCAFNQDMAGWCEKSCQAAEGKNGYCHGTKCKCGKPLSYRRK 53 Scorpine-like peptide (OcyC7; Arthropods, animals) C5J891 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Opisthacanthus cayaporum (South American scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Has antibacterial activity (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19379768 Toxicon. 2009 Sep 1;54(3):252-561. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03712 IFKAIWSGIKSLF 13 Peptide Hp1090 (Non-disulfide-bridged peptide 5.9, NDBP-5.9; Arthropods, animals) P0DJ02 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial, Antibacterial, Antiviral Transcript level Alpha helix (CD) CD spectroscopy analysis indicates that Hp1090 is an amphipathic α-helical peptide that prevents the initiation of HCV infection by directly interactingwith viral particles and rapidly permeabilizing their phospholipid membranes. "Function: The peptide showed antibacterial activity against both Gram-negative and Gram-positive bacteria. Tissue specificity: Expressed by the venom gland. Miscellaneous: This peptide has a significant inhibitory effect on hepatitis C virus (HCV) infection (IC50=7.62 µg/ml). Furthermore, this peptide potently inhibits HCV before viral entry into cells and kills HCV rapidly in vitro. PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Binding to HCV 20950663 Peptides. 2011 Jan;32(1):11-19. Yan R, Zhao Z, He Y, Wu L, Cai D, Hong W, Wu Y, Cao Z, Zheng C, Li W. A new natural alpha-helical peptide from the venom of the scorpion Heterometrus petersii kills HCV. DRAMP03713 IFSAIGGFLKSIF 13 Peptide Hp1035 (Non-disulfide-bridged peptide 5.10, NDBP-5.10; Arthropods, animals) P0DJ03 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Amphipathic peptide with probable antibacterial activities. Hp1035 peptide, showing high homology to Hp1090, exhibited no anti-HCV activity. Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20950663 Peptides. 2011 Jan;32(1):11-19. Yan R, Zhao Z, He Y, Wu L, Cai D, Hong W, Wu Y, Cao Z, Zheng C, Li W. A new natural alpha-helical peptide from the venom of the scorpion Heterometrus petersii kills HCV. DRAMP03716 KSTVGQKLKKKLNQAVDKVKEVLNKSEYMCPVVSSFCKQHCARLGKSGQCDLLECICS 58 Potassium channel toxin Hge-beta-KTx (HgebetaKTx; Arthropods, animals) Q0GY41 Long chain scorpion toxin family (Class 2 subfamily) Not found Hadrurus gertschi (Scorpion) Antimicrobial, Antibacterial Protein level Not found Not found "Function: The full peptide presents antibacterial and cytotoxic activities. The C-terminus (33-76aa) blocks potassium channels Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA3. Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17506894##18030427 BMC Genomics. 2007 May 16;8:119.##Cell Mol Life Sci. 2008 Jan;65(1):187-200. Schwartz EF, Diego-Garcia E, Rodríguez de la Vega RC, Possani LD.##Diego-García E, Abdel-Mottaleb Y, Schwartz EF, de la Vega RC, Tytgat J, Possani LD. Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones).##Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like peptides purified from scorpion venoms. DRAMP03717 GRGREFMSNLKEKLSGVKEKMKNS 24 Meucin-24 (Arthropods, animals) P0CH57 Long chain scorpion toxin family (Class 2 subfamily) Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimalarial Protein level Alpha helix (1 helices; 17 residues) Circular dichroism (CD) analysis of chemically synthesized peptides demonstrates that meucin-24 presents an essential random coil conformation in water, but its alpha-helical content largely increases in the presence of 50% trifluoroethanol, a membrane-mimicking environment. 2KFE resolved by NMR. "Function: The synthetic meucin-24 inhibits the development of P. berghei ookinetes, kills intraerythrocytic P.falciparum, and is cytotoxic to the Drosophila S2 cell at micromolar concentrations. No hemolytic activities have been found at micromolar concentrations. Tissue specificity: Expressed by the venom gland. Miscellaneous: The RNA coding for this protein is silently edited. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database [Ref.20097251]Non-hemolytic effect against mouse erythrocytes even at 100 μM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20097251 Biochimie. 2010 Apr;92(4):350-359. Gao B, Xu J, Rodriguez Mdel C, Lanz-Mendoza H, Hernández-Rivas R, Du W, Zhu S. Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus. DRAMP03718 VKLIQIRIWIQYVTVLQMFSMKTKQ 25 Meucin-25 (BeL-170; Arthropods, animals) P0CH58 Not found Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimalarial Transcript level Not found CD results indicate that meucin-25 mainly adopts a beta-sheet structure in water but TFE promotes its alpha-helical formation, suggesting its conformational flexibility. "Function: This synthetic cationic peptide inhibits the development of Plasmodium berghei ookinetes, kills intraerythrocytic P. falciparum, and is cytotoxic to the Drosophila S2 cell at micromolar concentrations. No hemolytic activities have been found at micromolar concentrations. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database [Ref.20097251]Non-hemolytic effect against mouse erythrocytes even at 101 μM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20097251 Biochimie. 2010 Apr;92(4):350-359. Gao B, Xu J, Rodriguez Mdel C, Lanz-Mendoza H, Hernández-Rivas R, Du W, Zhu S. Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus. DRAMP03719 GFGCPLNQGACHRHCRSIRRRGGYCAGFFKQTCCYRN 37 Scorpion defensin (Arthropods, animals) No entry found Not found Not found Leiurus quinquestriatus Antimicrobial, Antibacterial Not found Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8333834 Biochem Biophys Res Commun. 1993 Jul 15;194(1):17-22. Cociancich S, et al Hoffmann J. Purification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins. DRAMP03720 GFGCPLNQGACHRHCRSIRRRGGYCAGFFKQTCTCYRN 38 4 kDa defensin (Antibacterial 4 kDa peptide; Arthropods, animals) P41965 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Leiurus quinquestriatus hebraeus (Yellow scorpion) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial protein against Gram-positive bacteria; may act via membrane-permeabilization of these cells. PTM: Contains three disulfide bonds 4-25; 11-33; 15-35 (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8333834 Biochem Biophys Res Commun. 1993 Jul 15;194(1):17-22. Cociancich S, Goyffon M, Bontems F, Bulet P, Bouet F, Menez A, Hoffmann J. Purification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins. DRAMP18417 FFGTLFKLGSKLIPGVMKLFSKKKER 26 ToAP2 A0A1D3IXJ5 Derived from NDBP subfamily 3 Not found Tityus obscurus Antimicrobial, Antifungal, Antibiofilm Transcript level Alpha helix The peptide adopts a structure with 57.69% alpha helix Function: antifungal activity. Has hemolytic activity. [Ref.27917162] Fungi:Candida albicans (SC5314)(MIC=12.5μM);Candida tropicalis (ATCC 750)(MIC=3.12μM);Candida parapsilosis (ATCC 22019)(MIC=50μM);Candida glabrata (ATCC 90030)(MIC=200μM);Candida neoformans (H99 serotype A)(MIC=12.5μM) [Ref.27917162] 30% hemolysis at 1.58 μM, 37% hemolysis at 3.16 μM, 45% hemolysis at 6.31 μM, 46% hemolysis at 12.59 μM, 48% hemolysis at 25.12 μM, 47% hemolysis at 50.11 μM , 50% hemolysis at 100μM against human red blood cell Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27917162 Front Microbiol. 2016 Nov 18;7:1844. eCollection 2016. Guilhelmelli F, Vilela N, Smidt KS, de Oliveira MA, da Cunha Morales ?lvares A, Rigonatto MC, da Silva Costa PH, Tavares AH, de Freitas SM, Nicola AM, Franco OL, Derengowski LD, Schwartz EF, Mortari MR, Bocca AL, Albuquerque P, Silva-Pereira I. Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms. DRAMP03725 IFSAIAGLLSNLL 13 Non-disulfide-bridged peptide 5.5 (NDBP-5.5; Arthropods, animals) P0C8W1 Belongs to the scorpion NDBP 5 family Not found Hadrurus gertschi (Scorpion) Antimicrobial, Antibacterial Transcript level Alpha helix Not found Function: Has weak hemolytic activity. No MICs found in DRAMP database [Ref.17506894]Weak hemolytic activity against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17506894 BMC Genomics. 2007 May 16;8:119. Schwartz E.F, Diego-Garcia E, Rodriguez de la Vega R.C, Possani L.D. Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). DRAMP03726 FIFDLLKKLV 10 Non-disulfide-bridged peptide 5.6 (NDBP-5.6; Arthropods, animals) P0C8W2 Belongs to the scorpion NDBP 5 family Not found Hadrurus gertschi (Scorpion) Antimicrobial, Antibacterial Transcript level Alpha helix Not found Function: Has weak hemolytic activity. No MICs found in DRAMP database [Ref.17506894]Weak hemolytic activity against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17506894 BMC Genomics. 2007 May 16;8:119. Schwartz E.F, Diego-Garcia E, Rodriguez de la Vega R.C, Possani L.D. Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). DRAMP03727 GWMSEKKVQGILDKKLPEGIIRNAAKAIVHKMAKNQFGCFANVDVKGDCKRHCKAEDKEGICHGTKCKCGVPISYL 76 Hge-scorpine (Hg-scorpine-like 1, HgeScplp1, Hgscplike1; Arthropods, animals) Q0GY40, A8SDT6 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Hadrurus gertschi (Scorpion) Antimicrobial, Antibacterial Protein level Not found Not found 5IPO##5JYH "Function: Hge-scorpine has antibacterial activity against B. subtilis, but not against S. aureus. Also has hemolytic and cytolytic activities. Hge36 peptide blocks Kv1.1/KCNA1 (IC50=185 nM) potassium channels. Shows a weak hemolytic activity. Tissue specificity: Expressed by the venom gland. Miscellaneous: The C-terminus (AA 52-95) blocks Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA2 potassium channels, showing a potential important role of AA 48-51. Hge36 peptide does not block Kv1.2/KCNA2 and Kv1.3/KCNA3. PTM: Contains three disulfide bonds (By similarity)." [Ref.18030427]Gram-postive bacteria:Bacillus subtilis(++), Staphylococcus aureus(-) [Swiss_Prot Entry Q0GY40]has hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18030427 Cell Mol Life Sci. 2008 Jan;65(1):187-200. Diego-García E, Abdel-Mottaleb Y, Schwartz EF, de la Vega RC, Tytgat J, Possani LD. Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like peptides purified from scorpion venoms. DRAMP03728 GILREKYAHKAIDVLTPMIGVPVVSKIVNNAAKQLVHKIAKNQQLCMFNKDVAGWCEKSCQQSAHQKGYCHGTKCKCGIPLNYK 84 Hg-scorpine-like 2 (Arthropods, animals) P0C8W5 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Hadrurus gertschi (Scorpion) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against yeasts and bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." Yeasts No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17506894 BMC Genomics. 2007 May 16;8:119. Schwartz EF, Diego-Garcia E, Rodríguez de la Vega RC, Possani LD. Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). DRAMP03730 KWLNEKSIQNKIDEKIGKNFLGGMAKAVVHKLAKNEFMCMANMDPTGSCETHCQKASGEKGYCHGTKCKCGVPLSY 76 Opiscorpine-2 (Arthropods, animals) Q5WR01, Q5WR02 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against yeasts and bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." Yeasts No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15241551 Cell Mol Life Sci. 2004 Jul;61(14):1751-1763. Zhu S, Tytgat J. The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition. DRAMP03731 KWLNEKSIQNKIDEKIGKNFLGGMAKAVVHKLAKNEFMCVANVDMTKSCDTHCQKASGEKGYCHGTKCKCGVPLSY 76 Opiscorpine-3 (Arthropods, animals) Q5WQZ7 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against yeasts and bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." Yeasts No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15241551 Cell Mol Life Sci. 2004 Jul;61(14):1751-1763. Zhu S, Tytgat J. The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition. DRAMP03732 KWLNEKSIQNKIDEKIGKNFLGGMAKAVVHKLAKNEFMCVANIDMTKSCDTHCQKASGEKGYCHGTKCKCGVPLSY 76 Opiscorpine-4 (Arthropods, animals) Q5WQZ9 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Antifungal Transcript level Not found Not found "Function: Has antimicrobial activity against yeasts and bacteria (By similarity). Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." Yeasts No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15241551 Cell Mol Life Sci. 2004 Jul;61(14):1751-1763. Zhu S, Tytgat J. The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition. DRAMP03733 SIYERCELARELINR 15 Lysozyme (Arthropods, animals) P0C8X2 Belongs to the glycosyl hydrolase 22 family Not found Tityus stigmurus (Brazilian scorpion) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Lysozymes have primarily a bacteriolytic Function: (By similarity). Catalytic activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17270501 Comp Biochem Physiol C Toxicol Pharmacol. 2007 Jul-Aug;146(1-2):147-157. Batista C.V.F, Roman-Gonzalez S.A, Salas-Castillo S.P, Zamudio F.Z, Gomez-Lagunas F, Possani L.D. Proteomic analysis of the venom from the scorpion Tityus stigmurus: biochemical and physiological comparison with other Tityus species. DRAMP03736 GKVWDWIKSTAKKLWNSEPVKELKNTALNAAKNFVAEKIGATPS 44 Opistoporin-2 (OP2; Non-disulfide-bridged peptide 3.6, NDBP-3.6; Arthropods, animals) P83314 Belongs to the antimicrobial peptide scorpion family Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix Not found "Function: At high concentrations, acts as pore former in cellular membranes and causes the leakage of the cells. At submicromolar concentrations, degranulates granulocytes and has weak hemolytic activity against human red blood cells. Also strongly inhibits the production of superoxide anions. Has a strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. (By similarity) Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P83314]strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. [Swiss_Prot Entry P83314]Weak hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12354111 Eur J Biochem. 2002 Oct;269(19):4799-4810. Moerman L, Bosteels S, Noppe W, Willems J, Clynen E, Schoofs L, Thevissen K, Tytgat J, Van Eldere J, Van Der Walt J, Verdonck F. Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa. DRAMP03737 GKVWDWIKKTAKDVLNSDVAKQLKNKALNAAKNFVAEKIGATPS 44 Opistoporin-4 (Non-disulfide-bridged peptides 3.7, NDBP-3.7; Arthropods, animals) Q5VJS9 Belongs to the antimicrobial peptide scorpion family Not found Opistophthalmus carinatus (African yellow leg scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: At high concentrations, acts as pore former in cellular membranes and causes the leakage of the cells. At submicromolar concentrations, degranulates granulocytes and has weak hemolytic activity against human red blood cells. Also strongly inhibits the production of superoxide anions. Has a strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. (By similarity) Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry Q5VJS9]strong antibacterial activity against Gram-negative bacteria but is less active against Gram-positive bacteria. Also has antifungal activity. [Swiss_Prot Entry Q5VJS9]Weak hemolytic activity against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane PubMed ID is not available Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Zhu S, Tytgat J. Precursor organization and gene structure of scorpion venom antimicrobial peptides. DRAMP03739 SIVPIRCRSNRDCRRFCGFRGGRCTYARQCLCGY 34 Buthinin (Sahara scorpion; Arthropods, animals) P56685, P81617 Not found Not found Androctonus australis (Sahara scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Active against both Gram-positive and Gram-negative bacteria. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Has three disulfide bonds L No cytotoxicity information found Not found 8939880 J Biol Chem. 1996 Nov 22;271(47):29537-29544. Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann JA, van Dorsselaer A, Bulet P. Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood. DRAMP03740 GFGCPFNQGACHRHCRSIRRRGGYCAGLFKQTCTCYR 37 Androctonus defensin (4 kDa defensin; Arthropods, animals) P56686, P81618 Belongs to the invertebrate defensin family (Type 2 subfamily) Not found Androctonus australis (Sahara scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Bridge Not found Function: Active against both Gram-positive and Gram-negative bacteria. Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8939880 J Biol Chem. 1996 Nov 22;271(47):29537-29544. Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann JA, van Dorsselaer A, Bulet P. Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood. DRAMP03741 IFGSLFSLGSKLLPSVFKLFSRKKQ 25 Ponericin-W-like 32.1 (Arthropods, animals) P0CI91 Belongs to the ponericin-W family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Insecticidal Transcript level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities (By similarity). Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P0CI91]Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae [Swiss_Prot Entry P0CI91]has hemolytic activities Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20663230 BMC Genomics. 2010 Jul 28;11:452. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03742 IFGSLFSLGSKLLPTVFKLFSRKKQ 25 Ponericin-W-like 32.2 (Arthropods, animals) P0CI92 Belongs to the ponericin-W family Not found Lychas mucronatus (Chinese swimming scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Insecticidal Transcript level Not found Not found "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities (By similarity). Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P0CI92]Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae [Swiss_Prot Entry P0CI92]has hemolytic activities Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20663230 BMC Genomics. 2010 Jul 28;11:452. Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L. Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03744 DNGYLLDKYTGCKVWCVINNESCNSECKIRGGYYGYCYFWKLACFCQGARKSELWNYNTNKCNGKL 66 Beta-toxin BmKAS (BmK AS, BmK-AS; BmK-PL; Arthropods, animals) Q9UAC9 Not found Not found Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Unknown Protein level Not found Not found Function: Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. It binds to distinct receptor sites of mammal and insect voltage-gated sodium channels. It displays antinociceptive effect in rat models, which is due to its specific modulation of sodium channels of sensory neurons. It also significantly stimulates the binding of [3H]-ryanodine to ryanodine receptors on the sarcoplasmic reticulum of the skeletal muscle through an indirect mechanism. And it promotes noradrenaline release from the rat hippocampus slice. Tissue specificity: Expressed by the venom gland. PTM: Contains four disulfide bonds 12-62; 16-37; 23-44; 27-46. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10191265##12376194 Biochem J. 1999 Apr 15;339 (Pt 2):343-350.##Brain Res. 2002 Oct 18;952(2):322-326. Kuniyasu A, Kawano S, Hirayama Y, Ji YH, Xu K, Ohkura M, Furukawa K, Ohizumi Y, Hiraoka M, Nakayama H.##Chen B, Ji Y. A new scorpion toxin (BmK-PL) stimulates Ca2+-release channel activity of the skeletal-muscle ryanodine receptor by an indirect mechanism.##Antihyperalgesia effect of BmK AS, a scorpion toxin, in rat by intraplantar injection. DRAMP03745 FIGAVAGLLSKIF 13 Peptide BmKn1 (Biologically active peptide 4; NDBP-5.1; Arthropods, animals) Q9GQW4 Belongs to the scorpion NDBP 5 family Kn1 Mesobuthus martensii (Buthus martensii) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Antibacterial peptide (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11463163##PubMed ID is not available IUBMB Life. 2001 Feb;51(2):117-120.##Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. Zeng XC, Li WX, Wang SX, Zhu SY, Luo F.##Li WX, Zhu SY. Precursor of a novel scorpion venom peptide (BmKn1) with no disulfide bridge from Buthus martensii Karsch.##A full-length cDNA encoding a putative active peptide, peptide 4, from Buthus martensii Karsch. DRAMP03747 FLSSLIPSAISGLISAFK 18 Peptide BmKb2 (Arthropods, animals) Q2M591 Not found Kb2 Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Antimicrobial Homology Not found Not found Function: May be an antimicrobial peptide (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet cell membrane 16040157 Peptides. 2005 Dec;26(12):2427-2433. Luo F, Zeng XC, Hahin R, Cao ZJ, Liu H, Li WX. Genomic organization of four novel nondisulfide-bridged peptides from scorpion Mesobuthus martensii Karsch: gaining insight into evolutionary mechanism. DRAMP03749 YPASMDNYDDALEELDNLDLDDYFDLEPADFVLLDMWANMLESSDFDDME 50 Peptide BmKa2 (Acidic venom peptide Ka2; NDBP-6.2; Arthropods, animals) Q8N0N8 Not found Ka2 Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Highly acidic peptide that may have antibacterial activity. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15062994##16040157 Peptides. 2004 Feb;25(2):143-150.##Peptides. 2005 Dec;26(12):2427-2433. Zeng XC, Wang SX, Zhu Y, Zhu SY, Li WX.##Luo F, Zeng XC, Hahin R, Cao ZJ, Liu H, Li WX. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch.##Genomic organization of four novel nondisulfide-bridged peptides from scorpion Mesobuthus martensii Karsch: gaining ins DRAMP03755 QFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS 37 Potassium channel toxin alpha-KTx 1.1 (ChTX-Lq1; charybdotoxin; Arthropods, animals) P13487 Not found Not found Leiurus quinquestriatus hebraeus (Yellow scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral Protein level Combine helix and strand structure These structures show that charybdotoxin is composed of a beta-sheet linked to an alpha-helix by two disulphide bridges and to an extended fragment by the third disulphide bridge. 1BAH, 2CRD resolved by NMR. "Function: Potent selective inhibitor of high conductance (maxi-K), different medium and small conductance calcium-activated potassium channels (KCa/KCNM), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3). It appears to block channel activity by a simple bimolecular inhibition process. Tissue specificity: Expressed by the venom gland. Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta). PTM: Contains three disulfide bonds." Gram-positive bacteria: B.subtilis, S.aureus;##Gram-negative bacterium: E.coli.##Yeast: Candida albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15118082##1705886##9092804##1380828 Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-7368.##Eur J Biochem. 1991 Feb 26;196(1):19-28.##Biochemistry. 1997 Apr 1;36(13):3760-3766.##Biochemistry. 1992 Sep 1;31(34):7756-7764. Yount NY, Yeaman MR.##Bontems F, Roumestand C, Boyot P, Gilquin B, Doljansky Y, Menez A, Toma F.##Song J, Gilquin B, Jamin N, Drakopoulou E, Guenneugues M, Dauplais M, Vita C, Ménez A.##Bontems F, Gilquin B, Roumestand C, Ménez A, Toma F. Multidimensional signatures in antimicrobial peptides.##Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins.##NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.##Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional i DRAMP03756 FLGGLWKAMSNLL 13 Cytotoxic linear peptide (Non-disulfide bridged protein family 5, NDBP-5; Arthropods, animals) H2CYR5 Not found Not found Pandinus cavimanus (Tanzanian red clawed scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Amphipathic peptide that has antibacterial activities. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 22121013 Proteomics. 2012 Jan;12(2):313-328. Diego-García E, Peigneur S, Clynen E, Marien T, Czech L, Schoofs L, Tytgat J. Molecular diversity of the telson and venom components from Pandinus cavimanus (Scorpionidae Latreille 1802): transcriptome, venomics and function. DRAMP03757 FIMDLLGKIF 10 Amphipathic peptide Tx348 (BoiTx348; Arthropods, animals) B8XH50 Not found Not found Buthus occitanus israelis (Common yellow scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "PTM: C-terminal amidation and Cleavage on pair of basic residues. Function: Amphipathic peptide that shows antibacterial acitivities." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane PubMed ID is not available Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Zilberberg N, Kozminsky-Atias A. Buthus occitanus israelis scorpion toxin. DRAMP18191 FLFSLIPHAISGLISAFK 18 Antimicrobial peptide AcrAP1 A0A0A1I6E7 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an Not found Androctonus crassicauda (Arabian fat-tailed scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found Has antimicrobial activity against the Gram-positive bacteria S.aureus and the yeast C.albicans. Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Gram-positive bacteria: S.aureus (MIC=8 uM, MBC=32 uM);##Yeast: C.albicans (MIC=16 uM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 25332684 Int. J. Biol. Sci. 10:1097-1107(2014) Du Q., Hou X., Ge L., Li R., Zhou M., Wang H., Wang L., Wei M.,Chen T., Shaw C. Cationicity-enhanced analogues of the antimicrobial peptides, AcrAP1and AcrAP2, from the venom of the scorpion, Androctonus crassicauda,display potent growth modulation effects on human cancer cell lines. DRAMP03759 FFSLIPSLIGGLVFAIK 17 Putative antimicrobial peptide clone 5 (Arthropods, animals) Q5G8B4 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial peptide.(By similarity) Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03760 FFSLIPSLIGGLVSAIK 17 Putative antimicrobial peptide clone 6 (Arthropods, animals) Q5G8B3 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Antibacterial peptide.(By similarity) Tissue specificity: Expressed by the venom gland. PTM: C-terminal amidation." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03761 GLREKHVQKLVALIPNDQLRSILKAVVHKVAKTQFGCPAYEGYCNNHCQDIERKDGECHGFKCKCAKD 68 Scorpine-like peptide Tco 41.46-2 (Arthropods, animals) Q5G8A6, Q5G8A7 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Scorpine-like peptide Tco 41.46-2 may have anti-bacterial activity.(By similarity) Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03762 YPTSYDDDFDALDDLDDLDLDDLLDLEPADLVLLDMWANMLDSQDFEDFE 50 Anionic peptide clone 7 (Asp-rich; Arthropods, animals) Q5G8B2 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial Transcript level Not found Not found "Function: May be an antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03763 YPASYDDDFDALDDLDDLDLDDLLDLEPADLVLLDMWANMLDSQDFEDFE 50 Anionic peptide clone 8 (Asp-rich; Arthropods, animals) Q5G8B1 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial Transcript level Not found Not found "Function: May be an antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03764 YPASYDDDFDALDDLDGLDLDDLLDSEPADLVLLDMWANMLDSQDFEDFE 50 Anionic peptide clone 9 (Asp-rich; Arthropods, animals) Q5G8B0 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial Transcript level Not found Not found "Function: May be an antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03765 YPASYDGDFDALDDLDDLDLDDLLDLEPADLVLLDMWANMLDSQDFEDFE 50 Anionic peptide clone 10 (Asp-rich; Arthropods, animals) Q5G8A9 Not found Not found Tityus costatus (Brazilian scorpion) Antimicrobial Transcript level Not found Not found "Function: May be an antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15683865 Toxicon. 2005 Mar 1;45(3):273-283. Diego-García E, Batista CV, García-Gómez BI, Lucas S, Candido DM, Gómez-Lagunas F, Possani LD. The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. DRAMP03766 GWINEEKIQKKIDEKIGNNILGGMAKAVVHKLAKGEFQCVANIDTMGNCETHCQKTSGEKGFCHGTKCKCGKPLSY 76 Heteroscorpine-1 (HS-1; defensins; Arthropods, animals) P0C2F4 Belongs to the long chain scorpion toxin family (Class 3 subfamily) Not found Heterometrus laoticus (Thai giant scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has antibacterial activity. Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds (By similarity). Toxic dose: PD50 is 80 ul to crickets (Gryllus sp)." Gram-positive bacterium: Bacillus subtilis (5.2 mm);##Gram-negative bacteria: Klebsiella pneumoniae (10.57 mm), Pseudomonas aeruginosa (6.4 mm).##NOTE: Diameter of clear zone from disc diffusion assay. Total protein is 6.25 µmole. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17056081 Toxicon. 2007 Jan;49(1):19-29. Uawonggul N, Thammasirirak S, Chaveerach A, Arkaravichien T, Bunyatratchata W, Ruangjirachuporn W, Jearranaiprepame P, Nakamura T, Matsuda M, Kobayashi M, Hattori S, Daduang S. Purification and characterization of Heteroscorpine-1 (HS-1) toxin from Heterometrus laoticus scorpion venom. DRAMP03768 ILSAIWSGIKS 11 OcyC1f (one chain of Non-disulfide-bridged peptide 5.7; Arthropods, animals) C5J886 Not found Not found isthacanthus cayaporum (South American scorpion) Antimicrobial Protein level Not found Not found "PTM: C-terminal amidation. Function: Amphipathic peptide with probable antimicrobial activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19857508##18695936 Toxicon. 2009 Sep 1;54(3):252-561.##Toxicon. 2008 Jun 15;51(8):1499-508. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF.##Schwartz EF, Camargos TS, Zamudio FZ, Silva LP, Bloch C Jr, Caixeta F, Schwartz CA, Possani LD. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum.##Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03769 GILGKIWEGVKSLI 14 OcyC2 (one chain of Non-disulfide-bridged peptide 5.8; Arthropods, animals) C5J887 Not found Not found isthacanthus cayaporum (South American scorpion) Antimicrobial Protein level Not found Not found "PTM: C-terminal amidation. Function: Amphipathic peptide with probable antimicrobial activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19379768 Toxicon. 2009 Sep 1;54(3):252-261. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03770 GILGKIWEGVKS 12 OcyC2f (one chain of Non-disulfide-bridged peptide 5.8; Arthropods, animals) C5J887 Not found Not found isthacanthus cayaporum (South American scorpion) Antimicrobial Protein level Not found Not found "PTM: C-terminal amidation. Function: Amphipathic peptide with probable antimicrobial activity." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19379768 Toxicon. 2009 Sep 1;54(3):252-261. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03771 FWATLAKGALKLIPTIANAFSSKS 24 Non-disulfide-bridged peptide 4.3 (NDBP-4.3; OcyC3; Arthropods, animals) C5J888 Not found Not found Opisthacanthus cayaporum (South American scorpion) Antimicrobial, Antibacterial Protein level Not found Not found Function: Amphipathic peptide with probable antimicrobial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19379768##18502464 Toxicon. 2009 Sep 1;54(3):252-261.##Toxicon. 2008 Jun 15;51(8):1499-508. Silva EC, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF.##Schwartz EF, Camargos TS, Zamudio FZ, Silva LP, Bloch C Jr, Caixeta F, Schwartz CA, Possani LD. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum.##Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum. DRAMP03772 FLGALLSKIF 10 Amphipathic peptide Hj0164 (Non-disulfide bridged protein family 5, NDBP-5; Arthropods, animals) F1CJ89 Not found Not found Buthotus judaicus (Scorpion) (Hottentotta judaica) Antimicrobial, Antibacterial Transcript level Not found Not found "PTM: C-terminal amidation and Cleavage on pair of basic residues. Function: Amphipathic peptide that shows antibacterial acitivities." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 21329713 Toxicon. 2011 Apr;57(5):695-703. Morgenstern D, Rohde BH, King GF, Tal T, Sher D, Zlotkin E. The tale of a resting gland: transcriptome of a replete venom gland from the scorpion Hottentotta judaicus. DRAMP03773 FKFGSFIKRMWRSKLAKKLRAKGKELLRDYANRVLSPEEEAAAPAPVPA 49 Meucin-49 (Arthropods, animals) P86407 Not found Not found Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) Antimicrobial Protein level Not found Not found "Function: Antimicrobial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2009) to UniProtKB Zhu S.Y, Gao B. Characterization of an antimicrobial peptide from the scorpion Mesobuthus eupeus venom. DRAMP03778 ANDPQCLYGNVAAKF 15 Agrocybin (Fungus) P84797 Not found Not found Agrocybe cylindracea (Toadstool) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Not found Not found Function: Has mitogenic activity towards murine splenocytes. Lacks antiproliferative activity towards HepG2 hepatoma cells. Mycosphaerella arachidicola (IC50=125 µM), HIV-1 reverse transcriptase (IC50=60 µM), Pseudomonas fluorescens. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15629530 Peptides. 2005 Feb;26(2):191-196. Ngai PH, Zhao Z, Ng TB. Agrocybin, an antifungal peptide from the edible mushroom Agrocybe cylindracea. DRAMP03779 XTYNGKCYKKDNICKYKAQSGKTAICKCYVKKCPRDGAKCEFDSYKGKCYC 51 Antifungal protein (AFP; Fungi) P17737 Not found afp Aspergillus giganteus Antimicrobial, Antifungal Protein level Beta strand (6 strands; 15 residues) The folding of AFP consists of five antiparallel beta strands connected in a -1, -1, +3, +1 topology and highly twisted, defining a small and compact beta barrel stabilized by four internal disulfide bridges. A cationic site formed by up to three lysine side chains adjacent to a hydrophobic stretch, both at the protein surface, may constitute a potential binding site for phospholipids which would be the basis of its biological function. 1AFP resolved by NMR. "Function: This protein inhibits the growth of a variety of fungal species. PTM: Contains four disulfide bonds 7-33; 14-40; 26-28; 49-51." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Phospholipids 2226447##7893713 Eur J Biochem. 1990 Oct 5;193(1):31-38.##Biochemistry. 1995 Mar 7;34(9):3009-3021. Nakaya K, Omata K, Okahashi I, Nakamura Y, Kolekenbrock H, Ulbrich N.##Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M. Amino acid sequence and disulfide bridges of an antifungal protein isolated from Aspergillus giganteus.##NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism. DRAMP03780 AIPIAYVGMAVAPQVFRWLVRAYGAAAVTAAGVTLRRVINRSRSNDNHSCYGNRGWCRSSCRSYEREYRGGNLGVCGSYKCCVT 84 Big defensin (AiBD) Q0H293 Not found Not found Argopecten irradians (Bay scallop) (Aequipecten irradians) Antimicrobial, Antibacterial Transcript level Not found Not found "Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro. Tissue specificity: Expressed in hemocytes. PTM: Contains three disulfide bonds 50-81; 57-76; 61-82." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16597463 Mol Immunol. 2007 Jan;44(4):360-368. Zhao J, Song L, Li C, Ni D, Wu L, Zhu L, Wang H, Xu W. Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein. DRAMP03781 MGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARGGRATAAVNAAQQAIGLGQITADRTHQGVREIKKGIKKLWG 81 CECdir-CECret No entry found Not found Not found Unknown Antimicrobial Not found Not found Not found CECdir-CECret displays an enhanced in vitro antimicrobial activity and action spectrum in comparison to the monomer Cecropin A. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18325631 Peptides. 2008 Apr;29(4):512-519. Schmitt P, Mercado L, Díaz M, Guzmán F, Arenas G, Marshall SH. Characterization and functional recovery of a novel antimicrobial peptide (CECdir-CECret) from inclusion bodies after expression in Escherichia coli. DRAMP03782 CPCGRRRCCVRGLNVYCCF 19 Corticostatin-related peptide LCRP (alpha-defensin) Q10996 Belongs to the alpha-defensin family Not found Petromyzon marinus (Sea lamprey) Antimicrobial Protein level Not found Not found "Function: May have microbicidal activities. May inhibit corticotropin (ACTH) stimulated steroidogenesis and the microbial actions of the corticostatins. PTM: Problely contains three disulfide bonds 1-18; 3-9; 8-17." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8759287 Comp Biochem Physiol B Biochem Mol Biol. 1996 Jun;114(2):133-137. Conlon JM, Sower SA. Isolation of a peptide structurally related to mammaliancorticostatins from the lamprey Petromyzon marinus. DRAMP03783 QWGYGGMPYGGYGGMGGYGMGGYGMGYRRRMWGSPYGGYGGYGGYGGWG 49 Neuropeptide-like protein 27 (NLP-27; Gly-rich, Tyr-rich; nematodes, animals; Predicted) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03784 QWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK 43 Neuropeptide-like protein 28 (NLP-28; Gly-rich, Tyr-rich; nematodes, animals; Predicted) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03785 QWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK 51 Neuropeptide-like protein 29 (NLP-29; nematodes, animals) O44664 Not found nlp-29 Caenorhabditis elegans Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Antimicrobial peptides that have antibacterial and antifungal activity. Tissue specificity: Weakly or not expressed in absence of infection. Upon infection by D. coniospora, it is expressed in hypoderm. Also expressed in perivulval cells when D. coniospora spores adhere to this region. Induction: Upon D. coniospora and S. marcescens infection. PTM: C-terminal amidation." Gram-negative bacterium: S. marcescens.##Fungi: D. coniospora. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11717458##15048112 Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):14000-14005.##Nat Immunol. 2004 May;5(5):488-494. Nathoo AN, Moeller RA, Westlund BA, Hart AC.##Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. Identification of neuropeptide-like protein gene families in Caenorhabditiselegans and other species.##TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03786 QWGYGGYGRGYGGYGGYGRGYGGYGRGYGGYGRGMWGRPYGGYGWGK 47 Neuropeptide-like protein 30 (NLP-30; Gly-rich, Tyr-rich; nematodes, animals; Predicted) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03787 NAQWGYGGYGRGYGGYGGYGRGYGGYGGYGRGYGGYGRGMYGGYGRPYGGYGWGK 55 Neuropeptide-like protein 31 (NLP-31; nematodes, animals) O44662 Belongs to the YARP family nlp-31 Caenorhabditis elegans Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found "Function: Antimicrobial peptide that has antifungal and weak antibacterial activity. Tissue specificity: Expressed in hypoderm. Developmental stage: Expressed in precomma stasge embryos. Induction: Strongly up-regulated upon D. coniospora infection. PTM: C-terminal amidation." Gram-positive bacterium: Micrococcus luteus;##Gram-negative bacterium: E.coli.##Fungi: D.coniospora. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11717458##15048112 Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):14000-5.##Nat Immunol. 2004 May;5(5):488-494. Nathoo AN, Moeller RA, Westlund BA, Hart AC.##Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. Identification of neuropeptide-like protein gene families in Caenorhabditis elegans and other species.##TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03788 QWGYGGPYGGYGGGYGGGPWGYGGGWRRRHWGGYGGGPWGGYGGGPWGGYY 51 Neuropeptide-like protein 33 (NLP-33; nematodes, animals) Q95ZN4 Not found nlp-33 Caenorhabditis elegans Antimicrobial, Antibacterial Transcript level Not found Not found "Function: May have antifungic activity. Tissue specificity: Expressed in hypoderm. Induction: Strongly up-regulated upon D. coniospora infection. PTM: C-terminal amidation." Fungi: Drechmeria coniospora. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9851916##15048112 Science. 1998 Dec 11;282(5396):2012-2018.##Nat Immunol. 2004 May;5(5):488-494. C. elegans Sequencing Consortium.## Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. Genome sequence of the nematode C. elegans: a platform for investigating biology.##TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03789 EASCARMDVPVMQRIAQGLCTSSCTAQKCMTGICKKVDSHPTCFCGGCSNANDVSLDTLISQLPHN 66 ABF-1 (nematodes, animals) No entry found Not found abf-1 Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11772394 Biochem J. 2002 Jan 15;361(Pt 2):221-230. Kato Y, Aizawa T, Hoshino H, Kawano K, Nitta K, Zhang H. abf-1 and abf-2, ASABF-type antimicrobial peptide genes in Caenorhabditis elegans. DRAMP03790 DIDFSTCARMDVPILKKAAQGLCITSCSMQNCGTGSCKKRSGRPTCVCYRCANGGGDIPLGALIKRG 67 ABF-2 (nematodes, animals) G5EC68 Not found abf-2 Caenorhabditis elegans Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Predicted Not found Not found 5IX5 Comment: No comments found on DRAMP database Gram-positive bacteria: Bacillus subtilis IFO3134 (BC50=0.09 µM), Kocuria varians MAFF118076 (BC50=0.008 µM), Staphylococcus aureus ATCC6538P (BC50=0.005 µM);##Gram-negative bacteria: Agrobacterium tumefaciens MAFF1001 (BC50=0.05 µM), Bdellovibrio bacteriovorus MAFF106101 (BC50=0.06 µM), Klebsiella pneumoniae MAFF519002 (BC50=0.9 µM), Escherichia coli JM109 (BC50>15 µM).##Fungi: Candida krusei MAFF114085 (BC50=0.3 µM), Debaryomyces hansenii MAFF113836 (BC50>15 µM), Kluyveromyces thermotolerans MAFF113848 (BC50=0.3 µM), Paeonia anomala MAFF113717 (BC50=0.08 µM), Saccharomyces cerevisiae MAFF113011 (BC50=0.6 µM), Torulaspora delbrueckiiMAFF113811 (BC50>15 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11772394 Biochem J. 2002 Jan 15;361(Pt 2):221-230. Kato Y, Aizawa T, Hoshino H, Kawano K, Nitta K, Zhang H. abf-1 and abf-2, ASABF-type antimicrobial peptide genes in Caenorhabditis elegans. DRAMP03791 QWGYNSYGYGNYGGYGGYPMYGGYGMNGGYGGGGLLGMFLGKKK 44 Caenacin-1 (Gly-rich, Tyr-rich; CNC-1; nematode, invertebrate, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03792 QYGYGGYPGMMGGYGGYPGMMGGYGMRPYGMGYGMGMGGMGMYRPGLLGMLMGK 54 Caenacin-2 (Gly-rich, Tyr-rich; CNC-2, nematode, invertebrate, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03793 QYGYGPMMGGYGPGMMGGYGPGMMGGYGPGMMGGYGPGMMGGYGMSPMYGGYGMYRPGLLGMLLG 65 Caenacin-3 (Gly-rich, Tyr-rich; CNC-3, nematode, invertebrate, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03794 QWGYGPYGGYGGGYPGMYGGYGMRPYGMYGGYGMGMYRPGLLGMLIGK 48 Caenacin-4 (Gly-rich, Tyr-rich; CNC-4, nematode, invertebrate, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03795 QWGYNSYGGYNSYGNYGGYGGGYNNGYGVNANLGVGGRGG 40 Caenacin-5 (Gly-rich, Tyr-rich; CNC-5, nematode, invertebrate, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15048112 Nat Immunol. 2004 May;5(5):488-494. Couillault C, Pujol N, Reboul J, Sabatier L, Guichou JF, Kohara Y, Ewbank JJ. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. DRAMP03796 NPANPLNLKKHHGVFCDVCKALVEGGEKVGDDDLDAWLDVNIGTLCWTMLLPLHHECEEELKKVKKELKKDIENKDSPDKACKDVDLC 88 T07C4.4 (SPP-1; saposin-like protein, SAPLIP; roundworm, nematoda, animals) No entry found Not found Not found Caenorhabditis elegans Antimicrobial, Antibacterial Not found Alpha helix (CD) The CD spectrum of recombinant DEL βgalSAP of T07C4.4 is found to have a minimum at 208 nm, a distinct shoulder at 222 nm and a maximum at about 193 nm, typical of alpha-helical proteins. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9920402 Biochim Biophys Acta. 1998 Dec 8;1429(1):259-264. Bányai L, Patthy L. Amoebapore homologs of Caenorhabditis elegans. DRAMP03798 MPCSCKKYCDPWEVIDGSCGLFNSKYICCREK 32 Corticostatin-related peptide RK-1 (RK-1; lagomorphs, mammals, animals) P81655 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial, Anti-Gram- Protein level Beta strand(3 strands; 13 residues) RK-1 consists of 32 residues, including six cysteines arranged into three disulfide bonds. The three-dimensional solution structure, determined by NMR, consists of a triple-stranded antiparallel beta-sheet and a series of turns and is similar to the known structures of other alpha-defensins (Ref.3). 1EWS resolved by NMR. "Function: Has antimicrobial activity against Escherichia coli and activates Ca(2+) channels in vitro. PTM: Contains three disulfide bonds 3-29; 5-19; 9-28." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys29,Cys5 and Cys19,Cys9 and Cys28. L No cytotoxicity information found Not found 8631871##11123900 J Biol Chem. 1996 May 3;271(18):10654-10659.##Biochemistry. 2000 Dec 26;39(51):15757-15764. Bateman A, MacLeod RJ, Lembessis P, Hu J, Esch F, Solomon S.##McManus AM, Dawson NF, Wade JD, Carrington LE, Winzor DJ, Craik DJ. The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney.##Three-dimensional structure of RK-1: a novel alpha-defensin peptide. DRAMP03799 KPYCSCKWRCGIGEEEKGICHKFPIVTYVCCRRP 34 Rabbit kidney defensin RK-2 (alpha-defensins; lagomorphs, mammals, animals) No entry found Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial, Anti-Gram- Not found Bridge Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9663443 Peptides. 1998;19(5):793-799. Wu ER, Daniel R, Bateman A. RK-2: a novel rabbit kidney defensin and its implications for renal host defense. DRAMP03800 VFCTCRGFLCGSGERASGSCTINGVRHTLCCRR 33 Neutrophil antibiotic peptide NP-5 (Microbicidal peptide NP-5; lagomorphs, mammals, animals) P07466 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Unknown Protein level Not found Not found Function: Microbicidal activity. PTM: Contains three disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8439302##2843652 Biochem Biophys Res Commun. 1993 Feb 15;190(3):1009-1016.##J Mol Biol. 1988 Jun 5;201(3):625-636. Sadro LC, Tremblay A, Solomon S, Palfree RG.##Pardi A, Hare DR, Selsted ME, Morrison RD, Bassolino DA, Bach AC 2nd. Differential expression of corticostatins/defensins: higher levels of CS-4 (NP-2) transcripts compared with CS-6 (NP-5) in rabbit lung.##Solution structures of the rabbit neutrophil defensin NP-5. DRAMP03801 VSCTCRRFSCGFGERASGSCTVNGVRHTLCCRR 33 Neutrophil antibiotic peptide NP-4 (Microbicidal peptide NP-4; lagomorphs, mammals, animals) P07467 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Unknown Protein level Not found Not found Function: Microbicidal activity. PTM: Contains three disulfide bonds (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1613398##3988726 J Leukoc Biol. 1992 Jun;51(6):634-639.##J Biol Chem. 1985 Apr 25;260(8):4579-4584. Michaelson D, Couto M, Rayner J.R, Ganz T.##Selsted ME, Brown DM, DeLange RJ, Harwig SS, Lehrer RI. Cationic defensins arise from charge-neutralized propeptides: amechanism for avoiding leukocyte autocytotoxicity?##Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils. DRAMP03802 GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR 34 Corticostatin 1 (Antiadrenocorticotropin peptide I; lagomorphs, mammals, animals) P07469 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Microbicidal activity and inhibits corticotropin (ACTH) stimulated corticosterone production. PTM: Problely contains three disulfide bonds 3-31; 5-20; 11-30." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3988726##2829194##1311240 J Biol Chem. 1985 Apr 25;260(8):4579-4584.##Proc Natl Acad Sci U S A. 1988 Jan;85(2):592-596.##Endocrinology. 1992 Mar;130(3):1413-1423. Selsted ME, Brown DM, DeLange RJ, Harwig SS, Lehrer RI.##Zhu QZ, Hu J, Mulay S, Esch F, Shimasaki S, Solomon S.##Zhu Q, Solomon S. Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils.##Isolation and structure of corticostatin peptides from rabbit fetal and adult lung.##Isolation and mode of action of rabbit corticostatic (antiadrenocorticotropin) peptide DRAMP03803 GRCVCRKQLLCSYRERRIGDCKIRGVRFPFCCPR 34 Corticostatin-2 (Antiadrenocorticotropin peptide II; Corticostatin II; lagomorphs, mammals, anima P07468 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Unknown Protein level Not found Not found "Function: Microbicidal activity and inhibits corticotropin (ACTH) stimulated corticosterone production. PTM: Problely contains three disulfide bonds 3-32; 5-21; 11-31." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3988726##1311240 J Biol Chem. 1985 Apr 25;260(8):4579-4584.##Endocrinology. 1992 Mar;130(3):1413-1423. Selsted ME, Brown DM, DeLange RJ, Harwig SS, Lehrer RI.##Zhu Q, Solomon S. Primary structures of six antimicrobial peptides of rabbit peritonealneutrophils.##Isolation and mode of action of rabbit corticostatic (antiadrenocorticotropin) peptides. DRAMP03804 VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR 33 Corticostatin-3 (Corticostatin III; Macrophage antibiotic peptide MCP-1; lagomorphs, mammals, ani P01376 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Bridge Not found "Function: This peptide has antibiotic, anti-fungi and antiviral activity. It also inhibits corticotropin (ACTH) stimulated corticosterone production. PTM: Contains three disulfide bonds (By similarity)." herpes simplex virus type I No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 6643497##3988726##1311240 J Immunol. 1989 Aug 15;143(4):1358-1365.##J Biol Chem. 1985 Apr 25;260(8):4579-4584.##Endocrinology. 1992 Mar;130(3):1413-1423. Ganz T, Rayner JR, Valore EV, Tumolo A, Talmadge K, Fuller F.##Selsted ME, Brown DM, DeLange RJ, Harwig SS, Lehrer RI.##Zhu Q, Solomon S. The structure of the Rabbit macrophage defensin genes and their organ-specific expression.##Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils.##Isolation and mode of action of rabbit corticostatic (antiadrenocorticotropin) peptides. DRAMP03805 VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR 33 Corticostatin-4 (Corticostatin IV; Macrophage antibiotic peptide MCP-2; lagomorphs, mammals, anim P01377 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial, Antifungal, Antiviral Protein level Bridge Not found "Function: This peptide has antibiotic, anti-fungi and antiviral activity. It also inhibits corticotropin (ACTH) stimulated corticosterone production. PTM: Problely contains three disulfide bonds 3-31; 5-20; 10-30." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 6643497##3988726##1311240 J Biol Chem. 1983 Dec 10;258(23):14485-14489.##J Biol Chem. 1985 Apr 25;260(8):4579-4584.##Endocrinology. 1992 Mar;130(3):1413-1423. Selsted ME, Brown DM, DeLange RJ, Lehrer RI.##Selsted ME, Brown DM, DeLange RJ, Harwig SS, Lehrer RI.##Zhu Q, Solomon S. Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of Rabbit lung macrophages.##Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils.##Isolation and mode of action of rabbit corticostatic (antiadrenocorticotrop DRAMP03806 GICACRRRFCLNFEQFSGYCRVNGARYVRCCSRR 34 Corticostatin-6 (Corticostatin VI; Neutrophil antibiotic peptide NP-6; lagomorphs, mammals, anima P80223, P80224 Belongs to the alpha-defensin family Not found Oryctolagus cuniculus (Rabbit) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Microbicidal activity and inhibits corticotropin (ACTH) stimulated corticosterone production. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8397087 Eur J Biochem. 1993 Sep 1;216(2):653-659. Fuse N, Hayashi Y, Fukata J, Tominaga T, Ebisui O, Satoh Y, Isohara T, Uno I, Imura H. Purification and characterization of new anti-adrenocorticotropin Rabbit neutrophil peptides (defensins). DRAMP03807 GFFALIPGIE 10 Pardaxin-1 (Pardaxin I) P81863 Belongs to the pardaxin family Not found Pardachirus marmoratus (Finless sole) (Achirus marmoratus) Cytotoxic Protein level Not found Not found Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Shown to be 5-10 times more toxic, cytolytic and active in membrane pore formation than pardaxin-2. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 3782138 J Biol Chem. 1986 Dec 15;261(35):16704-13. Lazarovici P, Primor N, Loew LM. Purification and pore-forming activity of two hydrophobic polypeptides from the secretion of the Red sea moses sole (Pardachirus marmoratus). DRAMP03808 GFFFP 5 Pardaxin-2 (Pardaxin II) P81864 Belongs to the pardaxin family Not found Pardachirus marmoratus (Finless sole) (Achirus marmoratus) Cytotoxic Protein level Not found Not found Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 3782138 J Biol Chem. 1986 Dec 15;261(35):16704-13. Lazarovici P, Primor N, Loew LM. Purification and pore-forming activity of two hydrophobic polypeptides from the secretion of the Red sea moses sole (Pardachirus marmoratus). DRAMP03809 GFFALIPKIISSPLFKTLLSAVGSALSSSGEQE 33 Pardaxin P-1 (Pardaxin Pa1) P81865 Belongs to the pardaxin family Not found Pardachirus pavoninus (Peacock sole) (Achirus pavoninus) Cytotoxic Protein level Not found Not found "Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Causes death in killfish oryzias latipes in 30 minutes at a concentration of 25 micrograms/ml. Subunit structure: In aqueous solution exists as a tetramer. Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17737623 Science. 1986 Jul 18;233(4761):341-343. Thompson SA, Tachibana K, Nakanishi K, Kubota I. Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus. DRAMP03810 GFFALIPKIISSPIFKTLLSAVGSALSSSGGQE 33 Pardaxin P-2 (Pardaxin Pa2) P23067 Belongs to the pardaxin family Not found Pardachirus pavoninus (Peacock sole) (Achirus pavoninus) Cytotoxic Protein level Alpha helix Pardaxin P-2 adopts a novel amphiphilic helix (7-11)-bend (12-13)-helix (14-26) motif with Pro-13 forming the focal point of the turn or bend between the two helices.(Ref.2) "Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Subunit structure: In aqueous solution exists as a tetramer. Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17737623##1868074 Science. 1986 Jul 18;233(4761):341-343.##Biochemistry. 1991 Aug 13;30(32):8009-8017. Thompson SA, Tachibana K, Nakanishi K, Kubota I.##Zagorski MG, Norman DG, Barrow CJ, Iwashita T, Tachibana K, Patel DJ. Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus.##Solution structure of pardaxin P-2. DRAMP03811 GFFAFIPKIISSPLFKTLLSAVGSALSSSGEQE 33 Pardaxin P-3 (Pardaxin Pa3) P81866, Q7LZJ4 Belongs to the pardaxin family Not found Pardachirus pavoninus (Peacock sole) (Achirus pavoninus) Cytotoxic Protein level Not found Not found "Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Subunit structure: In aqueous solution exists as a tetramer. Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 17737623 Science. 1986 Jul 18;233(4761):341-343. Thompson SA, Tachibana K, Nakanishi K, Kubota I. Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus. DRAMP03812 GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE 33 Pardaxin P-4 (Pardaxin P1a; Pardaxin Pa4) P81861 Belongs to the pardaxin family Not found Pardachirus marmoratus (Finless sole) (Achirus marmoratus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytotoxic Protein level Alpha helix (2 helices; 15 residues) The peptide adopts a bend-helix-bend-helix motif with an angle between the two structure helices of 122 +/- 9 degrees, making this structure substantially different from the one previously determined in organic solvents. 1XC0, 2KNS resolved by NMR. "Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria" [Ref.23598079] Gram-positive bacteria : Micrococcus luteus(MIC=100 mg/L), Staphylococcus aureus(MIC=50 mg/L), Streptococcus pneumoniae(MIC=100 mg/L), Streptococcus agalactiae(MIC=100 mg/L), Staphylococcus sp.(MIC=6.25 mg/L);##Gram-negative bacteria : Grouper Vibrio alginolyticus(MIC=50 mg/L), Vibrio harveyi(MIC=50 mg/L), Vibrio vulnificus(MIC=100 mg/L) [Ref.23598079] 7% hemolysis at 12.5 mg/L , 10% hemolysis at 25 mg/L , 27% hemolysis at 50 mg/L , 55% hemolysis at 100 mg/L , 95% hemolysis at 200 mg/L , 90% hemolysis at 400 mg/L against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 12124282##19959835##15292173##23598079 Biophys J. 2002 Aug;83(2):1004-1013.##J Biol Chem. 2010 Feb 5;285(6):3883-3895.##J Biol Chem. 2004 Oct 29;279(44):45815-23.##Peptides. 2013 Jun;44:139-48. Hallock KJ, Lee DK, Omnaas J, Mosberg HI, Ramamoorthy A.##Bhunia A, Domadia PN, Torres J, Hallock KJ, Ramamoorthy A, Bhattacharjya S.##Porcelli F, Buck B, Lee DK, Hallock KJ, Ramamoorthy A, Veglia G.##Lin MC, Hui CF, Chen JY, Wu JL Membrane composition determines pardaxin's mechanism of lipid bilayer disruption.##NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization.##Structure and orientation of pardaxin determined by NMR experiments in model membranes.##Truncated antimicrobial peptides from marine organisms retain anticancer activity and antibacterial activity against multidrug-resistant Staphylococcus aureus. DRAMP03813 GFFALIPKIISSPLFKTLLSAVGSALSSSGDQE 33 Pardaxin P-5 (Pardaxin P1a; Pardaxin Pa5) P81862 Belongs to the pardaxin family Not found Pardachirus marmoratus (Finless sole) (Achirus marmoratus) Cytotoxic Protein level Not found Not found "Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 9762902 FEBS Lett. 1998 Sep 18;435(2-3):173-177. Adermann K, Raida M, Paul Y, Abu-Raya S, Bloch-Shilderman E, Lazarovici P, Hochman J, Wellhöner H. Isolation, characterization and synthesis of a novel paradaxin isoform. DRAMP03817 RRWWFR 6 cRW2 peptide No entry found Not found Not found synthetic construct Antimicrobial Synthetic No secondary structure Not found 2OX2 resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17985394 J Pept Sci. 2008 Apr;14(4):524-527. Appelt C, Wessolowski A, Dathe M, Schmieder P. Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity. DRAMP03818 RRWFWR 6 cRW3 cationic antimicrobial peptide No entry found Not found Not found synthetic construct Antimicrobial Synthetic No secondary structure Not found 2OTQ resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17985394 J Pept Sci. 2008 Apr;14(4):524-527. Appelt C, Wessolowski A, Dathe M, Schmieder P. Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity. DRAMP03010 IKIMDILAKLGKVLAHV 17 Bombolitin III (insects, arthropods, invertebrates, animals) P07494 Not found Not found Megabombus pennsylvanicus (Bumblebee) Antimicrobial, Antibacterial, Anti Mammalian Cells Protein level Not found Not found Function: Mast cell degranulating peptide. Has hemolytic activity. No MICs found in DRAMP database [Ref.2578459] Hemolysis: ED50=2.8±0.05 µg/ml. Histamine release: ED50=10.4±0.4 µg/ml against guinea pig erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2578459 J Biol Chem. 1985 Feb 10;260(3):1437-144. Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. DRAMP03009 SKITDILAKLGKVLAHV 17 Bombolitin II (insects, arthropods, invertebrates, animals) P07493 Not found Not found Megabombus pennsylvanicus (Bumblebee) Antimicrobial, Antibacterial, Anti Mammalian Cells Protein level Not found Not found Function: Mast cell degranulating peptide. Has hemolytic activity. No MICs found in DRAMP database [Ref.2578459] Hemolysis: ED50=3.9±0.06 µg/ml. Histamine release: ED50=15.8±0.5 µg/ml against guinea pig erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2578459 J Biol Chem. 1985 Feb 10;260(3):1437-144. Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. DRAMP03008 IKITTMLAKLGKVLAHV 17 Bombolitin I (insects, arthropods, invertebrates, animals) P10521 Not found Not found Megabombus pennsylvanicus (Bumblebee) Antimicrobial, Antibacterial, Anti Mammalian Cells Protein level Not found Not found Function: Mast cell degranulating peptide. Has hemolytic activity. No MICs found in DRAMP database [Ref.2578459] Hemolysis: ED50=4.0±0.05 µg/ml. Histamine release: ED50=16.3±0.5 µg/ml against guinea pig erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2578459 J Biol Chem. 1985 Feb 10;260(3):1437-144. Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. DRAMP03822 RRAARF 6 Cyclic hexapeptide RR(NAL)(NAL)RF No entry found Not found Not found Synthetic construct Antimicrobial Synthetic No secondary structure Not found 1SKL resolved by NMR. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16075425 Chembiochem. 2005 Sep;6(9):1654-1662. Appelt C, Wessolowski A, SöderhÃäll JA, Dathe M, Schmieder P. Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles. DRAMP03836 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFLNVNCWCET 44 ETD135 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found 1P0A Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=1.56 µg/ml), Candida albicans No.245962 (MIC50=1.56 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=6.25 µg/ml), Cryptococcus neoformans A (MIC50=6.25 µg/ml), Fusarium solani FFUS 8591 (MIC50=1.56 µg/ml), Scedosporium prolificans FSSP 8591 (MIC50=0.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03837 DKLIGSCVWGAVNYTSNCRAECKRRGYKGGHCGSFLNVNCWCET 44 ETD179 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=1.56 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03838 DKLIGSCVWGAVNYTSNCRAECKRRGYKGGHCGSFANVNCWCET 44 ETD151 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found 1P00 Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Candida albicans No.245962 (MIC50=0.4 µg/ml), Aspergillus fumigatus GASP 4707 (MIC50=6.25 µg/ml), Cryptococcus neoformans A (MIC50=1.56 µg/ml), Fusarium solani FFUS 8591 (MIC50=0.4 µg/ml), Scedosporium prolificans FSSP 8591 (MIC50=0.1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03839 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCQT 44 ETD131 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=3.125 µg/ml), Cryptococcus neoformans A (MIC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03840 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCER 44 ETD130 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found 1OZZ Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=1.56 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03841 NKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCET 44 ETD140 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03842 DKLIGSCVWGAVNYTRNCNAECKRRGYKGGHCGSFANVNCWCET 44 ETD150 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=6.25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03843 DKLIGSCVWGAVNYTSRCNAECKRRGYKGGHCGSFANVNCWCET 44 ETD152 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03844 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFINVNCWCET 44 ETD132 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=6.25 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=6.25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03845 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANINCWCET 44 ETD133 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=6.25 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03846 DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFLNINCWCET 44 ETD134 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=1.56 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=3.125 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03847 DKLIGSCVWLAVNYTSNCNAECKRRGYKGGHCGSFLNVNCWCET 44 ETD154 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=6.25 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=12.5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP18190 FLSTIWNGIKSLL 13 Pantinin-3 (Non-disulfide-bridged peptide 4.22, NDBP-4.22, Non-disulfide-bridged peptide 5.23, ND R4JJN6 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Amphipathic peptide that possesses relatively strong activities against Gram-positive bacteria and a fungus, but has very weak antimicrobial activities against Gram-negative bacteria. Also exhibits hemolytic activities against human erythrocytes. Furthermore, this peptide potently inhibits the growth of vancomycin-resistant Enterococcus (VRE) S13, a pathogen that can cause a number of human infections.Forms an alpha-helical membrane channel in the prey. [Ref.23624072]Gram-positive bacteria: S.aureus (MIC=16 μM), B.magaterium (MIC=6 μM), M.luteus (MIC=8 μM ), VRE (MIC=4 μM), MRSA (MIC=12 μM);##Gram-negative bacteria: E.coli (MIC=36 μM), P.putida (MIC >87 μM), K.oxytoca (MIC=87 μM), E.cloacae (MIC >87 μM), S.enterica (MIC=84 μM);##Fungus: C.tropicalis (MIC=17 μM). [Ref.23624072]70% hemolytic activity at 16 μM, 100% hemolytic activity at 32 μM, 100% hemolytic activity at 64 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 23624072##24184590 Peptides 45:28-34(2013)##Peptides 51:35-45(2014 Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,Cao B., Cao H.##Almaaytah A., Albalas Q. Three new antimicrobial peptides from the scorpion Pandinusimperator.##Scorpion venom peptides with no disulfide bridges: a review. DRAMP03849 DKLIGSCVWLAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCET 44 ETD156 (Mutant of ARD1; Heliomicin analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Candida albicans IHEM 8060 (MIC50=3.125 µg/ml), Aspergillus fumigatus GASP4707 (MIC50=25 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14978308 Protein Sci. 2004 Mar;13(3):703-713. Landon C, Barbault F, Legrain M, Menin L, Guenneugues M, Schott V, Vovelle F, Dimarcq JL. Lead optimization of antifungal peptides with 3D NMR structures analysis. DRAMP03850 FALALKALKKALKKLKKALKKAL 23 Antibacterial peptide/melittin homolog No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8714745 Scanning Microsc. 1995 Jun;9(2):501-507. Henk WG, Todd WJ, Enright FM, Mitchell PS. The morphological effects of two antimicrobial peptides, hecate-1 and melittin, on Escherichia coli. DRAMP03851 TWLKKRRWKKAKPP 14 Cyclic L27-11 (protegrin-1-mimetic) No entry found Not found Not found Synthetic construct (peptide library screen) Antimicrobial, Antibacterial Synthetic Not found Not found Function: This circular peptide is designed as a mimic of PG-1. The peptidomimetics had a non-membrane-lytic mechanism of action and identified a homolog of the beta-barrel protein LptD (Imp/OstA), which functions in outer-membrane biogenesis, as a cellular target. Animal model (mouse): The peptide showed in vivo efficacy in a mouse septicemia infection model. The original LLP1 (lentivirus lytic peptide 1) has been replaced. Pseudomonas aeruginosa (Remarkably). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Gram-negative bacterial outer membrane protein LptD 20167788 Science. 2010 Feb 19;327(5968):1010-1013. Srinivas N, Jetter P, Ueberbacher BJ, Werneburg M, Zerbe K, Steinmann J, Van der Meijden B, Bernardini F, Lederer A, Dias RL, Misson PE, Henze H, Zumbrunn J, Gombert FO, Obrecht D, Hunziker P, Schauer S, Ziegler U, KÃäch A, Eberl L, Riedel K, DeMarco SJ, Robinson JA. Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa. DRAMP03872 FQWQRNMRKV 10 hLf 21-30 (fragment of human lalctoferricin, residues 21-30) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>300 µM), Escherichia coli (wild strain) (MIC>300 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>300 µM), Enterococcus faecalis ATCC 29212 (MIC>300 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03873 LRWQNEMRKV 10 mLf 20-29 (fragment of murine lalctoferricin, residues 20-29) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>300 µM), Escherichia coli (wild strain) (MIC>300 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>300 µM), Enterococcus faecalis ATCC 29212 (MIC>300 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03874 RQWQSKIRRT 10 pLf20-29 (fragment of porcine lactoferricin, residues 20-29) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC>300 µM), Escherichia coli (wild strain) (MIC>300 µM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC>300 µM), Enterococcus faecalis ATCC 29212 (MIC>300 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 13677384 Am J Vet Res. 2003 Sep;64(9):1088-1092. Chen PW, Shyu CL, Mao FC. Antibacterial activity of short hydrophobic and basic-rich peptides. DRAMP03913 KWKWKW 6 (KW)3 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03914 KWKWKWKW 8 (KW)4 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03915 KWKWKWKWKW 10 (KW)5 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03916 RWRW 4 (RW)2 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03917 RWRWRW 6 (RW)3 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03918 RWRWRWRW 8 (RW)4 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03919 RWRWRWRWRW 10 (RW)5 No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antifungal Synthetic Not found Not found Function: Possess antifungal activity. Fungi: Fusarium solani, Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23203110 Int J Mol Sci. 2012; 13(11): 15042-15053. Gopal R, Na H, Seo CH, Park Y. Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum. DRAMP03926 GWLRKLGAVLKVLTT 15 Cecropin B (1-7)-melittin (4-11)hybrid peptide (CBM) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Function: The hemolytic assays indicated CBM had no hemolytic in vivo and in vitro. [Ref.20111863]Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumoniae, Bacillus subtilis, Bacillus thuringiensis, Salmonella derby. [Ref.20111863]0.05% hemolytic activity at 5 mg/kg, 0.14% hemolytic activity at 10 mg/kg in vivo Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20111863 Curr Microbiol. 2010 Sep;61(3):169-175. Cao Y, Yu RQ, Liu Y, Zhou HX, Song LL, Cao Y, Qiao DR. Design, recombinant expression, and antibacterial activity of the cecropins-melittin hybrid antimicrobial peptides. DRAMP03932 ILRWPWWPWRRKM 13 Indolicidin derivative No entry found Not found Not found Synthetic construct Antimicrobial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15154847 Biotechnol Appl Biochem. 2004 Jun;39(Pt 3):339-345. Metlitskaia L, Cabralda JE, Suleman D, Kerry C, Brinkman J, Bartfeld D, Guarna MM. Recombinant antimicrobial peptides efficiently produced using novel cloning and purification processes. DRAMP03940 FPWWWPF 7 Peptide 4 (Trp- and Arg-rich; derivative of Tritrpticin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Rich Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8706838 FEBS Lett. 1996 Jul 15;390(1):95-98. Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. DRAMP03941 RFPWWWPFLR 10 Peptide 3 (Trp- and Arg-rich; derivative of Tritrpticin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Rich Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Pseudomonas, Klebsiella, Proteus species;##Gram-positive bacteria: Streptococcus, Staphylococcus species. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8706838 FEBS Lett. 1996 Jul 15;390(1):95-98. Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. DRAMP03942 RRRFPWVCWPFLRRR 15 Peptide 2 (Trp- and Arg-rich; derivative of Tritrpticin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Rich Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumonia, Proteus mirabilis;##Gram-positive bacteria: Staphylococcus epidermidis, Streptococcus group D.##Fungi: Aspergillus fumigatus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8706838 FEBS Lett. 1996 Jul 15;390(1):95-98. Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. DRAMP03943 VXLFPKKPFLXV 12 Gratisin analogue No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Its activity against Pseudomonas aeruginosa IFO 3080 was two times higher than gramicidin S. Gram-negative bacterium: Pseudomonas aeruginosa IFO 3080. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18305357 J Antibiot (Tokyo). 2008 Jan;61(1):33-35. Tamaki M, Kokuno M, Suzuki Y, Iwama M, Shindo M, Uchida Y. A novel polycationic analogue of gratisin with antibiotic activity against both Gram-positive and Gram-negative bacteria. DRAMP18396 FFWHHIGHALDAAKRVHGMLSG 22 moroNC-NH2 (moronecidin-like peptide; fish, animals) No entry found Not found Not found Notothenia coriiceps Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against Gram- S. sonnei (ATCC 29930) (MIC 12.5 uM), Psychrobacter sp. (PAMC 25501) (MIC 5 uM), E. coli DH5alpha (MIC 12.5 uM), Gram+ S. pyogenes (ATCC 19615) (MIC 25 uM), S. aureus (ATCC 33591) (MIC 25 uM) , L. monocytogenes (ATCC 15313) (MIC 12.5 uM), and yeast C. tropicalis (ATCC 20115) (MIC 5 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28122029 PLoS One. 2017 Jan 25;12(1):e0170821. Shin SC, Ahn IH, Ahn DH, Lee YM, Lee J, Lee JH, Kim HW, Park H. Characterization of Two Antimicrobial Peptides from Antarctic Fishes (Notothenia coriiceps and Parachaenichthys charcoti) DRAMP03946 GLIKIVPAMICAVTKKC 17 Del 1-3 (Ranalexin analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-positive bacterium: Staphylococcus aureus (MIC>256 µg/ml);##Gram-negative bacteria: Escherichia coli (MIC>256 µg/ml), Pseudomonas aeruginosa (MIC>256 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8144672 J Biol Chem. 1994 Apr 8;269(14):10849-10855. Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. DRAMP03950 QKLCMRPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC 51 Rs-AFP2 variant (Mutation: Q5M) P30230, Q003I2 Not found Not found Synthetic construct (Mutation of Rs-AFP2) Antimicrobial, Antifungal Synthetic Not found Not found Compared to Rs-AFP2, the mutation Rs-AFP2(Q5M) has increased antifungal potency. SMF- (synthetic low ionic strength medium): Fusarium culmorum (IC50=4.1±0.2); SMF+ (SMF +1 mM CaCl2 and 50 mM KCl): Fusarium culmorum (IC50=5.4±1.2) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8995418 J Biol Chem. 1997 Jan 10;272(2):1171-1179. De Samblanx GW, Goderis IJ, Thevissen K, Raemaekers R, Fant F, Borremans F, Acland DP, Osborn RW, Patel S, Broekaert WF. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. DRAMP03951 QKLCQRPSGTWSGVCMNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC 51 Rs-AFP2 variant (Mutation: G16M) P30230, Q003I2 Not found Not found Synthetic construct (Mutation of Rs-AFP2) Antimicrobial, Antifungal Synthetic Not found Not found Compared to Rs-AFP2, the mutation Rs-AFP2(G16M) has increased antifungal potency. SMF- (synthetic low ionic strength medium): Fusarium culmorum (IC50=2.2±0.3);##SMF+ (SMF + 1 mM CaCl2 and 50 mM KCl): Fusarium culmorum (IC50=5.0±0.9). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8995418 J Biol Chem. 1997 Jan 10;272(2):1171-1179. De Samblanx GW, Goderis IJ, Thevissen K, Raemaekers R, Fant F, Borremans F, Acland DP, Osborn RW, Patel S, Broekaert WF. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. DRAMP03952 QKLCQRPSRTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC 51 Rs-AFP2 variant (Mutation: G9R) P30230, Q003I2 Not found Not found Synthetic construct (Mutation of Rs-AFP2) Antimicrobial, Antifungal Synthetic Not found Not found Compared to Rs-AFP2, the mutation Rs-AFP2(G9R) has increased antifungal potency. SMF- (synthetic low ionic strength medium): Fusarium culmorum (IC50=3±0.5);##SMF+ (SMF + 1 mM CaCl2 and 50 mM KCl): Fusarium culmorum (IC50=3.3±0.6). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8995418 J Biol Chem. 1997 Jan 10;272(2):1171-1179. De Samblanx GW, Goderis IJ, Thevissen K, Raemaekers R, Fant F, Borremans F, Acland DP, Osborn RW, Patel S, Broekaert WF. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. DRAMP03953 QKLCQRPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYRFPAHKCICYFPC 51 Rs-AFP2 variant (Mutation: V39R) P30230, Q003I2 Not found Not found Synthetic construct (Mutation of Rs-AFP2) Antimicrobial, Antifungal Synthetic Not found Not found Compared to Rs-AFP2, the mutation Rs-AFP2(V39R) has increased antifungal potency. SMF- (synthetic low ionic strength medium): Fusarium culmorum (IC50=4.0±0.2);##SMF+ (SMF + 1 mM CaCl2 and 50 mM KCl): Fusarium culmorum (IC50=3.2±0.3). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8995418 J Biol Chem. 1997 Jan 10;272(2):1171-1179. De Samblanx GW, Goderis IJ, Thevissen K, Raemaekers R, Fant F, Borremans F, Acland DP, Osborn RW, Patel S, Broekaert WF. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. DRAMP03961 KRIVQRIKDFLR 12 KR-12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Comment: No comments found on DRAMP database Gram-positive bacterium: Bacillus megaterium.##Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18818205 J Biol Chem. 2008 Nov 21;283(47):32637-32643. Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. DRAMP03962 KWKLFKKIGIGKFLHSAKKF 20 Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide (CAMA) P01507 Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Alpha helix Not found 1F0D, 1D9J resolved by NMR. MOA: The partial insertion of the Trp2 of CA-MA into the membrane, as well as the electrostatic interactions between the positively charged Lys residues at the N-terminus of the CA-MA and the anionic phospholipid headgroups, leads to the primary binding to the cell membrane. Then, the flexibility or bending potential induced by the Gly-Ile-Gly hinge sequence or the Pro residue in the central part of the peptides may allow the alpha-helix in the C-terminus to span the lipid bilayer. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11009597 Biochemistry. 2000 Oct 3;39(39):11855-11864. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. DRAMP03963 KWKLFKKIKFLHSAKKF 17 Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide analogue (P1) P01507 Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Alpha helix (1 helices; 9 residues) Not found 1F0F resolved by NMR. P1 has significantly decreased lytic activities against bacterial and tumor cells and PC/PS vesicles (3:1, w/w), and reduced pore-forming activity on lipid bilayers. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11009597 Biochemistry. 2000 Oct 3;39(39):11855-11864. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. DRAMP03964 KWKLFKKIPKFLHSAKKF 18 Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide analogue (P2) P01507 Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Alpha helix Not found 1F0E, 1D9M resolved by NMR. P2 retained effective lytic activities and pore-forming activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11009597 Biochemistry. 2000 Oct 3;39(39):11855-11864. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. DRAMP03965 KAKLFKKIGIGKFLHSAKKF 20 Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide analogue (P3) P01507 Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Alpha helix (1 helices; 10 residues) Not found 1F0H resolved by NMR. The N-terminal region of P3 has a flexible structure without any specific secondary structure. The P3 modification caused a drastic decrease in the antibiotic activities. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11009597 Biochemistry. 2000 Oct 3;39(39):11855-11864. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. DRAMP03966 KLKLFKKIGIGKFLHSAKKF 20 Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide analogue (P4) P01507 Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Alpha helix Not found 1F0G, 1D9P resolved by NMR. The hydrophobic Leu side chain of P4 is at position 2, retained its activities. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11009597 Biochemistry. 2000 Oct 3;39(39):11855-11864. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. DRAMP02092 FLPAIAGMAAKFLPKIFCAISKKC 24 Brevinin-1Bb (Frogs, amphibians, animals) P82834 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=1 μM);##Gram-negative bacterium: Escherichia coli (MIC=3 μM).##Yeast: Candida albicans (MIC=10 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP04006 GLVSGLLNTAGGLLGDLLGSLGSLSGGES 29 Plasticin-A1 (PTC-A1; DRP-AA-2-5; frogs, amphibians, animals) No entry found Not found Not found Agalychnis annae (AA) Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9774745 Biochim Biophys Acta. 1998 Oct 14;1388(1):279-283. Wechselberger C. Cloning of cDNAs encoding new peptides of the dermaseptin-family. DRAMP18189 IFGAIWKGISSLL 13 Pantinin-2 (Non-disulfide-bridged peptide 4.21, NDBP-4.21, Non-disulfide-bridged peptide 5.22, ND R4JQZ0 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Amphipathic peptide that possesses relatively strong activities against Gram-positive bacteria and a fungus, but has very weak antimicrobial activities against Gram-negative bacteria. Also exhibits mild hemolytic activities against human erythrocytes.Forms an alpha-helical membrane channel in the prey. [Ref.23624072]Gram-positive bacteria: S.aureus (MIC=48 μM), B.magaterium (MIC=36 μM), M.luteus (MIC=18 μM ), VRE (MIC=36 μM), MRSA (MIC=28 μM);##Gram-negative bacteria: E.coli (MIC=48 μM), P.putida (MIC >87 μM), K.oxytoca (MIC >87 μM), E.cloacae (MIC >87 μM), S.enterica (MIC=68 μM);##Fungus: C.tropicalis (MIC=16 μM). [Ref.23624072]10% hemolytic activity at 16 μM, 80% hemolytic activity at 32 μM, 100% hemolytic activity at 64 μM against human red bood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 23624072##24184590 Peptides 45:28-34(2013)##Peptides 51:35-45(2014 Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,Cao B., Cao H.##Almaaytah A., Albalas Q. Three new antimicrobial peptides from the scorpion Pandinusimperator.##Scorpion venom peptides with no disulfide bridges: a review. DRAMP04008 GLLSGILNTAGGLLGNLIGSLSN 23 Plasticin-C1 (PTC-C1; DRP-AC-1; frogs, amphibians, animals) No entry found Not found Not found Agalychnis callidryas Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP04009 GLLSGILNSAGGLLGNLIGSLSN 23 Plasticin-C2 (PTC-C2; DRP-AC-2; frogs, amphibians, animals) No entry found Not found Not found Agalychnis callidryas Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12709067 Eur J Biochem. 2003 May;270(9):2068-2081. Vanhoye D, Bruston F, Nicolas P, Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. DRAMP04010 GLVSDLLSTVTGLLGNLGGGGLKKI 25 Plasticin-S1 (PTC-S1; frogs, amphibians, animals) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal, Antiviral Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18644413 Peptides. 2008 Nov;29(11):2074-2082. Amiche M, Ladram A, Nicolas P. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. DRAMP04018 ALYKKFKKKLLKSLKRLG 18 Rp-1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found 2RLH, 2RLG resolved by NMR. Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria and the yeast candian Gram-positive bacteria: Staphylococcus, Streptococcus, Bacillus species;##Gram-negative bacteria: Escherichia, Salmonella, Pseudomonas species.##Fungi: Candida and Cryptococcus species. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18712851 Biopolymers. 2009 Jan;91(1):1-13. Bourbigot S, Dodd E, Horwood C, Cumby N, Fardy L, Welch WH, Ramjan Z, Sharma S, Waring AJ, Yeaman MR, Booth V. Antimicrobial peptide RP-1 structure and interactions with anionic versus zwitterionic micelles. DRAMP04037 LKLLKKL 7 Immobilized peptide E07LKK No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04038 LKLLKKLLKLLKKL 14 Immobilized peptide E14LKK/H14LKK No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922 (MBC=1496 µg/ml), Klebsiella pneumoniae ATCC 4352 (MBC=1496 µg/ml);##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923 (MBC=1496 µg/ml), Bacillus subtilis ATCC 6051 (MBC=1995 µg/ml).##Yeast: Candida albicans ATCC 10231 (MBC=3200 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04039 LKLLKKLLKLLKKLGK 16 Immobilized peptige E16KGL/H16KGL No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04040 LKLLKKLLKLLKKLGGK 17 Immobilized peptide E17KGG No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04041 LKLLKKLLKLLKKLGGGK 18 Immobilized peptide E18KGG No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04042 KGLKKLLKLLKKLLKL 16 Immobilized peptide E16LKL No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04043 LKKLLKKLKK 10 Immobilized peptid E10KKL No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04044 LKKLLKKLKKLL 12 Immobilized peptid E12LLK No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04045 LKKLLKKLKKLLKK 14 Immobilized peptid E14KKL No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04046 SNMIEGVFAKGFKKASHLFKGIG 23 Immobilized peptide E23GIG magainin2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04047 SNMIEGVFAKGFKKASH 17 Immobilized peptide E17HSA magainin 2 deletion No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Has antibacterial activiy against Gram-negative and Gram-positive bacteria. Gram-negative bacteria: Escherichia coli ATCC 25922, Klebsiella pneumoniae ATCC 4352;##Gram-positive bacteria: Staphylococcus aureus ATCC 6538 and ATCC 25923, Bacillus subtilis ATCC 6051.##Yeast: Candida albicans ATCC 10231. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7726486 Antimicrob Agents Chemother. 1995 Feb;39(2):301-307. Haynie SL, Crum GA, Doele BA. Antimicrobial activities of amphiphilic peptides covalently bonded to a water-insoluble resin. DRAMP04071 LLGNFFRKSKQKIGKQFKRIVQRIKNFFRNLVPRTQS 37 LL-37 pentamide No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Has antibacterial activiy against Gram-positive bacteria. Gram-positive bacteria: Staphylococcus aureus 930918-3, S. aureuss 710A, S. aureuss ATCC (MRSA) 33591, Staphylococcus epidermidis ATCC 49741. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11557457 Antimicrob Agents Chemother. 2001 Oct;45(10):2695-2702. Zhao C, Nguyen T, Boo LM, Hong T, Espiritu C, Orlov D, Wang W, Waring A, Lehrer RI. RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey. DRAMP04072 KWKIFKKIEHMGQNIRDGLIKAGPAVQVVGQAATIYKGSYSMEHFRWGKPV 51 Hinnavin II/MSH hybrid (rhin/MSH) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Function: rhin/MSH has a broader spectrum of activity than did the parental hinnavin II or MSH against fungi and Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20221725 J Microbiol. 2010 Feb;48(1):24-29. Bang SK, Kang CS, Han MD, Bang IS. Expression of recombinant hybrid peptide hinnavin II/alpha-melanocyte-stimulating hormone in Escherichia coli: purification and characterization. DRAMP04073 KTCENLADTYRGPCFTTGSCDDHCKNKEHLLSGRCRDDFRCWCTKRC 47 TvD1 (Recombinant peptide; alpha-defensin) No entry found Not found Not found Synthetic construct Antimicrobial Synthetic Not found Not found Function: The purified peptide also showed significant inhibition of root elongation in Arabidopsis seedlings, subsequently affecting the extension of growing root hairs indicating that it has the potential to disturb the plant growth and development. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18726095 Appl Microbiol Biotechnol. 2008 Oct;80(6):1023-1032. Vijayan S, Guruprasad L, Kirti PB. Prokaryotic expression of a constitutively expressed Tephrosia villosa defensin and its potent antifungal activity. DRAMP04074 PFWRIRIRR 9 PFR peptide (Recombinant peptide) No entry found Not found Not found Synthetic construct Antimicrobial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19026609 Biochim Biophys Acta. 2009 Feb;1788(2):314-323. Zorko M, Japelj B, Hafner-Bratkovic I, Jerala R. Expression, purification and structural studies of a short antimicrobial peptide. DRAMP04084 ATCDLASKFNWNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 W9F (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (W9F) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=4 µg/mL), Staphylococcus aureus strain 4 (IC90=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04085 ATCDLASIFNWNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 K8I,W9F (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I,W9F) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2-4 µg/mL), Staphylococcus aureus strain 4 (IC90=2-4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04086 ATCDLASKFNVNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 W9F,W11V (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (W9F,W11V) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=4-8 µg/mL), Staphylococcus aureus strain 4 (IC90=8-16 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04087 ATCDLASIFNVNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 K8I,W9F,W11V (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I,W9F,W11V) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2-4 µg/mL), Staphylococcus aureus strain 4 (IC90=2-4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04088 ATCDLASKFNWNHALCAAHCIARRYRGGYCNSKAVCVCR 39 W9F,T14A (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (W9F,T14A) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2-4 µg/mL), Staphylococcus aureus strain 4 (IC90=2-4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04089 ATCDLASIFNWNHALCAAHCIARRYRGGYCNSKAVCVCR 39 K8I,W9F,T14A (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I,W9F,T14A) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2-4 µg/mL), Staphylococcus aureus strain 4 (IC90=2-4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04090 ATCDLASKWNVNHALCAAHCIARRYRGGYCNSKAVCVCR 39 W11V,T14A (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (W11V,T14A) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=4 µg/mL), Staphylococcus aureus strain 4 (IC90=8-16 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04091 ATCDLASIWNVNHALCAAHCIARRYRGGYCNSKAVCVCR 39 K8I,W11V,T14A (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I,W11V,T14A) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=4 µg/mL), Staphylococcus aureus strain 4 (IC90=2-4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04092 ATCDLASKWNVNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 W11V (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (W11V) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2-4 µg/mL), Staphylococcus aureus strain 4 (IC90=4-8 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04093 ATCDLASIWNVNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 K8I,W11V (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I,W11V) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=4 µg/mL), Staphylococcus aureus strain 4 (IC90=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04094 ATCDLASIWNWNHTLCAAHCIARRYRGGYCNSKAVCVCR 39 K8I (mutant of Def-DAA defensin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Mutant of Def-DAA defensin (K8I) is active against sensitive and resistant strains of S. aureus. All the mutants are less toxic than Def-DAA except one (W11V) but are more toxic than Def-AcAA. Gram-positive bacteria: Staphylococcus aureus strain 21 (IC90=2 µg/mL), Staphylococcus aureus strain 4 (IC90=4 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18214975 Proteins. 2008 Jul;72(1):229-239. Landon C, Barbault F, Legrain M, Guenneugues M, Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. DRAMP04130 FVDLKKIANIINSIFKK 17 LK1 (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=20.97 µM), Bcap-37 (IC50=18.7 µM), MDA-MB-231 (IC50=66.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04131 FKDLKKIANIINSIFKK 17 LK2(5) (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=44.7 µM), Bcap-37 (IC50=83.49 µM), MDA-MB-231 (IC50=894.7 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04132 FVKLKKIANIINSIFKK 17 LK2(6) (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=15.54 µM), MDA-MB-231 (IC50=85.41 µM), Bcap-37 (IC50=18.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04133 FKKLKKIANIINSIFKK 17 LK3 (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=27.72 µM), MDA-MB-231 (IC50=224.8 µM), Bcap-37 (IC50=25.04 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04134 FVKLKKILNIINSIFKK 17 LK2(6)A(L) (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=9.01 µM), MDA-MB-231 (IC50=34.74 µM), Bcap-37 (IC50=10.52 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04135 FVKLKKILNIILSIFKK 17 LK2(6)AN(2L) (Temporin-1CEa analog peptide) No entry found Not found Not found Synthetic construct Anti-cancer Synthetic Not found Not found Function: Has anticancer activity. Cancer cell lines: MCF-7 (IC50=11 µM), MDA-MB-231 (IC50=41.55 µM), Bcap-37 (IC50=9.39 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23609760 Arch Pharm Res. 2013 Apr 23. Yang QZ, Wang C, Lang L, Zhou Y, Wang H, Shang DJ. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. DRAMP04148 VXLFPPFLXV 10 Gramicidin S No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 58 Biochemistry. 1975 Dec 16;14(25):5500-5511. Balerna M, Fosset M, Chicheportiche R, Romey G, Lazdunski M. Constitution and properties of axonal membranes of crustacean nerves. DRAMP04149 VXLPFFPLXV 10 Gramicidin Analogue No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 58 Biochemistry. 1975 Dec 16;14(25):5500-5511. Balerna M, Fosset M, Chicheportiche R, Romey G, Lazdunski M. Constitution and properties of axonal membranes of crustacean nerves. DRAMP04150 VXLPFPFLXV 10 Gramicidin Analogue 1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 58 Biochemistry. 1975 Dec 16;14(25):5500-5511. Balerna M, Fosset M, Chicheportiche R, Romey G, Lazdunski M. Constitution and properties of axonal membranes of crustacean nerves. DRAMP04151 IKRFWPVVIRTVVAGYNLYRAIKKK 25 RL1 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04152 KRFWPVVIRTVVAGYNLYRAIKKK 24 RL2 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04153 RFWPVVIRTVVAGYNLYRAIKKK 23 RL3 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04154 FWPVVIRTVVAGYNLYRAIKKK 22 RL4 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04155 WPVVIRTVVAGYNLYRAIKKK 21 RL5 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04156 PVVIRTVVAGYNLYRAIKKK 20 RL6 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04157 VVIRTVVAGYNLYRAIKKK 19 RL7 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04158 VIRTVVAGYNLYRAIKKK 18 RL8 (homologue of Pc-CATH1) No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Natural Products and Bioprospecting. 2012 Apr;2(2):81-86. Li Dong, Juan-Juan Yang, Ying Wang, Huan Liu, Li-Xian Mu, Dong-Hai Lin, Ren Lai. Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1. DRAMP04172 WLKKW 5 LK2W2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC>80 µg/ml), S. aureus (MIC>80 µg/ml), S. epidermis (MIC>80 µg/ml), M. luteus (MIC>80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC>80 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC>80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04173 WLLKW 5 L2KW2 (LlKmW2 model peptides) No entry found Not found Not found Synthetic construct (De novo design) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activities against Gram-negative and Gram-positive bacteria, including a multi-drug resistant strain. Chemical modification: C-terminal amidation." Gram-positive bacteria: B. subtilis (MIC>80 µg/ml), S. aureus (MIC>80 µg/ml), S. epidermis (MIC>80 µg/ml), M. luteus (MIC>80 µg/ml), S. aureus (MRSA) (MIC>80 µg/ml).##Gram-negative bacteria: E. coli (MIC>80 µg/ml), S. dysentariae (MIC>80 µg/ml), S. typhimorium (MIC>80 µg/ml), K. pneumoniae (MIC>80 µg/ml), P. aeruginosa (MIC>80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20736034 Regul Pept. 2011 Jan 17;166(1-3):36-41. Lee SH, Kim SJ, Lee YS, Song MD, Kim IH, Won HS. De novo generation of short antimicrobial peptides with simple amino acid composition. DRAMP04197 RQIKIWFQNRRMKWKK 16 Penetratin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04198 RQIRIWFQNRRMRWRR 16 PenArg No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=16 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=8 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04199 KQIKIWFQNKKMKWKK 16 PenLys No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Alpha helix Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=256 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=64 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04200 RQIKIWFQNRRLKWKK 16 PenLeu No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=64 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=32 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04201 KIWFQNRRMKWKK 13 Pen13 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=256 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=128 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04202 RIWFQNRRMRWRR 13 Pen13Arg No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=32 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=32 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04203 KIWFQNKKMKWKK 13 Pen13Lys No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=256 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=256 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04204 RWFKIQMQIRRWKNKK 16 PenShuf No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=64 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=32 μM) [Ref.23085001] HC50>128 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04205 RWFKIQLQIRRWKNKK 16 PenShufLeu No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=16 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=32 μM) [Ref.23085001] HC50=65±2.5 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04206 KWFKIQLQIKKWKNKK 16 PenShufLysLeu No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=32 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=32 μM) [Ref.23085001] HC50=91±2.3 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04207 RWFRIQLQIRRWRNRR 16 PenShufArgLeu No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=16 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=16 μM) [Ref.23085001] HC50=39±1.4 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04208 WRRRRRRR 8 WR8 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP04209 WGRKKRRQRRRPPQ 14 Tat13 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23085001##20845937 Biochim Biophys Acta. 2013 Feb;1828(2):223-232. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure. DRAMP02126 FIGSALKVLAGVLPSIVSWVKQ 22 Melittin-like peptide (MLP; Frogs, amphibians, animals) P56924 Not found Not found Rana temporaria (European common frog) Defense response, Anti-cancer, Protein kinase inhibitor activity Protein level Not found Not found "Function: Peptide has cellular defense response, inflammatory response, behavioral defense response, defense response to tumor cell, defense response by callose deposition, clearance of foreign intracellular nucleic acids, innate immune response, defense response by cell wall thickening, defense response to other organism, protein serine/threonine kinase inhibitor activity, calcium-dependent protein kinase inhibitor activity, protein tyrosine kinase inhibitor activity in GO analysis. Has hemolytic activity. PTM: Glutamine amide at position 22. Tissue specificity: Expressed by the skin dorsal glands." No MICs found in DRAMP database [Ref.9022710] LC=0.5 µM against human red blood cells. (LC: Lethal concentration) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9022710 Eur J Biochem. 1996 Dec 15;242(3):788-792. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. DRAMP04211 GIGKHVGKALKGLKGLLKGLGEC 23 ADP2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23196344 Biochim Biophys Acta. 2013 Mar;1828(3):1004-1012. Ilić N, Novković M, Guida F, Xhindoli D, Benincasa M, Tossi A, Juretić D. Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. DRAMP04212 GLKGLLGKALKGIGKHIGKAQGC 23 ADP3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23196344 Biochim Biophys Acta. 2013 Mar;1828(3):1004-1012. Ilić N, Novković M, Guida F, Xhindoli D, Benincasa M, Tossi A, Juretić D. Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. DRAMP04214 RRLFRRILRYL 11 R-BP100 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23246973 Biochim Biophys Acta. 2013 Mar;1828(3):944-955. Torcato IM, Huang YH, Franquelim HG, Gaspar D, Craik DJ, Castanho MA, Troeira Henriques S. Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria. DRAMP04215 RRLFRRILRWL 11 RW-BP100 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23246973 Biochim Biophys Acta. 2013 Mar;1828(3):944-955. Torcato IM, Huang YH, Franquelim HG, Gaspar D, Craik DJ, Castanho MA, Troeira Henriques S. Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria. DRAMP04216 KQSHKKGGHSFPKEKIS 17 P1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23022146 Biochimie. 2013 Feb;95(2):231-240. Yamane ES, Bizerra FC, Oliveira EB, Moreira JT, Rajabi M, Nunes GL, de Souza AO, da Silva ID, Yamane T, Karpel RL, Silva PI Jr, Hayashi MA. Unraveling the antifungal activity of a South American rattlesnake toxin crotamine. DRAMP04217 KMDSRWRWKSSKK 13 P2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23022146 Biochimie. 2013 Feb;95(2):231-240. Yamane ES, Bizerra FC, Oliveira EB, Moreira JT, Rajabi M, Nunes GL, de Souza AO, da Silva ID, Yamane T, Karpel RL, Silva PI Jr, Hayashi MA. Unraveling the antifungal activity of a South American rattlesnake toxin crotamine. DRAMP04218 KIFGAIWPLALGALKNLIK 19 Lys-a1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23340019 Peptides. 2013 Apr;42:78-83. da Silva BR, de Freitas VA, Carneiro VA, Arruda FV, Lorenzón EN, de Aguiar AS, Cilli EM, Cavada BS, Teixeira EH. Antimicrobial activity of the synthetic peptide Lys-a1 against oral streptococci. DRAMP04219 KSSTRGRKSSRRKK 14 CHRG01 (hBD3 derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial characterization of human beta-defensin 3 derivatives. DRAMP04220 RGRKSSRRKK 10 CHRG02 (hBD3 derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial characterization of human beta-defensin 3 derivatives. DRAMP04221 RGRKSSRRK 9 CHRG04 (hBD3 derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial characterization of human beta-defensin 3 derivatives. DRAMP04222 KYYSRVRGGRSAVLSSLDK 19 CHRG06 (hBD3 derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial characterization of human beta-defensin 3 derivatives. DRAMP04223 GIINTLQKYYSRVRGGR 17 CHRG07 (hBD3 derivative) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial characterization of human beta-defensin 3 derivatives. DRAMP04224 RPDKPRPYLPRPRPPRPVR 19 A3-APO No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20031377 Int J Antimicrob Agents. 2010 Apr;35(4):357-361. Szabo D, Ostorhazi E, Binas A, Rozgonyi F, Kocsis B, Cassone M, Wade JD, Nolte O, Otvos L Jr. The designer proline-rich antibacterial peptide A3-APO is effective against systemic Escherichia coli infections in different mouse models. DRAMP04225 GKPRPYLPRPTSHPRPIRV 19 Dros-Pyrr-Dros No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Letters in Peptide Science. 2001;8(3-5):201-209. Bencivengo AM, Cudic M, Hoffmann R, Jr LO. The efficacy of the antibacterial peptide, pyrrhocoricin, is finely regulated by its amino acid residues and active domains. DRAMP04226 VDKGSYLPRPTSHPRPIRV 19 Pyrr-Pyrr-Dros No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Letters in Peptide Science. 2001;8(3-5):201-209. Bencivengo AM, Cudic M, Hoffmann R, Jr LO. The efficacy of the antibacterial peptide, pyrrhocoricin, is finely regulated by its amino acid residues and active domains. DRAMP04227 GLLRRLRKKIGEIFKKYG 18 PGG No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9428709 Eur J Biochem. 1997 Dec 1;250(2):549-558. Tossi A, Tarantino C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. DRAMP04228 GRFRRLGRKFKKLFKKYGP 19 PGP No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9428709 Eur J Biochem. 1997 Dec 1;250(2):549-558. Tossi A, Tarantino C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. DRAMP04229 GLLRRLRDFLKKIGEKFKKIGY 22 PGYa No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9428709 Eur J Biochem. 1997 Dec 1;250(2):549-558. Tossi A, Tarantino C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. DRAMP04230 GILSKLGKALKKAAKHAAKA 20 PGAa No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9428709 Eur J Biochem. 1997 Dec 1;250(2):549-558. Tossi A, Tarantino C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. DRAMP04231 GLRKRLRKARNKIKEKLKKI 20 C18A No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8313956 FEBS Lett. 1994 Feb 14;339(1-2):108-112. Tossi A, Scocchi M, Skerlavaj B, Gennaro R. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit Leukocytes. DRAMP04232 GLRKRLRKFRNKIKQKLKKI 20 C18Q No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8313956 FEBS Lett. 1994 Feb 14;339(1-2):108-112. Tossi A, Scocchi M, Skerlavaj B, Gennaro R. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit Leukocytes. DRAMP04236 GLFDKLKSLVSDF 13 Antibacterial peptide A2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix (1 helices; 10 residues) Not found 1VM2 resolved by NMR. Function: Has antibacterial activity against the Gram-negative bacterium E. coli. Gram-negative bacterium: Escherichia coli (MIC>250 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15572363 J Biol Chem. 2005 Feb 18;280(7):5803-5811. Wang G, Li Y, Li X. Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor. DRAMP04239 ERPPGFSPFR 10 Neurotensin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12074933 Life Sci. 2002 Jul 5;71(7):747-750. Kowalska K, Carr DB, Lipkowski AW. Direct antimicrobial properties of substance P. DRAMP04245 LLLFLLKKRKKRKY 14 Dhvar5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10518718 FEMS Microbiol Lett. 1999 Oct 15;179(2):217-222. Groenink J, Walgreen-Weterings E, van 't Hof W, Veerman EC, Nieuw Amerongen AV. Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. DRAMP04246 KRLFKKLLFSLRKY 14 Dhvar4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10518718 FEMS Microbiol Lett. 1999 Oct 15;179(2):217-222. Groenink J, Walgreen-Weterings E, van 't Hof W, Veerman EC, Nieuw Amerongen AV. Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. DRAMP04247 KEEQIGKSSTRGRKSSRRKK 20 STRO06 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12936977 Antimicrob Agents Chemother. 2003 Sep;47(9):2804-2809. Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J. Antimicrobial Characterization of Human -Defensin 3 Derivatives. DRAMP04248 KIGAKIKIGAKIKIGAKI 18 (KIGAKI)3-NH2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11352918 J Biol Chem. 2001 Jul 27;276(30):27899-27906. Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, Epand RF, Maloy WL, Kari UP. A Novel Linear Amphipathic b-Sheet Cationic Antimicrobial Peptide with Enhanced Selectivity for Bacterial Lipids. DRAMP04249 KIAGKIAKIAGKIAKIAGKIA 21 (KIAGKIA)3-NH2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11352918 J Biol Chem. 2001 Jul 27;276(30):27899-27906. Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, Epand RF, Maloy WL, Kari UP. A Novel Linear Amphipathic b-Sheet Cationic Antimicrobial Peptide with Enhanced Selectivity for Bacterial Lipids. DRAMP04250 KLAGLAKKLAGLAKKLAGLAK 21 (KLAGLAK)3-NH2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11352918 J Biol Chem. 2001 Jul 27;276(30):27899-27906. Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, Epand RF, Maloy WL, Kari UP. A Novel Linear Amphipathic b-Sheet Cationic Antimicrobial Peptide with Enhanced Selectivity for Bacterial Lipids. DRAMP04251 RRWVRRVRRWVRRVVRVVRRWVRR 24 WLBU2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15616311 Antimicrob Agents Chemother. 2005 Jan;49(1):316-322. Deslouches B, Phadke SM, Lazarevic V, Cascio M, Islam K, Montelaro RC, Mietzner TA. De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. DRAMP04252 GFKLKGMARISCLPNGQWSNFPPKCIRECAMVSS 34 Sushi peptide 1 (truncated fragment) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10973930 FASEB J. 2000 Sep;14(12):1801-1813. Tan NS, Ng ML, Yau YH, Chong PK, Ho B, Ding JL. Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides. DRAMP04253 HAEHKVKIGVEQKYGQFPQGTEVTYTCSGNYFLM 34 Sushi peptide 3 (truncated fragment) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10973930 FASEB J. 2000 Sep;14(12):1801-1813. Tan NS, Ng ML, Yau YH, Chong PK, Ho B, Ding JL. Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides. DRAMP04254 YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY 36 Neuropeptide Y (NPY) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found 1RON Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9756788 Antimicrob Agents Chemother. 1998 Oct;42(10):2745-2746. Shimizu M, Shigeri Y, Tatsu Y, Yoshikawa S, Yumoto N. Enhancement of antimicrobial activity of neuropeptide Y by N-terminal truncation. DRAMP04255 YPSKPDNPGEDAPAEDLARYYSALRHYINLITRQRY 36 Neuropeptide Y (NPY) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found 1F8P Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9756788 Antimicrob Agents Chemother. 1998 Oct;42(10):2745-2746. Shimizu M, Shigeri Y, Tatsu Y, Yoshikawa S, Yumoto N. Enhancement of antimicrobial activity of neuropeptide Y by N-terminal truncation. DRAMP04256 DKLIGSCVWGAVNYTSDCNGECKRRGYKGGYCGSFANVNCWRT 43 R No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11580275 Biochemistry. 2001 Oct 9;40(40):11995-2003. Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Solution structures of the antigungal heliomicin and a selected variant whit both antibacterial and antifungal activities. DRAMP04257 AAAAGSVWGAVNYTSDCNGECKRRGYKGGYCGSFANVNCWCET 43 4A No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11580275 Biochemistry. 2001 Oct 9;40(40):11995-2003. Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Solution structures of the antigungal heliomicin and a selected variant whit both antibacterial and antifungal activities. DRAMP04258 DKLIGSCVWGAVNYTSDCAAEKRRGYKGGYCGSFANVNCWCET 43 AA No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11580275 Biochemistry. 2001 Oct 9;40(40):11995-2003. Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Solution structures of the antigungal heliomicin and a selected variant whit both antibacterial and antifungal activities. DRAMP04259 DKLIGSCVWGAVNYTSDCNGECLLRGYKGGYCSGFANVNCWCET 44 LL No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11580275 Biochemistry. 2001 Oct 9;40(40):11995-2003. Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F. Solution structures of the antigungal heliomicin and a selected variant whit both antibacterial and antifungal activities. DRAMP04260 LALLKVLLRKIKKAL 15 CM-1 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04261 LULLLKILLLKKLKA 15 CM-2 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04262 ALKAALLAILKIVRVIKK 18 CM-3 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04263 LLAILLLALLALRKKVLA 18 CM-4 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04266 KWKSFIKKLPSAAKKVTTAAKPLTK 25 CPα1 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=43 μg/ml), Pseudomonas aeruginosa K799 (MIC=64 μg/ml), Pseudomonas aeruginosa Z61 (MIC=24 μg/ml), Pseudomonas aeruginosa H744 (MIC=8 μg/ml), Pseudomonas aeruginosa H374 (MIC=8 μg/ml), Pseudomonas aeruginosa H547 (MIC=16 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04267 KWKKFIKKIGIGAVLKVLTTGLPALKLTKK 30 CPα2 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=2 μg/ml), Pseudomonas aeruginosa K799 (MIC=4 μg/ml), Pseudomonas aeruginosa Z61 (MIC=4 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H374 (MIC=4 μg/ml), Pseudomonas aeruginosa H547 (MIC=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04268 KKWKKFIKKIGIGAVLTTPGAKK 23 CPα3 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=4 μg/ml), Salmonella typhimurium (MIC=4 μg/ml), Pseudomonas aeruginosa K799 (MIC=64 μg/ml), Pseudomonas aeruginosa Z61 (MIC=32 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H374 (MIC=8 μg/ml), Pseudomonas aeruginosa H547 (MIC=16 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04269 KWKSFIKNLTKGGSKILTTGLPALIS 26 CP201 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=4 μg/ml), Salmonella typhimurium (MIC=43 μg/ml), Pseudomonas aeruginosa K799 (MIC=64 μg/ml), Pseudomonas aeruginosa Z61 (MIC=32 μg/ml), Pseudomonas aeruginosa H744 (MIC=16 μg/ml), Pseudomonas aeruginosa H374 (MIC=8 μg/ml), Pseudomonas aeruginosa H547 (MIC=32 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04270 KWKKFIKNLTKGGSKILTTGLPALIS 26 CP202 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=16 μg/ml), Pseudomonas aeruginosa K799 (MIC=32 μg/ml), Pseudomonas aeruginosa Z61 (MIC=19 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H374 (MIC=4 μg/ml), Pseudomonas aeruginosa H547 (MIC=16 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04271 KWKSFIKKLTSAAKKVLTTGLPALIS 26 CP203 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=4 μg/ml), Pseudomonas aeruginosa K799 (MIC=5 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H374 (MIC=4 μg/ml), Pseudomonas aeruginosa H547 (MIC=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04274 KKWWKFIKKAVNSGTTGLQTLAS 23 CP206 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=8 μg/ml), Pseudomonas aeruginosa H744 (MIC=16 μg/ml), Pseudomonas aeruginosa H374 (MIC=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04275 KWKSFIKKLTSVLKKVVTTAKPLISS 26 CP207 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=5 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H374 (MIC=8 μg/ml), Pseudomonas aeruginosa H547 (MIC=8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04276 KKKSFIKLLTSAKVSVLTTAKPLISS 26 CP208 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=32 μg/ml), Pseudomonas aeruginosa H744 (MIC=64 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04277 WKVFKSFIKKASSFAQSVLD 20 CP209 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=11 μg/ml), Pseudomonas aeruginosa Z61 (MIC=64 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04280 KWKSFIKKLPSAAKKVVTTAKPLALIS 27 CM1 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=5 μg/ml), Pseudomonas aeruginosa K799 (MIC=4 μg/ml), Pseudomonas aeruginosa Z61 (MIC=4 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H547 (MIC=16 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04281 KWKSFIKKLPKAAKKVVTTAKKPLIV 26 CM2 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=4 μg/ml), Pseudomonas aeruginosa K799 (MIC=3 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=1 μg/ml), Pseudomonas aeruginosa H547 (MIC=4 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04282 KWKKFIKSLTKSAAKTVVKTAKKPLIV 27 CM3 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=1 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=4 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H374 (MIC=2 μg/ml), Pseudomonas aeruginosa H547 (MIC=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04283 KWKLFKKIGIGAVLKVLTTGLPALKLTLK 29 CM4 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=3 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=4 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H547 (MIC=4 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04284 KLFKKIGIGAVLKVLTTGLPALKLTK 26 CM5 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=5 μg/ml), Salmonella typhimurium (MIC=29 μg/ml), Pseudomonas aeruginosa K799 (MIC=32 μg/ml), Pseudomonas aeruginosa Z61 (MIC=19 μg/ml), Pseudomonas aeruginosa H744 (MIC=4 μg/ml), Pseudomonas aeruginosa H547 (MIC=32 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04285 KWKFKKIGIGAVLKVLTTGLPALKLTLK 28 CM6 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=4 μg/ml), Pseudomonas aeruginosa K799 (MIC=6 μg/ml), Pseudomonas aeruginosa Z61 (MIC=5 μg/ml), Pseudomonas aeruginosa H744 (MIC=1 μg/ml), Pseudomonas aeruginosa H547 (MIC=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04286 KLWKLFKKIGIGAVLKVLTTGLPALKLTK 29 CM7 No entry found Derived from the peptide CP26, CP29, CEME and CEMA Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=4 μg/ml), Pseudomonas aeruginosa Z61 (MIC=3 μg/ml), Pseudomonas aeruginosa H744 (MIC=16 μg/ml), Pseudomonas aeruginosa H547 (MIC=32 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipopolysaccharide (LPS)-binding 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04287 AASKAAKTLAKLLSSLLKL 19 MC-03 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04288 LLKKLLRAASKALSLL 16 MC-04 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04289 AAKKLSKLLKTLLKLL 16 MC-05 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04290 KALKKLLKLASSLLTAL 17 MC-08 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04291 AASKALRTASRLARSLLT 18 MC-10 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04292 LKLLKKLLKKLKKLL 15 MB-00 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04293 VSSKYLSKVKVKAGK 15 MB-03 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04294 ARLAKKALRRLAKKD 15 MB-04 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04295 GESLASKAAKAAER 14 MB-10 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04296 ESLAKALSKEALKALK 16 MB-15 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04297 LKALKKLAKKLKKLA 15 MB-18 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04298 FASLLGKALKALAKQ 15 MB-21 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04299 GWLLLEYIPVIAAL 14 MB-22 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04300 LSSALSALSSALSSK 15 MB-25 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04301 EAALKAALDLAAKLA 15 MB-31 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04302 ERSAAKSAARSLARR 15 MB-32 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04303 EKTLARTAAKTALKK 15 MB-33 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04304 EKAAAKSAAAKTLARR 16 MB-34 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04305 VSSKYLSKALVKAGR 15 MB-35 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04306 FASLLGKALKALLAKLAKQ 19 MB-36 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04307 FASLLGKLAKKLAKKALK 18 MB-37 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04308 ESLKARSLKKSLKLKKLL 18 MB-38 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04309 ETELAKKALKALKLKKLA 18 MB-40 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04310 ELAKKALKALKKALKSAR 18 MB-41 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04311 ELAKKALRALKKALKSAK 18 MB-43 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04312 ETFAKKALKALEKLLKKG 18 MB-45 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04313 ESSLKKKALSKLSKLLKKG 19 MB-46 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04314 QKAASRLLRALSKLLEAF 18 MB-47 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04315 QKALAKLAKKALKALAKQ 18 MB-48 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04316 ESKAAKAAKKAAKAKASE 18 MB-50 No entry found Not found Not found Synthetic construct (Computer-Aided Molecular Design) Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9879502 J Comput Aided Mol Des. 1998 Nov;12(6):543-556. Patel S, Stott IP, Bhakoo M, Elliott P. Patenting computer-designed peptides. DRAMP04317 FFGKVLKLIRKIF 13 DASamP1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22445495 Int J Antimicrob Agents. 2012 May;39(5):402-406. Menousek J, Mishra B, Hanke ML, Heim CE, Kielian T, Wang G. Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300. DRAMP04318 IKWKKLLRAAKRIL 14 DASamP2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22445495 Int J Antimicrob Agents. 2012 May;39(5):402-406. Menousek J, Mishra B, Hanke ML, Heim CE, Kielian T, Wang G. Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300. DRAMP04319 ALRLAIRRR 9 22A-30R-NH2 fragment 1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04320 ALLLAIRRR 9 22A-30R-NH2 fragment 2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04321 AWLLAIRRR 9 22A-30R-NH2 fragment 3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04322 ALYLAIRRR 9 22A-30R-NH2 fragment 4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04323 ALWLAIRRR 9 22A-30R-NH2 fragment 5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04324 LCAAHCLAIGRR 12 19L-30R-NH2 fragment 1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04325 LCAAHCLAIRRR 12 19L-30R-NH2 fragment 2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04326 LCAAHCLAILRR 12 19L-30R-NH2 fragment 3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04327 LCAARCLAIGRR 12 19L-30R-NH2 fragment 4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04328 LCAALCLAIGRR 12 19L-30R-NH2 fragment 5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04329 LRAAHRLAIGRR 12 19L-30R-NH2 fragment 6 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04330 LLAAHLLAIGRR 12 19L-30R-NH2 fragment 7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04331 AAHCLAIGRR 10 19L-30R-NH2 fragment 8 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04332 AHCLAIGRR 9 19L-30R-NH2 fragment 9 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04333 HCLAIGRR 8 19L-30R-NH2 fragment 10 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04334 CLAIGRR 7 19L-30R-NH2 fragment 11 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9931294 Biochem J. 1999 Feb 15;338 ( Pt 1):29-33. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. DRAMP04335 FLFSLIPKAIGGLISAFK 18 AamAP-S1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22484288 Peptides. 2012 Jun;35(2):291-299. Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C. Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: Biochemical and functional characterization of natural peptides and a single site-substituted analog. DRAMP04336 IGKEFKRIVQRIKDFLRNL 19 IG-19 (residues 13-31 of LL-37) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=16 μM), Salmonella typhimurium (KCTC 1926)(MIC=8 μM) [Ref.22521196] MHC10=21.6 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04337 IGKKFKRIVQRIKDFLRNL 19 a1 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=2 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.22521196] MHC10=13.8 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04338 IGKKFKRIVQRIKKFLRNL 19 a2 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=2 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=8 μM) [Ref.22521196] MHC10=11.2 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04339 IGKKFKRIVQRIKKFLRKL 19 a3 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=2 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.22521196] MHC10=23.7 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04340 IGKKFKRIVKRIKKFLRKL 19 a4 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.22521196] MHC10=33.2 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04341 IGKLFKRIVQRIKKFLRNL 19 a5 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=8 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.22521196] MHC10=3.0 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04342 IGKLFKRIVQRILKFLRNL 19 a6 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=8 μM), Staphylococcus aureus (KCTC 1621)(MIC=8 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.22521196] MHC10=1.2 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04343 IGKLFKRIVKRILKFLRKL 19 a7 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.22521196] MHC10=1.1 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04344 ILKLFKRIVKRILKFLRKL 19 a8 (IG-19 analogs) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=8 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=8 μM) [Ref.22521196] MHC10=1.6 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04345 IGKKWKRIVKRIKKFLRKL 19 a4-W1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=4 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.22521196] MHC10=9.2 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04346 IGKKFKRIVKRIKKWLRKL 19 a4-W2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix All of the peptides exhibited a predominantly-helical structure characterized by double minima at 208 and 222 nm in the presence of LPS. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.22521196] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=4 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.22521196] MHC10=8.4 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22521196 Peptides. 2012 Jun;35(2):239-247. Nan YH, Bang JK, Jacob B, Park IS, Shin SY. Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37. DRAMP04347 RAGLQFPVGRLLRRLLRRLLR 21 Buforin No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306477 Peptides. 2012 Apr;34(2):283-289. Jang SA, Kim H, Lee JY, Shin JR, Kim da J, Cho JH, Kim SC. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. DRAMP04348 RAGLQWPIGRLLRRLLRRLLR 21 Buf IIIa No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306477 Peptides. 2012 Apr;34(2):283-289. Jang SA, Kim H, Lee JY, Shin JR, Kim da J, Cho JH, Kim SC. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. DRAMP04349 RVVRQWPIGRVVRRVVRRVVR 21 Buf IIIb No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306477 Peptides. 2012 Apr;34(2):283-289. Jang SA, Kim H, Lee JY, Shin JR, Kim da J, Cho JH, Kim SC. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. DRAMP04350 KLLKQWPIGKLLKKLLKKLLK 21 Buf IIIc No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306477 Peptides. 2012 Apr;34(2):283-289. Jang SA, Kim H, Lee JY, Shin JR, Kim da J, Cho JH, Kim SC. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. DRAMP04351 KVVKQWPIGKVVKKVVKKVVK 21 Buf IIId No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306477 Peptides. 2012 Apr;34(2):283-289. Jang SA, Kim H, Lee JY, Shin JR, Kim da J, Cho JH, Kim SC. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. DRAMP04352 INWKKLLDAAKQIL 14 Asn-2-Polybia-MP No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20108158 Amino Acids. 2011 Jan;40(1):77-90. de Souza BM, Dos Santos Cabrera MP, Neto JR, Palma MS. Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities. DRAMP04353 INWLKAKKVAGMIL 14 MK-578 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20108158 Amino Acids. 2011 Jan;40(1):77-90. de Souza BM, Dos Santos Cabrera MP, Neto JR, Palma MS. Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities. DRAMP04354 GLFRALLRLLRSLWRLLLRA 20 PpTG20 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22819152 Int J Antimicrob Agents. 2012 Oct;40(4):337-343. Li L, Shi Y, Su G, Le G. Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue. DRAMP04355 GLRRALLRLLRSLRRLLLRA 20 P7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22819152 Int J Antimicrob Agents. 2012 Oct;40(4):337-343. Li L, Shi Y, Su G, Le G. Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue. DRAMP04356 KWKLFKKIEKVGQRVDAVISAGPAVATVAQAATALAK 37 CAD No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22651919 Protein Expr Purif. 2012 Oct;85(2):200-203. Yang K, Su Y, Li J, Sun J, Yang Y. Expression and purification of the antimicrobial peptide cecropin AD by fusion with cationic elastin-like polypeptides. DRAMP04357 KWKLFKKIGIGAVLKVLTTGLIALIS 26 CEME(MBI-27) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=2 μg/ml), Pseudomonas aeruginosa K799 (MIC=5 μg/ml), Pseudomonas aeruginosa Z61 (MIC=4 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H374 (MIC=2 μg/ml), Pseudomonas aeruginosa H547 (MIC=2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04358 KWKLFKKIGIGAVLKVLTPGLPALKLTK 28 CEMA(MBI-28) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli (MIC=2 μg/ml), Salmonella typhimurium (MIC=3 μg/ml), Pseudomonas aeruginosa K799 (MIC=3 μg/ml), Pseudomonas aeruginosa Z61 (MIC=2 μg/ml), Pseudomonas aeruginosa H744 (MIC=2 μg/ml), Pseudomonas aeruginosa H374 (MIC=2 μg/ml), Pseudomonas aeruginosa H547 (MIC=4 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10085049 Infect Immun. 1999 Apr;67(4):2005-2009. Scott MG, Yan H, Hancock RE. Biological properties of structurally related alpha-helical cationic antimicrobial peptides. DRAMP04366 INWSSIFESVSNLV 14 PDD-A-8 (PDD-A analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04375 INSLKLGKKILGAL 14 PDD-B-5 (PDD-B analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04384 KIASIGKEVLKAL 13 PMM-5 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP04388 INWKKIASIGKEV 13 PMM-9 (PMM analog) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Has antimicrobial activity against the Gram-positive bacterium B. subtilis and Gram-negative bacterium E. coli. Chemical modification: C-terminal amidation." Gram-negative bacterium: Escherichia coli (MIC>100 µM);##Gram-positive bacterium: Bacillus subtilis (MIC>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18375018 Peptides. 2008 Jun;29(6):992-1003. Cerovský V, Slaninová J, Fucík V, Hulacová H, Borovicková L, Jezek R, Bednárová L. New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs. DRAMP01823 FLPFLATLLSKVL 13 Temporin-1Ce (Temporin 1Ce; Frogs, amphibians, animals) P82884 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Rana clamitans (Green frog) (Lithobates clamitans) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacterium Staphylococcus aureus. Tissue specificity: Expressed by the skin glands." [Ref.10822101] Gram-positive bacterium: Staphylococcus aureus (MIC=100 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10822101 Peptides. 2000 Apr;21(4):469-476. Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. DRAMP04396 AIGNILKTLGNLAQKILGKQPKMLKLWKWNWKSSDVEYHLAKC 43 Antimicrobial peptide OGC1 C3RTH6 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Ma Y, Lai R, Wu J, Li J. Antimicrobial peptide from skin of Odorrana grahami. DRAMP04397 AIGNILKTLGNLAQKILGK 19 Antimicrobial peptide OGC2 C3RTH7 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Ma Y, Lai R, Wu J, Li J. Antimicrobial peptide from skin of Odorrana grahami. DRAMP04398 AKYTGKCTKSKNECKYKNDAGKDTFIKCPKFDNKKCTKDNNKCTVDTYNNAVDCD 55 Antifungal protein (PAF) Q01701 Not found paf Penicillium chrysogenum (Penicillium notatum) Antimicrobial, Antifungal, Antiviral Protein level Beta strand (5 strands; 24 residues) PAF comprises five beta-strands forming two orthogonally packed beta-sheets that share a common interface. 2KCN resolved by NMR. Function: It exhibits antifungal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19459942##8566771 FEBS J. 2009 May;276(10):2875-2890.##Gene. 1995 Dec 29;167(1-2):167-171. Batta G, Barna T, Gáspári Z, Sándor S, Kövér KE, Binder U, Sarg B, Kaiserer L, Chhillar AK, Eigentler A, Leiter E, Hegedüs N, Pócsi I, Lindner H, Marx F.##Marx F, Haas H, Reindl M, Stöffler G, Lottspeich F, Redl B. Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum.##oning, structural organization and regulation of expression of the Penicillium chrysogenum paf gene encoding an abundantly secreted protein with antifungal activity. DRAMP04399 MFTLKKSLLLLFFLGTINLSLCQEEERNADEEERRDERDVEVEKRVIPFVASVAAEMMQHVYCAASKKR 69 Odorranain-P1g antimicrobial peptide (Frogs, amphibians, animals) B5L162 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04400 MFTLKKPLLLLFFLGTINLSLCQEEERNADEEERRDERDVEVEKRVIPSVASVAAEMMQHVYCAASKKC 69 Odorranain-P1c antimicrobial peptide (Frogs, amphibians, animals) B5L177 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04401 MFTMKKSLLLLFFLGAINLSFCQEEERNADEEERRDERDVEVEKRVIPFVASVAAEKMQHVYCAASKKC 69 Odorranain-P1e antimicrobial peptide (Frogs, amphibians, animals) B5L1A0 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04402 MFTMKKSLLLLFFLGTINLSLCQEEERNADEEERRDERDVEVEKRVIPSVASVAAEMMQHVYCAASKKC 69 Odorranain-P1c antimicrobial peptide (Frogs, amphibians, animals) B5L1A3 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04403 MFTLKKSLLLLFFLGTINLSLCQEEERNADEEERRDERDIEVEKRVIPFVASVAAEMMQHVYCAASKKMLKLNWKSSDVENHLAKC 86 Odorranain-P1h antimicrobial peptide (Frogs, amphibians, animals) B5L163 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04404 MFTMKKSLLLLFFLGTINLSFCQEEERNADEEERRDERDVEVEKRVIPFVASVAAEMMQPVYCAASKKC 69 Odorranain-P1d antimicrobial peptide (Frogs, amphibians, animals) B5L196 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ database Wang X, Lai R. Odorrana grahmi antimicrobial peptide cDNA sequences. DRAMP04405 MFTMKKSLLVLFFLGIVSLSLCEEERNADEDDGEMTEEVKRGILDTLKQLGKAAAQSLLSKAACKLAKTC 70 Granulosusin-E1 antimicrobial peptide (Frogs, amphibians, animals) E1AXE7 Not found Not found Amolops granulosus (granular torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops granulosus. DRAMP04406 MFTLKKSMLLLLFLGTVSLSLCDQERAADEDEGEVIEEEVKRGFMDTAKNVFKNVAVTLLDKLKCKIAGGC 71 Granulosusin-D1 antimicrobial peptide (Frogs, amphibians, animals) E1AXE5 Not found Not found Amolops granulosus (granular torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops granulosus. DRAMP04407 MFSKKSLLVLFFLGTISLSLCQEERGADEDEAVEFTEEEKRSILSTLKDVGISALKNAGSGVLKTLLCKLNKNCEK 76 Taipehensin-A1 antimicrobial peptide (Frogs, amphibians, animals) E7EKG5 Not found Not found Hylarana taipehensis (Taipei frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (DEC-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Hylarana (Hylarana)taipehensis. DRAMP04408 GLFPNKDCKYWCKDNLGLNYCCGQPGVTYPPFTKKHLGRCPAVRDTCTGVRTQLPTYCPHDGACQFRSKCCYDTCLKHHVCKTAEYPY 88 Carcinin Q8WQ91 Not found Not found Carcinus maenas (Common shore crab) (Green crab) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16712935 Mol Immunol. 2007 Feb;44(5):943-949. Brockton V, Hammond JA, Smith VJ. Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas. DRAMP04409 MFTLKKSLLLLFFLGIISLSLCEQERDANDEEDGGEVTKEVVKRSLRGCWTKSYPPQPCLGKR 63 Ranacyclin Ca antimicrobial peptide C5IAX6 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Zhao R, Han W, Han J, Lei L, Feng X, Sun C, Jiang L. Identification and characterization of a novel antimicrobial peptide from Rana catesbeiana. DRAMP04410 GDVHAQTTWPCATVGVSVALCPTTKCTSQC 30 Lantibiotic cytolysin Q9KFM6 Not found Not found Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM9153 / C-125) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11058132 Nucleic Acids Res. 2000 Nov 1;28(21):4317-4331. Takami H, Nakasone K, Takaki Y, Maeno G, Sasaki R, Masui N, Fuji F, Hirama C, Nakamura Y, Ogasawara N, Kuhara S, Horikoshi K. Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. DRAMP04411 ALPCAKKSCDSWCRRLDYPGGECVTKWKCSCNWMQIDK 38 Defensin like protein 2 (Predicted) B5MF85 Not found defensin2 Bombyx mori (Silk moth) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18776686 Biosci Biotechnol Biochem. 2008 Sep;72(9):2353-2361. Kaneko Y, Tanaka H, Ishibashi J, Iwasaki T, Yamakawa M. Gene expression of a novel defensin antimicrobial peptide in the silkworm, Bombyx mori. DRAMP04412 ASCYLLDGYAAGRDDCRAHCIAPRNRRLYCASYQVCVCRY 40 Defensin Q8WQZ3 Not found Not found Mamestra brassicae (Cabbage moth) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12753953 Biol Cell. 2003 Jan-Feb;95(1):53-57. Mandrioli M, Bugli S, Saltini S, Genedani S, Ottaviani E. Molecular characterization of a defensin in the IZD-MB-0503 cell line derived from immunocytes of the insect Mamestra brassicae (Lepidoptera). DRAMP04413 ASGCKADACKSYCKSLGSGGGYCDQGTWCVCN 32 Defensin-like protein (Predicted) Q6YC89 Not found Not found Dermacentor variabilis (American dog tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17261604 Infect Immun. 2007 Apr;75(4):1973-1983. Ceraul SM, Dreher-Lesnick SM, Gillespie JJ, Rahman MS, Azad AF. New tick defensin isoform and antimicrobial gene expression in response to Rickettsia montanensis challenge. DRAMP04414 ATCDLFSFESKWFTPNHAACAAHCILLGNRGGHCVGTVCHCRK 43 Defensin 1 (Def1) Q4VSI0 Not found def1 Triatoma brasiliensis (Blood-sucking bug) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19505471 J Insect Physiol. 2009 Sep;55(9):840-848. Waniek PJ, Castro HC, Sathler PC, Miceli L, Jansen AM, Araújo CA. Two novel defensin-encoding genes of the Chagas disease vector Triatoma brasiliensis (Reduviidae, Triatominae): gene expression and peptide-structure modeling. DRAMP04415 ATCDLFSLQSKWVTPNHAACAAHCLLRGNRGGQCKGTICHCRK 43 Defensin 2 (Def2) Q102J4 Not found Def2 Triatoma brasiliensis (Blood-sucking bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19505471 J Insect Physiol. 2009 Sep;55(9):840-848. Waniek PJ, Castro HC, Sathler PC, Miceli L, Jansen AM, Araújo CA. Two novel defensin-encoding genes of the Chagas disease vector Triatoma brasiliensis (Reduviidae, Triatominae): gene expression and peptide-structure modeling. DRAMP04416 ATCDLFSFQSQWVTPNHAACAAHCLLRGNRGGECKGTICHCRK 43 Defensin 3 (Def3) C6ZEC4 Not found def3 Triatoma brasiliensis (Blood-sucking bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19505471 J Insect Physiol. 2009 Sep;55(9):840-848. Waniek PJ, Castro HC, Sathler PC, Miceli L, Jansen AM, Araújo CA. Two novel defensin-encoding genes of the Chagas disease vector Triatoma brasiliensis (Reduviidae, Triatominae): gene expression and peptide-structure modeling. DRAMP04417 ATCDLFSFQSKWVTPNHAACAAHCLLRGNRGGQCKGTICHCRK 43 Defensin 4 (Def4) C6ZEC5 Not found def4 Triatoma brasiliensis (Blood-sucking bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19505471 J Insect Physiol. 2009 Sep;55(9):840-848. Waniek PJ, Castro HC, Sathler PC, Miceli L, Jansen AM, Araújo CA. Two novel defensin-encoding genes of the Chagas disease vector Triatoma brasiliensis (Reduviidae, Triatominae): gene expression and peptide-structure modeling. DRAMP04418 ATCDLLSFEIKGFKLNDSACAAHCIQLGKRGGHCNNSKVCVCRR 44 Defensin B6RQP4 Not found Not found Sitophilus zeamais (Maize weevil) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18925938 BMC Biol. 2008 Oct 16;6:43. Anselme C, Pérez-Brocal V, Vallier A, Vincent-Monegat C, Charif D, Latorre A, Moya A, Heddi A. Identification of the weevil immune genes and their expression in the bacteriome tissue. DRAMP04419 ATCDLLSFLNVKDAACAAHCLAKGYRGGYCDGRKVCNCRR 40 Putative uncharacterized protein A4VBA2 Not found Not found Eristalis tenax (Drone fly) (Musca tenax) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17875201 BMC Genomics. 2007 Sep 17;8:326. Altincicek B, Vilcinskas A. Analysis of the immune-inducible transcriptome from microbial stress resistant, rat-tailed maggots of the drone fly Eristalis tenax. DRAMP04420 ATCDLLSFSSKWVTPNHAGCAAHCLLRGNRGGHCKGTICHCRK 43 Defensin B Q86MY2 Not found DEFB Rhodnius prolixus (Triatomid bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP04421 ATCDLLSGFGVNDSACAAHCIARGNRGGYCNSKKVCVCRN 40 Defensin B9UKD3 Not found Def Apis cerana cerana (Oriental honeybee) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available PLoS ONE 2009, 4:E4239-E4239. Xu P, Chen X.X. Molecular cloning of antimicrobial peptide genes of Chinese honeybee (Apis cerana cerana Fabricius) and comparison with Italian honeybee (Apis mellifera L.). DRAMP04422 ATCDLLSGMGVNHSACAAHCVLRGNRGGYCNSKAVCVCR 39 Defensin 1 P82380 Not found fbd1 Stomoxys calcitrans (Stable fly) (Conops calcitrans) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Munks R.J.L, Lehane S.M, Lehane M.J. Expression and regulation of the genes, smd1 and smd2, which encode midgut-specific defensin molecules in Stomoxys calcitrans. DRAMP04423 ATCDLLSGTGVGHSACAAHCLLRGNRGGYCNGKGVCVCRN 40 Defensin Q86BU1 Not found Not found Musca domestica (House fly) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Dong Wu Xue Bao 2003, 49:0-0. Wang LC, Wang JX, Wang LY, Zhao XF. Cloning and sequence analysis of the full-length cDNA encoding defensin, an antimicrobial peptide from the housefly (Musca domestica). DRAMP04424 ATYYGNGLYCNKQKCWVDWNKASREIGKIIVNGNVQHGPWAPR 43 BacA protein Q47778 Not found bacA Enterococcus faecalis (Streptococcus faecalis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8655558 J Bacteriol. 1996 Jun;178(12):3585-3593. Tomita H, Fujimoto S, Tanimoto K, Ike Y. Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17. DRAMP04425 DCNTKACWALCQREHGIYFRRAVCEGSRCKCILVNGR 37 Termicin Q5SDH7 Not found Not found Drepanotermes rubriceps Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15317879 Mol Biol Evol. 2004 Dec;21(12):2256-2264. Bulmer MS, Crozier RH. Duplication and diversifying selection among termite antifungal peptides. DRAMP04426 MKCILSLFTLFLVATLVYSYPAEWNSQHQLDDAQWEPAGELTEEHLSRMKRATCDLLSLTSKWFTPNHAGCAAHCIFLGNRGGRCVGTVCHCRK 94 Defensin C Q86MY1 Not found DEFC Rhodnius prolixus (Triatomid bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP04427 NHRSCYRNKGVCAPARCPRNMRQIGTCHGPPVKCCRKK 38 Beta defensin-2 O97942 Not found Not found Capra hircus (Goat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531296 Infect Immun. 1999 Nov;67(11):6221-6224. Zhao C, Nguyen T, Liu L, Shamova O, Brogden K, Lehrer RI. Differential expression of caprine beta-defensins in digestive and respiratory tissues. DRAMP04428 SFSCSQNGGFCISPKCLPGSKQIGTCILPGSKCCR 35 Beta defensin 1 (Beta-defensin-1) Q865P6 Not found Not found Equus caballus (Horse) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15113660 Vet Immunol Immunopathol. 2004 May;99(1-2):127-132. Davis EG, Sang Y, Blecha F. Equine beta-defensin-1: full-length cDNA sequence and tissue expression. DRAMP04429 HSACAANCLSMGKAGGRCENGVCLCR 26 Defensin Q6TAX6 Not found Not found Bombus ignitus (Bumblebee) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Byeon G.M, Lee K.S, Choi Y.S, Jin B.R, Sohn H.D. Molecular cloning and expression of defensin gene from Bee, Bombus ignitus. DRAMP04430 DKYCSENPLDCNEHCLKTKNQIGICHGANGNEKCSCMES 39 Putative potassium channel blocker TXKs2 Q95P88 Not found Not found Mesobuthus martensii (Manchurian scorpion) (Buthus martensii) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11087122 IUBMB Life. 2000 Jul;50(1):57-61. Zhu S, Li W, Jiang D, Zeng X. Evidence for the existence of insect defensin-like peptide in scorpion venom. DRAMP04431 ENDHRMPYELNRPNNLSKGGAKCAAGILGAGLGAVGGGPGGFISAGISAVLGCM 54 Precursor of durancin TW-49M (Prepeptide of durancin TW-49M) B3IUC6 Not found durM Enterococcus durans Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hu C, Zendo T, Nakayama J, Sonomoto K. Characterization of durancin TW-49M and its atypical genetic locus: a novel bacteriocin produced by carrot-isolated Enterococcus durans QU 49. DRAMP04432 EPEPSYFNDCGSNGGSCTRGYCSYSNRLPYTCSLGRTCCRLAYV 44 Defensin 1 B9UZC8 Not found Not found Panulirus japonicus (Japanese spiny lobster) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19073210 Dev Comp Immunol. 2009 Apr;33(4):434-438. Pisuttharachai D, Yasuike M, Aono H, Yano Y, Murakami K, Kondo H, Aoki T, Hirono I. Characterization of two isoforms of Japanese spiny lobster Panulirus japonicus defensin cDNA. DRAMP04433 EPEPSYILDCRTNGGRCVTGYCSNTLPYSCGGGAICCRHAYG 42 Defensin 2 B9UZC9 Not found Not found Panulirus japonicus (Japanese spiny lobster) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19073210 Dev Comp Immunol. 2009 Apr;33(4):434-438. Pisuttharachai D, Yasuike M, Aono H, Yano Y, Murakami K, Kondo H, Aoki T, Hirono I. Characterization of two isoforms of Japanese spiny lobster Panulirus japonicus defensin cDNA. DRAMP04435 FCHNSISCMMGGDSTCNNVCVRQGNPNGGRCLPRDGCPGYDICACYPNN 49 Defensin domain protein Q4WGI8 Not found Not found Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSCA1100) (Aspergillus fumigatus) Antimicrobial Predicted Not found Not found Caution: The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16372009 Nature. 2005 Dec 22;438(7071):1151-6. Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, et al. Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus. DRAMP04436 FTAGIETSFSCSQNGGFCISPKCLPGSKQIGTCILPGSKCCRKK 44 Beta defensin 1 (Beta-defensin-1) Q865P6 Not found defb1 Equus caballus (Horse) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15113660 Vet Immunol Immunopathol. 2004 May;99(1-2):127-132. Davis EG, Sang Y, Blecha F. Equine beta-defensin-1: full-length cDNA sequence and tissue expression. DRAMP04437 GALWGAPAGGVGALPGAFVGAHVGAIAGGFACMGGMIGNKFN 42 Amphipathic pore-forming peptide O54454 Not found thmA Streptococcus thermophilus Antimicrobial, Antibacterial, Antilisterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9162062 J Biol Chem. 1997 May 30;272(22):14277-84. Marciset O, Jeronimus-Stratingh MC, Mollet B, Poolman B. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. DRAMP04438 ITCGQVNSAVGPCLTYARGGGAGPSAACCNGVRSLKSAARTTADRRTACNCLKNAARGIKGLNAGNAASIPSKCGVSVPYTISASIDCSRVR 92 Non-specific lipid-transfer protein A2ZDR8 Belongs to the plant LTP family Not found Oryza sativa subsp. indica (Rice) Antimicrobial Transcript level Not found Not found Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 15685292 PLoS Biol. 2005 Feb;3(2):e38. Yu J, Wang J, Lin W, Li S, Li H, Zhou J, Ni P, Dong W, et al. The Genomes of Oryza sativa: A History of Duplications. DRAMP04439 IWCEFEEATETAICQEHCLPKGYSYGICVSNTCSCI 36 Defensin-like protein (Putative defensin; Predicted) Q45RF8 Not found Not found Bombyx mori (Silk moth) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Kang SJ, Park KS, Park BR. Defensin-like protein encoding cysteine-rich peptides in immune response of silkworm Bombyx mori. DRAMP04440 KSCCKDIMARNCYNVCRIPGTPRPVCATTCRCKIISGNKCPKDYPK 46 Leaf thionin Asthi1 Q8LT03 Not found Asthi1 Avena sativa (Oat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12059099 Mol Plant Microbe Interact. 2002 Jun;15(6):515-521. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y. Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. DRAMP04441 KSCCKDTTARNCYNVCRIPGTPRPVCATTCRCKIISGNKCPKDYPK 46 Leaf thionin Asthi2 Q8LT02 Not found Asthi2 Avena sativa (Oat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12059099 Mol Plant Microbe Interact. 2002 Jun;15(6):515-521. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y. Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. DRAMP04442 NTCCKDDIARNCYNVCRIPGTPTFICANMCRCIITRRNECPNDYPK 46 Leaf thionin Asthi3 Q8LT01 Not found Asthi3 Avena sativa (Oat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12059099 Mol Plant Microbe Interact. 2002 Jun;15(6):515-521. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y. Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. DRAMP04443 KSCCKSTTAINCYNVCRLAGAPRPVCAGPCGCKLLDVTTCPSDWPK 46 Thionin Asthi4 Q8LT00 Not found Asthi4 Avena sativa (Oat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12059099 Mol Plant Microbe Interact. 2002 Jun;15(6):515-521. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y. Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. DRAMP04444 KSCCPSTSARNCYNVCRLTGTSRPRCASLCGCKIVDGTCPDGYSK 45 Thionin Asthi5 Q8LSZ9 Not found Asthi5 Avena sativa (Oat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12059099 Mol Plant Microbe Interact. 2002 Jun;15(6):515-521. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y. Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. DRAMP04445 MALALRFFICFVLTVCIVSSVDAEISCGTVVSNLAPCANYLSKGGVVPDLCCEGVEKLNGVAQTMPMPTVHCKGHFWSQPKSSLWSS 87 Lipid binding protein Q1PDH3 Not found Not found Arabidopsis thaliana (Mouse-ear cress) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Silverstein K.A.T, Moskal W.A.Jr, Wu H.C, Underwood B.A, Graham M.A, Town C.D, VandenBosch K.A. Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. DRAMP04446 LSHSFKGTCLSDTNCANVCHSERFSGGKCRGFRRRCFCTTHC 42 Alcohol dehydrogenase 6 Q9M6B5 Not found ADH6 Vitis vinifera (Grape) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Plant Physiol. 2000, 122:619-619. Or E, Baybik J, Lavee S, Sadka A, Ogredovitch A. Isolation and Characterization of Two cDNA Clones (Accession No. AF195866 and AF195867) Encoding Alcohol Dehydrogenase from Grape (Vitis vinifera cv. Perlette) Developing Fruits. (PGR00-022). DRAMP04447 MADKGVCSRLSALFLLVLLVISIGMMQLELAEARTCKTPSGKFKGVCASSNNCKNVCQTEGFPSGSCDFHVANRKCYCSKPCP 83 Defensin Q6RSS6 Not found Not found Picea glauca (White spruce) (Pinus glauca) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Physiol. Mol. Plant Pathol. 2004, 64:331-341. Pervieux I, Bourassa M, Laurans F, Hamelin R, Seguin A. A spruce defensin showing strong antifungal activity and increased transcript accumulation after wounding and jasmonate treatments. DRAMP04448 MADKGVGSRLSAIFLLVLLVISIGMMQLELAEGRTCKTPSGKFKGVCASSNNCKNVCQTEGFPSGSCDFHVANRKCYCSKPCP 83 Putative gamma-thionin protein Q40779 Not found SPI1 Picea abies (Norway spruce) (Picea excelsa) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8790304 Plant Mol Biol. 1996 Jun;31(3):707-712. Sharma P, Lönneborg A. Isolation and characterization of a cDNA encoding a plant defensin-like protein from roots of Norway spruce. DRAMP04449 MAKFASIIALLFAALVLFSAFEAPSMVEAQKLCEKSSGTWSGVCGNNNACKNQCINLEGARHGSCNYIFPYHRCICYFPC 80 Gamma-thionin 1 Q9FS38 Not found Not found Eutrema japonica (Wasabi plant) (Eutrema wasabi) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11204773 Mol Plant Microbe Interact. 2001 Feb;14(2):111-115. Saitoh H, Kiba A, Nishihara M, Yamamura S, Suzuki K, Terauchi R. Production of antimicrobial defensin in Nicotiana benthamiana with a potato virus X vector. DRAMP04450 MAKFVSIITLLFAALVLFAAFDAPTMVKAQKLCERSSGTWSGVCGNNNACKNQRINLEGARHGSCNYVFP 70 Defensin Q6TXV2 Not found Not found Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassicapekinensis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Park YS, Cho TJ. Characterization of ethylene-inducible genes in Chinese cabbage. DRAMP04451 MAPSRRMVASAFLLLAILVATEMGTTKVAEARHCLSQSHRFKGMCVSSNNCANVCRTESFPDGECKSHGLERKCFCKKVC 80 Os02g0629800 protein (Putative defensin) Q6K209 Not found B1469H02.30 Oryza sativa subsp. japonica (Rice) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Sasaki T, Matsumoto T, Katayose Y. Oryza sativa nipponbare(GA3) genomic DNA, chromosome 2, BAC clone:B1469H02. DRAMP04452 MATQRREISWTFGPLYTWRTTKGYGTTLETTNATSTSSKPSRRYENPYGCPTDEGKCFDRCNDSEFEGGYCGGSYRATCVCYRT 84 Defensin protein 2 Q5VJF8 Not found Not found Amblyomma hebraeum (bont tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Lai R, Turner PC, Lomas LO, Jonczy J, Rees HH. Two Novel Anionic Defensin-like antimicrobial proteins from Hemolymph of the Female Tick, Amblyomma hebraeum. DRAMP04453 MATVRNSRPEAAGEPSGVSSTEGDWRHIEKRDVSYQGEGNTRRFDNPFGCPADEGKCFDHCNNKAYDIGYCGGSYRATCVCYRK 84 Defensin protein 1 Q5VJF9 Not found Not found Amblyomma hebraeum (bont tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Lai R, Turner PC, Lomas LO, Jonczy J, Rees HH. Two Novel Anionic Defensin-like antimicrobial proteins from Hemolymph of the Female Tick, Amblyomma hebraeum. DRAMP04454 MEHSRRMLPAILLLLFLLMPSEMGTKVAEARTCESQSHKFQGTCLRESNCANVCQTEGFQGGVCRGVRRRCFCTRLC 77 Defensin EGAD1 Q8H766 Not found Not found Elaeis guineensis var. tenera (Oil palm) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12021286 J Exp Bot. 2002 Jun;53(373):1387-1396. Tregear JW, Morcillo F, Richaud F, Berger A, Singh R, Cheah SC, Hartmann C, Rival A, Duval Y. Characterization of a defensin gene expressed in oil palm inflorescences: induction during tissue culture and possible association with epigenetic somaclonal variation events. DRAMP04455 MEKKSLAGLCFLFLVLFVAQEIVVTEAKTCENLADKYRGPCFSGCDTHCTTKEHAVSGRCRDDFRCWCTKRC 72 Antifungal protein defensin Q6Y4S5 Not found Not found Arachis diogoi Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases Olli S, Kirthi PB. RT-PCR based cloning of defensin cDNA from Arachis chacoense. DRAMP04456 MEKKSLAGLCFLFLVLFVAQEIVVTEAKTCENLADKYRGPCFSGCDTHCTTKENAVSGRCRDDFRCWCTKRC 72 Defensin Q5YLG8 Not found Def1 Medicago truncatula (Barrel medic) (Medicago tribuloides) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16021402 Plant Mol Biol. 2005 Jun;58(3):385-399. Hanks JN, Snyder AK, Graham MA, Shah RK, Blaylock LA, Harrison MJ, Shah DM. Defensin gene family in Medicago truncatula: structure, expression and induction by signal molecules. DRAMP04457 MEKKSLAGLCFLFLVLFVAQEVMVQTEAKTCENLANTYRGPCFTTGSCDDHCKNKEHLRSGRCRDDFRCWCTRNC 75 PDF1 Q8W434 Not found pDF1 Vigna radiata (Mung bean) Antimicrobial Protein level Not found Not found 2GL1 Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17444520 Proteins. 2007 Aug 1;68(2):530-540. Lin KF, Lee TR, Tsai PH, Hsu MP, Chen CS, Lyu PC. Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin. DRAMP04458 MKCILSLVTLFLVAVLVHSHPAEWNTHQQLDDALWEPAGEVTEEHVARLKRATCDLFSFRSKWVTPNHAACAAHCLLRGNRGGRCKGTICHCRK 94 Defensin A Q86MY3 Not found DEFA Rhodnius prolixus (Triatomid bug) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. DRAMP04459 MKFFITFTFVLSLVVLTVYSAPREFAEPEEQDEGHFRVKRFTCDVLSVEAKGVKLNHAACGIHCLFRRRTGGYCNKKRVCICR 83 Defensin 1 Q9BK52 Not found Not found Acalolepta luxuriosa (Udo longhorn beetle) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Appl. Entomol. Zool. (Jpn.) 2005, 40:335-345. Ueda K, Imamura M, Saito A, Sato R. Purification and cDNA cloning of an insect defensin from larvae of the longicorn beetle, Acalolepta luxuriosa. DRAMP04460 MKFFSLFPVILVVVACLTMRANAAPSAGDEVDHHPDYVDGVEALRQLEPELHGRYKRATCDLLSMWNVNHSACAAHCLLLGKSGGRCNDDAVCVCRK 97 Defensin 2a P82379 Not found smd2a Stomoxys calcitrans (Stable fly) (Conops calcitrans) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Munks R.J.L, Lehane S.M, Lehane M.J. Expression and regulation of the genes, smd1 and smd2, which encode midgut-specific defensin molecules in Stomoxys calcitrans. DRAMP04461 MKFLNVVAIALLVVACLSVYSNAAPHEGVKEVAAAKPMGITCDLLSLWKVGHAACAAHCLVLGNVGGYCTKEGLCVCKE 79 Defensin 1a P82378 Not found smd1a Stomoxys calcitrans (Stable fly) (Conops calcitrans) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Munks R.J.L, Lehane S.M, Lehane M.J. Expression and regulation of the genes, smd1 and smd2, which encode midgut-specific defensin molecules in Stomoxys calcitrans. DRAMP04462 MKFLQIFVLIATLWIAIVTANPVDDQKTAEIQENSNLIDETNNDEVIIQPRLSCQALGPIGCAANCKRLGFRGGWCTTGNTCRCFR 86 Putative uncharacterized protein Q5QBJ4 Not found Not found Culicoides sonorensis Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Insect Mol. Biol. 2005, 0:0-0. Campbell C.L, VanDyke K.A, Letchworth G.J, Drolet B.S, Hanekamp T, Wilson W.C. Midgut and salivary gland transcriptomes of the arbovirus vector Culicoides sonorensis (Diptera: Ceratopogonidae). DRAMP04463 MKQYKVLNEKEMKKPIGGESVFSKIGNAVGPAAYWILKGLGNMSDVNQADRINRKKH 57 Enterocin 1071A (Enterocin EntC1 peptide) Q9L9U6 Not found ent1071A Enterococcus faecalis (Streptococcus faecalis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10742203 Appl Environ Microbiol. 2000 Apr;66(4):1298-1304. Balla E, Dicks LM, Du Toit M, Van Der Merwe MJ, Holzapfel WH. Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071. DRAMP04464 MKTFSVAVAVAIVLAFICTQESSALPVTGVEELVELVSSDDPVADHQELPVELGERLFNIRKKRASPKCTPYCYPTRDGV 80 Hepcidin 1 D3Y2R5 Not found Not found Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-568. Zhou J.G, Wei J.G, Xu D, Cui H.C, Yan Y, Ou-Yang Z.L, Huang X.H, Huang Y.H, Qin Q.W. Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides. DRAMP04465 MKTFSVAVAVAVVLAFICTQESSALPVTGIEELVEPVSSDNNDNHQGLPVELRERLVNIRKKRAPTDCIPYCYPTGDGFH 80 Hepcidin 2 D3Y2R6 Not found Not found Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-568. Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW. Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides. DRAMP04466 MMKIAVPVFLILALFAMSQAAPSLALPGTVQVANVQPRGYCNLSNCLSQCYRRGFRWGWCDFFNTCHCS 69 Defensin TY 2 C1IBY6 Not found Not found Tabanus yao (Horsefly) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Xu X, Ma D, Wu J, Lai R. Cloning and characterization of defensin in horsefly (Tabanus Yao). DRAMP04467 MMNATENQIFVETVSDQELEMLIGGAGRGWIKTLTKDCPNVISSICAGTIITACKNCA 58 Columbicin A A0FL76 Not found colA Enterococcus columbae Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Martin M, Brede D.A, Herranz C, Nes I.F, Cintas L.M, Hernandez P.E. Amino acid and nucleotide sequence of columbicin A, a novel lantibiotic variant produced by Enterococcus columbae PLCH2, isolated from wood pigeons (Columba palumbus). DRAMP04468 MNFKLLNLFAMVLFGVVVISNAAKPPSGFLTPDADNDENGNGVEEQTLERFTCDIWQNQAACAIHCIANGFRGGYCNAQKVCVCRR 86 Defensin I Q2QKD4 Not found Not found Mayetiola destructor (Hessian fly) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17070830 J Insect Physiol. 2006 Nov-Dec;52(11-12):1143-1152. Mittapalli O, Shukle RH, Sardesai N, Giovanini MP, Williams CE. Expression patterns of antibacterial genes in the Hessian fly. DRAMP04469 MNFNKLFVFVALVLAVCIGQSEAGWLKKIGKKIERVGQHTRDATIQTIGVAQQAANVAATLKG 63 Cecropin (Cecropin 1 (Cecropin A) Q95VE8 Not found Cep 1 Musca domestica (House fly) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Wang J, Zhao X. Molecular cloning and recombinant expression of a new gene encoding an antimicrobial peptide from house fly. DRAMP04470 MNNLNKFSTLGKSSLSQIEGGSVPTSVYTLGIKILWSAYKHRKTIEKSFNKGFYH 55 Plantaricin NC8 beta peptide Q84HW1 Not found plnc8B Lactobacillus plantarum Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12514019 Appl Environ Microbiol. 2003 Jan;69(1):383-389. Maldonado A, Ruiz-Barba JL, Jiménez-Díaz R. Purification and genetic characterization of plantaricin NC8, a novel coculture-inducible two-peptide bacteriocin from Lactobacillus plantarum NC8. DRAMP04471 MQTIKELNTMELQEIIGGENDHRMPYELNRPNNLSKGGAKCAAGILGAGLGAVGGGPGGFISAGISAVLGCM 72 Durancin Q prepeptide (Prepeptide of durancin Q) B5BP43 Not found duqQ Enterococcus durans Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Hu C, Zendo T, Nakayama J, Sonomoto K. Functional analysis and comparison of genes in the durM and the duqQ loci in durancin TW-49M and durancin Q biosynthesis and regulation. DRAMP04472 MRAIVFVLIFAIAFAATREGSILCNLCKDTVNLIENLLTVDGAQAVRQYIDNLCAKADGFLGTLCNKILSFGVDELVKLIENHVDPVVICEKIHAC 96 Pore-forming protein isoform B Q9U8G5 Not found Dp-B Entamoeba dispar Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10518795 Eur J Biochem. 1999 Nov;265(3):1002-1007. Nickel R, Ott C, Dandekar T, Leippe M. Pore-forming peptides of Entamoeba dispar. Similarity and divergence to amoebapores in structure, expression and activity. DRAMP04473 VPGGCTYTRSNRDVIGTCKTGSGQFRIRLDCNNAPDKTSVWAKPKVMVSVHCLVGQPRSISFETK 65 Propionicin T1 Q9F6C4 Not found pctA Propionibacterium thoenii Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11010864 Appl Environ Microbiol. 2000 Oct;66(10):4230-4236. Faye T, Langsrud T, Nes IF, Holo H. Biochemical and genetic characterization of propionicin T1, a new bacteriocin from Propionibacterium thoenii. DRAMP04474 VSCDFEEANEDAVCQEHCLPKGYTYGICVSHTCSCI 36 Defensin (Spodoptericin) Q7Z0G6 Not found Def Spodoptera frugiperda (Fall armyworm) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14597170 Gene. 2003 Nov 13;319:43-53. Volkoff AN, Rocher J, d'Alençon E, Bouton M, Landais I, Quesada-Moraga E, Vey A, Fournier P, Mita K, Devauchelle G. Characterization and transcriptional profiles of three Spodoptera frugiperda genes encoding cysteine-rich peptides. A new class of defensin-like genes from lepidopteran insects? DRAMP04475 VTCDLLGPTGWGDALCAAHCISKGYRGGYCNAQKVCVCR 39 Putative defensin A8CWF7 Not found DEF Lutzomyia longipalpis (Sand fly) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18194529 BMC Genomics. 2008 Jan 14;9:15. Jochim RC, Teixeira CR, Laughinghouse A, Mu J, Oliveira F, Gomes RB, Elnaiem DE, Valenzuela JG. The midgut transcriptome of Lutzomyia longipalpis: comparative analysis of cDNA libraries from sugar-fed, blood-fed, post-digested and Leishmania infantum chagasi-infected sand flies. DRAMP04476 MRILHFLLAFLIVFLLPVPGFTAGIETSFSCSQNGGFCISPKCLPGSKQIGTCILPGSKCCRKK 64 Beta defensin 1 (Beta-defensin-1) Q865P6 Not found defb1 Equus caballus (Horse) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15113660 Vet Immunol Immunopathol. 2004 May;99(1-2):127-132. Davis EG, Sang Y, Blecha F. Equine beta-defensin-1: full-length cDNA sequence and tissue expression. DRAMP04477 MRLHHLLLALFFLVLSAGSGFTQGIINHRSCYRNKGVCAPARCPRNMRQIGTCHGPPVKCCRKK 64 Beta defensin-2 O97942 Not found Not found Capra hircus (Goat) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10531296 Infect Immun. 1999 Nov;67(11):6221-6224. Zhao C, Nguyen T, Liu L, Shamova O, Brogden K, Lehrer RI. Differential expression of caprine beta-defensins in digestive and respiratory tissues. DRAMP04478 MNFLKVFLVICAILATVWASPLGASEDREHHPEERAPCAQSEKDRCVAFCLTNGFSGGFCTSRGCKCEE 69 Defensin TY 1 C1IBY5 Not found Not found Tabanus yao (Horsefly) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Xu X, Ma D, Wu J, Lai R. Cloning and characterization of defensin in horsefly (Tabanus Yao). DRAMP04479 MRLLFLLFLLLVCLIQMASGHEKTGRKHECQNMGGACKHQKTHGCAILPADCKSRNKHCCRV 62 Defensin like 3 (Predicted) Q0W9Q3 Not found defl3 Equus caballus (Horse) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16723195 Gene. 2006 Jul 19;376(2):192-198. Looft C, Paul S, Philipp U, Regenhard P, Kuiper H, Distl O, Chowdhary BP, Leeb T. Sequence analysis of a 212 kb defensin gene cluster on ECA 27q17. DRAMP04480 MRTFALLAATVLLVILQAQAEPVQARADEVAAQEQPGGHAQEASVSFVWDEGAAGQVSGERGQHAKLQSLEGQTGNGLWNRVSMVHVT 88 Alpha defensin Q6KFT8 Not found DEFA1 Saguinus labiatus (Red-chested mustached tamarin) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15019196 ptides. 2003 Nov;24(11):1647-1654. Nguyen TX, Cole AM, Lehrer RI. Evolution of primate theta-defensins: a serpentine path to a sweet tooth. DRAMP04481 MSLLALVAGTLGVSQSIATTVVSIVLTGSTLISIILGITAILSGGVDAILEIGWSAFVATVKKIVAERGKAAAIAW 76 Circularin A Q5L226 Not found Not found Geobacillus kaustophilus (strain HTA426) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal L No cytotoxicity information found Not found 15576355 Nucleic Acids Res. 2004 Dec 1;32(21):6292-303. Takami H, Takaki Y, Chee GJ, Nishi S, Shimamura S, Suzuki H, Matsui S, Uchiyama I. Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus. DRAMP04482 MYSKYERQKDKRPYSERKDQYTGPQFLYPPDRIPPSKAIKWNEEGLPMYEVLPDGAGAKTAVEAAAE 67 Antimicrobial-like peptide PP-1 (Predicted) Q867H2 Not found Pp-1 Pheretima tschiliensis Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Wang X, Wang X.X. cDNA cloning and molecular characterization of a new antimicrobial-like peptide from Pheretima tschiliensis. DRAMP04483 NKWGNAVIGAATGATRGVSWCRGFGPWGMTACALGGAAIGGYLGYKSN 48 Acidocin LF221B (Gassericin K7 B) Q7WRX6 Not found Not found Lactobacillus gasseri Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14504837 Appl Microbiol Biotechnol. 2004 Feb;63(6):705-714. Majhenic AC, Venema K, Allison GE, Matijasić BB, Rogelj I, Klaenhammer TR. DNA analysis of the genes encoding acidocin LF221 A and acidocin LF221 B, two bacteriocins produced by Lactobacillus gasseri LF221. DRAMP04484 QNKDDTRFLGGVPGVGGGFVPGVPGHGGVAPVGGGLVPGGGGLIPGGGFECNYCRTRYGYVCCSDKCCYDVCLNDTVCKPIVLGSEG 87 Crustin-like protein fc-2 (Predicted) Q102W4 Not found Not found Fenneropenaeus chinensis (Fleshy prawn) (Penaeus chinensis) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16987562 J Biotechnol. 2007 Jan 20;127(4):605-614. Zhang J, Li F, Wang Z, Xiang J. Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. DRAMP04485 RCICGRGICRCICGRGIC 18 Retrocyclin Q8TEZ3 Not found DEFQ1 Homo sapiens (Human) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11854483 Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1813-1818. Cole AM, Hong T, Boo LM, Nguyen T, Zhao C, Bristol G, Zack JA, Waring AJ, Yang OO, Lehrer RI. Retrocyclin: a primate peptide that protects cells from infection by T- and M-tropic strains of HIV-1. DRAMP04486 SFPKKIDCGGACAARCQLSSRPHLCKRACGTCCARSRCVPPGTAGNQEMCPCYASLTTHGGKRKCP 66 Cold-regulated LTCOR12 O65313 Not found LtCor12 Lavatera thuringiaca Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Vazquez-Tello A. Cloning and characterization of low temperature-regulated genes from Lavatera thuringiaca. DRAMP04487 SSPKKIDCGGACAARCQLSSRPHLCKRACGTCCARCACVPPGTAGNQEMCPKCYASLTTHGGKRKCP 67 LTCOR11 O24040 Not found LtCor11 Lavatera thuringiaca Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Vazquez-Tello A, Uozumi T. LtCor11, a low-temperature-regulated gene from Lavatera thuringiaca homologous to the gibberellin-regulated GAS1 gene from Arabidopsis thaliana. DRAMP04488 SYFTAWAGPGCNNHAARYSKCGCSNIGNNVHGGYEFMYQGQTAAAYNTDNCKGVAQTRFSSSVNQACSSFGWKSFFIQC 79 Antimicrobial peptide 2 (Antimicrobial peptide 4) Q71QD7 Not found AMP4 Pinus sylvestris (Scots pine) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 14612232 FEMS Microbiol Lett. 2003 Nov 7;228(1):27-31. Asiegbu FO, Choi W, Li G, Nahalkova J, Dean RA. Isolation of a novel antimicrobial peptide gene (Sp-AMP) homologue from Pinus sylvestris (Scots pine) following infection with the root rot fungus Heterobasidion annosum. DRAMP04489 SYREAVLRAVDQFNERSAEANLYRLLELDPPPEQDAEDQGARKPVSFRVKETVCPRTSQQPVEQCD 66 MAP34-A protein (MAP34-B protein) P82017, P82016 Not found map34-A Capra hircus (Goat) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Zhao C, Nguyen T, Brogden K, Lehrer R. cDNA cloning of goat cathelin related peptides. DRAMP04490 SYREAVLRAVDQFNERSAEANLYRLLELDPPPEQDAEDRGARKPVSFKVKETVCPRTSQQPVEQCD 66 Myeloid antimicrobial peptide P79360 Not found Map-34 Ovis aries (Sheep) Antimicrobial, Antibacterial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8549789 FEBS Lett. 1995 Dec 27;377(3):519-522. Mahoney MM, Lee AY, Brezinski-Caliguri DJ, Huttner KM. Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide. DRAMP04491 VASCGQVVSYLAPCIGYAMGRERAPGGGCCTGVRSLNAAAATPADRQATCTCLKQQTSGMGGIKPDLVAGIPSKCGVNIPYAISPRTDCSKVR 93 Non-specific lipid-transfer protein Q5UNP2 Not found Ltp6 Hordeum vulgare var. distichum (Two-rowed barley) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Lipid-binding 15821867 Plant Mol Biol. 2005 Jan;57(1):35-51. Federico ML, Kaeppler HF, Skadsen RW. The complex developmental expression of a novel stress-responsive barley Ltp gene is determined by a shortened promoter sequence. DRAMP04492 GFGCPFNQGACHRHCRSIGRRGGYCAGLFKQTCTCYSR 38 Persulcatusin B7XFT1 Not found Not found Ixodes persulcatus (Taiga tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Insect Mol. Biol. 2009, 18:531-539. Saito Y, Konnai S, Yamada S, Imamura S, Nishikado H, Ito T, Onuma M, Ohashi K. Identification and characterization of antimicrobial peptide, defensin, in the taiga tick, Ixodes persulcatus. DRAMP04493 GFGCPFNQYQCHSHCLSIGRRGGYCGGSFKTTCTCYN 37 Amercin A0F088 Not found amn Amblyomma americanum (Lone star tick) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17550433 Med Vet Entomol. 2007 Jun;21(2):141-147. Todd SM, Sonenshine DE, Hynes WL. Tissue and life-stage distribution of a defensin gene in the Lone Star tick, Amblyomma americanum. DRAMP04494 GGYCSGIIKQTCTCYRN 17 Defensin B6UYK4 Not found Not found Dermacentor reticulatus Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Matejovska T, Golovchenko M, Rudenko N, Grubhoffer L. Cloning and sequencing of defensins in hard and soft ticks. DRAMP04495 GGYYCPFFQDKCHRHCRSFGRKAGYCGGFLKKTCICVMK 39 Preprodefensin Q7YXK5 Not found Not found Ixodes ricinus (Common tick) Antimicrobial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15691006 J Med Entomol. 2005 Jan;42(1):36-41. Rudenko N, Golovchenko M, Edwards MJ, Grubhoffer L. Differential expression of Ixodes ricinus tick genes induced by blood feeding or Borrelia burgdorferi infection. DRAMP04496 GICYVLTCNSLCFPKLGRCSYNTCYCY 27 Cysteine-rich protein Q5DIE2 Not found Not found Apriona germari (Mulberry longhorn beetle) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Gui Z.-Z, Lu W, Sohn H.D, Jin B.R. Molecular cloning a cDNA encoding the cysteine-rich protein from the mulberry longicorn beetle, Apriona germari. DRAMP04497 GSLKSSQCNPECTRRCSKTQYHKPCMFFCQKCCRKCLCVPPGFYGNKAVCPCYNNWKTQQGGPKCP 66 Gasa4-like protein (Predicted) Q6V0P7 Not found Not found Pelargonium zonale Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Rosenwasser S, Granot D, Friedman H. A homolog of gip-1 (gibberellic acid-induced gene). DRAMP04498 GSVSIEECPQKCDYRCSATKRQEPCLKYCNICCQKCLCVPSGTSGNKEECPCYNNLKSSQGNSKCP 66 GAST1 protein, putative Q10P25 Not found Not found Oryza sativa subsp. japonica (Rice) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16109971 Genome Res. 2005 Sep;15(9):1284-91. Buell CR, Yuan Q, Ouyang S, Liu J, Zhu W, et al, Jiang J, Jackson S. Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species. DRAMP04499 HISHISMCRWCCNCCKAKGCGFCCKF 26 Hepcidin (Hepcidin type I) Q49SH5 Not found Not found Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041149 Biosci Biotechnol Biochem. 2005 Jul;69(7):1411-1414. Kim YO, Hong S, Nam BH, Lee JH, Kim KK, Lee SJ. Molecular cloning and expression analysis of two hepcidin genes from olive flounder Paralichthys olivaceus. DRAMP04500 IAASKINCGAACKARCRLSSRPNLCHRACGTCCARCRCVPPGTSGNQKVCPCYYNMTTHGGRRKCP 66 GEG protein Q9XGJ3 Not found geg Gerbera hybrida (Daisy) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10368180 Plant Cell. 1999 Jun;11(6):1093-1104. Kotilainen M, Helariutta Y, Mehto M, Pollanen E, Albert VA, Elomaa P, Teeri TH. GEG participates in the regulation of cell and organ shape during corolla and carpel development in gerbera hybrida. DRAMP04501 VTCDLLSFGGKVGHSACAANCLSMGKAGGRCNGGVCQCRKTTFGDLWNKRF 51 Antimicrobial peptide Def1-2 D0EZK5 Not found Not found Nasonia vitripennis (Parasitic wasp) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20097222 Dev Comp Immunol. 2010 Jun;34(6):659-668. Gao B, Zhu S. Identification and characterization of the parasitic wasp Nasonia defensins: positive selection targeting the functional region? DRAMP04502 VTCDLLSFGGVVGDSACAANCLSMGKAGGSCNGGICECRKTTFKELWDQRF 51 Antimicrobial peptide Def1-1 D0EZK4 Not found Not found Nasonia vitripennis (Parasitic wasp) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20097222 Dev Comp Immunol. 2010 Jun;34(6):659-668. Gao B, Zhu S. Identification and characterization of the parasitic wasp Nasonia defensins: positive selection targeting the functional region? DRAMP04503 GILTDTLKGAAKNVAGVLLDKLKCKITGGC 30 Pelophylaxin-1 (Frogs, amphibians, animals) Q2WCN8 Not found pelophylaxin-1 Pelophylax plancyi fukienensis (Fukien gold-striped pond frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139927 Peptides. 2006 Jan;27(1):36-41. Zhou M, Chen T, Walker B, Shaw C. "Pelophylaxins: novel antimicrobial peptide homologs from the skin secretion of the Fukien gold-striped pond frog, Pelophylax plancyi fukienensis: identification by ""shotgun"" cDNA cloning and sequence analysis." DRAMP04504 GILLNTLKGAAKNVAGVLLDKLKCKITGGC 30 Pelophylaxin-2 (Frogs, amphibians, animals) Q2WCN7 Not found pelophylaxin-2 Pelophylax plancyi fukienensis (Fukien gold-striped pond frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139927 Peptides. 2006 Jan;27(1):36-41. Zhou M, Chen T, Walker B, Shaw C. "Pelophylaxins: novel antimicrobial peptide homologs from the skin secretion of the Fukien gold-striped pond frog, Pelophylax plancyi fukienensis: identification by ""shotgun"" cDNA cloning and sequence analysis." DRAMP04505 GLMDSLKGLAATAGKTVLQGLLKTASCKLEKTC 33 Pelophylaxin-3 (Frogs, amphibians, animals) Q2WCN6 Not found pelophylaxin-3 Pelophylax plancyi fukienensis (Fukien gold-striped pond frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139927 Peptides. 2006 Jan;27(1):36-41. Zhou M, Chen T, Walker B, Shaw C. "Pelophylaxins: novel antimicrobial peptide homologs from the skin secretion of the Fukien gold-striped pond frog, Pelophylax plancyi fukienensis: identification by ""shotgun"" cDNA cloning and sequence analysis." DRAMP04506 ILPFLAGLFSKIL 13 Pelophylaxin-4 (Frogs, amphibians, animals) Q2WCN5 Not found pelophylaxin-4 Pelophylax plancyi fukienensis (Fukien gold-striped pond frog) Antimicrobial, Antibacterial, Antifungal, Antiviral Homology Not found Not found Function: Amphibian defense peptide. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16139927 Peptides. 2006 Jan;27(1):36-41. Zhou M, Chen T, Walker B, Shaw C. "Pelophylaxins: novel antimicrobial peptide homologs from the skin secretion of the Fukien gold-striped pond frog, Pelophylax plancyi fukienensis: identification by ""shotgun"" cDNA cloning and sequence analysis." DRAMP04507 MLTLKKSMLLLFFLGTISLSLCEEERSADEDDGEKEVKRGIFSLIKTAAKFVGKNLLKQAGKAGLEHLACKAKNEC 76 Esculentin-2-AJ2 antimicrobial peptide (Frogs, amphibians, animals) K7Z8Z8 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04508 MLTLKKSMLLLFFLGTISLSLCEEERSADEDDGEKEVKRGIFSLIKTAAKFVGKNLLKQAGKAGLEHLACKAENEC 76 Esculentin-2-AJ3 antimicrobial peptide (Frogs, amphibians, animals) K7ZGR7 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04509 MLTLKKSMLLLFFLGTISLSLCEEERSADEDDGEKEVKRGILSLIKNAAKFVGKNLHKQAGKGGLEHLACKAKNEC 76 Esculentin-2-AJ4 antimicrobial peptide (Frogs, amphibians, animals) K7ZAL5 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04510 MFTMKKSLLVLFLLGIISLSFCEEERNADEDDGEMTEEEKRGILSTLKQFGKAAVKGVAQSLLNTASCKLAKTC 74 Esculentin-2-AJ5 antimicrobial peptide (Frogs, amphibians, animals) K7Z8Z5 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04511 MFTMKKSLLVLFFLGIISLFFCEEERNADEDDGEMTEEEKRGILSTLKQFGKAAVKGVAQSFLNTASCKLAKTC 74 Esculentin-2-AJ6 antimicrobial peptide (Frogs, amphibians, animals) K7ZGR5 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04512 MFTMKKSLLVLFFLGTISLSLCEEERNADEDDGEMTEEEKRGLMSTFKQVGISAIKGAAKNVLDVLSCKIAKTC 74 Brevinin-2-AJ2 antimicrobial peptide (Frogs, amphibians, animals) K7ZAL2 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04513 MFTLKKSMLLLFFLGTISLSFCEEERSADEVDGEKEVKRGIFSIIKTAAKFLGKNLLKEAGKAGMEHLACKAKNEC 76 Esculentin-2-AJ1 antimicrobial peptide (Frogs, amphibians, animals) K7ZJ57 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04514 MFTMKKSLLVLFFLGTISLSLCEEERNADEDDGEMTEEEKRGLVSTFKQVGISAIKGAAKNVLDVLSCKIAKTC 74 Brevinin-2-AJ7 antimicrobial peptide (Frogs, amphibians, animals) K7ZAL3 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04515 MFTLKKSLLLLFFLATINLSLCEEERNADEDDGEMTEEEKRGFMSTFKQVGISAIKGAAKNVLDVLSCKIAKTC 74 Brevinin-2-AJ4 antimicrobial peptide (Frogs, amphibians, animals) K7ZJ56 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04516 MFTMKKSLLVIFFLGTISLSLCEEERNADEDDGEMTEEEKRGLMSTFKRVGISAIKGAAKNVLDVLSCKIAKTC 74 Brevinin-2-AJ1 antimicrobial peptide (Frogs, amphibians, animals) K7ZGR3 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04517 MFTMKKSLLVLFFLGTISLSLCEEERNADEDDGEMTEEEKRGLMSTFKQVGISAIKGAAQNVLGVLSCKLAKTC 74 Brevinin-2-AJ3 antimicrobial peptide (Frogs, amphibians, animals) K7Z432 Not found Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22828809 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04518 MFTLKKSLLLLFFLGTINLFFCQEEERNADEEERRDERDVEVEKRVIPFVASVAAETMQHVYCAASKKMLKLNWKSSDVENHLAKC 86 Odorranain-P1a antimicrobial peptide (Frogs, amphibians, animals) A6MBQ0 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04519 MFTMKKSLLLLFFLGTINLSLCQEEERNADEEERRDERDVEVEKRVIPFVASVAAEMMQHVYCAASKKC 69 Odorranain-P1b antimicrobial peptide (Frogs, amphibians, animals) A6MBR0 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol Cell Proteomics. 2007 May;6(5):882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y, Rees HH, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04520 MFTMKKPLLLLFFLGTISLSLCEEERNADEDDGEKEVKRGIFALIKTAAKFVGKNLLKQAGKAGLEHLACKANNQC 76 Esculentin-2MT1 antimicrobial peptide (Frogs, amphibians, animals) E1AXF6 Not found Not found Amolops mantzorum Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops mantzorum. DRAMP04521 MFTLKKSMLLLFFLGTISLSLCEEERSADEDDGEKEVKRGIFSLIKTAAKFVGKNLLKQAGKAGMEHLACKANNQC 76 Esculentin-2MT2 antimicrobial peptide (Frogs, amphibians, animals) E1B242 Not found Not found Amolops mantzorum Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2010) to the EMBL/GenBank/DDBJ database Wang H, Liu J. Antimicrobial peptides from amphibian skin of Amolops mantzorum. DRAMP04522 MFTMKKSMLLLFFLGMISLSLCQDERGADEDDGGEMTEEEKRGAFGDFLKGAAKKAGLKILSIAQCKLSGTC 72 Brevinin-2LT2 antimicrobial peptide (Frogs, amphibians, animals) B9W1P5 Not found Not found Hylarana latouchii (broad-folded frog) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JAN-2009) to the EMBL/GenBank/DDBJ database Wang H, Hu Y. Construction of cDNA library of Hylarana latouchii skin tissue withcloning and sequence analysis of the cDNA encoding antimicrobialpeptides brevinin-2LTs. DRAMP04523 MFTMKKSLLLLFFLGTINLSFCQEEVRNADEEERRDERDVEVEKRVIPFVASVAAEMMQHVYCAASKKC 69 Odorranain-P1b antimicrobial peptide (Frogs, amphibians, animals) A6MBQ7 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol. Cell. Proteomics. 2007,6:882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y,Rees H.H, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04524 MFTMKKSLLLLFFLGTINLSLCQEEVRNADEEERRDERDVEVEKRVIPFVASVAAEMMQHVYCAASKKC 69 Odorranain-P1b antimicrobial peptide (Frogs, amphibians, animals) A6MBQ9 Not found Not found Odorrana grahami (Yunnanfu frog) (Rana grahami) Antimicrobial Homology Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17272268 Mol. Cell. Proteomics. 2007,6:882-894. Li J, Xu X, Xu C, Zhou W, Zhang K, Yu H, Zhang Y, Zheng Y,Rees H.H, Lai R, Yang D, Wu J. Anti-infection peptidomics of amphibian skin. DRAMP04525 RSALSCQMCELVVKKYEGSADKDANVIKKDFDAECKKLFHTIPFGTRECDHYVNSKVDPIIHELEGGTAPKDVCTKLNECP 81 Caenopore-5 No entry found Not found Not found Not found Not found Not found Not found The overall structure of the two caenopore-5 conformers consists of five amphiphatic helices connected by three disulfide bonds. The five helices are arranged in a folded leaf which is the characteristic signature of the SAPLIP family. 2JS9 Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19917307 Dev Comp Immunol. 2010 Mar;34(3):323-330. Mysliwy J, Dingley AJ, Stanisak M, Jung S, Lorenzen I, Roeder T, Leippe M, Grötzinger J. Caenopore-5: The three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans. DRAMP04526 SCVFIPCITSLAGCSCKNKVCYYDGGSVPCGE 32 Parigidin-br1 (Cyclotides; Plants) No entry found Not found Not found Palicourea rigida (Rubiaceae) Insecticidal Not found Not found Not found Function: Parigidin-br1 showes potent insecticidal activity against neonate larvae of Lepidoptera (Diatraea saccharalis), causing 60% mortality at a concentration of 1 µm but had no detectable antibacterial effects. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22074926 J Biol Chem. 2012 Jan 2;287(1):134-147. Pinto MF, Fensterseifer IC, Migliolo L, Sousa DA, de Capdville G, Arboleda-Valencia JW, Colgrave ML, Craik DJ, Magalhães BS, Dias SC, Franco OL. Identification and structural characterization of novel cyclotide with activity against an insect pest of sugar cane. DRAMP04527 SVRTQDNAVNRQIFGSNGPYRDFQLSDCYLPLETNPYCNEWQFAYHWNNALMDCERAIYHGCNRTRNNFITLTACKNQAGPICNRRRH 88 Luxuriosin No entry found Not found Not found Acalolepta luxuriosa (longicorn beetle) Antimicrobial, Antibacterial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15716136 Biochim Biophys Acta. 2005 Feb 11;1722(1):36-42. Ueda K, Saito A, Imamura M, Miura N, Atsumi S, Tabunoki H, Watanabe A, Kitami M, Sato R. Purification and cDNA cloning of luxuriosin, a novel antibacterial peptide with Kunitz domain from the longicorn beetle, Acalolepta luxuriosa. DRAMP04529 FTQGVRNSQSCRRNKGICVPIRCPGSMRQIGTCLGAQVKCCRRK 44 LAP-like antimicrobial peptide (Bovine beta-defensins) Q5W5H8 Not found lap-like Bos taurus (Bovine) Antimicrobial, Antibacterial Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15520886 Mamm Genome. 2004 Oct;15(10):834-842. Roosen S, Exner K, Paul S, Schröder JM, Kalm E, Looft C. Bovine beta-defensins: identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue. DRAMP01097 GIGASILSAGKSALKGLAKGLAEHFAN 27 Bombinin-like peptide 1 (toads, amphibians, animals) P29002? Belongs to the bombinin family Not found Bombina orientalis (Oriental fire-bellied toad) Antimicrobial Protein level Alpha helix These peptides are cationic but otherwise differ considerably in such basic featuresa st heir size (Mr ~2300-4000), presence of disulfide bonds, and structural motifs. Function: Has antimicrobial activity, but no significant hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. [Ref.1744108] 82% inhibition Neisseria meningitidis 118V C (MIC=20 µg/ml), 98% inhibition Neisseria meningitidis 15240 IAI(MIC=20 µg/ml), 85% inhibition Neisseria meningitidis 126E IC1(MIC=20 µg/ml), 98% inhibition Neisseria gonorrhoeoe F62 (MIC=20 µg/ml), 96% inhibition Neisseria Iactamica 15323(MIC=20 µg/ml), 100% inhibition Neisseria Iactamica 15215A(MIC=20 µg/ml), 98% inhibition Neisseria cinerea 15461 (MIC=20 µg/ml), Bacillus megaterium BmII(MIC=0.3 µM), Staphylococcus aureus Cowan1 (MIC=3.4 µM), Escherichia coli D21 (MIC=1.7 µM), Escherichia coli D22(MIC=1.5 µM), Yersinia pseudotubercolosis (MIC=0.8 µM), Pseudomonas aeruginosa ATCC 15692(MIC=6.3 µM), Candida albicans(MIC=0.4 µM). [Ref.1744108] No significant hemolytic activity against human red blood cell. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 1744108 J Biol Chem. 1991 Dec 5;266(34):23103-23111. Gibson BW, Tang DZ, Mandrell R, Kelly M, Spindel ER. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. DRAMP04533 AKRHHGYKRKFH 12 P-113D No entry found Not found Not found Homo sapiens Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11709321 Antimicrob Agents Chemother. 2001 Dec;45(12):3437-3444. Sajjan US, Tran LT, Sole N, Rovaldi C, Akiyama A, Friden PM, Forstner JF, Rothstein DM. P-113D, an Antimicrobial Peptide Active against Pseudomonas aeruginosa, Retains Activity in the Presence of putum from Cystic Fibrosis Patients. DRAMP04534 EPHPDEFVGLM 11 PG-KI No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04535 EPNPDEFVGLM 11 PG-KII No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04536 EPHPNEFVGLM 11 PG-KIII No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04537 EPNPDEFFGLM 11 PG-SPI No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04538 EPNPNEFFGLM 11 PG-SPII No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04539 EGGGPQWAVGHFM 13 PG-L No entry found Not found Not found Pseudophryne guntheri (Australian myobatrachid frog) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2356157 Peptides. 1990 Mar-Apr;11(2):299-304. Simmaco M, Severini C, De Biase D, Barra D, Bossa F, Roberts JD, Melchiorri P, Erspamer V. Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne guntheri. DRAMP04540 EKKPPRPPQWAVGHFM 16 PR-bombesin No entry found Not found Not found Bombina maxima (Chinese red belly toad) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11835992 Peptides. 2002 Mar;23(3):437-442. Lai R, Liu H, Lee WH, Zhang Y. A novel proline rich bombesin-related peptide (PR-bombesin) from toad Bombina maxima. DRAMP04541 PSCVCSGFETSGIHFC 16 Bb-AMP4 No entry found Not found Not found Bellamya bengalensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21262297 Peptides. 2011 Apr;32(4):691-696. Gauri SS, Mandal SM, Pati BR, Dey S. Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis. DRAMP04547 NALSMPRNKCNRALMCFG 18 Shuchin 1 No entry found Not found Not found Rana shuchinae Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20553780 Peptides. 2010 Sep;31(9):1674-1677. Zheng R, Yao B, Yu H, Wang H, Bian J, Feng F. Novel family of antimicrobial peptides from the skin of Rana shuchinae. DRAMP04548 NALSSPRNKCDRASSCFG 18 Shuchin 2 No entry found Not found Not found Rana shuchinae Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20553780 Peptides. 2010 Sep;31(9):1674-1677. Zheng R, Yao B, Yu H, Wang H, Bian J, Feng F. Novel family of antimicrobial peptides from the skin of Rana shuchinae. DRAMP04549 WLNALLHHGLNCAKGVL 17 17Hc No entry found Not found Not found Halocynthia aurantium Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878508 Antimicrob Agents Chemother. 2003 Aug;47(8):2481-2486. Jang WS, Kim CH, Kim KN, Park SY, Lee JH, Son SM, Lee IH. Biological Activities of Synthetic Analogs of Halocidin, an Antimicrobial Peptide from the Tunicate Halocynthia aurantium. DRAMP04550 WLNALLKKGLNCAKGVLA 18 18HcKK No entry found Not found Not found Halocynthia aurantium Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878508 Antimicrob Agents Chemother. 2003 Aug;47(8):2481-2486. Jang WS, Kim CH, Kim KN, Park SY, Lee JH, Son SM, Lee IH. Biological Activities of Synthetic Analogs of Halocidin, an Antimicrobial Peptide from the Tunicate Halocynthia aurantium. DRAMP04551 KWLNALLHHGLNCAKGVLA 19 K19Hc No entry found Not found Not found Halocynthia aurantium Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878508 Antimicrob Agents Chemother. 2003 Aug;47(8):2481-2486. Jang WS, Kim CH, Kim KN, Park SY, Lee JH, Son SM, Lee IH. Biological Activities of Synthetic Analogs of Halocidin, an Antimicrobial Peptide from the Tunicate Halocynthia aurantium. DRAMP04552 KWLNALLKKGLNCAKGVLA 19 K19HcKK No entry found Not found Not found Halocynthia aurantium Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12878508 Antimicrob Agents Chemother. 2003 Aug;47(8):2481-2486. Jang WS, Kim CH, Kim KN, Park SY, Lee JH, Son SM, Lee IH. Biological Activities of Synthetic Analogs of Halocidin, an Antimicrobial Peptide from the Tunicate Halocynthia aurantium. DRAMP04554 VDKPPYLPRPPPPRRIYNNR 20 Oncopeltus antibacterial peptide 4 No entry found Not found Not found Oncopeltus fasciatus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11812116 J Invertebr Pathol. 2001 Oct;78(3):135-140. Schneider M, Dorn A. Differential infectivity of two Pseudomonas species and the immune response in the milkweed bug, Oncopeltus fasciatus (Insecta: Hemiptera). DRAMP04555 VGKTWIKVIRGIGKSKIKWQ 20 Bactrocerin-1 No entry found Not found Not found Bactrocera dorsalis Antimicrobial Not found Not found Not found Function: Shows a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19479741 Arch Insect Biochem Physiol. 2009 Jul;71(3):117-129. Dang XL, Tian JH, Yang WY, Wang WX, Ishibashi J, Asaoka A, Yi HY, Li YF, Cao Y, Yamakawa M, Wen SY. Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel. DRAMP04556 GWANTLKNVAGGLCKITGAA 20 Parkerin No entry found Not found Not found Nanorana parkeri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20153801 Biochimie. 2010 May;92(5):475-481. Lu Z, Zhai L, Wang H, Che Q, Wang D, Feng F, Zhao Z, Yu H. Novel families of antimicrobial peptides with multiple functions from skin of Xizang plateau frog, Nanorana parkeri. DRAMP04557 GKLNLFLSRLEILKLFVGAL 20 Pelteobagrin No entry found Not found Not found Pelteobagrus fulvidraco (Yellow catfish) Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21073979 Comp Biochem Physiol B Biochem Mol Biol. 2011 Feb;158(2):149-154. Su Y. Isolation and identification of pelteobagrin, a novel antimicrobial peptide from the skin mucus of Yellow catfish (Pelteobagrus fulvidraco). DRAMP04558 GLRKRLRKFRNKIKEKLKKI 20 C18 No entry found Not found Not found Oryctolagus cuniculus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8313956 FEBS Lett. 1994 Feb 14;339(1-2):108-112. Tossi A, Scocchi M, Skerlavaj B, Gennaro R. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit Leukocytes. DRAMP04559 GLRKALRKFRNKIKEALKKI 20 C18AA No entry found Not found Not found Oryctolagus cuniculus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8313956 FEBS Lett. 1994 Feb 14;339(1-2):108-112. Tossi A, Scocchi M, Skerlavaj B, Gennaro R. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit Leukocytes. DRAMP04560 HVDKKVADKVLLLKQLRIMRL 21 Spingerin C-4 No entry found Not found Not found Pseudacanthotermes spiniger Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11053427 J Biol Chem. 2001 Feb 9;276(6):4085-4092. Lamberty M, Zachary D, Lanot R, Bordereau C, Robert A, Hoffmann JA, Bulet P. Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect. DRAMP04561 ALRSAVRTVARVGRAVLPHVAI 22 Ci-PAP-A2 No entry found Not found Not found Ciona intestinalis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17658598 Dev Comp Immunol. 2008;32(3):286-298. Fedders H, Leippe M. A reverse search for antimicrobial peptides in Ciona intestinalis: identification of a gene family expressed in hemocytes and evaluation of activity. DRAMP04562 WRSLGRTLLRLSHALKPLARRSGW 24 Ci-MAM-A24 No entry found Not found Not found Ciona intestinalis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18598239 Biochem J. 2008 Nov 15;416(1):65-75. Fedders H, Michalek M, Grötzinger J, Leippe M. An exceptional salt-tolerant antimicrobial peptide derived from a novel gene family of haemocytes of the marine invertebrate Ciona intestinalis. DRAMP04563 RSQMQDGQLQSCCQELQNVEEQCQC 25 2S albumin large chain 25 No entry found Not found Not found Taraxacum officinale Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19594427 Protein Pept Lett. 2010 Apr;17(4):522-529. Odintsova TI, Rogozhin EA, Sklyar IV, Musolyamov AK, Kudryavtsev AM, Pukhalsky VA, Smirnov AN, Grishin EV, Egorov TA. Antifungal activity of storage 2S albumins from seeds of the invasive weed dandelion Taraxacum officinale Wigg. DRAMP04564 FIFHIIKGLFHAGKMIHGLVTRRRH 25 Epinecidin-1 (Epi-1; fish, animals) No entry found Not found Not found Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus) Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17570764 DNA Cell Biol. 2007 Jun;26(6):403-413. Pan CY, Chen JY, Cheng YS, Chen CY, Ni IH, Sheen JF, Pan YL, Kuo CM. Gene expression and localization of the epinecidin-1 antimicrobial peptide in the grouper (Epinephelus coioides), and its role in protecting fish against pathogenic infection. DRAMP04565 GVVDILKGAAKDLAGHLATKVMNKL 25 Laticeptin No entry found Not found Not found Leptodatylus laticeps Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16712520 Protein Pept Lett. 2006;13(4):411-415. Conlon JM, Al-Ghaferi N, Abraham B, Sonnevend A, King JD, Nielsen PF. Purification and properties of laticeptin, an antimicrobial peptide from skin secretions of the South American frog Leptodactylus laticeps. DRAMP04566 GKQYFPKVGGRLSGKAPLAAKTHRRLKP 28 Kenojeinin I No entry found Not found Not found Raja kenojei Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15752571 Peptides. 2005 Apr;26(4):581-587. Cho SH, Lee BD, An H, Eun JB. Kenojeinin I, antimicrobial peptide isolated from the skin of the fermented skate, Raja kenojei. DRAMP04567 GWFKKTFHKVSHAVKSGIHAGQRGCSALGF 30 Centrocin 1 No entry found Not found Not found Strongylocentrotus droebachiensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20438753 Dev Comp Immunol. 2010 Sep;34(9):959-968. Li C, Haug T, Moe MK, Styrvold OB, Stensvåg K. Centrocins: Isolation and characterization of novel dimeric antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. DRAMP04568 SWFSRTVHNVGNAVRKGIHAGQGVCSGLGL 30 Centrocin 2 No entry found Not found Not found Strongylocentrotus droebachiensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20438753 Dev Comp Immunol. 2010 Sep;34(9):959-968. Li C, Haug T, Moe MK, Styrvold OB, Stensvåg K. Centrocins: Isolation and characterization of novel dimeric antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. DRAMP04569 KPWRFRRAIRRVRWRKVAPYIPFVVKTVGKK 31 Arminin-1a No entry found Not found Not found Hydra magnipapillata Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19770277 Antimicrob Agents Chemother. 2009 Dec;53(12):5245-5250. Augustin R, Anton-Erxleben F, Jungnickel S, Hemmrich G, Spudy B, Podschun R, Bosch TC. Activity of the novel peptide arminin against multiresistant human pathogens shows the considerable potential of phylogenetically ancient organisms as drug sources. DRAMP04570 WNSNRRFRVGRPPVVGRPGCVCFRAPCPCSNY 32 Callinectin No entry found Not found Not found Callinectes sapidus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21115038 Dev Comp Immunol. 2011 Apr;35(4):409-415. Noga EJ, Stone KL, Wood A, Gordon WL, Robinette D. Primary structure and cellular localization of callinectin; an antimicrobial peptide from the blue crab. DRAMP04571 IIKVPLKKFKSMREVMRDHGIKAPVVDPATKY 32 bullfrog pepsinogen C-derived antimicrobial peptide (bPcAP) No entry found Not found Not found Rana catesbeiana Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9639668 Biochim Biophys Acta. 1998 Jul 1;1407(1):31-39. Minn I, Kim HS, Kim SC. Antimicrobial peptides derived from pepsinogens in the stomach of the bullfrog, Rana catesbeiana. DRAMP04572 GVVKVSRLKGESLRARL 17 bullfrog pepsinogen A-derived antimicrobial peptide (bPaAP) No entry found Not found Not found Rana catesbeiana Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9639668 Biochim Biophys Acta. 1998 Jul 1;1407(1):31-39. Minn I, Kim HS, Kim SC. Antimicrobial peptides derived from pepsinogens in the stomach of the bullfrog, Rana catesbeiana. DRAMP04573 CIAKGNGCQPSGVQGNCCSGHCHKEPGWVAGYCK 34 Psacotheasin No entry found Not found Not found Psacothea hilaris Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20467242 J Microbiol Biotechnol. 2010 Apr;20(4):708-711. Hwang JS, Lee J, Hwang B, Nam SH, Yun EY, Kim SR, Lee DG. Isolation and Characterization of Psacotheasin, a Novel Knottin-Type Antimicrobial Peptide, from Psacothea hilaris. DRAMP04574 TTLTLHNLCPYPVWWLVTPNNGGFPIIDNTPVVLG 35 Dendrocin No entry found Not found Not found Dendrocalamus latiflorus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12893287 Biochem Biophys Res Commun. 2003 Aug 1;307(3):750-755. Wang HX, Ng TB. Dendrocin, a distinctive antifungal protein from bamboo shoots. DRAMP04575 LTCDILGSTPACAAHCIARGYRGGWCDGQSVCNCRR 36 Chironomus defensin No entry found Not found Not found Chironomus plumosus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9887520 Insect Biochem Mol Biol. 1998 Dec;28(12):1059-1066. Lauth X, Nesin A, Briand JP, Roussel JP, Hetru C. Isolation, characterization and chemical synthesis of a new insect defensin from Chironomus plumosus (Diptera). DRAMP04576 ILENLLARSTNEDREGSIFDTGPIRRPKPRPRPRPEG 37 Cg-Prp No entry found Not found Not found Crassostrea gigas Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18962895 Mol Immunol. 2009 Feb;46(4):516-522. Gueguen Y, Bernard R, Julie F, Paulina S, Delphine DG, Franck V, Philippe B, Evelyne B. Oyster hemocytes express a proline-rich peptide displaying synergistic antimicrobial activity with a defensin. DRAMP04577 RWKIFKKIEKVGRNVRDGIIKAGPAVAVVGQAATVVK 37 Papiliocin No entry found Not found Not found Papilio xuthus Antimicrobial Not found Not found Not found 2LA2 Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20213310 Mol Cells. 2010 Apr;29(4):419-423. Kim SR, Hong MY, Park SW, Choi KH, Yun EY, Goo TW, Kang SW, Suh HJ, Kim I, Hwang JS. Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus. DRAMP04578 KRFGRLAKSFLRMRILLPRRKILLAS 26 ECATH-1 No entry found Not found Not found Equus asinus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10471829 FEBS Lett. 1999 Sep 3;457(3):459-464. Scocchi M, Bontempo D, Boscolo S, Tomasinsig L, Giulotto E, Zanetti M. Novel cathelicidins in horse leukocytes(1). DRAMP04579 KRRHWFPLSFQEFLEQLRRFRDQLPFP 27 ECATH-2 No entry found Not found Not found Equus asinus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10471829 FEBS Lett. 1999 Sep 3;457(3):459-464. Scocchi M, Bontempo D, Boscolo S, Tomasinsig L, Giulotto E, Zanetti M. Novel cathelicidins in horse leukocytes(1). DRAMP04580 KRFHSVGSLIQRHQQMIRDKSEATRHGIRIITRPKLLLAS 40 ECATH-3 No entry found Not found Not found Equus asinus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10471829 FEBS Lett. 1999 Sep 3;457(3):459-464. Scocchi M, Bontempo D, Boscolo S, Tomasinsig L, Giulotto E, Zanetti M. Novel cathelicidins in horse leukocytes(1). DRAMP04581 TYMPVEEGEYIVNISYADQPKKNSPFTAKKQPGPKVDLSGVKAYGPG 47 Ap No entry found Not found Not found Argopecten purpuratus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19481126 Peptides. 2009 Aug;30(8):1405-1411. Arenas G, Guzmán F, Cárdenas C, Mercado L, Marshall SH. A novel antifungal peptide designed from the primary structure of a natural antimicrobial peptide purified from Argopecten purpuratus hemocytes. DRAMP04582 IFGSIYHRKCVVKNRCETVSGHKTCKDLTCCRAVIFRHERPEVCRPQT 48 Strongylocin 1 (Cys-rich; sea urchin, Echinoidea, animals) No entry found Not found Not found Strongylocentrotus droebachiensis Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18656496 Dev Comp Immunol. 2008;32(12):1430-1440. Li C, Haug T, Styrvold OB, Jørgensen TØ, Stensvåg K. Strongylocins, novel antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. DRAMP04583 WNPFKKIANRNCYPKTTCETAGGKKTCKDFSCCQIVLFGKKTRAKCTVVTS 51 Strongylocin 2 (Cys-rich; sea urchin, Echinoidea, animals) No entry found Not found Not found Strongylocentrotus droebachiensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18656496 Dev Comp Immunol. 2008;32(12):1430-1440. Li C, Haug T, Styrvold OB, Jørgensen TØ, Stensvåg K. Strongylocins, novel antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. DRAMP04584 IFNSIYHRKCVVKNRCETVSGHKTCKDLTCCRAVIFRHERPEVCRPST 48 SpStrongylocin 1 (S. purpuratus Strongylocin, sea urchin, Echinoidea, animals) No entry found Not found Not found Strongylocentrotus purpuratus Antimicrobial, Antibacterial, Antifungal, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19852980 Dev Comp Immunol. 2010 Mar;34(3):286-292. Li C, Blencke HM, Smith LC, Karp MT, Stensvåg K. Two recombinant peptides, SpStrongylocins 1 and 2, from Strongylocentrotus purpuratus, show antimicrobial activity against Gram-positive and Gram-negative bacteria. DRAMP04585 WNPFRKLYRKECNDVTSCDTVSGVKTCTKKNCCHRKFFGKTILKAPECTVIS 52 SpStrongylocin 2 (S. purpuratus Strongylocin; sea urchin, Echinoidea, animals) No entry found Not found Not found Strongylocentrotus purpuratus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19852980 Dev Comp Immunol. 2010 Mar;34(3):286-292. Li C, Blencke HM, Smith LC, Karp MT, Stensvåg K. Two recombinant peptides, SpStrongylocins 1 and 2, from Strongylocentrotus purpuratus, show antimicrobial activity against Gram-positive and Gram-negative bacteria. DRAMP04586 GIWSSIKNLASKAWNSDIGQSLRNKAAGAINKFVADKIGVTPSQAASMTLDEIVDAMYYD 60 Vejovine F1AWB0 Not found Not found Vaejovis mexicanus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20969885 Toxicon. 2011 Jan;57(1):84-92. Hernández-Aponte CA, Silva-Sanchez J, Quintero-Hernández V, Rodríguez-Romero A, Balderas C, Possani LD, Gurrola GB. Vejovine, a new antibiotic from the scorpion venom of Vaejovis mexicanus. DRAMP04587 RMRRSKSGKGSGGSKGSGSKGSKGSKGSGSKGSGSKGGSRPGGGSSIAGGGSKGKGGTQTA 61 aCATH No entry found Not found Not found Plecoglossus altivelis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21397030 Fish Shellfish Immunol. 2011 Jul;31(1):52-57. Lu XJ, Chen J, Huang ZA, Shi YH, Lv JN. Identification and characterization of a novel cathelicidin from ayu, Plecoglossus altivelis. DRAMP04588 RICSRDKNCVSRPGVGSIIGRPGGGSLIGRPGGGSVIGRPGGGSPPGGGSFNDEFIRDHSDGNRFA 66 rtCATH 1 No entry found Not found rtCATH_1 Oncorhynchus mykiss (rainbow trout) Antimicrobial Predicted Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16041021 Infect Immun. 2005 Aug;73(8):5053-5064. Chang CI, Pleguezuelos O, Zhang YA, Zou J, Secombes CJ. Identification of a novel cathelicidin gene in the rainbow trout, Oncorhynchus mykiss. DRAMP04589 SRSGRGSGKGGRGGSRGSSGSRGSKGPSGSRGSSGSRGSKGSRGGRSGRGSTIAGNGNRNNGGTRTA 67 Cod cathelicidin No entry found Not found Not found Gadus morhua Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20950641 Dev Comp Immunol. 2011 Mar;35(3):296-303. Broekman DC, Frei DM, Gylfason GA, Steinarsson A, Jörnvall H, Agerberth B, Gudmundsson GH, Maier VH. Cod cathelicidin: Isolation of the mature peptide, cleavage site characterisation and developmental expression. DRAMP04590 ERILDLRKTKKSCKNGEVLGCVSGHGPPGCSENECGMGPRPKACFFDCHYGCWCTGKLYRRKRDRKCVPKHECLL 75 Rhamp No entry found Not found Not found Rhipicephalus haemaphysaloides Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21168461 Peptides. 2011 Mar;32(3):441-446. Zhang H, Zhang W, Wang X, Zhou Y, Wang N, Zhou J. Identification of a cysteine-rich antimicrobial peptide from salivary glands of the tick Rhipicephalus haemaphysaloides. DRAMP04591 SKCKCSRKGPKIRYSDVKKLEMKPKYPHCEEKMVIITTKSVSRYRGQEHCLHPKLQSTKRFIKWYNAWNEKRRVYEE 77 CXCL14 No entry found Not found Not found Homo sapiens Antimicrobial Not found Not found Not found 2HDL Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19109182 J Immunol. 2009 Jan 1;182(1):507-514. Maerki C, Meuter S, Liebi M, Mühlemann K, Frederick MJ, Yawalkar N, Moser B, Wolf M. Potent and broad-spectrum antimicrobial activity of CXCL14 suggests an immediate role in skin infections. DRAMP04592 SSFSPPRGPPGWGPPCVQQPCPKCPYDDYKCPTCDKFPECEECPHISIGCECGYFSCECPKPVCEPCESPIAELIKKGGYKG 82 Ls-Stylicin 1 No entry found Not found Not found Litopenaeus stylirostris Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20061030 Mol Immunol. 2010 Mar;47(6):1269-1277. Rolland JL, Abdelouahab M, Dupont J, Lefevre F, Bachère E, Romestand B. Stylicins, a new family of antimicrobial peptides from the Pacific blue shrimp Litopenaeus stylirostris. DRAMP04593 RVPPYLGRDCKHWCRDNNQALYCCGPPGITYPPFIRKHPGKCPSVRSTCTGVRSSRPKFCPHDDACEFRSKCCYDACVKHHVCKTVEFY 89 CrusSp No entry found Not found Not found Scylla paramamosain Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18425600 Mol Biol Rep. 2009 May;36(5):841-850. Imjongjirak C, Amparyup P, Tassanakajon A, Sittipraneed S. Molecular cloning and characterization of crustin from mud crab Scylla paramamosain. DRAMP04594 NLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHV 80 TCP No entry found Not found Not found Homo sapiens Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20421939 PLoS Pathog. 2010 Apr 22;6(4):e1000857. Papareddy P, Rydengård V, Pasupuleti M, Walse B, Mörgelin M, Chalupka A, Malmsten M, Schmidtchen A. Proteolysis of human thrombin generates novel host defense peptides. DRAMP04595 SPRPDDKKNQGSASVDVQNERGEGTKVDARVRQELWRSDDGRTRAQAYGHWDRTYGGRNHGERSYGGGMRIEHTWGN 77 Prolixicin No entry found Not found Not found Rhodnius prolixus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21906194 Insect Mol Biol. 2011 Dec;20(6):775-786. Ursic-Bedoya R, Buchhop J, Joy JB, Durvasula R, Lowenberger C. Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi. DRAMP04596 FPVTWRWWKWWKG 13 PuroA No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2012 Sep;56(2):171-180. Ramalingam A, Palombo EA, Bhave M. The Pinb-2 genes in wheat comprise a multigene family with great sequence diversity and important variants. DRAMP04597 FPVTWPTKWWKG 12 PuroB No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2012 Sep;56(2):171-180. Ramalingam A, Palombo EA, Bhave M. The Pinb-2 genes in wheat comprise a multigene family with great sequence diversity and important variants. DRAMP04598 FSIARLLKWWKG 12 Pinb-2v1 No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2012 Sep;56(2):171-180. Ramalingam A, Palombo EA, Bhave M. The Pinb-2 genes in wheat comprise a multigene family with great sequence diversity and important variants. DRAMP04599 FPISTLLKWWKG 12 Pinb-2v3 No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2012 Sep;56(2):171-180. Ramalingam A, Palombo EA, Bhave M. The Pinb-2 genes in wheat comprise a multigene family with great sequence diversity and important variants. DRAMP04600 FPVTWPTKWWKS 12 Pinb-B No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04601 FPVTWPTKWRKG 12 Pinb-D No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04602 FPVTWPTKWLKG 12 Pinb-Q No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04603 FSVTWRWWKWWKG 13 Pina-M No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04604 FPVTWGWWKWWKG 13 Pina-R39 G No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04605 FPVTFRFFKFFKG 13 Pina-W No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04606 FPVTWRWWTWWKG 13 Hina No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04607 MPLSWFFPRTWGKR 14 GSP-5D No entry found Not found Not found Triticum aestivum Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Journal of Cereal Science. 2011 Jan;53(1):112-117. Phillipsa RL, Palomboa EA, Panozzob JF, Bhave M. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. DRAMP04608 AINXDAAYL 9 BCP61 No entry found Not found Not found Bacillus sp. CS61 Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22578764 Int J Antimicrob Agents. 2012 Jul;40(1):80-83. Choi YH, Cho SS, Simkhada JR, Yoo JC. A novel thermotolerant and acidotolerant peptide produced by a Bacillus strain newly isolated from a fermented food (kimchi) shows activity against multidrug-resistant bacteria. DRAMP04609 GPIRRPKPRPRPRPE 15 Cg-lgPrp No entry found Not found Not found Crassostrea gigas Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22327168 Dev Comp Immunol. 2012 Jul;37(3-4):363-370. Schmitt P, de Lorgeril J, Gueguen Y, Destoumieux-Garzón D, Bachère E. Expression, tissue localization and synergy of antimicrobial peptides and proteins in the immune response of the oyster Crassostrea gigas. DRAMP04610 GPIRRPKPRPRQRPE 15 Cg-lgPrp P/Q No entry found Not found Not found Crassostrea gigas Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22327168 Dev Comp Immunol. 2012 Jul;37(3-4):363-370. Schmitt P, de Lorgeril J, Gueguen Y, Destoumieux-Garzón D, Bachère E. Expression, tissue localization and synergy of antimicrobial peptides and proteins in the immune response of the oyster Crassostrea gigas. DRAMP04611 GFGCPRDQYKCNSHCQSIGCRAGYCDAVTLWLRCTCTDCNGKK 43 Cg-Defh1 No entry found Not found Not found Crassostrea gigas Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22327168 Dev Comp Immunol. 2012 Jul;37(3-4):363-370. Schmitt P, de Lorgeril J, Gueguen Y, Destoumieux-Garzón D, Bachère E. Expression, tissue localization and synergy of antimicrobial peptides and proteins in the immune response of the oyster Crassostrea gigas. DRAMP04612 GFGCPGDQYECNRHCRSIGCRAGYCDAVTLWLRCTCTGCSGKK 43 Cg-Defh2 No entry found Not found Not found Crassostrea gigas Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22327168 Dev Comp Immunol. 2012 Jul;37(3-4):363-370. Schmitt P, de Lorgeril J, Gueguen Y, Destoumieux-Garzón D, Bachère E. Expression, tissue localization and synergy of antimicrobial peptides and proteins in the immune response of the oyster Crassostrea gigas. DRAMP04613 IGCWTKSIPPRPCFVK 16 HV-BBI(3-18) (X) No entry found Not found Not found Odorrana grahami Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22516177 Peptides. 2012 Jun;35(2):276-284. Dębowski D, Łukajtis R, Łęgowska A, Karna N, Pikuła M, Wysocka M, Maliszewska I, Sieńczyk M, Lesner A, Rolka K. Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin. DRAMP04614 AVNIPFKVHFRCKSIFC 17 [Ser14,Ile15]OGTI (II) No entry found Not found Not found Odorrana grahami Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22516177 Peptides. 2012 Jun;35(2):276-284. Dębowski D, Łukajtis R, Łęgowska A, Karna N, Pikuła M, Wysocka M, Maliszewska I, Sieńczyk M, Lesner A, Rolka K. Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin. DRAMP04615 SVIGCWTKSIPPRPRCFVK 19 HV-BBI (IX) No entry found Not found Not found Odorrana grahami Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22516177 Peptides. 2012 Jun;35(2):276-284. Dębowski D, Łukajtis R, Łęgowska A, Karna N, Pikuła M, Wysocka M, Maliszewska I, Sieńczyk M, Lesner A, Rolka K. Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin. DRAMP04616 GSAQPYKQLHKVVNWDPYG 19 Cancrin No entry found Not found Not found Fejervarya cancrivora Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17707909 Mol Immunol. 2008 Feb;45(3):678-681. Lu Y, Ma Y, Wang X, Liang J, Zhang C, Zhang K, Lin G, Lai R. The first antimicrobial peptide from sea amphibian. DRAMP04617 SFKKFWGGVKAIFKGARKGWK 21 Hfp1 No entry found Not found Not found Gasterosteus aculeatus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP04618 FFKKFWGGVKAIFKGARKGWK 21 Hfp2 No entry found Not found Not found Gasterosteus aculeatus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP04619 SVKKFWGGVKAIFKGARKGLK 21 Hfp3 No entry found Not found Not found Gasterosteus aculeatus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP04620 FVKKFWGGVKAIFKGARKGLK 21 Hfp4 No entry found Not found Not found Gasterosteus aculeatus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22188679 FEBS J. 2012 Mar;279(5):724-736. Tessera V, Guida F, Juretić D, Tossi A. Identification of antimicrobial peptides from teleosts and anurans in expressed sequence tag databases using conserved signal sequences. DRAMP04621 FALGAVTKLLPSLLCMITRKC 21 Hainanenin-1 No entry found Not found Not found Amolops hainanensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306820 Peptides. 2012 Feb;33(2):251-257. Zhang S, Guo H, Shi F, Wang H, Li L, Jiao X, Wang Y, Yu H. Hainanenins: a novel family of�antimicrobial�peptides with strong activity from Hainan cascade-frog, Amolops hainanensis. DRAMP04622 FALGAVTKRLPSLFCLITRKC 21 Hainanenin-5 No entry found Not found Not found Amolops hainanensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22306820 Peptides. 2012 Feb;33(2):251-257. Zhang S, Guo H, Shi F, Wang H, Li L, Jiao X, Wang Y, Yu H. Hainanenins: a novel family of�antimicrobial�peptides with strong activity from Hainan cascade-frog, Amolops hainanensis. DRAMP04623 GFGSLGKALRLGANVL 16 X. clivii-C1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04624 GVGKFLHSAKKFGQALVSEIMKS 23 X. clivii-C2 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04625 GFKQFVHSMGKFGKAFVGEIINPK 24 X. borealis-B1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04626 GIGKFLHSAGKFGKAFLGEVMKS 23 X. borealis-B2 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04627 GLGSLLGSLFKFIPKLLPSIQQ 22 X. borealis-B3 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04628 GLLTNVLGFLKKAGKGVLSGLLPL 24 X. borealis-B4 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04629 GIKEFAHSLGKFGKAFVGGILNQ 23 X. amieti-AM1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04630 GLGSVLGKILKMGANLLGGAPKGA 24 X. amieti-AM3 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04631 GLGSLVGNALRIGAKLL 17 X. amieti-AM4 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04632 GWASKIGQALGKVAKVGLQQFIQPK 25 XPF-C1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04633 GFGSLLGKALRLGANVL 17 CPF-C1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04634 GLGSLLGKALKFGLKAAGKFMGGEPQQ 27 CPF-C2 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04635 GLASFLGKALKAGLKIGAHLLGGAPQQ 27 X. laevis 1 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04636 GFASFLGKALKAALKIGANMLGGTPQQ 27 X. laevis 2 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04637 GFGSFLGKALKAALKIGANALGGSPQQ 27 X. laevis 3 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04638 GLASLLGKALKAGLKIGTHFLGGAPQQ 27 X. laevis 4 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21199684 Comp Biochem Physiol C Toxicol Pharmacol. 2011 Apr;153(3):350-354. Conlon JM, Mechkarska M, Ahmed E, Leprince J, Vaudry H, King JD, Takada K. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). DRAMP04639 GVSKILHSAGKFGKAFLGEIMKS 23 Magainin-AN2 No entry found Not found Not found Xenopus clivii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP04641 GWASKIGQTLGKMAKVGLQELIQPK 25 XPF-AN1 No entry found Not found Not found Xenopus andrei Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21498136 Comp Biochem Physiol Part D Genomics Proteomics. 2011 Jun;6(2):206-212. Mechkarska M, Eman A, Coquet L, Jérôme L, Jouenne T, Vaudry H, King JD, Takada K, Conlon JM. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. DRAMP04642 GIGKFLHSAGKFGKAFIGEIMKS 23 Magainin-M1 No entry found Not found Not found Xenopus muelleri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21664395 Peptides. 2011 Jul;32(7):1502-1508. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. DRAMP04643 GLGSLLGKAFKFGLKTVGKMMAGAPREQ 28 CPF-M1 No entry found Not found Not found Xenopus muelleri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21664395 Peptides. 2011 Jul;32(7):1502-1508. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. DRAMP04644 GMASKAGSVLGKITKIALGAL 21 PGLa-MW1 No entry found Not found Not found Xenopus muelleri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21664395 Peptides. 2011 Jul;32(7):1502-1508. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. DRAMP04645 GLGSLLGKAFKFGLKTVGKMMGGAPREQ 28 CPF-MW1 No entry found Not found Not found Xenopus muelleri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21664395 Peptides. 2011 Jul;32(7):1502-1508. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. DRAMP04646 GLGSLLGKAFKFGLKTVGKMMGGAPREE 28 CPF-MW2 No entry found Not found Not found Xenopus muelleri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21664395 Peptides. 2011 Jul;32(7):1502-1508. Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. DRAMP04647 GIGSLLAKAAKLGANLL 17 CPF-L1 No entry found Not found Not found Xenopus lenduensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04648 GIGSALAKAAKLVAGIV 17 CPF-L2 No entry found Not found Not found Xenopus lenduensis Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04649 GLASFLGKALKAGLKIGSHLLGGAPQQ 27 CPF-P2 No entry found Not found Not found Xenopus petersii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04650 GFGSFLGKALKAALKIGANVLGGAPQQ 27 CPF-P3 No entry found Not found Not found Xenopus petersii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04651 GFGSFLGKALKAALKIGANVLGGAPEQ 27 CPF-P4 No entry found Not found Not found Xenopus petersii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04652 GFGSFLGKALKAALKIGADVLGGAPQQ 27 CPF-P5 No entry found Not found Not found Xenopus petersii Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04653 GFGSLLGKALKIGTNLL 17 CPF-PG1 No entry found Not found Not found Xenopus pygmaeus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22123629 Peptides. 2012 Jan;33(1):35-43. King JD, Mechkarska M, Coquet L, Leprince J, Jouenne T, Vaudry H, Takada K, Conlon JM. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). DRAMP04654 IKLSPETKDNLKKVLKGAIKGAIAVAKMV 29 H-0, Hymenochirin-1B No entry found Unknown Not found Hymenochirus boettgeri (Congo dwarf clawed frog) Antimicrobial, Anticancer Experimental evidence at transcript level α-helical (most likely) No detailed structure description found. "Function: Antimicrobial, Anticancer, Immunomodulatory and Antidiabetic activity. As a cationic, amphipathic, α-helical, 29-residue,host defense peptide, Hymenochirin-1B is the predominant pharmacological active component of four hymenochirins, which showed a wide range of biological activities, such as antimicrobial, anticancer, immunomodulatory, and antidiabetic activities. Surprisingly, we don't find the entry introducing Hymenochirin-1B in UniProt (2021-3-29)." [Ref.30789695] Cancer cell lines: A549 (IC50 = 15.22 ± 0.21 μM), HCT116 (IC50 = 12.76 ± 0.43 μM), HepG2 (IC50 = 8.07 ± 0.21 μM) [Ref.30789695] It has 5%, 6.3%, 7.7%, 10%, 10.7%, 15.3%, 9%, 15% and 9.7% hemolysis against fresh rabbit blood cells at 0.010, 0.25, 0.5, 1.0, 2.0, 5.0, 10.0, 20.0, 25.0μM Linear Free Amidation L No cytotoxicity information found in the reference Not found 30789695 ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1. Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy DRAMP04655 LKIPGFVKDTLKKVAKGIFSAVAGAMTPS 29 Hymenochirin-2B No entry found Not found Not found Hymenochirus boettgeri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497805 Peptides. 2012 Jun;35(2):269-275. Mechkarska M, Prajeep M, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. The hymenochirins: A family of host-defense peptides from the Congo dwarf clawed frog Hymenochirus boettgeri (Pipidae). DRAMP04656 IKIPAVVKDTLKKVAKGVLSAVAGALTQ 28 Hymenochirin-3B No entry found Not found Not found Hymenochirus boettgeri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497805 Peptides. 2012 Jun;35(2):269-275. Mechkarska M, Prajeep M, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. The hymenochirins: A family of host-defense peptides from the Congo dwarf clawed frog Hymenochirus boettgeri (Pipidae). DRAMP04657 IKIPAFVKDTLKKVAKGVISAVAGALTQ 28 Hymenochirin-4B No entry found Not found Not found Hymenochirus boettgeri Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497805 Peptides. 2012 Jun;35(2):269-275. Mechkarska M, Prajeep M, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. The hymenochirins: A family of host-defense peptides from the Congo dwarf clawed frog Hymenochirus boettgeri (Pipidae). DRAMP04658 IKIPPIVKDTLKKVAKGVLSTIAGALST 28 Hymenochirin-5B No entry found Not found Not found Hymenochirus boettgeri(Congo dwarf clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antimicrobial activity against both Gram-positive, Gram-negative bacteria and fungi. Gram-positive bacterium: Staphylococcus aureus (MIC=80 μM);##Gram-negative bacteria: Escherichia coli (MIC=40 μM);##Fungi: Candida albicans (MIC=160 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22497805 Peptides. 2012 Jun;35(2):269-275. Mechkarska M, Prajeep M, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, Conlon JM. The hymenochirins: A family of host-defense peptides from the Congo dwarf clawed frog Hymenochirus boettgeri (Pipidae). DRAMP04659 FKRLKKLFKKIWNWK 15 HPA3NT3(Derived from HP (2–20)) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-gram+, Anti-gram-, Antifungal Not found Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli [Ref.19642077] Gram-positive bacteria : Staphylococcus aureus(MIC=4 μM), Bacillus subtilis(MIC=4 μM), Listeria monocytogenes(MIC=22 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Salmonella typhimurium(MIC=2 μM), Pseudomonas aeruginosa(MIC=2 μM);##Fungi : Candida albicans(MIC=8 μM), Trichosporon beigelli(MIC=2-4 μM) [Ref.19642077] 32% hemolysis at 50 μM , 46% hemolysis at 100 μM , 70% hemolysis at 200 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494##19642077 Biochim Biophys Acta. 2013 Feb;1828(2):443-454.##J Pept Sci. 2009 Sep;15(9):589-94. doi: 10.1002/psc.1155. Lee JK, Park SC, Hahm KS, Park Y.##Gopal R, Park SC, Ha KJ, Cho SJ, Kim SW, Song PI, Nah JW, Park Y, Hahm KS Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action.##Effect of Leucine and Lysine substitution on the antimicrobial activity and evaluation of the mechanism of the HPA3NT3 analog peptide. DRAMP04660 AKRLKKLFKKIWNWK 15 HPA3NT3-F1A (HPA3NT3 peptide analogs) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-gram+, Anti-gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.22982494] Gram-positive bacteria : Staphylococcus aureus(MIC=2 μM), Listeria monocytogenes(MIC=2 μM), Staphylococcus epidermidis(MIC=2-4 μM), Bacillus subtilis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Pseudomonas aeruginosa(MIC=1 μM), Primula vulgaris(MIC=4 μM), Salmonella typhimurium(MIC=1 μM);##Fungi : Candida albicans(MIC=8 μM), Trichosporon beigelii(MIC=16 μM), Aspergillus awamori(MIC=16 μM), Aspergillus flavus(MIC=16 μM), Aspergillus fumigatus(MIC=8 μM), Aspergillus parasiticus(MIC=8 μM) [Ref.22982494] 7.1% hemolysis at 250 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494 Biochim Biophys Acta. 2013 Feb;1828(2):443-454. doi: 10.1016/j.bbamem.2012.09.005 Lee JK, Park SC, Hahm KS, Park Y. Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action. DRAMP04661 FKRLKKLAKKIWNWK 15 HPA3NT3-F8A (HPA3NT3 peptide analogs) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-gram+, Anti-gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.22982494] Gram-positive bacteria : Staphylococcus aureus(MIC=4 μM), Listeria monocytogenes(MIC=2 μM), Staphylococcus epidermidis(MIC=2-4 μM), Bacillus subtilis(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Pseudomonas aeruginosa(MIC=2 μM), Primula vulgaris(MIC=4 μM), Salmonella typhimurium(MIC=2 μM);##Fungi : Candida albicans(MIC=8 μM), Trichosporon beigelii(MIC=16 μM), Aspergillus awamori(MIC=16 μM), Aspergillus flavus(MIC=16 μM), Aspergillus fumigatus(MIC=8 μM), Aspergillus parasiticus(MIC=8 μM) [Ref.22982494] 4.6% hemolysis at 250 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494 Biochim Biophys Acta. 2013 Feb;1828(2):443-454. doi: 10.1016/j.bbamem.2012.09.005 Lee JK, Park SC, Hahm KS, Park Y. Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action. DRAMP04662 AKRLKKLAKKIWNWK 15 HPA3NT3-F1AF8A (HPA3NT3 peptide analogs) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-gram+, Anti-gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.22982494] Gram-positive bacteria : Staphylococcus aureus(MIC=16 μM), Listeria monocytogenes(MIC=2 μM), Staphylococcus epidermidis(MIC=16 μM), Bacillus subtilis(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(MIC=32 μM), Pseudomonas aeruginosa(MIC=2 μM), Primula vulgaris(MIC=4 μM), Salmonella typhimurium(MIC=2 μM);##Fungi : Candida albicans(MIC=16 μM), Trichosporon beigelii(MIC=32 μM), Aspergillus awamori(MIC=16 μM), Aspergillus flavus(MIC=32 μM), Aspergillus fumigatus(MIC=4 μM), Aspergillus parasiticus(MIC=8 μM) [Ref.22982494] 0% hemolysis at 250 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494 Biochim Biophys Acta. 2013 Feb;1828(2):443-454. doi: 10.1016/j.bbamem.2012.09.005 Lee JK, Park SC, Hahm KS, Park Y. Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action. DRAMP04663 AKRLKKLAKKIWKWL 15 HPA3NT3-A1 (HPA3NT3 peptide analogs) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.22982494] Gram-positive bacteria : Staphylococcus aureus(MIC=16 μM), Listeria monocytogenes(MIC=16 μM), Staphylococcus epidermidis(MIC=8 μM), Bacillus subtilis(MIC=8 μM);##Gram-negative bacteria : Escherichia coli(MIC=32 μM), Pseudomonas aeruginosa(MIC=32 μM), Primula vulgaris(MIC=8-16 μM), Salmonella typhimurium(MIC=8 μM);##Fungi : Candida albicans(MIC=16 μM), Trichosporon beigelii(MIC>128 μM), Aspergillus awamori(MIC=64 μM), Aspergillus flavus(MIC=64 μM), Aspergillus fumigatus(MIC=16 μM), Aspergillus parasiticus(MIC=16 μM) [Ref.22982494] 20.9% hemolysis at 250 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494 Biochim Biophys Acta. 2013 Feb;1828(2):443-454. doi: 10.1016/j.bbamem.2012.09.005 Lee JK, Park SC, Hahm KS, Park Y. Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action. DRAMP04664 AKRLKKLAKKIWKWK 15 HPA3NT3-A2 (HPA3NT3 peptide analogs) No entry found Not found Not found Helicobacter pylori Antimicrobial, Antibacterial, Anti-gram+, Anti-gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli, Aspergillus awamori, Aspergillus flavus, Aspergillus fumigatus, Aspergillus parasiticus [Ref.22982494] Gram-positive bacteria : Staphylococcus aureus(MIC=4 μM), Listeria monocytogenes(MIC=2 μM), Staphylococcus epidermidis(MIC=2-4 μM), Bacillus subtilis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Pseudomonas aeruginosa(MIC=2 μM), Primula vulgaris(MIC=2-4 μM), Salmonella typhimurium(MIC=2 μM);##Fungi : Candida albicans(MIC=8 μM), Trichosporon beigelii(MIC=16 μM), Aspergillus awamori(MIC=8 μM), Aspergillus flavus(MIC=8 μM), Aspergillus fumigatus(MIC=4 μM), Aspergillus parasiticus(MIC=8 μM) [Ref.22982494] 0% hemolysis at 250 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22982494##32781586 Biochim Biophys Acta. 2013 Feb;1828(2):443-454. doi: 10.1016/j.bbamem.2012.09.005##Int J Mol Sci. 2020 Aug 6;21(16):5632. doi: 10.3390/ijms21165632 Lee JK, Park SC, Hahm KS, Park Y.##Lee JK, Park Y. Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action.##All d-Lysine Analogues of the Antimicrobial Peptide HPA3NT3-A2 Increased Serum Stability and without Drug Resistance. DRAMP04666 KKSLLAKAKNFGGKVITIFKA 21 LtTx-1a No entry found Not found Not found Lachesana tarabaevi Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23088912 Biochim Biophys Acta. 2013 Feb;1828(2):724-731. Kuzmenkov AI, Fedorova IM, Vassilevski AA, Grishin EV. Cysteine-rich toxins from Lachesana tarabaevi spider venom with amphiphilic C-terminal segments. DRAMP04667 GIGAILKVLSTGLPALISWIKRKRQQ 26 Melt No entry found Not found Not found Lachesana tarabaevi Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23088912 Biochim Biophys Acta. 2013 Feb;1828(2):724-731. Kuzmenkov AI, Fedorova IM, Vassilevski AA, Grishin EV. Cysteine-rich toxins from Lachesana tarabaevi spider venom with amphiphilic C-terminal segments. DRAMP04668 VTCDVLSFEAKGIAVNHSACALHCIALRKKGGSCQNGVCVCRN 43 Coprisin No entry found Not found Not found Copris tripartitus Antimicrobial Not found Not found Not found 2LN4 Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23137439 Biochim Biophys Acta. 2013 Feb;1828(2):271-283. Lee E, Kim JK, Shin S, Jeong KW, Shin A, Lee J, Lee DG, Hwang JS, Kim Y. Insight into the antimicrobial activities of coprisin isolated from the dung beetle, Copris tripartitus, revealed by structure?activity relationships. DRAMP04669 ARRRRSSSRPIRRRRPRRRTTRRRRGARRRR 31 Protamine y1 No entry found Not found Not found Thunnus thynnus Antimicrobial Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23122778 Biochim Biophys Acta. 2013 Mar;1828(3):1143-1152. Roberts JM, Graham LL, Quinn B, Pink DA. Modeling the surface of campylobacter fetus: Protein surface layer stability and resistance to cationic antimicrobial peptides. DRAMP18188 GILGKLWEGFKSIV 14 Pantinin-1 (Non-disulfide-bridged peptide 4.20, NDBP-4.20, Non-disulfide-bridged peptide 5.21, ND R4JNJ5 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an Not found Pandinus imperator (Emperor scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Homology Not found Not found Function: Amphipathic peptide that possesses relatively strong activities against Gram-positive bacteria and a fungus, but has very weak antimicrobial activities against Gram-negative bacteria. Also exhibits very low hemolytic activities against human erythrocytes.Forms an alpha-helical membrane channel in the prey. [Ref.23624072]Gram-positive bacteria: S.aureus (MIC=8 μM), B.magaterium (MIC=32 μM), M.luteus (MIC=32 μM ), VRE (MIC=28 μM), MRSA (MIC=14 μM);##Gram-negative bacteria: E.coli (MIC=62 μM), P.putida (MIC >87 μM), K.oxytoca (MIC >87 μM), E.cloacae (MIC=76 μM), S.enterica (MIC=72 μM);##Fungus: C.tropicalis (MIC=16 μM). [Ref.23624072]0% hemolytic activity at 16 μM, 0% hemolytic activity at 32 μM, 20% hemolytic activity at 64 μM against human red bood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 23624072##24184590 Peptides 45:28-34(2013)##Peptides 51:35-45(2014 Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,Cao B., Cao H.##Almaaytah A., Albalas Q. Three new antimicrobial peptides from the scorpion Pandinusimperator.##Scorpion venom peptides with no disulfide bridges: a review. DRAMP04673 PAAAAQAVAGLAPVAAEQ 18 Alamethicin (ALM; fungi) No entry found Not found Not found Trichoderma viride Antimicrobial, Antibacterial, Antifungal, Antiparasitic Not found Alpha helix The molecular conformation of the three crystallographically independent molecules is largely alpha-helical with a bend in the helix axis at an internal proline residue. The helix structure is highly amphipathic as most of the solvent-accessible polar atoms lie on a narrow strip of surface parallel to the helix axis.(Ref.2) 1AMT resolved by X-ray. Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Experientia, 1967; 23: 85-86.##Nature. 1982 Nov 25;300(5890):325-330. Meyer CE, Reusser F.##Fox RO Jr, Richards FM. Polypeptide anti-bacterial agent isolated from Trichoderma viride.##A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution. DRAMP04674 VYINKLTPPCGTMYYACEAV 20 Antiviral protein Y3 (Fungi) P83477 Not found Not found Pleurotus citrinopileatus (Golden oyster mushroom) Antimicrobial, Antiviral Protein level Not found Not found Miscellaneous: Has antiviral activity against Tobacco mosaic virus and antitumor activity against stomach cancer cells in vitro. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Chinese J Biochem Mol Biol 2008; 24(7):597-603. Wu LP, Wu ZJ, Lin D, Fang F, Lin QY, Xie LH. Characterization and amino acid sequence of y3, an antiviral protein from mushroom Coprinus comatus. DRAMP04675 ALSFLFLFLFVAQEIVVTEANTCEHLADTYRGVCFTDASCDDHCKNKAHLISGTCHNFKC 60 Antimicrobial defensin peptide DRR230-c Q8H6L2 Not found DRR230-c Pisum sativum (Garden pea) Antimicrobial, Antifungal Transcript level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##6292726 Plant Sci. 2002, 163:855-864. Lai FM, DeLong C, Mei K, Wignes T, Fobert PR. Analysis of the DRR230 family of pea defensins: gene expression pattern and evidence of broad host-range antifungal activity. DRAMP04678 DSECLKEYGGDVGFGFCAPRIYPSFCVQRCRADKGALSGKCIWGQGSNVKCLCNFCRHEP 60 Defensin-like protein 4 P80301 Belongs to the DEFL family (RTI/MTI-2 subfamily) Not found Brassica napus (Rape) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Inhibits trypsin and chymotrypsin. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8143882 FEBS Lett. 1994 Apr 4;342(2):221-224. Ceciliani F, Bortolotti F, Menegatti E, Ronchi S, Ascenzi P, Palmieri S. Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seed. DRAMP04681 VIAGGXAAIIG 11 Antiviral serine protease P86931 Not found Not found Eisenia foetida (Common brandling worm) (Common dung-worm) Antimicrobial, Antiviral Protein level Not found Not found Function: Serine protease which has antiviral activity against cucumber mosaic virus and tobacco mosaic virus. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18775500 Comp Biochem Physiol B Biochem Mol Biol. 2008 Dec;151(4):381-385. Ueda M, Noda K, Nakazawa M, Miyatake K, Ohki S, Sakaguchi M, Inouye K. A novel anti-plant viral protein from coelomic fluid of the earthworm Eisenia foetida: purification, characterization and its identification as a serine protease. DRAMP04682 QGRMYQRFLRQHVDPDETGGNDHYLNLSRRNIQCPNRHEGVRFNTDIHEDLTNRRPIDEHEGVVRVTDKTEEG 73 Lactogenin P59761 Belongs to the pancreatic ribonuclease family Not found Bos taurus (Bovine) Antimicrobial, Antiviral Protein level Not found Not found "Function: Secretory RNase specific towards pyrimidine bases, with higher activity towards poly C than poly U. Inhibits cell-free translation. Miscellaneous: Inhibits HIV-1 reverse transcriptase in vitro." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10486275 Biochem Biophys Res Commun. 1999 Sep 16;263(1):187-191. Ye XY, Cheng KJ, Ng TB. Isolation and characterization of angiogenin-1 and a novel protein designated lactogenin from bovine milk. DRAMP04683 SMIGGVMSKG 10 NADPH oxidoreductase P84517 Not found Not found Bombyx mori (Silk moth) Antimicrobial, Antiviral Protein level Not found Not found "Function: NADPH oxidoreductase. Has antiviral activity against BmNPV. Miscellaneous: Expressed at high levels in BmNPV-resistant strains. Expressed at lower levels in moderately resistant and susceptible strains. " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17213661 Biosci Biotechnol Biochem. 2007 Jan;71(1):200-205. Selot R, Kumar V, Shukla S, Chandrakuntal K, Brahmaraju M, Dandin SB, Laloraya M, Kumar PG. Identification of a soluble NADPH oxidoreductase (BmNOX) with antiviral activities in the gut juice of Bombyx mori. DRAMP04684 NKPEALVDYTGVXNS 15 Bacteriocin BAC-IB17 C0HJE5 Not found Not found Bacillus subtilis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Has bactericidal activity. Miscellaneous: On the 2D-gel the determined pI of this protein is: 7.0, its MW is: 10.7 kDa." Gram-positive bacteria: M. luteus, methicillin-resistant S. aureus, methicillin-sensitive S. aureus and B. stearothermophilus;##Gram- negative bacteria: E. coli, S. typhi. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (AUG-2013) to UniProtKB Ansari A, Siddiqui NN, Zohra RR, Aman A, Qader SA. Isolation, purification and characterization of bacteriocin (BAC-IB17) produced from Bacillus subtilis KIBGE-IB17. DRAMP04685 VAAGGWRPIESLNSAEVQDV 20 Cysteine proteinase inhibitor 1 (KCPI1; Phytocystatin; Plant defensin) P86472 "Belongs to the cystatin family (Phytocystatin subfamily )" Not found Actinidia chinensis (Kiwi) (Yangtao) Not found Protein level Not found Not found Function: Specific inhibitor of papain family cysteine proteinases (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE 14697268##15536427 Phytochemistry. 2004 Jan;65(1):19-30.##J Allergy Clin Immunol. 2004 Nov;114(5):1169-1175. Rassam M, Laing WA.##Bublin M, Mari A, Ebner C, Knulst A, Scheiner O, Hoffmann-Sommergruber K, Breiteneder H, Radauer C. Purification and characterization of phytocystatins from kiwifruit cortex and seeds.##IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries. DRAMP04686 LSAGPNGGSIAKLSVK 16 Disease resistance response protein (Plant defensin) P85900 Belongs to the BetVI family Not found Pseudotsuga menziesii (Douglas-fir) (Abies menziesii) Not found Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18602030 J Proteomics. 2008 Oct 7;71(4):425-438. Islam MA, Sturrock RN, Ekramoddoullah AK. A proteomics approach to identify proteins differentially expressed in Douglas-fir seedlings infected by Phellinus sulphurascens. DRAMP04687 GSNIEVMLGLPNSDVK 16 Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform (Plant defensin) P86080 Belongs to the glycosyl hydrolase 17 family Not found Capsicum annuum var. annuum (Red pepper) Antimicrobial, Antibacterial, Antifungal Protein level Not found Not found Function: Implicated in the defense of plants against pathogens (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (JUL-2008) to UniProtKB Belchi-Navarro S, Almagro L, Pedreno MA. No title found DRAMP04688 NIFNAISAAGLGNQIKVSTAIDTGVLGTSYPPSK 34 Glucan endo-1,3-beta-glucosidase P86102 Belongs to the glycosyl hydrolase 17 family Not found Vitis rotundifolia (Muscadine grape) Antimicrobial, Antifungal Protein level Not found Not found "Function: Is thought to be an important plant defense-related product against fungal pathogens. Miscellaneous: On the 2D-gel the determined pI of this protein is: 6, its MW is: 25 kDa." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19412582 Appl Biochem Biotechnol. 2010 Mar;160(3):932-944. Basha SM, Mazhar H, Vasanthaiah HK. Proteomics approach to identify unique xylem sap proteins in Pierce's disease-tolerant Vitis species. DRAMP04689 AFVLDADNLIPKKITFGEGSQYGYVKVEGDALSDTLEKIDYETKLVSAPSSSTIIKTTSKYHTKGDVEIKEEHVKAGKEKAAHLFKLIEGYLKDHPSEYN 100 Allergen Fra a 1 Q5ULZ4 Belongs to the BetVI family Not found Fragaria ananassa (Strawberry) Antimicrobial, Antifungal Protein level Not found Not found Function: May be involved in ripening of fruits. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15507096 Allergy. 2004 Dec;59(12):1277-1284. Karlsson AL, Alm R, Ekstrand B, Fjelkner-Modig S, Schiött A, Bengtsson U, Björk L, Hjernø K, Roepstorff P, Emanuelsson CS. Bet v 1 homologues in strawberry identified as IgE-binding proteins and presumptive allergens. DRAMP04690 MREETVVYEQEESVSHGGGKHRILAELARVEQEVAFLEKELKEVENTDIVSTVCEELLSVIEKGPDPLLPLTNGPLNLGWDRWFEGPNGGEGCRC 95 Guanine nucleotide-binding protein subunit gamma 1 (Ggamma-subunit 1;Heterotrimeric G protein gam Q9FDX9, Q9LY73 Not found GG1 Arabidopsis thaliana (Mouse-ear cress) Antimicrobial, Antifungal Protein level Not found Not found "Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Involved in the abscisic acid (ABA) and ethylene signaling pathways. Regulates acropetal transport of auxin (IAA) in roots and hypocotyls, and thus modulates root architecture (e.g. lateral root formation). The heterotrimeric G- protein controls defense responses to necrotrophic and vascular fungi probably by modulating cell wall-related genes expression; involved in resistance to fungal pathogens such as Alternaria brassicicola, Plectosphaerella cucumerina and Fusarium oxysporum. Tissue specificity: Mostly expressed in seedlings (especially at the hypocotyl/root junction), young cauline leaves, open flowers, and floral stems, and, to a lower extent, in roots (restricted to the stele), rosette leaves (restricted to veins), siliques, and unopened floral buds. Also present in hydathods. Developmental stage: In seedlings, first observed at the hypocotyl/root junction but later confined to the hypocotyl. In flowers, restricted to the stigm" Fungi: Alternaria brassicicola, Plectosphaerella cucumerina and Fusarium oxysporum. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21980142##17468261 Mol Plant. 2012 Jan;5(1):98-114.##Plant Cell. 2007 Apr;19(4):1235-1250. Delgado-Cerezo M, Sánchez-Rodríguez C, Escudero V, Miedes E, Fernández PV, Jordá L, Hernández-Blanco C, Sánchez-Vallet A, Bednarek P, Schulze-Lefert P, Somerville S, Estevez JM, Persson S, Molina A.##Trusov Y, Rookes JE, Tilbrook K, Chakravorty D, Mason MG, Anderson D, Chen JG, Jones AM, Botella JR. Arabidopsis heterotrimeric G-protein regulates cell wall defense and resistance to necrotrophic fungi.##Heterotrimeric G protein gamma subunits provide functional selectivity in Gbetagamma dimer signaling in Arabidopsis. DRAMP04691 GGSVPCGESCVFIPCITSLAGCSCKNKVCYYD 32 Parigidin-br1 B3EWF1 Belongs to the cyclotide family (Bracelet subfamily) Not found Palicourea rigida Toxin Protein level Not found Not found "Function: Probably participates in a plant defense mechanism. Reduces growth of and increases mortality in larvae of D.saccharalis. Kills cultured SF-9 cells of S.frugiperda probably by disrupting plasma membranes. Has hemolytic activity against human erythrocytes. Has no antibacterial activity against E.coli strain ATCC 8739 and S.aureus strain ATCC 25923. Tissue specificity: Expressed in leaves, flowers, peduncles and seeds (at protein level). PTM: This is a cyclic peptide." [Swiss_Prot Entry B3EWF1]No antibacterial activity against E.coli strain ATCC 8739 and S.aureus strain ATCC 25923 [Ref.22074926] It has 28% and 41% hemolysis at 20 μM and 40 μM against human red blood cells. Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys6 and Cys22,Cys10 and Cys24,Cys15 and Cys29. L [Ref.22074926] It exhibited cytotoxic effects on SF-9 cells with CC50 values to be 1.7 μm at 24 h, 10.3 μm at 48 h and 73.1 μm at 72 h. Not found 22074926 J Biol Chem. 2012 Jan 2;287(1):134-147. Pinto MF, Fensterseifer IC, Migliolo L, Sousa DA, de Capdville G, Arboleda-Valencia JW, Colgrave ML, Craik DJ, Magalhães BS, Dias SC, Franco OL. Identification and structural characterization of novel cyclotide with activity against an insect pest of sugar cane. DRAMP04692 GVFTHESQETSVIAPARLFKALFLDSDNLIQKVLPQAIKSTEIIEGNGGP 50 Major pollen allergen Que a 1 (Que a 1; Plant defensin) P85126 Belongs to the BetVI family Not found Quercus alba (White oak) Not found Protein level Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet IgE PubMed ID is not available Allergy, 2008,146:203-211. Moverare R., Everberg H., Carlsson R., Holtz A., Thunberg R., Olsson P., Brostedt P., Hoegbom E. Purification and characterization of the major oak pollen allergenQue a 1 for use in component resolved diagnostics using ImmunoCAP. DRAMP04693 GSPRTEYEACRVRCQVAEHGVERQRRCQQVCEKRLREREGRRE 43 Luffin P1c (one chain of ribosome-inactivating protein luffin P1; Plant defensin) P56568, Q8GRS9 Not found Not found Luffa aegyptiaca (Sponge gourd) (Luffa cylindrica) Antimicrobial, Antiviral, Toxin Protein level Alpha helix Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds.(Ref.2) 2L37 resolved by NMR. Function: Inhibits protein synthesis in animal cells. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys10 and Cys31,Cys14 and Cys27. L [Ref.21195767] It exhibited ytotoxicity against uninfected C8166 cell line (IC50=235 μM). EC50 of the inhibition of syncytia formation and p24 antigen production were 50 μM (262 μg/ml) and 58 μM (306 μg/ml). Not found 9214759##21195767 Biosci Biotechnol Biochem. 1997 Jun;61(6):984-988.##J Struct Biol. 2011 Apr;174(1):164-172. Kimura M, Park SS, Sakai R, Yamasaki N, Funatsu G.##Ng YM, Yang Y, Sze KH, Zhang X, Zheng YT, Shaw PC. Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the seeds of sponge gourd (Luffa cylindrica).##Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica). DRAMP04694 VIIYELNLQGTTKAQYSTILKQLRDDIKDPNLXYGXXDYS 40 Ribosome-inactivating protein saporin-1 (SAP-1; SO-4; rRNA N-glycosidase; Plant defense) P98185 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) SAP1 Saponaria officinalis (Common soapwort) (Lychnis saponaria) Toxin Protein level Not found Not found Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2753596 Int J Pept Protein Res. 1989 Apr;33(4):263-267. Montecucchi PC, Lazzarini AM, Barbieri L, Stirpe F, Soria M, Lappi D. N-terminal sequence of some ribosome-inactivating proteins. DRAMP04695 ANIVFDVESATTGTYSTFLTSF 22 Dioicin-1 (Ribosome-inactivating protein; rRNA N-glycosidase; Plant defense) P86144 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Phytolacca dioica (Bella sombra tree) (Phytolacca arborea) Toxin Protein level Not found Not found Function: Nicks pBR322 dsDNA. Has adenine polynucleotide glycosidase activity on herring sperm ssDNA. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18704492 Planta. 2008 Nov;228(6):963-975. Parente A, Conforto B, Di Maro A, Chambery A, De Luca P, Bolognesi A, Iriti M, Faoro F. Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization. DRAMP04696 DVTFSLLGANTKSYAAFITNFRKDVASEKK 30 Ribosome-inactivating protein momorcochin-S (rRNA N-glycosidase; Plant defense) P20655 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Momordica cochinchinensis (Spiny bitter cucumber) Toxin Protein level Not found Not found "Function: Inactivates eukaryotic 60S ribosomal subunits. PTM: Glycosylated." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2597699 Biochim Biophys Acta. 1989 Dec 8;993(2-3):287-292. Bolognesi A, Barbieri L, Carnicelli D, Abbondanza A, Cenini P, Falasca AI, Dinota A, Stirpe F. Purification and properties of a new ribosome-inactivating protein with RNA N-glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis. DRAMP04697 DVTFSMLGANGATYYQFF 18 Ribosome-inactivating protein momorgrosvin (rRNA N-glycosidase; Plant defense) P83323 Belongs to the ribosome-inactivating protein family (Type 1 RIP subfamily) Not found Siraitia grosvenorii (Monk's fruit) (Luo han guo) Toxin Protein level Not found Not found "Function: Inhibits protein synthesis in the rabbit reticulocyte lysate system. Catalytic activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. PTM: Glycosylated." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11205869 Life Sci. 2001 Jan 5;68(7):773-784. Tsang KY, Ng TB. Isolation and characterization of a new ribosome inactivating protein, momorgrosvin, from seeds of the monk's fruit Momordica grosvenorii. DRAMP04698 FLKGIIDTVSNWL 13 Amphipathic peptide CT1 (VsCT1; Non-disulfide-bridged peptide 5.11, NDBP-5.11) I0DEB5 Belongs to the scorpion NDBP 5 family Not found Vaejovis subcristatus (Scorpion) (Thorellius subcristatus) Antimicrobial Transcript level Not found Not found Function: Amphipatic peptide that shows no antibacterial activity even at 50 uM but shows hemolytic activity against human erythrocytes. [Swiss_Prot Entry I0DEB5]No antibacterial activity even at 50 µM [Ref.22342498]10% hemolytic activity at 10 μM and 50 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 22342498 Peptides. 2012 Apr;34(2):290-295. Ramírez-Carreto S, Quintero-Hernández V, Jiménez-Vargas JM, Corzo G, Possani LD, Becerril B, Ortiz E. Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae. DRAMP04699 FLKGIIDTVSKLF 13 Amphipathic peptide CT2 (VsCT2; Non-disulfide-bridged peptide 5.12, NDBP-5.12) I0DEB6 Belongs to the scorpion NDBP 5 family Not found Vaejovis subcristatus (Scorpion) (Thorellius subcristatus) Antimicrobial Transcript level Not found Not found Function: Amphipatic peptide that shows no antibacterial activity even at 50 µM but shows hemolytic activity against human erythrocytes. [Swiss_Prot Entry I0DEB6]No antibacterial activity even at 50 µM [Ref.22342498]5% hemolytic activity at 12.5 μM, 25% hemolytic activity at 25 μM, 80% hemolytic activity at 50 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 22342498 Peptides. 2012 Apr;34(2):290-295. Ramírez-Carreto S, Quintero-Hernández V, Jiménez-Vargas JM, Corzo G, Possani LD, Becerril B, Ortiz E. Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae. DRAMP04700 DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC 50 Basic phospholipase A2 BnpTX-1 (BnPTx-I, svPLA2; Phosphatidylcholine 2-acylhydrolase) P0DM51 Belongs to the phospholipase A2 family (Group II subfamily D49 sub-subfami Not found Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedipauloensis) Antimicrobial, Antibacterial, Antiparasitic, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Snake venom phospholipase A2 (PLA2). In vitro, shows anticoagulant activity and induces cytotoxicity when tested on C2C12 myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity (intramuscular injection), edema (injection in the subplantar region) and lethality. Also induces neurotoxic effect on mouse neuromuscular preparations and has bactericidal activity on the Gram-negative bacteria E.coli (ATCC29648) and the Gram- positive S.aureus (ATCC 25923). The catalytic and anticoagulant activities of BnpTX-I are higher than those of BnpTX-II. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Toxic Dose: LD(50) is 5.1 +/- 1.3 mg/kg by intraperitoneal injection into mice. LD(50) is 2.3 +/- 0.8 mg/kg by intravenous injection into mice. Miscellaneous: Has a pI of approximately 7.8 and about 121 amino acids (PubMed:15302537). PTM: Contains seven disulfide bonds." Gram-negative bacterium: E. coli ATCC29648 and Gram-positive bacterium: S. aureus ATCC 25923. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15302537 Toxicon. 2004 Sep 1;44(3):305-314. Rodrigues VM, Marcussi S, Cambraia RS, de Araújo AL, Malta-Neto NR, Hamaguchi A, Ferro EA, Homsi-Brandeburgo MI, Giglio JR, Soares AM. Bactericidal and neurotoxic activities of two myotoxic phospholipases A2 from Bothrops neuwiedi pauloensis snake venom. DRAMP04701 SLLELGKMILQETGKMPSKSYGAYGCNCGVLGR 33 Phospholipase A2 homolog (BmarPLA2, svPLA2 homolog) P0DI92 Belongs to the phospholipase A2 family (Group II subfamily) Not found Bothrops marajoensis (Marajo lancehead) Antimicrobial, Antibacterial, Antiparasitic Protein level Not found Not found "Function: Snake phospholipase A2 homolog that lacks enzymatic activity. May display myotoxin activity. Does not show antimicrobial activity. PTM: Contains seven disulfide bonds (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19944711 Toxicon. 2010 Apr 1;55(4):795-804. Costa Torres AF, Dantas RT, Toyama MH, Diz Filho E, Zara FJ, Rodrigues de Queiroz MG, Pinto Nogueira NA, Rosa de Oliveira M, de Oliveira Toyama D, Monteiro HS, Martins AM. Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: Phospholipase A2 and L-amino acid oxidase. DRAMP04702 VAVKATTTEEETEIPAK 17 38 kDa autolysin (Beta-glycosidase; Peptidoglycan hydrolase) P81528 Not found lytA Mycobacterium phlei Antimicrobial, Toxin Protein level Not found Not found "Function: Hydrolyzes the cell walls of mycobacteria. May play an important role in cell wall growth and cell separation. Biophysicochemical properties: pH dependence (Optimum pH is 7.5). PTM: The N-terminus is blocked (Probable)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10206696 Microbiology. 1999 Jan;145 ( Pt 1):169-176. Li ZS, Beveridge TJ, Betts J, Clarke AJ. Partial characterization of a major autolysin from Mycobacterium phlei. DRAMP04703 YKQCHKKGGHCFPKEKICIPPSSDFGKMDCRWRWKCCKKGSGK 43 Crotamine CRO1 O57540 Belongs to the crotamine-myotoxin family CRO1 Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10484745 Toxicon. 1999 Jul;37(7):973-984. Rádis-Baptista G, Oguiura N, Hayashi MA, Camargo ME, Grego KF, Oliveira EB, Yamane T. Nucleotide sequence of crotamine isoform precursors from a single South American rattlesnake (Crotalus durissus terrificus). DRAMP04704 KQCHKKGGHCFPKEKICIPPSSDFGKMDCRWRWKCCKKGSGK 42 Crotamine CRO3 O73799 Belongs to the crotamine-myotoxin family CRO3 Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10484745 Toxicon. 1999 Jul;37(7):973-984. Rádis-Baptista G, Oguiura N, Hayashi MA, Camargo ME, Grego KF, Oliveira EB, Yamane T. Nucleotide sequence of crotamine isoform precursors from a single South American rattlesnake (Crotalus durissus terrificus). DRAMP04705 YKRCHIKGGHCFPKEKICIPPSSDFGKMDCPWRRKCCKKGSG 42 Myotoxin-1 (Crotamine-1) P24331 Belongs to the crotamine-myotoxin family Not found Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2389256 Toxicon. 1990;28(5):575-585. Smith LA, Schmidt JJ. Cloning and nucleotide sequences of crotamine genes. DRAMP04706 YKRCHKKEGHCFPKTVICLPPSSDFGKMDCRWKWKCCKKGSVN 43 Myotoxin-1 (Myotoxin I) P12028 Belongs to the crotamine-myotoxin family Not found Crotalus oreganus concolor (Midget faded rattlesnake) (Crotalusviridis concolor) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3629618 Toxicon. 1987;25(6):677-680. Bieber AL, McParland RH, Becker RR. Amino acid sequences of myotoxins from Crotalus viridis concolor venom. DRAMP04707 YKQCHKKGGHCFPKEKICIPPSSDLGKMDCRWKWKCCKKGSG 42 Myotoxin-A (Myotoxin-1) P01476 Belongs to the crotamine-myotoxin family Not found Crotalus viridis viridis (Prairie rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity).(Ref.2) Tissue specificity: Expressed by the venom gland. PTM: Contains three disulfide bonds.(Ref.1) Toxic Dose: LD(50) is 3.0 mg/kg by intramuscular injection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Sarcoplasmic reticulum calcium-ATPase (Ref.3) 570412##2048143##1329655 Biochemistry. 1979 Feb 20;18(4):678-684.##Toxicon. 1991;29(2):265-268.##Arch Biochem Biophys. 1992 Nov 1;298(2):325-331. Fox JW, Elzinga M, Tu AT.##Aird SD, Kruggel WG, Kaiser II.##Baker B, Utaisincharoen P, Tu AT. Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of Prairie rattlesnake (Crotalus viridis viridis).##Multiple myotoxin sequences from the venom of a single prairie rattlesnake (Crotalus viridis viridis).##Structure-function relationship of myotoxin a using peptide fragments. DRAMP04708 YKRCHIKGGHCFPKEKICIPPSSDFGKMDCPWRRKSLKKGSG 42 Myotoxin-2 (Crotamine-2 Fragment) P24332 Belongs to the crotamine-myotoxin family Not found Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2389256 Toxicon. 1990;28(5):575-585. Smith LA, Schmidt JJ. Cloning and nucleotide sequences of crotamine genes. DRAMP04709 YKRCHKKGGHCFPKEKICTPPSSDFGKMDCRWKWKCCKKGSVN 43 Myotoxin-2 (Myotoxin II) P12029 Belongs to the crotamine-myotoxin family Not found Crotalus oreganus concolor (Midget faded rattlesnake) (Crotalusviridis concolor) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 3629618 Toxicon. 1987;25(6):677-680. Bieber AL, McParland RH, Becker RR. Amino acid sequences of myotoxins from Crotalus viridis concolor venom. DRAMP04710 YKRCHKKEGHCFPKTVICLPPSSDFGKMDCRWKWKCCKKGSVNNA 45 Myotoxin-2 P63175, P19861 Belongs to the crotamine-myotoxin family Not found Crotalus viridis viridis (Prairie rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2253781 FEBS Lett. 1990 Nov 12;274(1-2):43-47. Griffin PR, Aird SD. A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis). DRAMP04711 YKRCHIKGGHCFPKGKICIPPSSDFGKMDCPWRRKCCKKGSG 42 Myotoxin-3 (Crotamine-3) P24333 Belongs to the crotamine-myotoxin family Not found Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2389256 Toxicon. 1990;28(5):575-585. Smith LA, Schmidt JJ. Cloning and nucleotide sequences of crotamine genes. DRAMP04712 YKRCHKKGGHCFPKTVICLPPSSDFGKMDCRWKWKCCKKGSVNNA 45 Myotoxin-3 P63176, P19861 Belongs to the crotamine-myotoxin family Not found Crotalus viridis viridis (Prairie rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2253781 FEBS Lett. 1990 Nov 12;274(1-2):43-47. Griffin PR, Aird SD. A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis). DRAMP04713 YKQCHKKGGHCFPKEKICIPPSSDFGKMDCRWRWKCCKKRSGK 43 Myotoxin-4 (Crotamine-4 Fragment) P24334 Belongs to the crotamine-myotoxin family Not found Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Toxin Transcript level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2389256 Toxicon. 1990;28(5):575-585. Smith LA, Schmidt JJ. Cloning and nucleotide sequences of crotamine genes. DRAMP04714 YKRCHIKGGHCFPKEKLICIPPSSDIGKMDCPWKRKCCKKRS 42 Crotamine-IV-2 P86193 Belongs to the crotamine-myotoxin family Not found Crotalus durissus cumanensis (South American rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, and hind limb paralysis (By similarity). It also induces potent blockade of neuromuscular transmission in young chicken biventer cervicis preparation and potent myotoxic effect. In mice, it induces myonecrosis, upon intramuscular or subcutaneous injections. Tissue specificity: Expressed by the venom gland. Toxic Dose: LD(50) is 0.07 mg/kg by subcutaneous injection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17828447 Protein J. 2007 Dec;26(8):533-540. Ponce-Soto LA, Martins-de-Souza D, Novello JC, Marangoni S. Structural and biological characterization of two crotamine isoformsIV-2 and IV-3 isolated from the Crotalus durissus cumanensis venom. DRAMP04715 YKQCHKKGGHCFPKEVLICIPPSSDFGKMDCRWKRKCCKKRS 42 Crotamine-IV-3 P86194 Belongs to the crotamine-myotoxin family Not found Crotalus durissus cumanensis (South American rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, and hind limb paralysis (By similarity). It also induces potent blockade of neuromuscular transmission in young chicken biventer cervicis preparation and potent myotoxic effect. In mice, it induces myonecrosis, upon intramuscular or subcutaneous injections. Tissue specificity: Expressed by the venom gland. Toxic Dose: LD(50) is 0.06 mg/kg by subcutaneous injection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17828447 Protein J. 2007 Dec;26(8):533-540. Ponce-Soto LA, Martins-de-Souza D, Novello JC, Marangoni S. Structural and biological characterization of two crotamine isoformsIV-2 and IV-3 isolated from the Crotalus durissus cumanensis venom. DRAMP04716 YKRCHKKGGHCFPKTVICLPPSSDFGKMDCRWKWKCCKKGSVNNAISI 48 Myotoxin (Crotamine-4; Toxic peptide C) P01477, G9DCI6 Belongs to the crotamine-myotoxin family Not found Crotalus oreganus helleri (Southern pacific rattlesnake) (Crotalusviridis helleri) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Tissue specificity: Expressed by the venom gland. Toxic Dose: LD(50) is 1.96 mg/kg by subcutaneous injection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 694946 Toxicon. 1978;16(5):431-441. Maeda N, Tamiya N, Pattabhiraman TR, Russell FE. Some chemical properties of the venom of the rattlesnake, Crotalus viridis helleri. DRAMP04717 YKRCHKKGGHCFPKTVICLPPSSDFGKMDCRWRWKCCKKGSVNNAISI 48 Myotoxin (CAM-toxin) P24330, F8S0Z6, J3RY57 Belongs to the crotamine-myotoxin family Not found Crotalus adamanteus (Eastern diamondback rattlesnake) Antimicrobial, Toxin Protein level Not found Not found "Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism (By similarity). Miscellaneous: This myotoxin is the most abundant transcript in the venom of the specimen analyzed (PubMed:23025625). Individuals of C. adamanteus from populations in southern and central Florida lack this toxin in their venoms (PubMed:23025625). Tissue specificity: Expressed by the venom gland.(Ref.3) Toxic Dose: LD(50) is 0.96 mg/kg by subcutaneous injection.(Ref.1)" No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23025625##1862521 BMC Genomics. 2012 Jul 16;13:312.##Toxicon. 1991;29(4-5):461-468. Rokyta DR, Lemmon AR, Margres MJ, Aronow K.##Samejima Y, Aoki Y, Mebs D. The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus).##Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus). DRAMP04718 YKQCHKKGGHCFPKEKICIPPSSDFGKMDCRWRWKCCKKGSG 42 Crotamine Ile-19 (CRO_Ile-19) P63327 Belongs to the crotamine-myotoxin family Not found Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraimarattlesnake) Antimicrobial, Toxin Protein level Combine helix and strand structure The crystal structure of the myotoxic, cell-penetrating, basic polypeptide crotamine isolated from the venom of Crotalus durissus terrificus has been determined by single-wavelength anomalous dispersion techniques and refined at 1.7 Å resolution. The structure reveals distinct cationic and hydrophobic surface regions that are located on opposite sides of the molecule. (Ref.2) 4GV5 resolved by X-ray Function: Cationic peptide that possess multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage- gated potassium channel (Kv) inhibitor and exhibits antimicrobial activities (By similarity). It also elicts a short-lasting hyperextension of the hind limb. It does not causes observable tissue damage (whereas the whole venom causes severe myonecrosis accompanied by edema and hemorrhage). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available##24100315 Toxicon 1993,31:166-166.##Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):1958-1964. Dos Santos M.C., Morhy L., Ferreira L.C.L., Oliveira E.B.##Coronado MA, Gabdulkhakov A, Georgieva D, Sankaran B, Murakami MT, Arni RK, Betzel C. Purification and properties of a crotamine analog from Crotalus durissus ruruima venom.##Structure of the polypeptide crotamine from the Brazilian rattlesnake Crotalus durissus terrificus. DRAMP18097 MPFHYFPKLNPITWIPGWIPGLGKDRCLLPKVTGPCKASLTRYYYDKDTKACVEFIYGGCRGNRNNFKRKDECEKACTDH 80 Kunitz-type serine protease inhibitor U1-aranetoxin-Av1a (U1-AATX-Av1a; Toxin 1; AvTox-1) Q8T3S7 Belongs to the venom Kunitz-type family Not found Araneus ventricosus (Orbweaver spider) (Epeira ventricosa) Insecticidal Transcript level Not found Not found Function: Putative insecticidal toxin that may inhibit trypsin.##Miscellaneous: Since this peptide has no sequence signal, its secretion is unsure. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Ind. Entomol. 4:43-49 (2002) Jung E.H., Lee K.S. , Han J.H., Je Y.H., Chang J.H., Roh J.Y., Sohn H.D., Jin B.R. Molecular cloning of two cDNAs encoding an insecticidal toxin fromthe spider, Araneus ventricosus, and construction of a recombinantbaculovirus expressing a spider toxin. DRAMP18098 MALALLGLTIKPEHVPEGTGKAVADVEALACDPAQCMRSCPFNPFLNQYGGICKNGQCVCVKPS 64 U2-aranetoxin-Av1a (U2-AATX-Av1a; Toxin 2; AvTox-2) Q8T3S6 Not found Not found Araneus ventricosus (Orbweaver spider) (Epeira ventricosa) Insecticidal Transcript level Not found Not found Function: Putative insecticidal toxin.##Miscellaneous: Since this peptide has no sequence signal, its secretion is unsure. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Ind. Entomol. 4:43-49 (2002). Jung E.H., Lee K.S. , Han J.H., Je Y.H., Chang J.H., Roh J.Y., Sohn H.D., Jin B.R. Molecular cloning of two cDNAs encoding an insecticidal toxin fromthe spider, Araneus ventricosus, and construction of a recombinantbaculovirus expressing a spider toxin. DRAMP18099 ECAAKNKRCADWAGPWCCEGLYCSCRSYPGCMCRPNS 37 Beta/delta-agatoxin-7 (Mu-2Aga_01; U3-agatoxin-Ao1a; U3-AGTX-Ao1a) Q5Y4V8 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18100 GCVGENQQCADWAGPHCCSGYYCTCRYFPKCICRKDS 37 Beta/delta-agatoxin-3 (Mu-2Aga_04; U3-agatoxin-Ao1c; U3-AGTX-Ao1c) Q5Y4V6 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18101 GDCVGESQQCADWSGPYCCKGYYCTCRYFPKCICVNDN 38 Beta/delta-agatoxin-1 (Mu-2Aga_07; U3-agatoxin-Ao1f; U3-AGTX-Ao1f) Q5Y4V3 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). Fly larvae (LD50=7 μg/g). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18102 GGCVGESQQCADWSGPYCCKGYYCTCRYFPKCICVNDN 38 Beta/delta-agatoxin-2 (Mu-2Aga_08; U3-agatoxin-Ao1g; U3-AGTX-Ao1g) Q5Y4V2 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18103 GCVGENQQCADWAGLHCCSGYYCTCRYFPKCICRKDS 37 Beta/delta-agatoxin-4 (Mu-2Aaga_12; U3-agatoxin-Ao1k; U3-AGTX-Ao1k) Q5Y4U8 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18104 DCVGENGRCRDWYNDCCDGFYCSCRQPPYCICRNNN 36 Beta/delta-agatoxin-5 (Mu-2Aaga_13; U3-agatoxin-Ao1l; U3-AGTX-Ao1l) Q5Y4U7 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18105 ECVGENGHCRSWYNDCCDGYYCSCMQPPNCICRNNN 36 Beta/delta-agatoxin-6 (Mu-2Aaga_14; U3-agatoxin-Ao1m; U3-AGTX-Ao1m) Q5Y4U6 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E. A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18106 IFECVFSCDIKKEGKPCKPKGEKKCTGGWRCKIKLCLKI 39 U1-theraphotoxin-Ba1b (U1-TRTX-Ba1b; Venom peptide 2) P85504 Belongs to the huwentoxin-2 family Not found Brachypelma ruhnaui (Mexican golden redrump tarantula) (Brachypelmaalbiceps) Insecticidal Protein level Beta sheet (3 strands; 10 residues) The three-dimensional conformation (Fig. 3B) of Ba2 consists in a three-stranded (residues 15–17, 29–32 and 35–38) anti-parallel beta-sheet. The first strand is connected with the second one by a large loop made of residues 19–28, whereas the second and third strands are connected by a β-turn. 2KGH resolved by NMR Function: Has insecticidal activity. Insect LD50=9.2 ± 0.9 μg/g No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19374957 BiochiM. BiophyS. Acta 1794:1190-1196 (2009). Corzo G., Bernard C. , Clement H., Villegas E., Bosmans F., Tytgat J., Possani L.D., Darbon H., Alagon A. Insecticidal peptides from the theraposid spider Brachypelmaalbiceps: an NMR-based model of Ba2. DRAMP18107 ILECVFSCDIKKEGKPCKPKGEKKCTGGWRCKIKLCLKI 39 U1-theraphotoxin-Ba1a (U1-TRTX-Ba1a; Venom peptide 1) P85497 Belongs to the huwentoxin-2 family Not found Brachypelma ruhnaui (Mexican golden redrump tarantula) (Brachypelmaalbiceps) Insecticidal Protein level Not found Not found Function: Has insecticidal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (FEB-2008) to UniProtK Corzo G., Clement H., Alagon A. Primary structure of two insecticidal peptides from the theraposid Brachypelma ruhnaui. DRAMP18108 YCGLFGDLCTLDGTLACCIALELECIPLNDFVGICL 36 Asteropin-A (Asteropine-A) P84702 Not found Not found Asteropus simplex (Marine sponge) (Stellettinopsis simplex) Antimicrobial, Antibacterial Protein level Not found Not found Function: Sialidase inhibitor. Competitively inhibits bacterial sialidases, but not viral sialidaseS. Does not inhibit glycosidases or proteaseS. Has no antitumor activity. V. cholerae (Ki values of 340 nM), S. typhimurium (Ki values of 350 nM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16793514 CheM. Biol. 13:569-574 (2006). Takada K., Hamada T., Hirota H., Nakao Y., Matsunaga S. , van Soest R.W.M. , Fusetani N. Asteropine A, a sialidase-inhibiting conotoxin-like peptide from themarine sponge Asteropus simplex. DRAMP18109 SDCTLRNHDCTDDRHSCCRSKMFKDVCTCFYPSQAKKELCTCQQPKHLKYIEKGLQKAKDYAT 63 U2-ctenitoxin-Cs1a (U1-CNTX-Cs2a; Neurotoxic enhancer CSTX-13; U1-ctenitoxin-Cs2a; Fragments) P83919, P83920 Belongs to the spider toxin CSTX superfamily Not found Cupiennius salei (Wandering spider) Insecticidal Protein level Not found Not found Function: This toxin alone has very weak insecticidal activity, with an unknown molecular target. Acts as a neurotoxic enhancer, synergistically enhancing the neurotoxic action of omega-CNTX-Cs1a (CSTX-1) (AC P81694). Fly (LD50=16.3 pmol/mg) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15272079##15914655 ProC. Natl. Acad. Sci. U.S. A. 101:11251-11256 (2004).##J. Exp. Biol. 208:2115-2121 (2005). Wullschleger B., Kuhn-Nentwig L., Tromp J., Kaempfer U., Schaller J., Schuerch S. , Nentwig W.##Wullschleger B., Nentwig W., Kuhn-Nentwig L. CSTX-13, a highly synergistically acting two-chain neurotoxicenhancer in the venom of the spider Cupiennius salei (Ctenidae).##Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. DRAMP18110 SSVCIPSGQPCPYNEHCCSGSCTYKENENGNTVQRCD 37 Omega-hexatoxin-Ar1a (Omega-HXTX-Ar1a; Omega-atracotoxin-Ar1a; Omega-AcTx-Ar1a) P83580, A5A3H0 Belongs to the omega-atracotoxin type 1 family Not found Atrax robustus (Sydney funnel-web spider) Insecticidal Protein level Not found Not found Function: Insecticidal toxin that reversibly and voltage- independently blocks both mid-low- (M-LVA) and high-voltage- activated (HVA) calcium channels (Cav) in cockroach DUM neuronS. Also causes a modest block of insect sodium channel currents (Nav). Induces potent excitatory symptoms, followed by flaccid paralysis leading to death in house cricketS. Miscellaneous: This toxin comes from a female specimen. It is observed that propeptide sequences coming from female specimen have only limited homology with the male paralogs, but the reason is unknown.Does not inhibit potassium channel currentS. Has no activity in vertebrate smooth and skeletal nerve-muscle preparations (PubMed: 17610847). House crickets (LD50=236±28 pmol/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17610847 BiocheM. Pharmacol. 74:623-638 (2007). Chong Y., Hayes J.L., Sollod B., Wen S. , Wilson D.T., Hains P.G., Hodgson W.C. , Broady K.W., King G.F., Nicholson G.M. The omega-atracotoxins: selective blockers of insect M-LVA and HVAcalcium channelS. DRAMP18111 GGCIKWNHSCQTTTLKCCGKCVVCYCHTPWGTNCRCDRTRLFCTED 46 Mu-hexatoxin-Mg2a (Mu-HXTX-Mg2a; Neurotoxin magi-3) P83559 Not found Not found Macrothele gigas (Spider) Insecticidal Protein level Not found Not found 6AX2 Function: Competes for binding at site 3 of the insect voltage- gated sodium channel (Nav). Insecticidal neurotoxin. Causes temporary paralysis to lepidopteran larvae when injected at 10.3 nmol/g. Is not toxic to mice when injected intracranially at 20 pmol/g.##PTM: Contains 5 disulfide bondS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet site 3 of the insect voltage- gated sodium channel (Nav) 12860384 FEBS Lett. 547:43-50 (2003). Corzo G., Gilles N., Satake H., Villegas E., Dai L., Nakajima T., Haupt J. Distinct primary structures of the major peptide toxins from thevenom of the spider Macrothele gigas that bind to sites 3 and 4 in thesodium channel. DRAMP18112 CMGYDIHCTDRLPCCFGLECVKTSGYWWYKKTYCRRKS 38 Mu-hexatoxin-Mg1b (Mu-HXTX-Mg1b; Neurotoxin magi-1) P83557 Belongs to the magi-1 family Not found Macrothele gigas (Spider) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin. Shows competition for site 3 of insect voltage-gated sodium channels (Nav). Has no effect on lepidopteran larvae when injected at 20 pmol/g, or on mice when injected intracranially at 32.8 nmol/g. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet site 4 of the insect voltage- gated sodium channel (Nav) 12860384 FEBS Lett. 547:43-50 (2003). Corzo G., Gilles N., Satake H., Villegas E., Dai L., Nakajima T., Haupt J. Distinct primary structures of the major peptide toxins from thevenom of the spider Macrothele gigas that bind to sites 3 and 4 in thesodium channel. DRAMP18113 ACVGDGQRCASWSGPYCCDGYYCSCRSMPYCRCRNNS 37 Delta-amaurobitoxin-Pl1b (Delta-AMATX-Pl1b; Delta-palutoxin IT2; Delta-paluIT2) P83257 Belongs to the beta/delta-agatoxin family Not found Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus) Insecticidal Protein level beta sheet (5 strands; 10 residues) The three-dimensional structure of δ-paluIT2 consists of a compact disulfide-bonded core, from which four loops emerge.In δ-paluIT2, the corresponding loops encompass residues 3–6 (loop I), 10–15 (loop II), 18–20 (loop III), and 25–31 (loop IV), and residues 7–9 are involved in an extended structure. The β-sheet structure is therefore made of three anti-parallel β-strands (Q7–R8, Y21–S24, and R32–N35 ). 1V91 resolved by NMR Function: Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation. Insect LD50=24.7 ± 11.8 mg/g No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10971590##15683238##15726637 Eur. J. BiocheM. 267:5783-5795 (2000).##Biochemistry 44:1542-1549 (2005).##Proteins 59:368-379 (2005). Corzo G., Escoubas P., Stankiewicz M. , Pelhate M. , Kristensen C. P., Nakajima T.##Corzo G., Escoubas P., Villegas E., Karbat I., Gordon D., Gurevitz M. , Nakajima T., Gilles N.##Ferrat G., Bosmans F., Tytgat J., Pimentel C. , Chagot B., Gilles N., Nakajima T., Darbon H., Corzo G. Isolation, synthesis and pharmacological characterization of delta-palutoxins IT, novel insecticidal toxins from the spider Paracoelotesluctuosus (Amaurobiidae).##A spider toxin that induces a typical effect of scorpion alpha-toxinsbut competes with beta-toxins on binding to insect sodium channelS. ##Solution structure of two insect-specific spider toxins and their pharmacological interaction with the insect voltage-gated Na+channel. DRAMP18114 DAINSPVTCCYTLTSKKISMQRLMSYRRVTSSKCPKEAVIFKTIAGKEICAEPKXXWVQDSISHLDKKNQXPKP 74 Monocyte chemotactic protein 1B (MCP-1B; Fragment) P80343 Belongs to the intercrine beta (chemokine CC) family Not found Bos taurus (Bovine) Antitumor Protein level Not found Not found Function: Chemotactic factor that attracts monocytes, but not neutrophilS. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin.##PTM: The N-terminus is blocked. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7947749 Biochemistry 33:13406-13412 (1994). Proost P., Wuyts A., Lenaerts J.-P., van Damme J. Purification, sequence analysis, and biological characterization of asecond bovine monocyte chemotactic protein-1 (Bo MCP-1B). DRAMP18115 QPVGINTSTTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWV 60 C-C motif chemokine 7 (Monocyte chemoattractant protein 3; Monocyte chemotactic protein 3; MCP-3; P80098, Q569J6 Belongs to the intercrine beta (chemokine CC) family CCL7 Homo sapiens (Human) Antitumor Protein level 14% helical (1 helices; 11 residues) The shape of the MCP-3 monomer is that of an elongated tetrahedral. It consists of a three-stranded antiparallel β sheet and a three turn C-terminal α helix lying above the sheet floor. The N-terminal extremity is disordered up to residue 12, but located close to the helix; it consists of a long mobile loop, spatially stabilized because of the two disulfide bonds which link Cys 11 with Cys 36 and Cys 12 with Cys 52. 1BO0, 1NCV resolved by NMR Function: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophilS. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3.##PTM: O-glycosylated. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8461011##7916328##8318676##15489334##1613466##15340161 BiocheM. BiophyS. ReS. Commun. 191:535-542 (1993).##Genomics 21:403-408 (1994).##Eur. Cytokine Netw. 4:99-110 (1993).##Genome ReS. 14:2121-2127 (2004).##J. Exp. Med. 176:59-65 (1992).##Protein Sci. 13:2819-282 Opdenakker G., Froyen G., Fiten P., Proost P., van Damme J.##Opdenakker G., Fiten P., Nys G., Froyen G., van Roy N., Speleman F., Laureys G., van Damme J.##Minty A., Chalon P., Guillemot J.-C. , Kaghad M. , Liauzun P., Magazin M. , Miloux B., Minty C. , Ramond P., Vita N., Lupker J., Shire D., Ferrara P., Caput D.##The MGC Project Team##van Damme J., Proost P., Lenaerts J.-P., Opdenakker G.##Zhang Z., Henzel W.J.##Kim K.-S. , Rajarathnam Human monocyte chemotactic protein-3 (MCP-3): molecular cloning ofthe cDNA and comparison with other chemokineS. ##The human MCP-3 gene (SCYA7): cloning, sequence analysis, andassignment to the C-C chemokine gene cluster on chromosome 17q11.2-q12.##Molecular cloning of the MCP-3 chemokine gene and regulation of its expression.##The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).##Structural and functional identification of two human, tumor- DRAMP18116 QDFMKHLDKKTQTPKL 16 U2-segestritoxin-Sf1b (U2-SGTX-Sf1b; F5.7; Toxin SFI 2) P61096 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found Function: Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.25 mg/kg body weight. Heliothis virescens (LD50=7 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233 Toxicon 40:125-130 (2002). Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E. Novel insecticidal toxins from the venom of the spider Segestriaflorentina. DRAMP18117 KECMTDGTVCYIHNHNDCCGSCLCSNGPIARPWEMMVGNCMCGPKA 46 U2-segestritoxin-Sf1a (U2-SGTX-Sf1a; F5.6; Toxin SFI 1) P61095 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found 2MF3 Function: Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.5 mg/kg body weight. Orally active against larvae of the tomato moth (Laconobia oleracea), the rice brown planthopper (Nilaparvata lugens), and the peach-potato aphid (Myzus persicae) when fused to snowdrop lectin. Heliothis virescens (LD50=10 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233##15037094 Toxicon 40:125-130 (2002).##J. Insect Physiol. 50:61-71 (2004). Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E.##Fitches E., Edwards M. G., Mee C. , Grishin E., Gatehouse A.M. , Edwards J.P., Gatehouse J.A. Novel insecticidal toxins from the venom of the spider Segestriaflorentina.##Fusion proteins containing insect-specific toxins as pest controlagents: snowdrop lectin delivers fused insecticidal spider venom toxinto insect haemolymph following oral ingestion. DRAMP18118 AECMVDETVCYIHNHNNC 18 U2-segestritoxin-Sf1i (U2-SGTX-Sf1i; Toxin F5.5; Fragment) P61094 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found Function: Insecticidal toxin. Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.1 mg/kg body weight. Heliothis virescens (LD50=4 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233 Toxicon 40:125-130 (2002). Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E. Novel insecticidal toxins from the venom of the spider Segestriaflorentina. DRAMP18119 ADCVGDGQRCADWAGPYCCSGYYCSCRSMPYCRCRSDS 38 Mu-agatoxin-Aa1c (Mu-AGTX-Aa1c; Mu-agatoxin III; Mu-agatoxin-3) P60178, P11059 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. M. sexta (LD50=28±12 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18186 AKKPFVQRVKNAASKAYNKLKGLAMQSQYGCPIISNMCEDHCRRKKMEGQCDLLDCVCS 59 Beta-KTx-like peptide LaIT2 C7G3K3 Belongs to the long chain scorpion toxin family. Class 2 subfamily. Not found Liocheles australasiae (Wood scorpion) Antimicrobial, Antibacterial Protein level Not found Not found 7WKF Function:Amphipathic peptide that causes significant antimicrobial activity in the growth inhibition assay against E.coli. Causes paralysis or death to crickets within 48 hours after injection at a dose of 1.3 ug/insect (26 ug/g of body weight). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19966481 Biosci. Biotechnol. Biochem. 73:2769-2772(2009) Matsushita N., Miyashita M., Ichiki Y., Ogura T., Sakuradani E.,Nakagawa Y., Shimizu S., Miyagawa H. Purification and cDNA cloning of LaIT2, a novel insecticidal toxinfrom venom of the scorpion Liocheles australasiae. DRAMP18187 IWLTALKFLGKNLGKHLAKQQLAKL 25 Toxin LyeTx 1 C0HJU9 Not found Not found Lycosa erythrognatha (Spider) (Scaptocosa raptoria) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found 7MMM Function: Has hemolytic activity against rabbit erythrocytes. Forms pores in lipid bilayers in vitro; pore formation is reduced when cholesterol is present in the bilayers. [Ref.19946788]Gram-positive bacterium: S.aureus (MIC=3.79 μM);##Gram-negative bacterium: E.coli (MIC=7.81 μM);##Yeasts: C.krusei (MIC=26.3 μM), C.neoformans (MIC=13.2 μM). [Ref.19946788]ED50=1.3 × 10−4 M against rabbit erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19946788 Amino Acids 39:135-144(2010) Santos D.M., Verly R.M., Pilo-Veloso D., de Maria M.,de Carvalho M.A., Cisalpino P.S., Soares B.M., Diniz C.G.,Farias L.M., Moreira D.F., Frezard F., Bemquerer M.P., Pimenta A.M.,de Lima M.E. LyeTx I, a potent antimicrobial peptide from the venom of the spiderLycosa erythrognatha. DRAMP18121 ADCVGDGQKCADWFGPYCCSGYYCSCRSMPYCRCRSDS 38 Mu-agatoxin-Hc1c (Mu-AGTX-Hc1c; CT-III; Curtatoxin-3) P15968 Belongs to the beta/delta-agatoxin family Not found Hololena curta (Funnel-web spider) (Agelena curta) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in the cricket A.domestica. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. A.domestica (LD50=4 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2298738##15066410 J. Biol. CheM. 265:2054-2059 (1990).##Toxicon 43:509-525 (2004). Stapleton A., Blankenship D.T., Ackermann D.L., Chen T.-M. , Gorder G.W., Manley G.D., Palfreyman M. G., Coutant J.E., Cardin A.D.##Adams M. E. CurtatoxinS. Neurotoxic insecticidal polypeptides isolated from thefunnel-web spider Hololena curta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18122 SCVGEYGRCRSAYEDCCDGYYCNCSQPPYCLCRNNN 36 Mu-agatoxin-Hc1a (Mu-AGTX-Hc1a; Curtatoxin-1; CT-I) P15967 Belongs to the beta/delta-agatoxin family Not found Hololena curta (Funnel-web spider) (Agelena curta) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in the cricket A.domestica. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. A.domestica (LD50=20 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2298738##15066410 J. Biol. CheM. 265:2054-2059 (1990).##Toxicon 43:509-525 (2004). Stapleton A., Blankenship D.T., Ackermann D.L., Chen T.-M. , Gorder G.W., Manley G.D., Palfreyman M. G., Coutant J.E., Cardin A.D.##Adams M. E. CurtatoxinS. Neurotoxic insecticidal polypeptides isolated from thefunnel-web spider Hololena curta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18123 DCVGESQQCADWAGPHCCDGYYCTCRYFPKCICVNNN 37 Mu-agatoxin-Aa1f (Mu-AGTX-Aa1f; Mu-agatoxin VI; Mu-agatoxin-6) P11062 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. M. sexta (LD50=38±12 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18124 ACVGENKQCADWAGPHCCDGYYCTCRYFPKCICRNNN 37 Mu-agatoxin-Aa1e (Mu-AGTX-Aa1e; Mu-agatoxin V; Mu-agatoxin-5) P11061 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. M. sexta (LD50=48±11 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18125 ACVGENQQCADWAGPHCCDGYYCTCRYFPKCICRNNN 37 Mu-agatoxin-Aa1d (Mu-AGTX-Aa1d; Mu-agatoxin IV; Mu-agatoxin-4) P11060 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. M. sexta (LD50=40±9 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410##8608119 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004).##Biochemistry 35:2836-2844 (1996). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E.##Omecinsky D.O., Holub K.E., Adams M. E., Reily M. D. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta.##Three-dimensional structure analysis of mu-agatoxins: furtherevidence for common motifs among neurotoxins with diverse ion channelspecificitieS. DRAMP18126 ECATKNKRCADWAGPWCCDGLYCSCRSYPGCMCRPSS 37 Mu-agatoxin-Aa1b (Mu-AGTX-Aa1b; Mu-agatoxin II; Mu-agatoxin-2) P11058 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. M. sexta (LD50=75±27 μg/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta. DRAMP18127 ECVPENGHCRDWYDECCEGFYCSCRQPPKCICRNNN 36 Mu-agatoxin-Aa1a (Mu-AGTX-Aa1a; Mu-agatoxin I; Mu-agatoxin-1) P11057 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level beta sheet (4 strands; 15 residues) Not found 1EIT resolved by NMR Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS. LD50 of 28±7 μg/g in M. sexta No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410##8608119 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004).##Biochemistry 35:2836-2844 (1996). Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E.##Omecinsky D.O., Holub K.E., Adams M. E., Reily M. D. Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta.##Three-dimensional structure analysis of mu-agatoxins: furtherevidence for common motifs among neurotoxins with diverse ion channelspecificitieS. DRAMP18128 SGTSEKERESGRLLGVVKRLIVGFRSPFR 29 Antimicrobial peptide HsAp4; P0DMJ0 Not found Not found Heterometrus spinifer (Asia giant forest scorpion) (Malaysian blackscorpion) Antimicrobial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Possesses antimicrobial activity against both Gram- negative and Gram-positive bacteria, as well as against the fungus C. tropicaliS. Also possess a relatively high hemolytic activity (By similarity). [Ref.23000095]Gram-positive bacteria: Staphylococcus aureus AB 94004 (MIC=23.6µM), Bacillus magaterium AB 90008 (MIC=11.8µM), Bacillus thuringiensis AB 93100 (MIC=46.5µM);##Gram-negative bacteria: Salmonella enterica AB 2010185 (MIC=25.0µM), E. coli DH5 (MIC=51.2µM), E. coli JM109 (MIC=50.4µM), Enterobacter cloacae subsp. cloacae AB 2010162 (MIC=47.9µM), Klebsiella oxytoca AB 2010143 (MIC=50.5µM);##Fungi: Candida tropicalis AY 91009 (MIC=48.6µM). [Ref.23000095]5% hemolytic activity at 0.8 μM, 35% hemolytic activity at 1.6 μM, 95% hemolytic activity at 3.2 μM, 100% hemolytic activity against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23000095 Peptides 38:389-394 (2012). Nie Y., Zeng X.C. , Yang Y., Luo F., Luo X., Wu S. , Zhang L., Zhou J. A novel class of antimicrobial peptides from the scorpionHeterometrus spinifer. DRAMP18129 SGTPEKERESGRLLGVVKRYIVCVRNPCP 29 Antimicrobial peptide HsAp3; P0DMI9 Not found Not found Heterometrus spinifer (Asia giant forest scorpion) (Malaysian blackscorpion) Antimicrobial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Possesses antimicrobial activity against both Gram- negative and Gram-positive bacteria, as well as against the fungus C. tropicali. Also possess a relatively high hemolytic activity (By similarity). [Ref.23000095]Gram-positive bacteria: Staphylococcus aureus AB 94004 (MIC=23.6μM), Bacillus magaterium AB 90008 (MIC=11.8μM), Bacillus thuringiensis AB 93100 (MIC=46.5μM);##Gram-negative bacteria: Salmonella enterica AB 2010185 (MIC=25.0μM), E. coli DH5 (MIC=51.2μM), E. coli JM109 (MIC=50.4μM), Enterobacter cloacae subsp. cloacae AB 2010162 (MIC=47.9μM), Klebsiella oxytoca AB 2010143 (MIC=50.5μM);##Fungi: Candida tropicalis AY 91009 (MIC=48.6μM). [Ref.23000095]5% hemolytic activity at 0.8 μM, 35% hemolytic activity at 1.6 μM, 95% hemolytic activity at 3.2 μM, 100% hemolytic activity against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23000095 Peptides 38:389-394 (2012). Nie Y., Zeng X.C. , Yang Y., Luo F., Luo X., Wu S. , Zhang L., Zhou J. A novel class of antimicrobial peptides from the scorpionHeterometrus spinifer. DRAMP18130 SGTSEKERESERLLGVVNPLIKCFRSPCP 29 Antimicrobial peptide HsAp2 P0DMI8 Not found Not found Heterometrus spinifer (Asia giant forest scorpion) (Malaysian blackscorpion) Antimicrobial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Possesses antimicrobial activity against both Gram- negative and Gram-positive bacteria, as well as against the fungus C. tropicaliS. Also possess a relatively high hemolytic activity (By similarity). [Ref.23000095]Gram-positive bacteria: Staphylococcus aureus AB 94004 (MIC=23.6μM), Bacillus magaterium AB 90008 (MIC=11.8μM), Bacillus thuringiensis AB 93100 (MIC=46.5μM);##Gram-negative bacteria: Salmonella enterica AB 2010185 (MIC=25.0μM), E. coli DH5 (MIC=51.2μM), E. coli JM109 (MIC=50.4μM), Enterobacter cloacae subsp. cloacae AB 2010162 (MIC=47.9μM), Klebsiella oxytoca AB 2010143 (MIC=50.5μM);##Fungi: Candida tropicalis AY 91009 (MIC=48.6μM). [Ref.23000095]5% hemolytic activity at 0.8 μM, 35% hemolytic activity at 1.6 μM, 95% hemolytic activity at 3.2 μM, 100% hemolytic activity against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23000095 Peptides 38:389-394 (2012). Nie Y., Zeng X.C. , Yang Y., Luo F., Luo X., Wu S. , Zhang L., Zhou J. A novel class of antimicrobial peptides from the scorpionHeterometrus spinifer. DRAMP18131 SGTSEKERESGRLLGVVKRLIVCFRSPFP 29 Antimicrobial peptide HsAp1 (HsAp) P0DMI7 Not found Not found Heterometrus spinifer (Asia giant forest scorpion) (Malaysian blackscorpion) Antimicrobial, Antifungal, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Possesses antimicrobial activity against both Gram- negative and Gram-positive. Also possess a relatively high hemolytic activity. [Ref.23000095]Gram-positive bacteria: Staphylococcus aureus AB 94004 (MIC=23.6μM), Bacillus magaterium AB 90008 (MIC=11.8μM), Bacillus thuringiensis AB 93100 (MIC=46.5μM);##Gram-negative bacteria: Salmonella enterica AB 2010185 (MIC=25.0μM), E. coli DH5 (MIC=51.2μM), E. coli JM109 (MIC=50.4μM), Enterobacter cloacae subsp. cloacae AB 2010162 (MIC=47.9μM), Klebsiella oxytoca AB 2010143 (MIC=50.5μM);##Fungi: Candida tropicalis AY 91009 (MIC=48.6μM). [Ref.23000095]5% hemolytic activity at 0.8 μM, 35% hemolytic activity at 1.6 μM, 95% hemolytic activity at 3.2 μM, 100% hemolytic activity against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23000095 Peptides 38:389-394 (2012). Nie Y., Zeng X.C. , Yang Y., Luo F., Luo X., Wu S. , Zhang L., Zhou J. A novel class of antimicrobial peptides from the scorpionHeterometrus spinifer. DRAMP18132 ADPRNPLEECFRETD 15 L-amino-acid oxidase Bfon20 (LAAO; LAO) P0DMG9 Belongs to the flavin monoamine oxidase family Not found Bothrops fonsecai (Fonseca's lancehead) (Rhinocerophis fonsecai) Antimicrobial, Antitumor, Antibacterial, Antiparasitic Protein level Not found Not found Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18760386 J. Proteomics 71:473-485 (2008). Tashima A.K., Sanz L., Camargo A.C. , Serrano S. M. , Calvete J.J. Snake venomics of the Brazilian pitvipers Bothrops cotiara andBothrops fonsecai. Identification of taxonomy markerS. DRAMP18133 NRILPTLIGPL 11 Peptide Ctri9819 P0DMG0 Not found Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Transcript level Not found Not found Function: Antimicrobial peptide (By similarity).##Miscellaneous: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells (PubMed: 23415044). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials 34:3511-3522 (2013). Hong W., Zhang R., Di Z., He Y., Zhao Z., Hu J., Wu Y., Li W., Cao Z. Design of histidine-rich peptides with enhanced bioavailability andinhibitory activity against hepatitis C viruS. DRAMP18134 INWDILIDTIKDKL 14 Peptide Ctri9677 P0DMF9 Not found Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Transcript level Not found Not found Function: Antimicrobial peptide (By similarity).##Miscellaneous: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells (PubMed: 23415045). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials 34:3511-3522 (2013). Hong W., Zhang R., Di Z., He Y., Zhao Z., Hu J., Wu Y., Li W., Cao Z. Design of histidine-rich peptides with enhanced bioavailability andinhibitory activity against hepatitis C viruS. DRAMP18135 ILGKFCDEIKRIV 13 Peptide Hp1478 (Non-disulfide-bridged peptide 5; NDBP-5) P0DMF0 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial Protein level Not found Not found Function: Amphipathic peptide with antimicrobial activity (By similarity). Does not show antiviral activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24315793 Antiviral ReS. 102:1-10 (2014). Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z. Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1. DRAMP18136 IFKAIWSGIKRLC 13 Peptide Hp1412 (Non-disulfide-bridged peptide 5; NDBP-5) P0DME9 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial Transcript level Not found Not found Function: Amphipathic peptide with antimicrobial activity (By similarity). Does not show antiviral activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20443192##24315793 Proteomics 10:2471-2485 (2010).##Antiviral ReS. 102:1-10 (2014). Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.##Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z. Molecular diversity of toxic components from the scorpionHeterometrus petersii venom revealed by proteomic and transcriptomeanalysiS. ##Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1. DRAMP18137 ILSYLWNGIKSIF 13 Peptide Hp1239 (Non-disulfide-bridged peptide 5; NDBP-5) P0DME8 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial, Antibacterial, Antiviral Transcript level Not found Not found Function: Amphipathic peptide with antibacterial activities (By similarity). Shows antiviral activities against the herpes simplex virus type-1. It potently inhibits the initial infection by provoking the rupture of viral envelop and the dissociation of proteins from the virions (EC (50) is 0.41 μM). It also effectively inhibits viral attachment (EC (50) is 5.73 μM), viral entry (EC (50) is 4.32 μM) and viral proliferation after infection (EC (50) is 8.41 μM). Morever, it enters mammalian tested cells (Vero) and reduces the intracellular infectivity. CC50=26.15 ± 1.91 μM; HC50= 33.32 ± 0.96 μM; EC50=0.41 ± 0.06 μM No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20443192##24315793 Proteomics 10:2471-2485 (2010).##Antiviral ReS. 102:1-10 (2014). Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.##Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z. Molecular diversity of toxic components from the scorpionHeterometrus petersii venom revealed by proteomic and transcriptomeanalysiS. ##Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1. DRAMP18138 ILGEIWKGIKDIL 13 Peptide Hp1165 (Non-disulfide-bridged peptide 5; NDBP-5) P0DME7 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial Transcript level Not found Not found Function: Amphipathic peptide with antimicrobial activity (By similarity). Does not show antiviral activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20443192##24315793 Proteomics 10:2471-2485 (2010).##Antiviral ReS. 102:1-10 (2014). Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.##Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z. Molecular diversity of toxic components from the scorpionHeterometrus petersii venom revealed by proteomic and transcriptomeanalysiS. ##Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1. DRAMP18139 ILGKIWEGIKSIF 13 Peptide Hp1036 (Non-disulfide-bridged peptide 5; NDBP-5) P0DME6 Belongs to the scorpion NDBP 5 family Not found Heterometrus petersii (Asian forest scorpion) Antimicrobial, Antibacterial, Antiviral Transcript level Not found Not found Function: Amphipathic peptide with antibacterial activities (By similarity). Shows antiviral activities against the herpes simplex virus type-1. It potently inhibits the initial infection by provoking the rupture of viral envelop and the dissociation of proteins from the virions (EC (50) is 0.43 μM). It also effectively inhibits viral attachment (EC (50) is 2.87 μM), viral entry (EC (50) is 4.29 μM) and viral proliferation after infection (EC (50) is 7.86). Morever, it enters mammalian tested cells (Vero) and reduces the intracellular infectivity. CC50=46.71 ± 3.80 μM; HC50=34.91 ± 0.47 μM; EC50=0.43 ± 0.09 μM No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20443192##24315793 Proteomics 10:2471-2485 (2010).##Antiviral ReS. 102:1-10 (2014). Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.##Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z. Molecular diversity of toxic components from the scorpionHeterometrus petersii venom revealed by proteomic and transcriptomeanalysiS. ##Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1. DRAMP18185 FLPLFLPKIICVITKKC 17 Jingdongin-1 K7ZGS2 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily Not found Amolops jingdongensis (Chinese torrent frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Has activity against Gram- negative bacterium and exhibits hemolytic activity. [Ref.22828809]Gram-negative bacterium: B.dysenteriae (MIC=35 μg/ml);##Gram-positive bacteria: S.aureus ATCC 2592 (MIC=4.7 μg/ml), B.subtilis ATCC 6633 (MIC=9.38 μg/ml);##Fungus: C.albicans (MIC=18.75 μg/ml) [Ref.22828809] It exhibits hemolysis of 1.32%, 5.37%, 6.35%, 16.55% at 25 μg/ml, 50 μg/ml, 100 μg/ml, 200 μg/ml against rabbit red blood cells Cyclic Free Cyclization(Cys11 and Cys17). Disulfide bond between Cys11 and Cys17. L No cytotoxicity information found Not found 22828809 Amino Acids 44:481-487(2013) He X., Yang S., Wei L., Liu R., Lai R., Rong M. Antimicrobial peptide diversity in the skin of the torrent frog,Amolops jingdongensis. DRAMP18141 PSPPGFSPFR 10 Nephilakinin-3 (Nephilakinin-III) P0DM74 Belongs to the bradykinin-related peptide family Not found Nephila clavipes (Golden silk orbweaver) Insecticidal Protein level Not found Not found Function: Causes constriction on isolated rat ileum preparations and relaxation on rat duodenum muscle preparations at amounts higher than bradykinin. Is a partial agonist bradykinin receptor B2 (BDKRB2). Has insecticidal propertieS. May be related to the predation of insects by the spider webS. ##Miscellaneous: Has been extracted from the spider web (PubMed: 16202476). Does not target bradykinin receptor B1 (BDKRB1) (PubMed: 16202476). ED50=0.7μM;LD50=70±17pmoles/mg honeybee No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16202476 Peptides 27:690-697 (2006). Volsi E.C. , Mendes M. A., Marques M. R., dos Santos L.D., Santos K.S. , de Souza B.M. , Babieri E.F., Palma M. S. Multiple bradykinin-related peptides from the capture web of thespider Nephila clavipes (Araneae, Tetragnatidae). DRAMP18142 EAPPGFSPFR 10 Nephilakinin-2 (Nephilakinin-II) P0DM73 Belongs to the bradykinin-related peptide family Not found Nephila clavipes (Golden silk orbweaver) Insecticidal Protein level Not found Not found Function: Causes constriction on isolated rat ileum preparations and relaxation on rat duodenum muscle preparations at amounts higher than bradykinin. Is a partial agonist bradykinin receptor B2 (BDKRB3). Has insecticidal propertieS. ED50=1.0μM;LD50=72±18pmoles/mg honeybee No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16202476 Peptides 27:690-697 (2006). Volsi E.C. , Mendes M. A., Marques M. R., dos Santos L.D., Santos K.S. , de Souza B.M. , Babieri E.F., Palma M. S. Multiple bradykinin-related peptides from the capture web of thespider Nephila clavipes (Araneae, Tetragnatidae). DRAMP18143 EELEAKDVIESKALATLDEER 21 Toxin OAIP 5 P0DM69 Belongs to the huwentoxin-2 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F. SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18144 YCQKWMWTCDAERKCCEDMACELWCKKRL 29 Toxin OAIP 4 P0DM68 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F. SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18145 ECGGLMTRCDGKTTFCCSGMNCSPTWKWCVYAP 33 Toxin OAIP 3 P0DM67 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F. SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18146 DCLGQWASCEPKNSKCCPNYACTWKYPWCRYRA 33 Toxin OAIP 2 P0DM66 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F. SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18147 LKCNKLVPLFYKTCPAGKNL 20 Cytotoxin drCT-1 (drCT-I; Fragment) P0C5H4 Belongs to the snake three-finger toxin family Not found Daboia russelii (Russel's viper) (Vipera russelii) Anti-cancer, Cytotoxic Protein level Not found Not found Function: This three-finger cytotoxin has antiproliferative, cytotoxic and apoptotic activitieS. Both in vivo and in vitro experimental results suggests that this protein possess anticancer potential. Also shows neurotoxicity, cardiotoxicity and myotoxicity. IC50=8.9 μg/ml for U937 and 6.7 μg/ml for K562 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17055549##16511326 Toxicon 49:46-56 (2007).##Acta Crystallogr. F 62:292-294 (2006). Gomes A., Choudhury S. R., Saha A., Mishra R., Giri B., Biswas A.K., Debnath A., Gomes A.##Choudhury S. R., Gomes A., Gomes A., Dattagupta J.K., Sen U. A heat stable protein toxin (drCT-I) from the Indian Viper (Daboiarusselli russelli) venom having antiproliferative, cytotoxic andapoptotic activitieS. ##Purification, crystallization and preliminary X-ray structuralstudies of a 7.2 kDa cytotoxin isolated from the venom of Daboiarusselli russelli of the Viperidae family. DRAMP18148 ATCAGQDQTCKVTCDCCGERGECVCGGPCICRQGNFLIAWYKLASCKK 48 Delta-ctenitoxin-Pn2c (Delta-CNTX-Pn2c; Neurotoxin Pn2-5A; Neurotoxin Tx2-5; PNTx2-5) O76199, P29424 Belongs to the spider toxin Tx2 family Not found Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) Insecticidal Protein level Not found Not found Function: Reversible inhibitor of voltage-gated sodium channels (Nav). Delays the fast inactivation kinetics of neuronal-type sodium channelS. Causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.24 mg/mouse. Insecticidal to the larval and adult forms of the house fly. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9839668##1397265##19231838##16278100##1801316 Toxicon 36:1843-1850 (1998).##FEBS Lett. 310:153-156 (1992).##Biochemistry 48:3078-3088 (2009).##Comp. BiocheM. Physiol. 142:173-187 (2006).##Toxicon 29:1225-1233 (1991). Kalapothakis E., Penaforte C. L., Beirao P.S. L., Romano-Silva M. A., Cruz J.S. , Prado M. A.M. , Guimaraes P.E.M. , Gomez M. V., Prado V.F.##Cordeiro M. N., Diniz C. R., Valentim A.D.C. , von Eickstedt V.R.D., Gilroy J., Richardson M. ##Matavel A., Fleury C. , Oliveira L.C. , Molina F., de Lima M. E., Cruz J.S. , Cordeiro M. N., Richardson M. , Ramos C. H., Beirao P.S. ##Richardson M. , Pimenta A.M. , Bemquerer M. P., Santoro M. M. , Bei Cloning of cDNAS encoding neurotoxic peptides from the spiderPhoneutria nigriventer.##The purification and amino acid sequences of four Tx2 neurotoxinsfrom the venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys).##Structure and activity analysis of two spider toxins that alter sodium channel inactivation kineticS. ##Comparison of the partial proteomes of the venoms of Brazilianspiders of the genus Phoneutria.##Isolation of neurotoxic peptides from the venom of the 'armed' spider DRAMP18149 DCGHLHDPCPNDRPGHRTCCIGLQCRYGKCLVRV 34 U1-TRTX-Sp1a (Orally active insecticidal peptide 1; OAIP-1) K7N5K9 Not found Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level beta sheet (7 strands; 13 residues) Not found 2LL1 resolved by NMR Function: Probable ion channel inhibitor. Shows insecticidal activity. Acts synergistically with the neonicotinoid insecticide imidacloprid. Is neither a repellent that repels insects nor an attractant that is preferentially consumed by insectS. Is very stable. Helicoverpa armigera (LD50=104.2±0.6 pmol/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279##24039872 PLoS ONE 8:E66279-E66279 (2013).##PLoS ONE 8:E73136-E73136 (2013). Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F.##Hardy M. C. , Daly N.L., Mobli M. , Morales R.A., King G.F. SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula.##Isolation of an orally active insecticidal toxin from the venom of anAustralian tarantula. DRAMP01274 QDRPKFCYLPADPAECNAYMPRFYYDSASNKCKEFIYGGCRGNANNFKNRAECRHTCVAS 60 Kunitz-type serine protease inhibitor PIVL; I2G9B4 Belongs to the venom Kunitz-type family Not found Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Viperalebetina transmediterranea) Antitumor Protein level Not found Not found Function: Serine protease inhibitor that inhibits trypsin. Exhibits an anti-tumor effect and displays integrin inhibitory activity without being cytotoxiC. Is able to dose-dependently inhibit the adhesion, migration and invasion of human glioblastoma U87 cellS. Also impairs the function of alphavbeta3 and to a lesser extent, the activity of alphavbeta6, alphavbeta5, alpha1beta1 and alpha5beta1 integrinS. ##Miscellaneous: Does not inhibit chymotrypsin (PubMed: 23262217).When intracerebroventricularly injected into mice, does not cause any toxic symptoms until a dose of 2 ug (PubMed: 23262217). IC50=250 nM on fibrinogen and 300 nM on fibronectin of glioblastoma cell line U87 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23262217 Matrix Biol. 32:52-62 (2013). Morjen M. , Kallech-Ziri O., Bazaa A., Othman H., Mabrouk K., Zouari-Kessentini R., Sanz L., Calvete J.J., Srairi-Abid N., El Ayeb M. , Luis J., Marrakchi N. PIVL, a new serine protease inhibitor from Macrovipera lebetinatransmediterranea venom, impairs motility of human glioblastomacellS. DRAMP01296 ASKCGRHGDSCVSSSDCCPGTWCHTYANRCQVRITEEELMKQREKILGRKGKDY 54 Omega-conotoxin-like protein 1 (OCLP1) H9KQJ7 Not found Not found Apis mellifera (Honeybee) Antimicrobial, Antibacterial Transcript level Not found Not found Function: The impact of this protein on the neuronal activity of the honeybee brain is not known. It does not affect apparent movement or hatching of blowfly larvae. However, when injected into fish, it induces a strong reversible paralytic effect. In addition, the presence of this small peptide in the hemolymph of adult drones together with its induction after bacterial infection suggests that this peptide exhibits antibacterial activity. This peptide may act by inhibiting ion channelS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17433819##22442369 J. Mol. Biol. 369:553-566 (2007).##J. Exp. Biol. 215:1313-1322 (2012). Kaplan N., Morpurgo N., Linial M. ##Gatschenberger H., Gimple O., Tautz J., Beier H. Novel families of toxin-like peptides in insects and mammals: acomputational approach.##Honey bee drones maintain humoral immune competence throughout alllife stages in the absence of vitellogenin production. DRAMP01297 SGYLPGKEYVYKYKGKVF 18 Longipin (Fragment) C0HJF8 Not found Not found Acutisoma longipes (Neotropical harvestman) (Goniosoma longipes) Antimicrobial, Antifungal, Anti-Gram+ Protein level Not found Not found Function: Has moderate antifungal activity. Has weak antimicrobial activity against the Gram-positive bacterium M. luteus A270 (MIC=83 μM) but not against S. aureus ATCC 29213 and S. epidermidis ATCC 12228. Inactive against the Gram-negative bacteria P.aeruginosa ATCC 14502, E.coli ATCC 25922 and E.coli SBS 363. Has no hemolytic activity against human erythrocytes at the highest concentration tested (125 μM).##Introduction: Constitutively expressed. [Swiss_Prot Entry C0HJF8]Fungi: C. albicans MDM8 (MIC=35 μM), C. tropicalis IOC 4560 (MIC=63 μM), C. guilliermondii IOC 4557 (MIC=32 μM), C. albicans IOC 4558 (MIC=125 μM);##Gram-positive bacterium: M. luteus A270 (MIC=83 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (OCT-2013) to the EMBL/GenBank/DDBJ database Sayegh R.S. R. Purification and characterization of antimicrobial peptides presentin the haemolymph of Acutisoma longipes (Gonyleptidae, Opiliones). DRAMP01272 ATCAGQDQPCKETCDCCGERGECVCGGPCICRQGYFWIAWYKLANCKK 48 Delta-ctenitoxin-Pn2a (Delta-CNTX-Pn2a; Neurotoxin Tx2-6; PnTx2-6) P29425, Q95UF2 Belongs to the spider toxin Tx2 family Not found Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) Insecticidal Protein level Not found Not found Function: Irreversible inhibitor of voltage-gated sodium channels (Nav). Binds voltage-dependently to sodium channels and inhibits the inactivation of the activated channelS. Also shifts the voltage dependence of the sodium conductance to negative potentials and decrease the peak inward current. Causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.79 mg/mouse. Is insecticidal to the larval and adult forms of the house fly. Enhances rat erectile function by increasing NO release in the cavernosum tissue. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet sodium channels 12123835##1397265##16278100##19231838##18397797 FEBS Lett. 523:219-223 (2002).##FEBS Lett. 310:153-156 (1992).##Comp. BiocheM. Physiol. 142:173-187 (2006).##Biochemistry 48:3078-3088 (2009).##Toxicon 51:1197-1206 (2008). Matavel A., Cruz J.S. , Penaforte C. L., Araujo D.A.M. , Kalapothakis E., Prado V.F., Diniz C. R., Cordeiro M. N., Beirao P.S. L.##;Cordeiro M. N., Diniz C. R., Valentim A.D.C. , von Eickstedt V.R.D., Gilroy J., Richardson M. ##Richardson M. , Pimenta A.M. , Bemquerer M. P., Santoro M. M. , Beirao P.S. , Lima M. E., Figueiredo S. G., Bloch C. Jr., Vasconcelos E.A., Campos F.A., Gomes P.C. , Cordeiro M. N.##Matavel A., Fleury C. , Oliveira Electrophysiological characterization and molecular identification ofthe Phoneutria nigriventer peptide toxin PnTx2-6.##The purification and amino acid sequences of four Tx2 neurotoxinsfrom the venom of the Brazilian ‘armed' spider Phoneutria nigriventer (Keys).##Comparison of the partial proteomes of the venoms of Brazilianspiders of the genus Phoneutria.##Structure and activity analysis of two spider toxins that altersodium channel inactivation kineticS. ##Tx2-6 toxin of the Phoneutria nigrive DRAMP02595 GWLRKAAKSVGKFYYKHKYYIKAAWQIGKHAL 32 Styelin-D (Styelin D; chordates) O18495 Not found Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial Protein level Not found Not found Function: Bactericidal against several Gram-positive and Gram- negative bacteria.PTM:Contains L-DOPA (3',4'-dihydroxyphenylalanine) No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9257708##10978343 FEBS Lett. 412:144-148(1997).##J. Biol. Chem. 275:38417-38426(2000). Zhao C., Liaw L., Lee I.H., Lehrer R.I.##Taylor S.W., Craig A.G., Fischer W.H., Park M., Lehrer R.I. cDNA cloning of three cecropin-like antimicrobial peptides (Styelins)from the tunicate, Styela clava.##Styelin D, an extensively modified antimicrobial peptide fromascidian hemocytes. DRAMP02515 RVKRVLPLVIRTVIAGYNLYRAIKRK 26 Cc-CATH1 No entry found Not found Not found Coturnix coturnix Not found Not found Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21375690 FEBS J. 2011 May;278(9):1573-1584. Feng F, Chen C, Zhu W, He W, Guang H, Li Z, Wang D, Liu J, Chen M, Wang Y, Yu H. Gene cloning, expression, and characterization of avian cathelicidin orthologue, Cc-CATHs, from Coturnix coturnix. DRAMP18184 SIGNKGISFETCTAIEGLCFFGCKLGWVWIAYCNNIMSCCRKDTDFVLPQTKGI 54 Beta-defensin 42 (BD-42, mBD-42 ) Q8BVB5, Q4FZ54 Belongs to the beta-defensin family. Defb42 Mus musculus (Mouse) Antimicrobial, Antibacterial Transcript level Not found Not found Function: Has bactericidal activity (By similarity). May play a role in the antimicrobial protection of sperm and urogenital tract epithelia. Epididymis-specific, with highest levels in the initial segment and distal caput. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16033865##16141072##19468303##15489334##16023745 Physiol. Genomics 23:5-17(2005)##Science 309:1559-1563(2005)##PLoS Biol. 7:E1000112-E1000112(2009)##Genome Res. 14:2121-2127(2004)##Biochim. Biophys. Acta 1730:22-30(2005) Patil A.A., Cai Y., Sang Y., Blecha F., Zhang G.##Carninci P., Kasukawa T., Katayama S. et al.##Church D.M., Goodstadt L., Hillier L.W. et al.##The MGC Project Team##Jalkanen J., Huhtaniemi I., Poutanen M. Cross-species analysis of the mammalian beta-defensin gene family:presence of syntenic gene clusters and preferential expression in themale reproductive tract.##The transcriptional landscape of the mammalian genome.##Lineage-specific biology revealed by a finished genome assembly ofthe mouse.##The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).##Discovery and characterization of new epididymis-specific beta-defensins in mice. DRAMP18405 VTQPLAPVHNPISV 14 PDC213 (beta-casein 213-224, human) No entry found Not found Not found milk, Homo sapiens Antimicrobial, Antibacterial Not found Not found It is a endogenous peptide with higher levels in preterm milk. Active against S. aureus and Y. enterocolitica (80% inhibition at 15 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28093229 Biochem Biophys Res Commun. 2017 Feb 26;484(1):132-137. Sun Y, Zhou Y, Liu X, Zhang F, Yan L, Chen L, Wang X, Ruan H, Ji C, Cui X, Wang J. Antimicrobial activity and mechanism of PDC213, an endogenous peptide from human milk. DRAMP18406 KEICCKELTKPVKCSSDPLCQKLCMEKEKYEDGHCFTILSKCLCMKRCNAKTLATELLA 59 CaThi (thionin-like peptide 2; plants) No entry found Not found Not found Fruits, Capsicum annuum Antimicrobial, Antifungal Bridge Not found Comment: No comments found on DRAMP database Active against C. albicans CE022, C. tropicalis CE017, C. parapsilosis CE002 (IC50 10 ug/ml), C. pelliculosa 3974 (IC50 40 ug/ml), and C. mogii 4674 (IC50 20 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23896704##26819228 Biopolymers. 2014 Jan;102(1):30-9.##BMC Microbiol. 2016 Jan 27;16:12. Taveira GB, Mathias LS, da Motta OV, Machado OL, Rodrigues R, Carvalho AO, Teixeira-Ferreira A, Perales J, Vasconcelos IM, Gomes VM.##Taveira GB, Carvalho AO, Rodrigues R, Trindade FG, Da Cunha M, Gomes VM. Thionin-like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts.##Thionin-like peptide from Capsicum annuum fruits: mechanism of action and synergism with fluconazole against Candida species. DRAMP18407 KEICCKVPTTPFLCTNDPQCKTLCSKVNYEDGHCFDILSKCVCMNRCVQDAKTLAAELIEEEFLKQ 66 Thionin-like peptide 1 (plants) No entry found Not found Not found Fruits, Capsicum annuum Antimicrobial, Antibacterial, Antifungal Bridge Not found Comment: No comments found on DRAMP database Active against S. cerevisiae, C. albicans, C. tropicalis, E. coli and P. aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23896704 Biopolymers. 2014 Jan;102(1):30-9. Taveira GB, Mathias LS, da Motta OV, Machado OL, Rodrigues R, Carvalho AO, Teixeira-Ferreira A, Perales J, Vasconcelos IM, Gomes VM. Thionin-like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts DRAMP18408 EVCEKASKTWSGNCGNTGHC 20 Dm-AMP2 (Dahlia defensin, plants) No entry found Belongs to the defensin family. Not found seeds, Dahlia merckii Antimicrobial, Antifungal Bridge Not found Fuction: The sequence is not yet complete.In medium A supplemented with 1 mM CaCl2 and 50 mM KCl, the peptide is active against fungi B. cinerea (IC50 10 ug/ml), C. sphaerospermum (IC50 3 ug/ml), F. culmorum (IC50 3 ug/ml), L. maculans (IC50 1.0 ug/ml), P. digitatum (IC50 2 ug/ml), S. tritici (IC50 1 ug/ml), and V. albo-atrum (IC50 2 ug/ml). Active against fungi B. cinerea (IC50 10 ug/ml), C. sphaerospermum (IC50 3 ug/ml), F. culmorum (IC50 3 ug/ml), L. maculans (IC50 1.0 ug/ml), P. digitatum (IC50 2 ug/ml), S. tritici (IC50 1 ug/ml), and V. albo-atrum (IC50 2 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7628617 FEBS Lett. 1995 Jul 17;368(2):257-62 Attenborough S, Rees SB, Broekaert WF. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae DRAMP18409 INWKKIKSIIKAAMN 15 Mastoparan V1 (MP-V1, insects, arthropods, invertebrates, animals) No entry found Not found Not found Venom; Social Wasp, Vespula vulgaris Antimicrobial, Antibacterial, Antifungal Helix Not found Weak hemolysis 6.6% at 50 uM (20% at 100 uM). Active against S. mutans, S. enterica, and S. aureus (MIC 50 uM), and C. albicans, C. grabrata (MIC 50 uM), and C. neoformans (MIC 0.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27104500 Molecules. 2016 Apr 19;21(4):512. Kim Y, Son M, Noh EY, Kim S, Kim C, Yeo JH, Park C, Lee KW, Bang WY. MP-V1 from the Venom of Social Wasp Vespula vulgaris Is a de Novo Type of Mastoparan that Displays Superior Antimicrobial Activities. DRAMP18410 ITCQQVTXELEPCVPYLTQGIP 22 Cc-LTP2 (Coffea canephora lipid transfer protein 2, plants) No entry found Not found Not found seeds, Coffea canephora Pierre Antimicrobial, Antibacterial, Antifungal Not found Not found The sequence is not yet complete. Active against Gram- bacteria X. euvesicatoria (inhibition zone of 0.25 mm at 75 ug/ml), and can permeate the memrbane of fungi F. solani at 200 ug/ml. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27813588 Genet Mol Res. 2016 Oct 24;15(4). Bard GC, Zottich U, Souza TA, Ribeiro SF, Dias GB, Pireda S, Da Cunha M, Rodrigues R, Pereira LS, Machado OL, Carvalho AO, Gomes VM. Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Coffea canephora seeds. DRAMP18411 NGNLLGGLLRPVLGVVKGLTGGLGKK 26 Thaulin-1 (frog, amphibians, animals; Other sequences reported: Thaulin-2, Thaulin-3, Thaulin-4) No entry found Not found Not found skin, a Patagonian frog, Pleurodema thaul, South America Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against E. coli ATCC 25922 (MIC 62.5 ug/ml), K. pneumoniae (MIC 125 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28025119 Gene. 2017 Mar 20;605:70-80 Marani MM, Perez LO, de Araujo AR, Pl Thaulin-1: The first antimicrobial peptide isolated from the skin of a Patagonian frog Pleurodema thaul (Anura: Leptodactylidae: Leiuperinae) with activity against Escherichia coli. DRAMP18412 SGYLPGKEYVYKYKGKVF 18 Longipin (arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found hemolymph, Acutisoma longipes Antimicrobial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against M. luteus A270, Gram- P. aeruginosa ATCC27853, S. marcescens ATCC4112 (MIC 60-120 uM), fungi C. albicans MDM8 (MIC 15-30 uM), C. albicans IOC4558 (7.5-15 uM), C. guilliermondii and C. tropicalis (MIC 3.8-7.5 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27997568 PLoS One. 2016 Dec 20;11(12):e0167953. Sayegh RS, Batista IF, Melo RL, Riske KA, Daffre S, Montich G, da Silva Junior PI Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles DRAMP18413 FFSMIPKIAGGIASLVKNLG 20 Phylloseptin-PBa (frog, amphibians, animals) No entry found Not found Not found the Peruvian Purple-Sided Leaf Frog, Phyllomedusa baltea , South America Antimicrobial, Antibacterial, Antifungal Not found Not found Fuction: It exhibited anti-proliferative activity against the human cancer cell lines, H460, PC3 and U251MG, but was less active against a normal human cell line (HMEC). Active against S. aureus (MIC 8 ug/ml), E. coli (MIC 128 ug/ml) and C. albicans (MIC 8 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26633506 Toxins (Basel). 2015 Dec 1;7(12):5182-93 Wan Y, Ma C, Zhou M, Xi X, Li L, Wu D, Wang L, Lin C, Lopez JC, Chen T, Shaw C Phylloseptin-PBa--A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity. DRAMP18414 GILGKIWEGVKSLI 14 NDBP-5.8 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Opisthacanthus cayaporum Antimicrobial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against C. albicans SC5314 (MIC 100 uM), C. tropicalis ATCC 750 (MIC 25 uM), C. parapsilosis ATCC 22019 (MIC 200 uM), C. neoformans H99 serotype A (MIC 100 uM), and C. neoformans B3501 serotype D (MIC 50 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27917162 Front Microbiol. 2016 Nov 18;7:1844. Guilhelmelli F, Vilela N, Smidt KS, de Oliveira MA, da Cunha Morales ?lvares A, Rigonatto MC, da Silva Costa PH, Tavares AH, de Freitas SM, Nicola AM, Franco OL, Derengowski LD, Schwartz EF, Mortari MR, Bocca AL, Albuquerque P, Silva-Pereira I. Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms DRAMP18415 FWSFLVKAASKILPSLIGGGDDNKSSS 27 Con10 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Opisthacanthus cayaporum Antimicrobial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against C. albicans SC5314 (MIC 100 uM), C. tropicalis ATCC 750 (MIC 12.5 uM), C. parapsilosis ATCC 22019 (MIC 200 uM), C. glabrata ATCC 90030 (MIC 200 uM), C. neoformans H99 serotype A (MIC 50 uM), and C. neoformans B3501 serotype D (MIC 25 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27917162 Front Microbiol. 2016 Nov 18;7:1844 Guilhelmelli F, Vilela N, Smidt KS, de Oliveira MA, da Cunha Morales ?lvares A, Rigonatto MC, da Silva Costa PH, Tavares AH, de Freitas SM, Nicola AM, Franco OL, Derengowski LD, Schwartz EF, Mortari MR, Bocca AL, Albuquerque P, Silva-Pereira I. Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms DRAMP18416 FIGMIPGLIGGLISAIK 17 ToAP3 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Tityus obscurus Antimicrobial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against C. albicans SC5314 (MIC 25 uM), C. tropicalis ATCC 750 (MIC 12.5 uM), C. parapsilosis ATCC 22019 (MIC 100 uM), C. neoformans H99 serotype A (MIC 100 uM), and C. neoformans B3501 serotype D (MIC 25 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27917162 Front Microbiol. 2016 Nov 18;7:1844 Guilhelmelli F, Vilela N, Smidt KS, de Oliveira MA, da Cunha Morales ?lvares A, Rigonatto MC, da Silva Costa PH, Tavares AH, de Freitas SM, Nicola AM, Franco OL, Derengowski LD, Schwartz EF, Mortari MR, Bocca AL, Albuquerque P, Silva-Pereira I. Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms DRAMP03018 INMKASAAVAKKLL 14 MP-VB1 (Insects, animals) No entry found Not found Not found vespine wasps Vespa bicolor Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Has antimicrobial activities against standard strains and strong antimicrobial ability against drug-resistant strains. Among the tested drug-resistant strains, Pseudemonas aeruginosa and Staphylococcus aureus were the most sensitive for this kind of antimicrobial peptide. Has a little hemolytic activity. [Ref.18723059] Gram-negative bacterium: Escherichia coli ATCC25922(MIC=15.0μg/ml), Escherichia coli 23A(MIC=15.0μg/ml), Escherichia coli 27A(MIC=60.0μg/ml), Pseudemonas aeruginosa 3A(MIC=15.0μg/ml), Pseudemonas aeruginosa 7A(MIC=120.0μg/ml), ;## Gram-positive bacterium: Staphylococcus aureus ATCC2592(MIC=3.75μg/ml), Staphylococcus aureus 6A(MIC=1.9μg/ml), Staphylococcus aureus 15A(MIC=3.75μg/ml);## Fungus: Candida albicans ATCC2002(MIC=15.0μg/ml) [Ref.18723059] MP-VB1 had almost no hemolytic activity of 1.7% and 2.7% against rabbit and human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18723059 Peptides. 2008 Nov;29(11):1887-1892. Chen W, Yang X, Yang X, Zhai L, Lu Z, Liu J, Yu H. Antimicrobial peptides from the venoms of Vespa bicolor Fabricius. DRAMP01875 GLMSLFRGVLKTAGKHIFKNVGGSLLDQAKCKITGEC 37 Brevinin-2PRa (Frogs, amphibians, animals) No entry found Not found Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC=6μM), Pseudemonas aeruginosa(MIC=3μM), Enterobacter cloacae(MIC=6μM), Klebsiella pneumoniae(MIC=6μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=25μM);## Yeast: Candida albicans(MIC>100μM) [Ref.15003829] HC50=55 μM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 15003829 Regul Pept. 2004 May 15;118(3):135-141. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP01876 GLMSLFRGGVLKTAGKHIFKNVGGSLLDQAKCKITGEC 38 Brevinin-2PRb (Frogs, amphibians, animals) No entry found Not found Not found Rana pirica (Hokkaido frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: activity against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. [Ref.15003829] Gram-negative bacterium: Escherichia coli(MIC=3μM), Pseudemonas aeruginosa(MIC=3μM), Enterobacter cloacae(MIC=6μM), Klebsiella pneumoniae(MIC=6μM);## Gram-positive bacterium: Staphylococcus aureus(MIC=25μM);## Yeast: Candida albicans(MIC>100μM) [Ref.15003829] HC50=65 μM against human erythrocytes Cyclic Free Cyclization (Cys31 and Cys37) Disulfide bond between Cys31 and Cys37. L No cytotoxicity information found Not found 15003829 Regul Pept. 2004 May 15;118(3):135-141. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, P A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. DRAMP18421 GFGCPKSALSCSQQCRENNTHSGGYCNGPFNIVCSCY 37 DefMT7 (defensin MT7; hard ticks, arachnids, arthropods, invertebrates, animals) No entry found Belongs to the defensin family. Not found Ixodes ricinus Antiparasitic, Antimalarial Bridge Not found Fuction: The peptide showed no activity against bacteria. It showed antimalarial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27822206##26255244 Front Microbiol. 2016 Oct 24;7:1682. ##Dev Comp Immunol. 2015 Dec;53(2):358-65. Cabezas-Cruz A, Tonk M, Bouchut A, Pierrot C, Pierce RJ, Kotsyfakis M, Rahnamaeian M, Vilcinskas A, Khalife J, Vald Antiplasmodial Activity Is an Ancient and Conserved Feature of Tick Defensins.##Ixodes ricinus defensins attack distantly-related pathogens. DRAMP18422 GYFCPYNGYCDHHCRKKLRWRGGYCGGRWKLTCICVRG 38 DefMT2 (defensin MT2;hard ticks, arachnids, arthropods, invertebrates, animals) No entry found Belongs to the defensin family. Not found Ixodes ricinus Antiparasitic, Antimalarial Bridge Not found Fuction: The peptide showed no activity against bacteria. It showed antimalarial activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27822206##26255244 Front Microbiol. 2016 Oct 24;7:1682. ##Dev Comp Immunol. 2015 Dec;53(2):358-65. Cabezas-Cruz A, Tonk M, Bouchut A, Pierrot C, Pierce RJ, Kotsyfakis M, Rahnamaeian M, Vilcinskas A, Khalife J, Vald Antiplasmodial Activity Is an Ancient and Conserved Feature of Tick Defensins.##Ixodes ricinus defensins attack distantly-related pathogens. DRAMP18423 EEESEVAHLRVRRGFGCPLNQGACHRHCRSIRRRGGYCSGIIKQTCTCYRN 51 HEdefensin (arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found hemolymph, Haemaphysalis longicornis Antimicrobial, Antiviral Bridge Not found Fuction: The synthetic peptide showed virucidal activity against Langat virus (LGTV). No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27871830 Dev Comp Immunol. 2017 Mar;68:98-107 Talactac MR, Yada Y, Yoshii K, Hernandez EP, Kusakisako K, Hiroki M, Galay RL, Fujisaki K, Mochizuki M, Tanaka T Characterization and antiviral activity of a newly identified defensin-like peptide, HEdefensin, in the hard tick Haemaphysalis longicornis DRAMP18424 TLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 58 TLN-58 (TLN58; human cathelicidin) No entry found Not found Not found the lesion vesicle, skin, Homo sapiens Antimicrobial, Antibacterial Not found Not found 2K6O##2FCG##2LMF##4EYC TLN-58 is an alternative processed form of hCAP-18, the precursor of human LL-37 and ALL-38. TLN-58 upregulated IL-17C, IL-8, IL-23, IL-1alpha, and IL-1beta mRNA and protein expression in normal human keratinocytes, similar to LL-37. Active against S. aureus, S. epidermidis, and Group A Streptococcus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27771329 J Invest Dermatol. 2017 Feb;137(2):322-331 Murakami M, Kameda K, Tsumoto H, Tsuda T, Masuda K, Utsunomiya R, Mori H, Miura Y, Sayama K. TLN-58, an additional hCAP18 processing form, found in the lesion vesicle of palmoplantar pustulosis in the skin. DRAMP18425 GVFDIIKGAGKQLIAHAMEKIAEKVGLNKDGN 32 Ocellatin-PT6 (frog, amphibians, animals) No entry found Not found Not found Skin Secretion, dorsal, Leptodactylus pustulatus Not found Helix Not found Fuction: It has leishmanicidal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26107622##27463422 J Nat Prod. 2015 Jul 24;78(7):1495-504. ##Biopolymers. 2016 Dec;105(12):873-86. Marani MM, Dourado FS, Quelemes PV, de Araujo AR, Perfeito ML, Barbosa EA, V Characterization and Biological Activities of Ocellatin Peptides from the Skin Secretion of the Frog Leptodactylus pustulatus. ##Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems. DRAMP18426 GVIDIIKGAGKDLIAHAIGKLAEKV 25 Ocellatin-PT3 (frog, amphibians, animals) No entry found Not found Not found Skin Secretion, dorsal, Leptodactylus pustulatus Antiparasitic Helix Not found Fuction: It has leishmanicidal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26107622##27463422 J Nat Prod. 2015 Jul 24;78(7):1495-504. ##Biopolymers. 2016 Dec;105(12):873-86. Marani MM, Dourado FS, Quelemes PV, de Araujo AR, Perfeito ML, Barbosa EA, V Characterization and Biological Activities of Ocellatin Peptides from the Skin Secretion of the Frog Leptodactylus pustulatus. ##Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems. DRAMP18427 DKGRRRSKFVLHRRQCAN 18 MrDN (pellino-1 derived, Crustaceans, arthropods, invertebrates, animals) No entry found Not found Not found Giant freshwater prawn, Macrobrachium rosenbergii Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27648859 Mol Immunol. 2016 Oct;78:171-182. Ravichandran G, Kumaresan V, Arasu MV, Al-Dhabi NA, Ganesh MR, Mahesh A, Dhayalan A, Pasupuleti M, Arockiaraj J Pellino-1 derived cationic antimicrobial prawn peptide: Bactericidal activity, toxicity and mode of action DRAMP18428 KRIRFFERIRDRLRDLGNRIKNRIRDFFS 29 Saha-CATH6 (cathelicidins; mammals, animals) No entry found Not found Not found Tasmanian devil, Sarcophilus harrisii Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27725697 Sci Rep. 2016 Oct 11;6:35019 Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K Cathelicidins in the Tasmanian devil (Sarcophilus harrisii). DRAMP18429 KRIGLIRLIGKILRGLRRLG 20 Saha-CATH5 (cathelicidins; mammals, animals) No entry found Not found Not found Tasmanian devil, Sarcophilus harrisii Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli ATCC 25922, P. aeruginosa, E. faecalis, S. aureus ATCC 29213 (MRSA), S. pneumoniae ATCC 49619, S. pyogenes ATCC 19615, S. agalactiae ATCC 12386, S. agalactiae, S. anginosus, S. equi, and C. neoformans (MIC 32-64 ug/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27725697 Sci Rep. 2016 Oct 11;6:35019 Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K Cathelicidins in the Tasmanian devil (Sarcophilus harrisii). DRAMP18430 KRMGIFHLFWAGLRKLGNLIKNKIQQGIENFLG 33 Saha-CATH3 (cathelicidins; mammals, animals) No entry found Not found Not found Tasmanian devil, Sarcophilus harrisii Antimicrobial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against C. neoformans (MIC 16 ug/mL). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27725697 Sci Rep. 2016 Oct 11;6:35019 Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K Cathelicidins in the Tasmanian devil (Sarcophilus harrisii). DRAMP18431 GHLGRPYIGGGGGFNRGGGFHRGGGFHRGGGFQSGGGFHRGGGFHSGGSFGYR 53 Armadillidin Q (Gly-rich; Terrestrial Isopod, Crustaceans, arthropods, invertebrates, animals) No entry found Not found Not found haemocytes, Armadillidium vulgare Antimicrobial, Antibacterial, Antifungal Rich Not found Comment: No comments found on DRAMP database Active against B. megaterium F04 (MBC 4.75 uM) and P. syringae DC3000 (MBC 1.18 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 27713732 Front Microbiol. 2016 Sep 22;7:1484. Verdon J, Coutos-Thevenot P, Rodier MH, Landon C, Depayras S, Noel C, La Camera S, Moumen B, Greve P, Bouchon D, Berjeaud JM, Braquart-Varnier C Armadillidin H, a Glycine-Rich Peptide from the Terrestrial Crustacean Armadillidium vulgare, Displays an Unexpected Wide Antimicrobial Spectrum with Membranolytic Activity DRAMP18432 GLLSALRKMIPHILSHIKK 19 Antapin (ANTP; insects, arthropods, invertebrates, animals) No entry found Not found Not found wild bee, Anthophora plumipes Antimicrobial, Antibacterial Helix Not found It became more helical in the presence of TFE, SDS, or anionic lipids. Active against B. subtilis, E. coli, S. aureus, and P. aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found J. Pept. Sci., 2014; 20:S263 S. Cujov Structural study of a novel antimicrobial peptide isolated from the venom of bee Anthophora plumipes DRAMP18433 GSEIRGPCIDRFCRVICRNNGYESGHCNRWARGCSCASWIGR 42 Cremycin-15 (nematode; invertebrates, animals) No entry found Not found Not found Caenorhabditis remanei Antimicrobial, Antibacterial, Anti-Gram+ Bridge Not found Comment: No comments found on DRAMP database Active against Gram-positive bacteria B. megaterium and S. marcescens (CL 14.1-17.7 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24434635 Nat Commun. 2014;5:3154. Zhu S, Gao B. Nematode-derived drosomycin-type antifungal peptides provide evidence for plant-to-ecdysozoan horizontal transfer of a disease resistance gene DRAMP18434 VKSGHYKGPCYHDENCNGVCRDEGYKSGHCSRWGGACWCDT 41 Cremycin-5 (nematode; invertebrates, animals) No entry found Not found Not found Caenorhabditis remanei Antimicrobial, Antifungal Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 24434635 Nat Commun. 2014;5:3154. Zhu S, Gao B. Nematode-derived drosomycin-type antifungal peptides provide evidence for plant-to-ecdysozoan horizontal transfer of a disease resistance gene DRAMP18435 VWTVWGTIAG 10 Labaditin (plants) No entry found Not found Not found Not found Antimicrobial, Antibacterial Not found Not found The cyclic structure is critical for antimicrobial activity against S. aureus. Active against S. mutans and S. aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20563613##27665378 Amino Acids. 2011 Jan;40(1):135-44.##Colloids Surf B Biointerfaces. 2016 Dec 1;148:453-459. Barbosa SC, Cilli EM, Dias LG, Stabeli RG, Ciancaglini P.##Barbosa SC, Nobre TM, Volpati D, Ciancaglini P, Cilli EM, Lorenz Labaditin, a cyclic peptide with rich biotechnological potential: preliminary toxicological studies and structural changes in water and lipid membrane environment. ##The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus. DRAMP18436 RTCESKSHRFKGPCVSTHNCANVCHNEGFGGGKCRGFRRRCYCTRHC 47 AtPDF2.3 (flowering plants) No entry found Not found Not found Arabidopsis thaliana Antimicrobial, Antifungal Bridge Not found Comment: No comments found on DRAMP database Active against S. cerevisiae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27573545 Sci Rep. 2016 Aug 30;6:32121. Vriens K, Peigneur S, De Coninck B, Tytgat J, Cammue BP, Thevissen K. The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels. DRAMP18437 LTCDLLSFEAKGFAANHSLCAAHCLAIGRKGGACQNGVCVCRR 43 Oryctes rhinoceros defensin (insects, arthropods, invertebrate, animals) No entry found Belongs to the defensin family. Not found Coconut rhinoceros beetle, Oryctes rhinoceros Antimicrobial, Antibacterial Bridge Not found Comment: No comments found on DRAMP database Active against S. aureus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10561605 Eur J Biochem. 1999 Dec;266(2):616-23 Ishibashi J, Saido-Sakanaka H, Yang J, Sagisaka A, Yamakawa M. Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros DRAMP18438 FFGRLKSMWRGARGGLKAYKYQKDMAKMNKRYGPNWQQGGGQEPPADAQANDQPP 55 SB Piscidin 6 (fish, animals) No entry found Not found Not found Morone saxatilis Antimicrobial, Antibacterial, Antiparasitic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27552222 PLoS One. 2016 Aug 23;11(8):e0159423. Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes DRAMP18439 LFGSVKAWFKGAKKGFQDYRYQKDMAKMNKRYGPNWQQRGGQEPPADAQANDQPP 55 WB Piscidin 6 (fish, animals) No entry found Not found Not found Morone chrysops Antimicrobial, Antibacterial, Antiparasitic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27552222 PLoS One. 2016 Aug 23;11(8):e0159423. Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes DRAMP18440 LIGSLFRGAKAIFRGARQGWRSHKAVSRYRARYVRRPVIYYHRVYP 46 WB Piscidin 5 (fish, animals) No entry found Not found Not found Morone chrysops Antimicrobial, Antibacterial, Antiparasitic Not found Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27552222 PLoS One. 2016 Aug 23;11(8):e0159423. Salger SA, Cassady KR, Reading BJ, Noga EJ A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes DRAMP18441 SYVGDCGSNGGSCVSSYCPYGNRLNYFCPLGRTCCRRSY 39 Panusin (beta defensins; crustaceans, arthropods, invertebrates, animals) No entry found Belongs to the beta-defensin family. Not found the Caribbean spiny lobster, Panulirus genus Antimicrobial, Antibacterial, Antifungal Bridge Not found Comment: No comments found on DRAMP database Active against E. coli, K. pneumonia, S. aureus, B. subtilisspizizenii, and C. albicans. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27616720 Dev Comp Immunol. 2017 Feb;67:310-321 Montero-Alejo V, Corzo G, Porro-Suard Panusin represents a new family of beta-defensin-like peptides in invertebrates. DRAMP18442 GVWDWIKKTAGKIWNSEPVKALKSQALNAAKNFVAEKIGATPS 43 Smp43 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found venom, Scorpio maurus palmatus Antimicrobial, Antibacterial, Antifungal Helix Not found Comment: No comments found on DRAMP database Active against B. subtilis NCIMB 8024 (MIC 4 ug/ml), S. epidermidis sp., S. aureus SH100 (MIC 32-64 ug/ml), E. coli JM109, K. pneumoniae NCTC 13439, and C. albicans (MIC 64-128 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 27019370 Toxicon. 2016 Jul;117:30-6. Harrison PL, Abdel-Rahman MA, Strong PN, Tawfik MM, Miller K. Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus DRAMP18443 IWSFLIKAATKLLPSLFGGGKKDS 24 Smp24 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found venom, Scorpio maurus palmatus Antimicrobial, Antibacterial, Antifungal Helix Not found Removal of the N-terminal four residues increases peptide cell selectivity. Active against B. subtilis NCIMB 8024, S. epidermidis sp., S. aureus SH100 (MIC 4-8 ug/ml), E. coli JM109 (MIC 64 ug/ml), and C. albicans (MIC 32 ug/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrance 27019370 Toxicon. 2016 Jul;117:30-6. Harrison PL, Abdel-Rahman MA, Strong PN, Tawfik MM, Miller K. Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus DRAMP18444 RYPAVGYT 8 Lacrain (myriapods, arthropods, invertebrates, animals) No entry found Not found Not found Brazilian centipede, Scolopendra viridicornis Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.27451089]Gram-negative bacteria : Pseudomonas aeruginosa ATCC 27853 (MIC=5.8 μg/ml;MBC=11.6 μg/ml), Alcaligenes faecalis ATCC 8750 (MIC=5.8 μg/ml;MBC=5.8 μg/ml), Serratia marcescens ATCC 4112 (MIC=5.8 μg/ml;MBC=5.8 μg/ml), Enterobacter cloacae β-12 (MIC=2.9 μg/ml;MBC=2.9 μg/ml), Salmonella serovars (MIC=5.8 μg/ml;MBC=11.6 μg/ml), Salmonella enterica subsp. arizonae (MIC=5.8 μg/ml;MBC=5.8 μg/ml), Escherichia coli SBS363 (MIC=5.8 μg/ml;MBC=5.8 μg/ml), Escherichia coli D31 (MIC=5.8 μg/ml;MBC=5.8 μg/ml) [Ref.27451089] 0% hemolysis at 0.5-500 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27451089 Int J Antimicrob Agents. 2016 Sep;48(3):277-85. doi: 10.1016/j.ijantimicag.2016.05.015. E. Chaparro,P.I. da Silva Junior Lacrain: the first antimicrobial peptide from the body extract of the Brazilian centipede Scolopendra viridicornis DRAMP18445 AATKPKKAGAEAAPKKPAKKQTKKKPAKKAGGKKKPKRAGAKKAKK 46 hdMolluscidin (mollusca/molluscs/mollusks, invertebrates, animals; Lys-rich; Ala-rich) No entry found Not found Not found gill, the abalone, Haliotis discus Antimicrobial, Antibacterial Not found Not found No hemolysis at 100 ug/mL. May target an intracellular target. Active against B. subtilis KCTC1021, B. subtilis RM125, S. aureus RM4220, E. coli D31, E. coli KCTC1116, P. aeruginosa KCTC2004, S. enterica KCTC2514, S. flexneri KCTC2517 (MIC 0.2-3.9 uM), fish pathogen A. hydrophila KCTC2358, and V. parahemolyticus KCCM41664 (MIC 0.4-0.7 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27033467 Fish Shellfish Immunol. 2016 May;52:289-97. Seo JK, Go HJ, Kim CH, Nam BH, Park NG. DRAMP18446 HKMDLHWYLRTLEEVVIRALQRFQFR 26 Gm0026x00785(77 No entry found Not found Not found soybean, Glycine max Antimicrobial, Antibacterial Not found Not found It inhibited the in vitro growth of X. axonopodis pv. glycines, the causative agent of the bacterial pustule disease, at 10 uM. Also active ex vivo and in vivo after vector transformation. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23029273 PLoS One. 2012;7(9):e45848. Brand GD, Magalh?es MT, Tinoco ML, Arag?o FJ, Nicoli J, Kelly SM, Cooper A, Bloch C Jr. Probing protein sequences as sources for encrypted antimicrobial peptides. DRAMP18447 RWRFLRKISSVHMFSVKALDDFRQL 25 Gm0025x00667(75 No entry found Not found Not found soybean, Glycine max Antimicrobial, Antibacterial Not found Not found It inhibited the in vitro growth of X. axonopodis pv. glycines, the causative agent of the bacterial pustule disease, at 5 uM. Also active ex vivo and in vivo after vector transformation. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23029273 PLoS One. 2012;7(9):e45848. Brand GD, Magalh?es MT, Tinoco ML, Arag?o FJ, Nicoli J, Kelly SM, Cooper A, Bloch C Jr. Probing protein sequences as sources for encrypted antimicrobial peptides. DRAMP18448 INNWVRVPPCDQVCSRSNPEKDECCRAHGHAFHAHCNGGMNCYRR 45 Diapausin-1 (insects, arthropods, invertebrates, animals) No entry found Not found Not found hemolymph, tobacco hornworm, Manduca sexta Antimicrobial, Antifungal Bridge Not found Fuction: Active against FUNGI such as S. cerevisiae (IC50 12 uM) but not bacteria. The peptide is inducible since mRNA level in fact body increased after yeast challege of larvae. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26976231 Dev Comp Immunol. 2016 Aug;61:258-68. Al Souhail Q, Hiromasa Y, Rahnamaeian M, Giraldo MC, Takahashi D, Valent B, Vilcinskas A, Kanost MR. Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta. DRAMP18449 AVNIPFKVHLRCKAAFC 17 Kunitzin-OS (amphibians, animals) No entry found Not found Not found Chinese frog, Odorrana schmackeri Antibacterial, Enzyme inhibitor, Anti-Gram-, Antimicrobial Not found Not found Comment: No comments found on DRAMP database Gram-negative bacteria: E. coli (MIC 20 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27311856 Biochem Biophys Res Commun. 2016 Aug 19;477(2):302-9. Chen X, Wang H, Shen Y, Wang L, Zhou M, Chen T, Shaw C. Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs DRAMP18450 AAKIILNPKFRCKAAFC 17 Kunitzin-RE (amphibians, animals) No entry found Not found Not found European frog, Rana esculenta Antibacterial, Enzyme inhibitor, Anti-Gram-, Antimicrobial Not found Not found Fuction: A change of the last K to F reduced activity (MIC 160 uM). Gram-negative bacteria: E. coli (MIC 30 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27311856 Biochem Biophys Res Commun. 2016 Aug 19;477(2):302-9. Chen X, Wang H, Shen Y, Wang L, Zhou M, Chen T, Shaw C. Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs DRAMP18451 GFLDVVKHIGKAALGAVTHLINQ 23 CZS-3 (cruzioseptin-3; frog, amphibians, animals) No entry found Not found Not found the splendid leaf frog, Cruziohyla calcarifer, South America Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli (13.3 uM), S. aureus (13.3 uM), and C. albicans (13.3 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27321580 J Proteomics. 2016 Sep 2;146:1-13. Proa?o-Bola?os C, Zhou M, Wang L, Coloma LA, Chen T, Shaw C. Peptidomic approach identifies cruzioseptins, a new family of potent antimicrobial peptides in the splendid leaf frog, Cruziohyla calcarifer. DRAMP18452 GFLDVIKHVGKAALGVVTHLINQ 23 CZS-2 (cruzioseptin-2; frog, amphibians, animals) No entry found Not found Not found the splendid leaf frog, Cruziohyla calcarifer, South America Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli (26.3 uM), S. aureus (6.6 uM), and C. albicans (13.2 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27321580 J Proteomics. 2016 Sep 2;146:1-13. Proa?o-Bola?os C, Zhou M, Wang L, Coloma LA, Chen T, Shaw C. Peptidomic approach identifies cruzioseptins, a new family of potent antimicrobial peptides in the splendid leaf frog, Cruziohyla calcarifer. DRAMP18453 GFLDIVKGVGKVALGAVSKLF 21 CZS-1 (cruzioseptin-1; frog, amphibians, animals) No entry found Not found Not found the splendid leaf frog, Cruziohyla calcarifer, South America Antimicrobial, Antibacterial, Antifungal Not found Not found Comment: No comments found on DRAMP database Active against E. coli (15.1 uM), S. aureus (3.8 uM), and C. albicans (3.8 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27321580 J Proteomics. 2016 Sep 2;146:1-13. Proa?o-Bola?os C, Zhou M, Wang L, Coloma LA, Chen T, Shaw C. Peptidomic approach identifies cruzioseptins, a new family of potent antimicrobial peptides in the splendid leaf frog, Cruziohyla calcarifer. DRAMP18454 FLPVIAGVLSKLF 13 Tepmporin-1Ee (frog, amphibians, animals) No entry found Not found Not found skin secretion, the European edible frog, Pelophylax kl. esculentus, Europe. Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Fuction: It showed no hemolytic activity at 10 μM. [Ref.27255993]Gram-positive bacteria: S. aureus (MIC= 10 μM);##Gram-negative bacteria: E. coli (MIC= 40 μM) [Ref.27255993]Non-hemolytic activity at 10 μM Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27255993 Biochem Biophys Res Commun. 2016 Aug 5;476(4):566-73. Chen X, Wang H, Yang M, Wang L, Zhou M, Chen T, Shaw C. Identification and bioactivity evaluation of two novel temporins from the skin secretion of the European edible frog, Pelophylax kl. esculentus. DRAMP18455 DSYKKIDCGGACAARCRLSSRPRLCHRACGTCCARCNCVPPGTSGNTETCPCYASLTTHGNKRKCP 66 Tomato Snakin-2 (plants) No entry found Not found Not found Solanum lycopersicum Antimicrobial, Antibacterial, Antifungal Bridge Not found Comment: No comments found on DRAMP database Active against E. coli, B. subtilis, and S. cerevisiae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21479554##27190708 Transgenic Res. 2012 Feb;21(1):23-37.##PeerJ. 2016 May 10;4:e1987. Balaji V, Smart CD.##Herbel V, Wink M. Over-expression of snakin-2 and extensin-like protein genes restricts pathogen invasiveness and enhances tolerance to Clavibacter michiganensis subsp. michiganensis in transgenic tomato (Solanum lycopersicum).##Mode of action and membrane specificity of the antimicrobial peptide snakin-2. DRAMP18456 FSLIPSAIGGLISA 18 Pepcon (peptide consensus sequence, synthetic) No entry found Not found Not found Designed based on sequence alignment with scorpion linear peptides Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Comment: No comments found on DRAMP database Gram-positive bacteria: S. epidermidis ATCC 12228 (MIC 7.5 uM),S. aureus (5 uM);##Gram-negative bacteria: E. coli ATCC 25922 (MIC 50 uM), S. enterica ATCC 10708 (60 uM), P. aeruginosa ATCC 27853 (40uM), A. baumannii ATCC 19606 (MIC 20 uM),K. pneumoniae (60 uM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28096686 Infect Drug Resist. 2016 Dec 29;10:1-17. Almaaytah A, Ajingi Y, Abualhaijaa A, Tarazi S, Alshar'i N, Al-Balas Q Peptide consensus sequence determination for the enhancement of the antimicrobial activity and selectivity of antimicrobial peptides. DRAMP18457 KRWWKWWRRC 10 Tet213 (synthetic, Trp-rich, Arg-rich) No entry found Not found Not found Synthetic Antimicrobial, Antibacterial Not found Not found Comment: No comments found on DRAMP database Active against S. aureus and P. aeruginosa. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found Not found Biomaterials. 2010 Dec;31(36):9519-26. Kazemzadeh-Narbat M, Kindrachuk J, Duan K, Jenssen H, Hancock RE, Wang R Antimicrobial peptides on calcium phosphate-coated titanium for the prevention of implant-associated infections DRAMP18458 TLISWIKNKRKQRPRVSRRRRRRGGRRRR 29 Melimine (a hybrid peptide of melittin and protamine, synthetic) No entry found Not found Not found Synthetic Antimicrobial, Antibacterial Not found Not found This peptide, consisting of the C-terminal regions of melittin and protamine, has been covalently immobilized 2008 via the N-terminus. Melimine coated contact lens reduced bacterial colonization (S. aureus and P. aeruginosa) by~70%. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19016975 J Appl Microbiol. 2008 Dec;105(6):1817-25. Willcox MD, Hume EB, Aliwarga Y, Kumar N, Cole N. A novel cationic-peptide coating for the prevention of microbial colonization on contact lenses. DRAMP18459 GRRRRSVQWCA 11 hLF(1-11) (hLF1-11, first 11 residues, human lactoferrin; synthetic) No entry found Not found Not found Synthetic fragment Antimicrobial, Antibacterial Not found Not found 1Z6V,1Z6W,1EH3 Fuction: hLF(1 Active against S. aureus, L. monocytogenes, E. coli, and K. pneumoniae. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11179314##24704699 Infect Immun. 2001 Mar;69(3):1469-76. ##Acta Biomater. 2014 Aug;10(8):3522-34. Nibbering PH, Ravensbergen E, Welling MM, van Berkel LA, van Berkel PH, Pauwels EK, Nuijens JH.##Godoy-Gallardo M, Mas-Moruno C, Fern Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria.##Covalent immobilization of hLf1-11 peptide on a titanium surface reduces bacterial adhesion and biofilm formation. DRAMP18419 GGFGCPFNIDNQGNCHNHCQSIRGRKGGYCHGIPKQTCKCYKPMGYKARPPFILG 55 STiDA-2 No entry found Belongs to the defensin family. Not found Deduced; synthetic Antiparasitic Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27822206 Front Microbiol. 2016 Oct 24;7:1682 Cabezas-Cruz A, Tonk M, Bouchut A, Pierrot C, Pierce RJ, Kotsyfakis M, Rahnamaeian M, Vilcinskas A, Khalife J, Vald Antiplasmodial Activity Is an Ancient and Conserved Feature of Tick Defensins. DRAMP18420 GGFGCPFNIDNQGNCHNHCQSIRGRKGGYCHGIPKQTCKCYKPMGYKTRPPFILG 55 STiDA-1 No entry found Belongs to the defensin family. Not found Deduced; synthetic Antiparasitic, Antimalarial Bridge Not found Comment: No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27822206 Front Microbiol. 2016 Oct 24;7:1682 Cabezas-Cruz A, Tonk M, Bouchut A, Pierrot C, Pierce RJ, Kotsyfakis M, Rahnamaeian M, Vilcinskas A, Khalife J, Vald Antiplasmodial Activity Is an Ancient and Conserved Feature of Tick Defensins. DRAMP20762 SDCNINSNTAADVILCFNQVGSCALCSPTLVGGPVP 36 Halocin S8 (HalS8, Halocin-S8; Microhalocin, Archaeocin, Bacteriocin, Archaea, Euryarchaeota, Prokaryotes) Q9HHA8 Not found halS8 Haloarchaeon S8a Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial activity against the haloarchaeons H.salinarium NRC817, Halobacterium GRB and H.gibbonsii. Miscellaneous: Halocin-S8 is quite robust, as it can be desalted, boiled, subjected to organic solvents, and stored at 4 degrees Celsius for extended periods without losing activity." [Ref.11114928] Archaea: Sulfolobus solfataricus (Inhibition Zone=4mm) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10940040##11114928 J Bacteriol. 2000 Sep;182(17):4951-8.##J Bacteriol. 2001 Jan;183(1):287-91. Lance B. Price and Richard F. Shand##Haseltine C, Hill T, Montalvo-Rodriguez R, Kemper SK, Shand RF, Blum P. Halocin S8, a 36-Amino-Acid Microhalocin from the Haloarchaeal Strain S8a.##Secreted euryarchaeal microhalocins kill hyperthermophilic crenarchaea. DRAMP18471 KKLALKALLLWLKALLKLAKLALKK 25 D-LAK60 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Peptides comprising all D-amino acids. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC>22.62 μM), Escherichia coli Top 10 (MIC=7.07±2.04 M), Pseudomonas aeruginosa (MIC>22.62 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18472 KKLALKALKLWLLALLKLAKLALKK 25 D-LAK80 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Peptides comprising all D-amino acids. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC>22.62 μM), Escherichia coli Top 10 (MIC=5.40±1.01 μM), Pseudomonas aeruginosa (MIC>22.62 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18473 KKLALKALKLWLLALKKLALLALKK 25 D-LAK100 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Peptides comprising all D-amino acids. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=4.14±1.03 μM), Escherichia coli Top 10 (MIC=1.51±0.23 M), Pseudomonas aeruginosa (MIC=7.92±2.06 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18474 KKLAKLALLKWLLALKKLALLALKK 25 D-LAK140 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Peptides comprising all D-amino acids. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=3.14±1.28 μM), Escherichia coli Top 10 (MIC=0.76±0.18 M), Pseudomonas aeruginosa (MIC=4.69±0.67 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18475 KKLAKLALLKWLLALKLLALKALKK 25 D-LAK160 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Peptides comprising all D-amino acids. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=3.85±0.64 μM), Escherichia coli Top 10 (MIC=1.49±0.56 μM), Pseudomonas aeruginosa (MIC=6.23±0.71 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18476 KKLAKALKLLALLWLKLAKALKKA 24 LAK80 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=13.05±0.13 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18477 KKLAKAPKLLALLWLKLAKALKKA 24 LAK80-P7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=2.97±0.15 μM), Escherichia coli Top 10 (MIC=1.26±0.49 μM), Pseudomonas aeruginosa (MIC=2.13±0.77 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18478 KKLAKALKLPALLWLKLAKALKKA 24 LAK80-P10 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.62±0.17 μM), Escherichia coli Top 10 (MIC=0.82±0.03 μM), Pseudomonas aeruginosa (MIC=1.18±0.53 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18479 KKLAKALKLLAPLWLKLAKALKKA 24 LAK80-P12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.80±0.27 μM), Escherichia coli Top 10 (MIC=0.80±0.01 μM), Pseudomonas aeruginosa (MIC=0.86±0.09 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18480 KKLALALKKLALLWKKLALALKKA 24 LAK120 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=2.95±0.06 μM), Escherichia coli Top 10 (MIC=1.47±0.64 μM), Pseudomonas aeruginosa (MIC=4.20±0.92 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18481 KKLALAPKKLALLWKKLALALKKA 24 LAK120-P7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.80±0.03 μM), Escherichia coli Top 10 (MIC=0.45±0.10 μM), Pseudomonas aeruginosa (MIC=4.45±0.19 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18482 KKLALALKKPALLWKKLALALKKA 24 LAK120-P10 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.78±0.01 μM), Escherichia coli Top 10 (MIC=0.47±0.15 μM), Pseudomonas aeruginosa (MIC=9.16±1.43 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18483 KKLALALKKLAPLWKKLALALKKA 24 LAK120-P12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.97±0.06 μM), Escherichia coli Top 10 (MIC=0.68±0.14 μM), Pseudomonas aeruginosa (MIC=2.14±0.53 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18484 KKLKLALAKLALLWKALALKLKKA 24 LAK160 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.11±0.48 μM), Escherichia coli Top 10 (MIC=0.73±0.40 μM), Pseudomonas aeruginosa (MIC=2.23±0.41 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18485 KKLKLAPAKLALLWKALALKLKKA 24 LAK160-P7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.79±0.41 μM), Escherichia coli Top 10 (MIC=0.46±0.11 μM), Pseudomonas aeruginosa (MIC=2.98±0.21 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18486 KKLKLALAKPALLWKALALKLKKA 24 LAK160-P10 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=2.22±0.63 μM), Escherichia coli Top 10 (MIC=0.45±0.24 μM), Pseudomonas aeruginosa (MIC=4.14±0.23 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18487 KKLKLALAKLAPLWKALALKLKKA 24 LAK160-P12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.48±0.20 μM), Escherichia coli Top 10 (MIC=0.38±0.08 μM), Pseudomonas aeruginosa (MIC=1.69±0.09 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides. DRAMP18488 FFGSLLSLGSKLLPSVFKLFQRKKE 25 Css54 (Css from the species name below; scorpions, arachnids, Chelicerata, arthropods, invertebra P0DL41 Not found Not found Centruroides suffusus (Mexican scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Cytolysis, Hemolytic Not found Not found Not found Function: Amphipathic peptide that shows antibacterial activity against Escherichia coli and Staphylococcus aureus. Increases efficacy of antibiotics when tested against S.aureus, probably by facilitating their incorporation into the bacteria. Has hemolytic activity against human erythrocytes. [Ref.23093034]Gram-positive bacterium: Staphylococcus aureus (MIC=12.5 μg/ml);##Gram-negative bacterium: Escherichia coli (MIC=12.5 μg/ml). [Ref.23093034]30% hemolytic activity at 9 μM, 67% hemolytic activity at 17 μM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23093034 J Antibiot (Tokyo). 2013 Jan;66(1):3-10. Garcia F, Villegas E, Espino-Solis GP, Rodriguez A, Paniagua-Solis JF, Sandoval-Lopez G, Possani LD, Corzo G. Antimicrobial peptides from arachnid venoms and their microbicidal activity in the presence of commercial antibiotics. DRAMP18489 RKCNFLCKLKEKLRTVITSHIDKVLRPQG 29 Cathelicidin-PY (Frog, amphibians, animals; BBL) No entry found Belongs to the cathelicidin family Not found Paa yunnanensis(Chinese Yunnan frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-inflammatory Not found Helix cathelicidin-PY adopts a tertiary structure with a mostly positively charged surface containing a helix (Thr15 2LR7 Function: Cathelicidin-PY exerted strong antimicrobial abilities and induced little hemolytic activity in a dose-dependent manner. [Ref.23594231]Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=2.74 µM). [Ref.23594231]2.5% hemolytic activity at 12.5 μg/mL, 3.5 hemolytic activity at 25 μg/mL, 5.5% hemolytic activity at 50 μg/mL against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23594231 J Med Chem. 2013 May 9;56(9):3546-56. Wei L, Yang J, He X, Mo G, Hong J, Yan X, Lin D, Lai R. Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide. DRAMP18491 RWKIFKKIEKMGRNIRDGIVKAGPAIEVLGSAKAIGK 37 CecropinXJ (Insects, arthropods, invertebrates, animals) No entry found Belongs to the cecropin family Not found Bombyx mori Antimicrobial, Antibacterial, Anti-Gram+, Anti-cancer Not found Not found Not found Function: Antimicrobial activity against Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Staphylococcus aureus (MIC= 1.81 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23500722 Protein Expr Purif. 2013 Jul;90(1):47-54. Xia L, Liu Z, Ma J, Sun S, Yang J, Zhang F. Expression, purification and characterization of cecropin antibacterial peptide from Bombyx mori in Saccharomyces cerevisiae. DRAMP18492 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR 74 cgUbiquitin (Oyster, mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Pacific oyster(Crassostrea gigas) Antimicrobial, Antibacterial, Anti-Gram+ Not found Helix and Beta Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and Yeast. Gram-positive bacteria: Bacillus subtilis KCTC1021 (MIC=0.4 No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22858580 Mol Immunol. 2013 Jan;53(1-2):88-98. Seo JK, Lee MJ, Go HJ, Kim GD, Jeong HD, Nam BH, Park NG. Purification and antimicrobial function of ubiquitin isolated from the gill of Pacific oyster, Crassostrea gigas. DRAMP03011 INIKDILAKLVKVLGHV 17 Bombolitin IV (insects, arthropods, invertebrates, animals) P07495 Not found Not found Megabombus pennsylvanicus (Bumblebee) Antimicrobial, Antibacterial, Anti Mammalian Cells Protein level Not found Not found Function: Mast cell degranulating peptide. Has hemolytic activity. No MICs found in DRAMP database [Ref.2578459] Hemolysis: ED50=1.8±0.05 µg/ml. Histamine release: ED50=12.5±0.7 µg/ml against guinea pig erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2578459 J Biol Chem. 1985 Feb 10;260(3):1437-144. Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. DRAMP03012 INVLGILGLLGKALSHL 17 Bombolitin V (insects, arthropods, invertebrates, animals) P07496 Not found Not found Megabombus pennsylvanicus (Bumblebee) Antimicrobial, Antibacterial, Anti Mammalian Cells Protein level Not found Not found Function: Mast cell degranulating peptide. Has hemolytic activity. No MICs found in DRAMP database [Ref.2578459] Hemolysis: ED50=0.7±0.05 µg/ml. Histamine release: ED50=2.0±0.3 µg/ml against guinea pig erythrocytes. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2578459 J Biol Chem. 1985 Feb 10;260(3):1437-144. Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. DRAMP02081 FLPLLAGLAANFLPKIFCKITRKC 24 Brevinin-1E (Frogs, amphibians, animals) P32412 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana esculenta (Edible frog) (Pelophylax esculentus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Anti Mammalian Cells Protein level Alpha helix Possess an intramo-lecular disulfide bridge located at the carboxyl-terminal end. Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity. [Ref.8163497] Gram-negative bacteria: Escherichia coliD21 (MIC=1.8 µM), Pseudomonas aeruginosa ATCC15692 (MIC=30.6 µM);##Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.4 µM), Staphylococcus aureus Cowan1 (MIC=0.6 µM);##Fungi: Candida albicans (MIC=4.7 µM);##Yeast: Saccharomyces cerevisiae (MIC=3.8 µM). [Ref.8163497] LC50=0.5 µM against human red blood cell. Cyclic Free Cyclization (Cys18 and Cys24) Disulfide bond between Cys18 and Cys24. L No cytotoxicity information found Not found 8508915##8163497 FEBS Lett. 1993 Jun 14;324(2):159-161.##J Biol Chem. 1994 Apr 22;269(16):11956-11961. Simmaco M, Mignogna G, Barra D, Bossa F.##Simmaco M, Mignogna G, Barra D, Bossa F. Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta.##Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. DRAMP02751 GRPNPVNNKPTPHPRL 16 Formaecin-1 (Pro-rich; ants, insects, animals) P81438 Not found Not found Myrmecia gulosa (Red bulldog ant) Antimicrobial, Antibacterial, Anti-Gram- Protein level Rich Not found "Function: Antibacterial activity against E.coli but none against other Gram-negative bacteria and Gram-positive bacteria. Induction: By bacterial infection. PTM: O-linked glycan consists of a Gal-GalNAc disaccharide, O-glycosylation is essential for full biological activity." [Ref.9497332] Gram-negative bacteria: Escherichia coli NCTC 8196, Escherichia coli BLR. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9497332 J Biol Chem. 1998 Mar 13;273(11):6139-6143. Mackintosh JA, Veal DA, Beattie AJ, Gooley AA. Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides. DRAMP02752 GRPNPVNTKPTPYPRL 16 Formaecin-2 (Pro-rich; ants, insects, animals) P81437 Not found Not found Myrmecia gulosa (Red bulldog ant) Antimicrobial, Antibacterial, Anti-Gram- Protein level Rich Not found "Function: Antibacterial activity against E.coli but none against other Gram-negative bacteria and Gram-positive bacteria. Induction: By bacterial infection. PTM: O-linked glycan consists of a Gal-GalNAc disaccharide, O-glycosylation is essential for full biological activity." [Ref.9497332] Gram-negative bacteria: Escherichia coli NCTC 8196, Escherichia coli BLR. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9497332 J Biol Chem. 1998 Mar 13;273(11):6139-6143. Mackintosh JA, Veal DA, Beattie AJ, Gooley AA. Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides. DRAMP03097 GKPRPYSPRPTSHPRPIRV 19 Drosocin (Glycopeptide,insects, arthropods, invertebrates, animals) P36193 Belongs to the drosocin family Dro Drosophila melanogaster (Fruit fly) Antimicrobial, Antibacterial, Anti-Gram- Protein level Beta turns The NMR data clearly indicate a difference between the glycosylated and nonglycosylated forms, i.e., in the perturbation of a turn directly adjacent to the glycosylation site. 4EZR resolved by X-ray. "Function: Antibacterial peptide with strong anti-Gram-negative bacteria activity. PTM: O-glycosylation is essential for full biological activity. Tissue specificity: In hemolymph 6 hours after immune challenge, levels of expression increase for first 24 hours and persist for the following two weeks. Developmental stage: Expressed in larvae and in adults. Induction: By bacterial infection." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9888811##8325867##9497332 "Biochemistry. 1999 Jan 12;38(2):705-14.## J Biol Chem. 1993 Jul 15;268(20):14893-7.##J Biol Chem. 1998 Mar 13;273(11):6139-6143." "McManus AM, Otvos L Jr, Hoffmann R, Craik DJ.## Bulet P, Dimarcq JL, Hetru C, Lagueux M, Charlet M, Hegy G, Van Dorsselaer A, Hoffmann JA.##Mackintosh JA, Veal DA, Beattie AJ, Gooley AA." Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: effects of glycosylation on solution conformation.##A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution.##Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides. DRAMP03575 FKRIVQRIKDFLR 13 LL-37(17-29) (C-terminal fragment of LL-37, LL; Human, mammals, animals) P49913 Belongs to truncated LL-37. Not found Homo sapiens Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anti-cancer Protein level Alpha helix##Random coil Not found 2FBS resolved by NMR. Function: LL-37(17-29) became slightly less active than the longer ones, indicating that the truncated hydrophobic residues L31 and V32 also play a role in interaction with human cells. Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. [Ref.16637646] Gram-negative bacterium: Escherichia coli K12(MIC=40 μM);##Drug-resistant KBv cancer cells (LC50=60 μM), Drug-sensitive KB cancer cells (LC50=57 μM).##[Ref.28178190]Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=16 μM), S. faecalis ATCC 29212 (MIC=32 μM), Bacillus subtilis CMCC 63501 (MIC=16 μM), Staphylococcus epidermidis ATCC 12228 (MIC=8 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16 μM), Escherichia coli UB 1005 (MIC=16 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μM), Pseudomonas aeruginosa PAO1 (MIC=16 μM), Salmonella typhimurium ATCC 14028 (MIC=32 μM), Salmonella typhimurium ATCC 7731 (MIC=16 μM). [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.28161291] HC50>256 μM against human red blood cells. [Ref.23894079] MHC10=160 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16637646##28178190##28161291##23894079 J Am Chem Soc. 2006 May 3;128(17):5776-5785.##Int J Mol Sci. 2017 Feb 6;18(2). pii: E339. ##Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733.##ChemMedChem. 2013 Oct;8(10):1638-42. Li X, Li Y, Han H, Miller DW, Wang G. ##Tan T, Wu D, Li W, Zheng X, Li W, Shan A.##Rajasekaran G, Kim EY, Shin SY##Son M, Lee Y, Hwang H, Hyun S, Yu J Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. ##High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7.##LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. ##Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP02093 FLPFIAGVAAKFLPKIFCAISKKC 24 Brevinin-1Bc (Frogs, amphibians, animals) P82835 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=13 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02094 FLPAIAGVAAKFLPKIFCAISKKC 24 Brevinin-1Bd (Frogs, amphibians, animals) P82836 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=3 μM);##Gram-negative bacterium: Escherichia coli (MIC=7 μM).##Yeast: Candida albicans (MIC=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02095 FLPAIVGAAAKFLPKIFCVISKKC 24 Brevinin-1Be (Frogs, amphibians, animals) P82837 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=3 μM);##Gram-negative bacterium: Escherichia coli (MIC=15 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02096 FLPFIAGMAANFLPKIFCAISKKC 24 Brevinin-1Bf (Frogs, amphibians, animals) P82838 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=8 μM);##Gram-negative bacterium: Escherichia coli (MIC=19 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02097 FLPIIAGVAAKVFPKIFCAISKKC 24 Brevinin-1Pa (Frogs, amphibians, animals) P82841 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=7 μM);##Gram-negative bacterium: Escherichia coli (MIC=14 μM).##Yeast: Candida albicans (MIC=5 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02098 FLPIIASVAAKVFSKIFCAISKKC 24 Brevinin-1Pc (Frogs, amphibians, animals) P82843 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=7 μM);##Gram-negative bacterium: Escherichia coli (MIC=5 μM).##Yeast: Candida albicans (MIC=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02099 FLPIIASVAANVFSKIFCAISKKC 24 Brevinin-1Pd (Frogs, amphibians, animals) P82844 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found "Function: Antimicrobial activity against the Gram-positive, Gram-negative bacteria and fungi. Tissue specificity: Expressed by the skin glands." [Ref.10651828]Gram-positive bacterium: Staphylococcus aureus (MIC=27 μM);##Gram-negative bacterium: Escherichia coli (MIC=78 μM).##Yeast: Candida albicans (MIC=29 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02255 GILSSIKGVAKGVAKNVAAQLLDTLKCKITGC 32 Ranatuerin-2Lb (Ranatuerin 2Lb; Ranaturin-2PRd; Frogs, amphibians, animals) P82829 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) (Rana pretiosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=4 µM);##Gram-negative bacterium: Escherichia coli (MIC=4 µM);##Yeast: Candida albicans (MIC=62 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02254 GILDSFKGVAKGVAKDLAGKLLDKLKCKITGC 32 Ranatuerin-2La (Ranatuerin 2La; Ranatuerin-2PRa; Frogs, amphibians, animals) P82828 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana luteiventris (Spotted frog) (Rana pretiosa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=11 µM);##Gram-negative bacterium: Escherichia coli (MIC=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02256 GLLDTIKGVAKTVAASMLDKLKCKISGC 28 Ranatuerin-2B (Ranatuerin 2B, Frog, amphibians, animals) P82840 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana berlandieri (Rio Grande leopard frog) (Rana luteiventris) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.10651828] Gram-positive bacterium: Staphylococcus aureus (MIC=2 µM);##Gram-negative bacterium: Escherichia coli (MIC=2 µM);##Yeast: Candida albicans (MIC=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10651828 Eur J Biochem. 2000 Feb;267(3):894-900. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP02257 LMDTVKNVAKNLAGHMLDKLKCKITGC 27 Ranatuerin-2P (Ranatuerin 2P; Frogs, amphibians, animals) Q8QFQ4, P82847 Belongs to the frog skin active peptide family (Brevinin subfamily) Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal,Antiviral Protein level Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.10651828] Gram-positive bacteria: Staphylococcus aureus (MIC=50 µM);##Gram-negative bacterium: Escherichia coli (MIC=13 µM);##Yeast: Candida albicans (MIC=67 µM).##[Ref.11601906]Virus:##Frog Virus 3: 90% inhibition at 500 µM;##Channel Catfish Virus: 99% inhibition at 50 µM. No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys22 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 11601906##10651828 Virology. 2001 Sep 30;288(2):351-7.##Eur J Biochem. 2000 Feb;267(3):894-900. Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L.##Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin.##Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. DRAMP18496 KRGFGCNGPWNEDDLRCHNHCKSIKGYKGGYCAKGGFVCKCY 42 rNZ2114 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found 6K50 Function: Antibacterial activity against Gram-positive bacteria. Weak hemolytic activity. [Ref.23624708]Gram-positive bacteria: Staphylococcus aureus(MSSA MIC=0.028 μM;MRSA MIC=0.90μM) [Ref.23624708]<0.1% hemolysis upto 128μg/ml against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23624708 Appl Microbiol Biotechnol Yong ZhangDa TengRuoyu MaoXiumin WangDi XiXiaoyuan HuJianhua Wang High expression of a plectasin-derived peptide NZ2114 in Pichia pastoris and its pharmacodynamics, postantibiotic and synergy against Staphylococcus aureus. DRAMP18497 WKSDVRRWRSRY 12 TSG-6 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity, [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC>100 μM);##Gram-negative bacteria: Escherichia coli (MIC=64 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]0.3±0.9% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18498 WKSYVRRWRSRY 12 TSG-7 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC=32 μM);##Gram-negative bacteria: Escherichia coli (MIC=16 μM), Pseudomonas aeruginosa (MIC=100 μM) [Ref.23570790]1.5±1.4% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18499 WKSYVRRWRSR 11 TSG-8 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC=32 μM);##Gram-negative bacteria: Escherichia coli (MIC=16 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]-1.2±2.6% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18500 WWSYVRRWRSR 11 TSG-8-1 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC=8 μM);##Gram-negative bacteria: Escherichia coli (MIC=16 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]3.4±1.3% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18501 WKSYVRRWRS 10 TSG-9 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC>100 μM);##Gram-negative bacteria: Escherichia coli (MIC=64 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]-0.4±0.5% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18502 WKSYVRRWR 9 TSG-10 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC=64 μM);##Gram-negative bacteria: Escherichia coli (MIC=64 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]1.1±1.3% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18503 WKSYVRRW 8 TSG-11 (Ixosin-B peptide derivative) No entry found Derived from Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23570790]Gram-positive bacteria: Staphylococcus aureus (MIC=100 μM);##Gram-negative bacteria: Escherichia coli (MIC=64 μM), Pseudomonas aeruginosa (MIC>100 μM) [Ref.23570790]2.0±0.3% hemolysis at 100μM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23570790 Bioorg Med Chem Lett. 2013 May 15;23(10):2929-32. Wu YS, Liao ZJ, Wang KS, Lung FD. Structure-activity relationship of potent antimicrobial peptide analogs of Ixosin-B amide. DRAMP18504 FSEAIKKIIDFLGEGLFDIIKKIAESF 27 E(AU)2 (Aurein 1.2 peptide derivative) No entry found Derived from Aurein 1.2 Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Coiled coil Not found Function: Antibacterial activity against Gram-negative bacteria, E(AU)2 has no hemolytic activity [Ref.23519707]Gram-negative bacterium: Escherichia coli (MIC=128 μmol/L) [Ref.23519707]~5% hemolysis at 128μmol/L, 0% hemolysis at 4 -32μmol/L against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23519707 Amino Acids. 2013 Jun;44(6):1521-8. Lorenzón EN, Sanches PR, Nogueira LG, Bauab TM, Cilli EM. Dimerization of aurein 1.2: effects in structure, antimicrobial activity and aggregation of C?ndida albicans cells DRAMP18505 GLFDIIKKIAESFKFSEAIKKIIDFLG 27 (AU)2K (Aurein 1.2 peptide derivative) No entry found Derived from Aurein 1.2 Not found Litoria raniformis (Southern bell frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria, Has hemolytic activity. [Ref.23519707]Gram-negative bacterium: Escherichia coli (MIC=128 μmol/L) [Ref.23519707]~30% hemolysis at 32μmol/L, 10% hemolysis at 4 μmol/L against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23519707 Amino Acids. 2013 Jun;44(6):1521-8. Lorenzón EN, Sanches PR, Nogueira LG, Bauab TM, Cilli EM Dimerization of aurein 1.2: effects in structure, antimicrobial activity and aggregation of C?ndida albicans cells DRAMP18506 KKFFLKVLTKIRCKVAGGCRT 21 OG2 (Palustrin-OG1 peptide derivative) No entry found Derived from Palustrin-OG1 Not found Synthetic construct (Modified Palustrin-OG1) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive, Gram-negative bacteria, and lower hemolytic activity than OG1. [Ref.22670762]Gram-positive bacteria: Bacillus subtilis 1A751 (MIC=128 μg/mL), Staphylococcus aureus ATCC25923 (MIC=8 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=8 μg/mL),Salmonella choleraesuis CMCC50020 (MIC=16 μg/mL) [Ref.22670762]7%±2% hemolysis at 2-256 μg/mL against porcine red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22670762 Protein Pept Lett. 2013 Jan;20(1):54-60. Xie YG, Luan C, Zhang HW, Han FF, Feng J, Choi YJ, Groleau D, Wang YZ. Effects of thioredoxin: SUMO and intein on soluble fusion expression of an antimicrobial peptide OG2 in Escherichia coli. DRAMP18508 KFAKKFKWFAKAAFKFFKK 19 gp41w-FKA (gp41 peptide derivative) No entry found Derived from the HIV glycoprotein, gp41 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix gp41w-FKA peptide to adopt a helical conformation in the cosolvent mixture of chloroform, methanol and water. The peptide formed a very well defined Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.23019445]Gram-positive bacterium: Staphylococcus aureus (MIC<10 μg/ml, MBC=20-30 μg/ml);##Gram-negative bacterium: Escherichia coli (MIC=10-30 μg/ml, MBC=40-50 μg/ml) [Ref.23019445]EC50=195 μg/mL against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet gp41w-FKA binds at the interfacial region of a phospholipid bilayer. 23019445 Beilstein J Org Chem. 2012;8:1172-84. Epub 2012 Jul 24. Haney EF, Nguyen LT, Schibli DJ, Vogel HJ. Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41. DRAMP18509 MAFKKLEKVGRNIRDGIIKAGPAVAVIGQATSIARPTGK 39 Px-cec1 (cecropin1 peptide derivative) No entry found Derived from the cecropin1 cecropin1 Diamondback moth(Plutella xylostella) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. No hemolytic activity. "[Ref.22921836]Gram-positive bacteria: Staphylococcus aureus (MIC=2.1 μg/mL), Bacillus cereus (MIC=2.6 μg/mL);##Gram-negative bacteria: Escherichia coli K12D31 (MIC=0.1 μg/mL), Escherichia coli K12 (MIC=0.23 μg/mL), Pseudomonas fluorescent (MIC=1.1 μg/mL), Salmonella choleraesuis (MIC=2.1 μg/mL);##Fungi: Aureobasidium pullulans (MIC=4.0 μg/mL), Aspergillus flavus (MIC=14.5 μg/mL), Aspergillus fumigatus (MIC=16.0 μg/mL), Aspergillus niger (MIC=14.6 μg/mL), Fusarium oxysporum (MIC=8.0 μg/mL)" [Ref.22921836]Non-hemolytic against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22921836 Protein Expr Purif. 2012 Oct;85(2):230-8. Jin F, Sun Q, Xu X, Li L, Gao G, Xu Y, Yu X, Ren S. cDNA cloning and characterization of the antibacterial peptide cecropin 1 from the diamondback moth, Plutella xylostella L. DRAMP18510 KKLALLALKKWLLALKKLALLALKK 25 D-LAK120 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antiplasmodial activity. Peptides comprising all D-amino acids. Has hemolytic activity. [Ref.22869378]Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.48±0.53 μM), Escherichia coli Top 10 (MIC=0.62±0.15 μM), Pseudomonas aeruginosa (MIC=2.71±1.07 μM);##Plasmodium: Plasmodium falciparum 3D7 (EC50=1.95±0.08 μM) [Ref.22869378]HC50=4.06±1.30 μM against Not found (The literature does not mention) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic DRAMP18511 KKLALLALKKWLPALKKLALLALKK 25 D-LAK120-P13 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antiplasmodial activity. Peptides comprising all D-amino acids. Has hemolytic activity. [Ref.22869378]Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.54±0.97 μM), Escherichia coli Top 10 (MIC=0.58±0.18 μM), Pseudomonas aeruginosa (MIC=1.42±0.41 μM);##Plasmodium: Plasmodium falciparum 3D7 (EC50=0.88±0.08 μM), Plasmodium falciparum C10 (EC50=2.18±0.41 μM), A549 (EC50=2.44±0.43 μM), RAW264.7 (EC50=3.80±0.34 μM) [Ref.22869378]HC50=11.66±0.03 μM against Not found (The literature does not mention) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic DRAMP18512 KKLALALAKKWLALAKKLALALAKK 25 D-LAK120-A No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antiplasmodial activity. Peptides comprising all D-amino acids. Has hemolytic activity. [Ref.22869378]Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.23±0.47 μM), Escherichia coli Top 10 (MIC=0.38±0.21 μM), Pseudomonas aeruginosa (MIC=1.83±0.63 μM);##Plasmodium: Plasmodium falciparum 3D7 (EC50=1.45±0.12 μM), Plasmodium falciparum C10 (EC50=2.13±0.14 μM), A549 (EC50=5.23±0.35 μM), RAW264.7 (EC50=7.31±2.13 μM) [Ref.22869378]HC50=17.42±2.17 μM against Not found (The literature does not mention) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic DRAMP18513 KKLALALAKKWLPLAKKLALALAKK 25 D-LAK120-AP13 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antiplasmodial activity. Peptides comprising all D-amino acids. Has hemolytic activity. [Ref.22869378]Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.08±0.62 μM), Escherichia coli Top 10 (MIC=0.29±0.09 μM), Pseudomonas aeruginosa (MIC=1.22±0.19 μM);##Plasmodium: Plasmodium falciparum 3D7 (EC50=0.88±0.06 μM), Plasmodium falciparum C10 (EC50=2.36±0.10 μM), A549 (EC50=3.11±0.57 μM), RAW264.7 (EC50=3.42±0.16 μM) [Ref.22869378]HC50=58.61±10.41 μM against Not found (The literature does not mention) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic DRAMP18514 KKLALHALKKWLHALKKLAHLALKK 25 D-LAK120-H No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antiplasmodial activity. Peptides comprising all D-amino acids. Has hemolytic activity. [Ref.22869378]Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=1.54±0.01 μM), Escherichia coli Top 10 (MIC=0.40±0.01 μM), Pseudomonas aeruginosa (MIC=1.35±0.07 μM);##Plasmodium: Plasmodium falciparum 3D7 (EC50=1.26±0.14 μM), Plasmodium falciparum C10 (EC50=4.43±0.33 μM), A549 (EC50=4.54±0.30 μM), RAW264.7 (EC50=5.21±0.57 μM) [Ref.22869378]HC50=20.29±2.42 μM against Not found (The literature does not mention) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22869378 J Biol Chem. 2012 Oct 5;287(41):34120-33. Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ. Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic DRAMP18515 KWKSFLkTFKSLKKTVLHTLLKAISS 26 A12L/A20L (V13KL peptide derivative) No entry found Derived from the framework peptide V13KL Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. A12L/A20L against HeLa cells. Leucine to replace Alanine at the position 12 and 20 on the peptide V13KL. Has hemolytic activity. [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=62.5 μg/ml), Pseudomonas aeruginosa WR5 (MIC=125 μg/ml), Pseudomonas aeruginosa PAK (MIC=62.5 μg/ml), Pseudomonas aeruginosa PA14 (MIC=125 μg/ml), Pseudomonas aeruginosa M2 (MIC=62.5 μg/ml), Pseudomonas aeruginosa CP204 (MIC=62.5 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=78.7 μg/ml).##[Ref.22837667]Cancer cell: HeLa cell (IC50=1.71±0.07 μmol/L). [Ref.22837667]MHC=8.0 μg/ml, MHC=5.20±0.02 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17158938##22837667 Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406.##Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS.##Huang YB, He LY, Jiang HY, Chen YX. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides.##Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18516 KWKSFLKTFKSLKkTVLHTLLKAISS 26 K7D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antiplasmodial Synthetic Alpha helix Not found Function: K7D against HeLa cells. D-Lysine replace L-Lysine at the position 7 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=1.29±0.03 μmol/L) [Ref.22837667]MHC=10.4±0.04 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18517 KWKSFLKTFKSLKKTVLHTLLkAISS 26 K14D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K14D against HeLa cells. D-Lysine replace L-Lysine at the position 14 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=1.52±0.05 μmol/L) [Ref.22837667]MHC=5.20±0.02 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18518 KWKSFLkTFKSLKkTVLHTLLKAISS 26 K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K22D against HeLa cells. D-Lysine replace L-Lysine at the position 22 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=1.39±0.02 μmol/L) [Ref.22837667]MHC=20.81±0.10 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18519 KWKSFLKTFKSLKkTVLHTLLkAISS 26 K7D/K14D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K7D/K14D against HeLa cells. D-lysine replace L-Lysine at the position 7 and 14 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=2.06±0.01 μmol/L) [Ref.22837667]MHC=20.81±0.15 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18520 KWKSFLkTFKSLKkTVLHTLLkAISS 26 K14D/K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K14D/K22D against HeLa cells. D-Lysine replace L-Lysine at the position 14 and 22 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=1.40±0.09 μmol/L) [Ref.22837667]MHC=20.81±0.06 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18521 KWKSFLkTFkSLKkTVLHTLLkAISS 26 K7D/K14D/K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K7D/K14D/K22D against HeLa cells. D-Lysine replace L-Lysine at the position 7,14 and 22 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=4.45±0.19 μmol/L) [Ref.22837667]MHC=81.31±0.17 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18522 KWKSFLkTFkSLKkTVLHTLLkAISS 26 K7D/K10D/K14D/K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K7D/K10D/K14D/K22D against HeLa cells. D-Lysine replace L-Lysine at the position 7,10,14 and 22 on the polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=4.79±0.23 μmol/L) [Ref.22837667]MHC=325.20±0.82 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18523 KWkSFLkTFkSLKkTVLHTLLkAISS 26 K3D/K7D/K10D/K14D/K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K3D/K7D/K10D/K14D/K22D against HeLa cells. D-Lysine replace L-Lysine at the position 3,7,10,14 and 22 on the polar face of peptide A12L/A20L. Weak hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=20.41±0.64 μmol/L) [Ref.22837667]MHC>325.20 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18524 kWkSFLkTFkSLKkTVLHTLLkAISS 26 K1D/K3D/K7D/K10D/K14D/K22D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: K1D/K3D/K7D/K10D/K14D/K22D against HeLa cells. D-Lysine replace L-Lysine at the position 1,3,7,10,14 and 22 on the polar face of peptide A12L/A20L. Weak hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=18.07±0.48 μmol/L) [Ref.22837667]MHC>325.20 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18525 KWKSFLKTFKSLKKTVLHTLLKAISS 26 L6D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L6D against HeLa cells. D-Leucine replace L-Leucine at the position 6 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=2.23±0.10 μmol/L) [Ref.22837667]MHC=10.40±0.08 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18526 KWKSFLKTFKSLKKTVLHTLLKAISS 26 L12D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L12D against HeLa cells. D-Leucine replace L-Leucine at the position 12 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=2.63±0.07 μmol/L) [Ref.22837667]MHC=20.81±0.03 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18527 KWKSFLKTFKSLKKTVLHTLLKAISS 26 L20D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L20D against HeLa cells. D-Leucine replace L-Leucine at the position 20 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=2.33±0.06 μmol/L) [Ref.22837667]MHC=20.81±0.13 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18528 KWKSFlKTFKSlKKTVLHTLLKAISS 26 L6D/L12D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L6D/L12D against HeLa cells. D-Leucine replace L-Leucine at the position 6 and 12 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=3.01±0.08 μmol/L) [Ref.22837667]MHC=20.81±0.10 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18529 KWKSFLKTFKSlKKTVLHTlLKAISS 26 L12D/L20D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L12D/L20D against HeLa cells. D-Leucine replace L-Leucine at the position 12 and 20 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=3.14±0.06 μmol/L) [Ref.22837667]MHC=81.31±0.43 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18530 KWKSFlKTFKSlKKTVLHTlLKAISS 26 L6D/L12D/L20D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L6D/L12D/L20D against HeLa cells. D-Leucine replace L-Leucine at the position 6,12 and 20 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=7.80±0.26 μmol/L) [Ref.22837667]MHC=162.61±0.19 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18531 KWKSFlKTFKSlKKTVlHTlLKAISS 26 L6D/L12D/L17D/L20D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L6D/L12D/L17D/L20D against HeLa cells. D-Leucine replace L-Leucine at the position 6,12,17 and 20 on the non-polar face of peptide A12L/A20L. Has hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=9.69±0.38 μmol/L) [Ref.22837667]MHC=81.31±1.05 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18532 KWKSFlKTFKSlKKTVlHTllKAISS 26 L6D/L12D/L17D/L20D/L21D (A12L/A20L peptide derivative) No entry found Derived from the framework peptide A12L/A20L Not found Synthetic construct Anti-Cancer Synthetic Alpha helix Not found Function: L6D/L12D/L17D/L20D/L21D against HeLa cells. D-Leucine replace L-Leucine at the position 6,12,17,20 and 21 on the non-polar face of peptide A12L/A20L. Weak hemolytic activity. [Ref.22837667]Cancer cell: HeLa cell (IC50=12.88 ± 0.15 μmol/L) [Ref.22837667]MHC>325.20 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22837667 Int J Mol Sci. 2012;13(6):6849-62. doi: 10.3390/ijms13066849. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. DRAMP18533 KWKSFLKTFKSAKKTVLHTALKAISS 26 V13KL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Lysine replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=64.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=64.0 μg/ml), Staphylococcus epidermidis C621 (MIC=5.0 μg/ml), Bacillus subtilis C971 (MIC=1.6 μg/ml), Enterococcus faecalis C625 (MIC=64.0 μg/ml), Corynebacterium xerosis C875 (MIC=1.3 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=11.8 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=1.6 μg/ml), Salmonella typhimurium C587 (MIC=4.0 μg/ml), Salmonella typhimurium C610 (MIC=1.3 μg/ml), Pseudomonas aeruginosa H187 (MIC=8.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=5.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=3.1 μg/ml).##[Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=31.3 μg/ml), Pseudomonas aeruginosa WR5 (MIC=250 μg/ml), Pseudomonas aeruginosa PAK (MIC=125 μg/ml), Pseudomonas aeruginosa PA14 (MIC=62.5 μg/ml), Pseudomonas aeruginosa M2 (MIC=31.3 μg/ml), Pseudomonas aeruginosa CP204 (MIC=7.8 μg/ml), The geometric mean of MIC values above six Pseudomonas aeruginosa strains (MIC=49.6 μg/ml) [Ref.17158938]MHC=250.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462##17158938 J Biol Chem. 2005 Apr 1;280(13):12316-29.##Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS.##Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index.##Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. DRAMP18534 KWKSFLKTFKSAKKTVLHTALKLISS 26 A23L (V13KL peptide derivative) No entry found Derived from the framework peptide V13KL Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Leucine to replace Alanine at the position 23 on the peptide V13KL. Has hemolytic activity. [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=31.3 μg/ml), Pseudomonas aeruginosa WR5 (MIC=62.5 μg/ml), Pseudomonas aeruginosa PAK (MIC=62.5 μg/ml), Pseudomonas aeruginosa PA14 (MIC=31.3 μg/ml), Pseudomonas aeruginosa M2 (MIC=31.3 μg/ml), Pseudomonas aeruginosa CP204 (MIC=15.6 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=35.1 μg/ml) [Ref.17158938]MHC=62.5 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17158938 Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. DRAMP18535 KWKSFLKTFKSLKKTVLHTALKAISS 26 A12L (V13KL peptide derivative) No entry found Derived from the framework peptide V13KL Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Leucine to replace Alanine at the position 12 on the peptide V13KL. Has hemolytic activity. [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=15.6 μg/ml), Pseudomonas aeruginosa WR5 (MIC=62.5 μg/ml), Pseudomonas aeruginosa PAK (MIC=31.3 μg/ml), Pseudomonas aeruginosa PA14 (MIC=31.3 μg/ml), Pseudomonas aeruginosa M2 (MIC15.6= μg/ml), Pseudomonas aeruginosa CP204 (MIC=15.6 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=24.8 μg/ml) [Ref.17158938]MHC=31.3 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17158938 Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. DRAMP18536 KWKSFLKTFKSAKKTVLHTLLKAISS 26 A20L (V13KL peptide derivative) No entry found Derived from the framework peptide V13KL Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Leucine to replace Alanine at the position 20 on the peptide V13KL. Has hemolytic activity. [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=7.8 μg/ml), Pseudomonas aeruginosa WR5 (MIC=31.3 μg/ml), Pseudomonas aeruginosa PAK (MIC=31.3 μg/ml), Pseudomonas aeruginosa PA14 (MIC=15.6 μg/ml), Pseudomonas aeruginosa M2 (MIC=15.6 μg/ml), Pseudomonas aeruginosa CP204 (MIC=7.7 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=15.6 μg/ml) [Ref.17158938]MHC=31.3 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17158938 Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. DRAMP18537 KWKSFLKTFKSLKKTVLHTALKLISS 26 A12L/A23L (V13KL peptide derivative) No entry found Derived from the framework peptide V13KL Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Leucine to replace Alanine at the position 12 and 23 on the peptide V13KL. Has hemolytic activity. [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=15.6 μg/ml), Pseudomonas aeruginosa WR5 (MIC=250 μg/ml), Pseudomonas aeruginosa PAK (MIC=15.6 μg/ml), Pseudomonas aeruginosa PA14 (MIC=62.5 μg/ml), Pseudomonas aeruginosa M2 (MIC=31.3 μg/ml), Pseudomonas aeruginosa CP204 (MIC=7.8 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=31.2 μg/ml) [Ref.17158938]MHC=15.6 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17158938 Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. DRAMP18538 KWKSFLKTFKSAVKTVLHTALKAISS 26 V681 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=16.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=9.0 μg/ml), Staphylococcus epidermidis C621 (MIC=5.0 μg/ml), Bacillus subtilis C971 (MIC=2.2 μg/ml), Enterococcus faecalis C625 (MIC=16.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.5 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=6.3 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=7.1 μg/ml), Escherichia coli DC2 (MIC=4.5 μg/ml), Salmonella typhimurium C587 (MIC=20.2 μg/ml), Salmonella typhimurium C610 (MIC=5.7 μg/ml), Pseudomonas aeruginosa H187 (MIC=6.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=20.2 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=8.8 μg/ml) [Ref.15677462]MHC=15.6 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18539 KWKSFLKTFKSALKTVLHTALKAISS 26 V13LL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Leucine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=32.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=25.4 μg/ml), Staphylococcus epidermidis C621 (MIC=8.0 μg/ml), Bacillus subtilis C971 (MIC=3.2 μg/ml), Enterococcus faecalis C625 (MIC=32.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.5 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=10.9 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=6.4 μg/ml), Escherichia coli DC2 (MIC=5.0 μg/ml), Salmonella typhimurium C587 (MIC=32.0 μg/ml), Salmonella typhimurium C610 (MIC=10.1 μg/ml), Pseudomonas aeruginosa H187 (MIC=12.7 μg/ml), Pseudomonas aeruginosa H188 (MIC=32.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=12.7 μg/ml) [Ref.15677462]MHC=7.8 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18540 KWKSFLKTFKSAAKTVLHTALKAISS 26 V13AL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Alanine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=8.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=5.0 μg/ml), Staphylococcus epidermidis C621 (MIC=3.2 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=16.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=4.5 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=6.4 μg/ml), Salmonella typhimurium C610 (MIC=2.5 μg/ml), Pseudomonas aeruginosa H187 (MIC=5.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=6.4 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=3.8 μg/ml) [Ref.15677462]MHC=31.2 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18541 KWKSFLKTFKSAGKTVLHTALKAISS 26 V13G (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Glycine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=25.4 μg/ml), Staphylococcus aureus SAP0017 (MIC=10.1 μg/ml), Staphylococcus epidermidis C621 (MIC=3.2 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=50.8 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=7.4 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=5.0 μg/ml), Salmonella typhimurium C610 (MIC=2.5 μg/ml), Pseudomonas aeruginosa H187 (MIC=6.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=4.1 μg/ml) [Ref.15677462]MHC=125.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18542 KWKSFLKTFKSASKTVLHTALKAISS 26 V13SL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Serine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=16.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=12.7 μg/ml), Staphylococcus epidermidis C621 (MIC=4.0 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=50.8 μg/ml), Corynebacterium xerosis C875 (MIC=1.6 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=7.4 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=6.4 μg/ml), Salmonella typhimurium C610 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=6.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=4.2 μg/ml) [Ref.15677462]MHC=125.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18543 KWKSFLKTFKSALKTVLHTALKAISS 26 V13LD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Leucine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=5.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=4.0 μg/ml), Staphylococcus epidermidis C621 (MIC=2.5 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=6.4 μg/ml), Corynebacterium xerosis C875 (MIC=1.6 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=3.3 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=3.2 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=16.0 μg/ml), Salmonella typhimurium C610 (MIC=3.2 μg/ml), Pseudomonas aeruginosa H187 (MIC=6.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=5.5 μg/ml) [Ref.15677462]MHC=7.8 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18544 KWKSFLKTFKSAVKTVLHTALKAISS 26 V13VD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Valine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=4.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=3.2 μg/ml), Staphylococcus epidermidis C621 (MIC=1.6 μg/ml), Bacillus subtilis C971 (MIC=1.3 μg/ml), Enterococcus faecalis C625 (MIC=12.7 μg/ml), Corynebacterium xerosis C875 (MIC=1.3 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=2.8 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=1.6 μg/ml), Salmonella typhimurium C587 (MIC=5.0 μg/ml), Salmonella typhimurium C610 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=8.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=3.3 μg/ml) [Ref.15677462]MHC=62.5 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18545 KWKSFLKTFKSAAKTVLHTALKAISS 26 V13AD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Alanine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=8.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=5.0 μg/ml), Staphylococcus epidermidis C621 (MIC=2.0 μg/ml), Bacillus subtilis C971 (MIC=1.6 μg/ml), Enterococcus faecalis C625 (MIC=32.0 μg/ml), Corynebacterium xerosis C875 (MIC=1.6 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=4.3 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=1.6 μg/ml), Escherichia coli DC2 (MIC=2.0 μg/ml), Salmonella typhimurium C587 (MIC=5.0 μg/ml), Salmonella typhimurium C610 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=3.3 μg/ml) [Ref.15677462]MHC=250.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18546 KWKSFLKTFKSASKTVLHTALKAISS 26 V13SD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Serine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Weak hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=64.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=64.0 μg/ml), Staphylococcus epidermidis C621 (MIC=12.7 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=64.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=16.0 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=3.2 μg/ml), Escherichia coli DC2 (MIC=2.0 μg/ml), Salmonella typhimurium C587 (MIC=12.7 μg/ml), Salmonella typhimurium C610 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=18.3 μg/ml), Pseudomonas aeruginosa H188 (MIC=20.2 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=6.3 μg/ml) [Ref.15677462]MHC>250.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18547 KWKSFLKTFKSAKKTVLHTALKAISS 26 V13KD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Lysine to replace L-Valine at the position 13 on the non-polar face of peptide V681. Weak hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=64.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=64.0 μg/ml), Staphylococcus epidermidis C621 (MIC=25.4 μg/ml), Bacillus subtilis C971 (MIC=3.2 μg/ml), Enterococcus faecalis C625 (MIC=64.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=18.7 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=3.2 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=32.0 μg/ml), Salmonella typhimurium C610 (MIC=1.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=32.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=25.4 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=7.7 μg/ml) [Ref.15677462]MHC>250.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18548 KWKSFLKTFKLAVKTVLHTALKAISS 26 S11LL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Leucine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=32.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=32.0 μg/ml), Staphylococcus epidermidis C621 (MIC=16.0 μg/ml), Bacillus subtilis C971 (MIC=5.0 μg/ml), Enterococcus faecalis C625 (MIC=50.8 μg/ml), Corynebacterium xerosis C875 (MIC=2.5 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=14.8 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=16.0 μg/ml), Escherichia coli DC2 (MIC=5.0 μg/ml), Salmonella typhimurium C587 (MIC=32.0 μg/ml), Salmonella typhimurium C610 (MIC=12.7 μg/ml), Pseudomonas aeruginosa H187 (MIC=20.2 μg/ml), Pseudomonas aeruginosa H188 (MIC=32.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=16.6 μg/ml) [Ref.15677462]MHC=4.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18549 KWKSFLKTFKVAVKTVLHTALKAISS 26 S11VL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Valine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=16.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=12.7 μg/ml), Staphylococcus epidermidis C621 (MIC=8.0 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=20.2 μg/ml), Corynebacterium xerosis C875 (MIC=1.3 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=6.9 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=6.4 μg/ml), Escherichia coli DC2 (MIC=4.0 μg/ml), Salmonella typhimurium C587 (MIC=32.0 μg/ml), Salmonella typhimurium C610 (MIC=5.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=10.1 μg/ml), Pseudomonas aeruginosa H188 (MIC=20.2 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=9.7 μg/ml) [Ref.15677462]MHC=7.8 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18550 KWKSFLKTFKAAVKTVLHTALKAISS 26 S11AL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Alanine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=16.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=12.7 μg/ml), Staphylococcus epidermidis C621 (MIC=4.0 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=20.2 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=6.6 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=6.4 μg/ml), Escherichia coli DC2 (MIC=4.0 μg/ml), Salmonella typhimurium C587 (MIC=20.2 μg/ml), Salmonella typhimurium C610 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=10.1 μg/ml), Pseudomonas aeruginosa H188 (MIC=16.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=8.3 μg/ml) [Ref.15677462]MHC=15.6 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18551 KWKSFLKTFKGAVKTVLHTALKAISS 26 S11G (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Glycine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=8.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=5.0 μg/ml), Staphylococcus epidermidis C621 (MIC=4.0 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=12.7 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=4.5 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=5.0 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=12.7 μg/ml), Salmonella typhimurium C610 (MIC=3.2 μg/ml), Pseudomonas aeruginosa H187 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=5.2 μg/ml) [Ref.15677462]MHC=7.8 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18552 KWKSFLKTFKKAVKTVLHTALKAISS 26 S11KL (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. L-Lysine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=32.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=16.0 μg/ml), Staphylococcus epidermidis C621 (MIC=6.4 μg/ml), Bacillus subtilis C971 (MIC=3.2 μg/ml), Enterococcus faecalis C625 (MIC=32.0 μg/ml), Corynebacterium xerosis C875 (MIC=4.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=10.5 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=10.1 μg/ml), Escherichia coli DC2 (MIC=4.0 μg/ml), Salmonella typhimurium C587 (MIC=25.4 μg/ml), Salmonella typhimurium C610 (MIC=8.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=25.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=32.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=13.7 μg/ml) [Ref.15677462]MHC=4.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18553 KWKSFLKTFKLAVKTVLHTALKAISS 26 S11LD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Leucine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=8.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=5.0 μg/ml), Staphylococcus epidermidis C621 (MIC=4.0 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=16.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=4.7 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=5.0 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=10.1 μg/ml), Salmonella typhimurium C610 (MIC=3.2 μg/ml), Pseudomonas aeruginosa H187 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=5.0 μg/ml) [Ref.15677462]MHC=31.2 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18554 KWKSFLKTFKVAVKTVLHTALKAISS 26 S11VD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Valine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=16.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=8.0 μg/ml), Staphylococcus epidermidis C621 (MIC=4.0 μg/ml), Bacillus subtilis C971 (MIC=2.5 μg/ml), Enterococcus faecalis C625 (MIC=32.0 μg/ml), Corynebacterium xerosis C875 (MIC=2.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=6.6 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=5.0 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=10.1 μg/ml), Salmonella typhimurium C610 (MIC=4.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=6.4 μg/ml), Pseudomonas aeruginosa H188 (MIC=16.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=6.1 μg/ml) [Ref.15677462]MHC=125.0 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18555 KWKSFLKTFKAAVKTVLHTALKAISS 26 S11AD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Alanine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=6.4 μg/ml), Staphylococcus aureus SAP0017 (MIC=5.0 μg/ml), Staphylococcus epidermidis C621 (MIC=2.5 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=12.7 μg/ml), Corynebacterium xerosis C875 (MIC=1.6 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=3.8 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=4.0 μg/ml), Escherichia coli DC2 (MIC=2.5 μg/ml), Salmonella typhimurium C587 (MIC=8.0 μg/ml), Salmonella typhimurium C610 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H187 (MIC=5.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=8.0 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=4.3 μg/ml) [Ref.15677462]MHC=15.6 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18556 KWKSFLKTFKSAVKTVLHTALKAISS 26 S11SD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Serine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=4.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=2.5 μg/ml), Staphylococcus epidermidis C621 (MIC=2.0 μg/ml), Bacillus subtilis C971 (MIC=1.3 μg/ml), Enterococcus faecalis C625 (MIC=6.4 μg/ml), Corynebacterium xerosis C875 (MIC=1.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=2.3 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=2.5 μg/ml), Escherichia coli DC2 (MIC=1.6 μg/ml), Salmonella typhimurium C587 (MIC=5.0 μg/ml), Salmonella typhimurium C610 (MIC=1.6 μg/ml), Pseudomonas aeruginosa H187 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=10.1 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=2.9 μg/ml) [Ref.15677462]MHC=15.6 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18557 KWKSFLKTFKKAVKTVLHTALKAISS 26 S11KD (V681 peptide derivative) No entry found Derived from the framework peptide V681 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. D-Lysine to replace L-Serine at the position 11 on the polar face of peptide V681. Has hemolytic activity. [Ref.15677462]Gram-positive bacteria: Staphylococcus aureus 25923 (MIC=4.0 μg/ml), Staphylococcus aureus SAP0017 (MIC=2.5 μg/ml), Staphylococcus epidermidis C621 (MIC=2.0 μg/ml), Bacillus subtilis C971 (MIC=2.0 μg/ml), Enterococcus faecalis C625 (MIC=12.7 μg/ml), Corynebacterium xerosis C875 (MIC=1.0 μg/ml), The geometric mean of MIC values above six Gram-positive strains (MIC=2.8 μg/ml);##Gram-negative bacteria: Escherichia coli UB1005 (MIC=3.2 μg/ml), Escherichia coli DC2 (MIC=1.6 μg/ml), Salmonella typhimurium C587 (MIC=3.2 μg/ml), Salmonella typhimurium C610 (MIC=1.6 μg/ml), Pseudomonas aeruginosa H187 (MIC=2.0 μg/ml), Pseudomonas aeruginosa H188 (MIC=6.4 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=2.6 μg/ml) [Ref.15677462]MHC=31.2 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15677462 J Biol Chem. 2005 Apr 1;280(13):12316-29. Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. DRAMP18558 FIKRIARLLRKIF 13 Kn2-7 (BmKn2 peptide derivative) No entry found Derived from the peptide BmKn2 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22792229]Gram-positive bacteria: Staphylococcus aureus AB94004 (MIC=3.13 μg/ml), Staphylococcus aureus ATCC 25923 (MIC=3.13 μg/ml), Bacillus subtilis AB91021 (MIC=6.25 μg/ml), Bacillus thuringiensis AB92037 (MIC=6.25 μg/ml), Micrococcus luteus AB93113 (MIC=6.25 μg/ml);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=6.25 μg/ml), Escherichia coli ATCC 25922 (MIC=25 μg/ml), Pseudomonas aeruginosa AB93066 (MIC=25 μg/ml), Pseudomonas aeruginosa A092994 (MIC=50 μg/ml), Pseudomonas aeruginosa A093052 (MIC=100 μg/ml), Pseudomonas aeruginosa A093056 (MIC=50 μg/ml), Pseudomonas aeruginosa A093085 (MIC=50 μg/ml), Pseudomonas aeruginosa A093115 (MIC=100 μg/ml). [Ref.22792229]Non-hemolysis at 6.25 μg/ml, 5% hemolysis at 12.5 μg/ml,10% hemolysis at 25 μg/ml 15% hemolysis at 50 μg/ml, 40% hemolysis at 100 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22792229 PLoS One. 2012;7(7):e40135. doi: 10.1371/journal.pone.0040135. Cao L, Dai C, Li Z, Fan Z, Song Y, Wu Y, Cao Z, Li W. Antibacterial activity and mechanism of a scorpion venom peptide derivative in vitro and in vivo. DRAMP18559 IWRIFRRIF 9 HFU3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22699557]Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=4 μM), Staphylococcus epidermidis ATCC 12228 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8 μM), Pseudomonas aeruginosa 27853 (MIC=4 μM) [Ref.22699557]MHC=101.4 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22699557 Amino Acids. 2012 Dec;43(6):2527-36. doi: 10.1007/s00726-012-1334-7. Ma QQ, Dong N, Shan AS, Lv YF, Li YZ, Chen ZH, Cheng BJ, Li ZY. Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. DRAMP18560 IWRIFRRIFRIF 12 HFU4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Has hemolytic activity. [Ref.22699557]Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=1 μM), Staphylococcus epidermidis ATCC 12228 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4 μM), Pseudomonas aeruginosa 27853 (MIC=4 μM) [Ref.22699557]MHC=19.6 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22699557 Amino Acids. 2012 Dec;43(6):2527-36. doi: 10.1007/s00726-012-1334-7. Ma QQ, Dong N, Shan AS, Lv YF, Li YZ, Chen ZH, Cheng BJ, Li ZY. Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. DRAMP18561 IWRIFRRIFRIFIRF 15 HFU5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22699557]Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=8 μM), Staphylococcus epidermidis ATCC 12228 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16 μM), Pseudomonas aeruginosa 27853 (MIC=16 μM) [Ref.22699557]MHC=15.0 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22699557 Amino Acids. 2012 Dec;43(6):2527-36. doi: 10.1007/s00726-012-1334-7. Ma QQ, Dong N, Shan AS, Lv YF, Li YZ, Chen ZH, Cheng BJ, Li ZY. Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. DRAMP18562 KSLVRRWRSRW 11 MAP-04-01 (Ixosin-B peptide derivative) No entry found Derived from the peptide Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. No hemolytic activity. [Ref.22578463]Gram-positive bacterium: Staphylococcus aureus (MIC90=30 μM);##Gram-negative bacterium: Escherichia coli (MIC90=30 μM), Pseudomonas aeroginosa (MIC90=40 μM) [Ref.22578463]Non-hemolysis at 100μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22578463 Bioorg Med Chem Lett. 2012 Jun 15;22(12):4185-8. Lung FD, Wang KS, Liao ZJ, Hsu SK, Song FY, Liou CC, Wu YS. Discovery of potent antimicrobial peptide analogs of Ixosin-B. DRAMP18563 KSLRRVWRSWR 11 MAP-04-02 (Ixosin-B peptide derivative) No entry found Derived from the peptide Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.No hemolytic activity. [Ref.22578463]Gram-positive bacterium: Staphylococcus aureus (MIC90=60 μM);##Gram-negative bacterium: Escherichia coli (MIC90=30 μM), Pseudomonas aeroginosa (MIC90=40 μM) [Ref.22578463]Non-hemolysis at 100μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22578463 Bioorg Med Chem Lett. 2012 Jun 15;22(12):4185-8. Lung FD, Wang KS, Liao ZJ, Hsu SK, Song FY, Liou CC, Wu YS. Discovery of potent antimicrobial peptide analogs of Ixosin-B. DRAMP18564 KWLRRVWRWWR 11 MAP-04-03 (Ixosin-B peptide derivative) No entry found Derived from the peptide Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Highly hemolytic activity. [Ref.22578463]Gram-positive bacterium: Staphylococcus aureus (MIC90=2.5 μM);##Gram-negative bacterium: Escherichia coli (MIC90=15 μM), Pseudomonas aeroginosa (MIC90=20 μM) [Ref.22578463]100% hemolysis at 100μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22578463 Bioorg Med Chem Lett. 2012 Jun 15;22(12):4185-8. Lung FD, Wang KS, Liao ZJ, Hsu SK, Song FY, Liou CC, Wu YS. Discovery of potent antimicrobial peptide analogs of Ixosin-B. DRAMP18565 KRLRRVWRRWR 11 MAP-04-04 (Ixosin-B peptide derivative) No entry found Derived from the peptide Ixosin-B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Weak hemolytic activity. [Ref.22578463]Gram-positive bacterium: Staphylococcus aureus (MIC90=5 μM);##Gram-negative bacterium: Escherichia coli (MIC90=30 μM), Pseudomonas aeroginosa (MIC90=20 μM) [Ref.22578463]3% hemolysis at 100μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22578463 Bioorg Med Chem Lett. 2012 Jun 15;22(12):4185-8. Lung FD, Wang KS, Liao ZJ, Hsu SK, Song FY, Liou CC, Wu YS. Discovery of potent antimicrobial peptide analogs of Ixosin-B. DRAMP18566 VNWKKSLGKSIKVVK 15 LL-IIIs-1 (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=0.7 μM), Bacillus cereus (MIC=0.8 μM), Staphylococcus aureus (MIC=12.5 μM);##Gram-negative bacteria: Escherichia coli (MIC=4.4 μM), Pseudomonas aeruginosa (MIC=78.7 μM);##Fungi: Candida albicans (MIC=100 μM) [Ref.22526241]LC50=31.3 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18567 VNWKKILGKSIKVSK 15 LL-IIIs-2 (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=0.9 μM), Bacillus cereus (MIC=1.2 μM), Staphylococcus aureus (MIC=20.3 μM);##Gram-negative bacteria: Escherichia coli (MIC=8.8 μM), Pseudomonas aeruginosa (MIC=86.7 μM);##Fungi: Candida albicans (MIC=100 μM) [Ref.22526241]LC50=69 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18568 VSWKKSLGKIIKVVK 15 LL-IIIs-3 (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.4 μM), Bacillus cereus (MIC=1.1 μM), Staphylococcus aureus (MIC=21.7 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.2 μM), Pseudomonas aeruginosa (MIC=76.3 μM);##Fungi: Candida albicans (MIC=93.3 μM) [Ref.22526241]LC50=30 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18569 VNSKKISGKSIKVSK 15 LL-IIIs-4 (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=2 μM), Bacillus cereus (MIC=1.1 μM), Staphylococcus aureus (MIC=80 μM);##Gram-negative bacteria: Escherichia coli (MIC=20 μM). [Ref.22526241]LC50>100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18570 VNRKKILGKSIKVVK 15 LL-IIIs-5 cis (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=0.9 μM), Bacillus cereus (MIC=0.9 μM), Staphylococcus aureus (MIC=45 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.5 μM), Pseudomonas aeruginosa (MIC=80 μM). [Ref.22526241]LC50=100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18571 VNRKKILGKSIKVVK 15 LL-IIIs-5 trans (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria .Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.1 μM), Bacillus cereus (MIC=1.3 μM), Staphylococcus aureus (MIC=65 μM);##Gram-negative bacteria: Escherichia coli (MIC=5.5 μM), Pseudomonas aeruginosa (MIC=80 μM). [Ref.22526241]LC50>100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18572 VNSKKISPKSIKVSK 15 LL-IIIs-6a (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1 μM), Bacillus cereus (MIC=1.1 μM), Staphylococcus aureus (MIC=93 μM);##Gram-negative bacteria: Escherichia coli (MIC=7.8 μM), Pseudomonas aeruginosa (MIC=93 μM). [Ref.22526241]LC50>100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18573 VNSKKISPKSIKVSK 15 LL-IIIs-6b (lasioglossin III peptide derivative) No entry found Derived from the peptide lasioglossin III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=0.9 μM), Bacillus cereus (MIC=0.8 μM), Staphylococcus aureus (MIC=50 μM);##Gram-negative bacteria: Escherichia coli (MIC=7.8 μM), Pseudomonas aeruginosa (MIC=63 μM). [Ref.22526241]LC50=82 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18574 GFLSILKKVLPKVXAHXK 18 MEP-N (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1 μM), Bacillus cereus (MIC=0.5 μM), Staphylococcus aureus (MIC=2.5 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.9 μM), Pseudomonas aeruginosa (MIC=17.3 μM);##Fungi: Candida albicans (MIC=15 μM) [Ref.22526241]LC50=50 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18575 GFLSILKKVLPKSXAHSK 18 MEP-Ns-1 (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=0.8 μM), Bacillus cereus (MIC=1.1 μM), Staphylococcus aureus (MIC=10.8 μM);##Gram-negative bacteria: Escherichia coli (MIC=2.5 μM), Pseudomonas aeruginosa (MIC=77 μM);##Fungi: Candida albicans (MIC=30 μM) [Ref.22526241]LC50=18.1 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18576 GFLSSLKKSLPKVXAHXK 18 MEP-Ns-2 (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.5 μM), Bacillus cereus (MIC=1.2 μM), Staphylococcus aureus (MIC=37 μM);##Gram-negative bacteria: Escherichia coli (MIC=7.8 μM). [Ref.22526241]LC50=14.7 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18577 GFLSSLKKSLPKSXAHSK 18 MEP-Ns-3 (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.3 μM), Bacillus cereus (MIC=1.2 μM) ;##Gram-negative bacteria: Escherichia coli (MIC=46.7 μM). [Ref.22526241]LC50=13.9 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18578 GFRSILKKVSPKVXAHXK 18 MEP-Ns-4 cis (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.5 μM), Bacillus cereus (MIC=1.3 μM), Staphylococcus aureus (MIC=37 μM);##Gram-negative bacteria: Escherichia coli (MIC=8.1 μM). [Ref.22526241]LC50=11 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18579 GFRSILKKVSPKVXAHXK 18 MEP-Ns-4 trans (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=2 μM), Bacillus cereus (MIC=1.7 μM), Staphylococcus aureus (MIC=63 μM);##Gram-negative bacteria: Escherichia coli (MIC=16.3 μM). [Ref.22526241]LC50=20 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18580 GFLSSLKKSLGKSXAHSK 18 MEP-Ns-5 (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.5 μM), Bacillus cereus (MIC=1.2 μM), Staphylococcus aureus (MIC=57 μM);##Gram-negative bacteria: Escherichia coli (MIC=5.6 μM). [Ref.22526241]LC50=29 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18581 GFLSSLKKSLAKSXAHSK 18 MEP-Ns-6 (melectin peptide derivative) No entry found Derived from the peptide melectin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.22526241]Gram-positive bacteria: Micrococcus luteus (MIC=1.5 μM), Bacillus cereus (MIC=1.2 μM), Staphylococcus aureus (MIC=43 μM);##Gram-negative bacteria: Escherichia coli (MIC=5.6 μM). [Ref.22526241]LC50=39.5 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. Chapuis H, Slaninová J, Bednárová L, Monincová L, Buděšínský M, Čeřovský V. Effect of hydrocarbon stapling on the properties of DRAMP18582 KWFRVYRGIYRRR 13 CDT (Tachyplesin-1 peptide derivative) No entry found Derived from the peptide Tachyplesin-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Beta strand All of the four Cys residues were deleted from the primary structure of AMP. Function: The MIC values of CDT were even found to be lower against Escherichia coli and Listeria monocytogenes in comparison to the native TP-1 peptide. No hemolytic activity. No MICs found in DRAMP database [Ref.22464970]Non-hemolysis at 200 μg/mL against Not found (The literature does not mention). Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22464970 Biochim Biophys Acta. 2012 Jul;1818(7):1613-24. Saravanan R, Mohanram H, Joshi M, Domadia PN, Torres J, Ruedl C, Bhattacharjya S. Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization. DRAMP18583 KWCFCVCYRGICYCRCRG 18 Tricystine cyclic cystine TP (ccTP, Tachyplesin-1 peptide derivative) No entry found Derived from the peptide Tachyplesin-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Beta tile Although there is insufficient information to deconvolute these CD spectra of these two-b-strand cyclic cystine-knot structures due to the various contributions by β-turns, aromatic residues, disulfides and b-sheet structures, it is reasonable to conclude that all cyclic tachyplesins 2–6 as well as RTD display ordered structures in methanol. Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria.Antifungal activity agaist Candida albicans, Candida kefyr, Candida tropicalis [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.0 μM in low-salt; MIC=0.8 μM in high-salt), Micrococcus luteus (MIC=0.5 μM in low-salt; MIC=0.4 μM in high-salt), Enterococcus faecalis (MIC=1.0 μM in low-salt; MIC=0.9 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=3.0 μM in low-salt; MIC=6.9 μM in high-salt), Pseudomonas aeruginosa (MIC=5.0 μM in low-salt; MIC=5.2 μM in high-salt), Primula vulgaris (MIC=6.0 μM in low-salt; MIC=14.4 μM in high-salt), Klebsiella oxytoca (MIC=2.1 μM in low-salt; MIC=7.8 μM in high-salt);##Fungi: Candida albicans (MIC=5.1 μM in low-salt; MIC=17.2 μM in high-salt), Candida kefyr (MIC=3.9 μM in low-salt; MIC=4.1 μM in high-salt), Candida tropicalis (MIC=5.2 μM in low-salt; MIC=1.1 μM in high-salt). [Ref.10673369] EC25=3800 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18584 KWCFCVCYRGICRCRCRG 18 [Arg13]ccTP (ccTP peptide derivative) No entry found Derived from the peptide ccTP Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.3 μM in low-salt; MIC=0.9 μM in high-salt), Micrococcus luteus (MIC=0.5 μM in low-salt; MIC=0.5 μM in high-salt), Enterococcus faecalis (MIC=1.9 μM in low-salt; MIC=1.3 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=10.4 μM in low-salt; MIC=0.9 μM in high-salt), Pseudomonas aeruginosa (MIC=6.2 μM in low-salt; MIC=10.4 μM in high-salt), Primula vulgaris (MIC=16.4 μM in low-salt; MIC=28.9 μM in high-salt), Klebsiella oxytoca (MIC=4.0 μM in low-salt; MIC=7.6 μM in high-salt);##Fungi: Candida albicans (MIC=24.2 μM in low-salt; MIC=30.2 μM in high-salt), Candida kefyr (MIC=1.1 μM in low-salt; MIC=4.3 μM in high-salt), Candida tropicalis (MIC=12.4 μM in low-salt; MIC=3.9 μM in high-salt). [Ref.10673369] EC25=590 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18585 KWCRCVCRRGICYCRCRG 18 [Arg4,8]ccTP (ccTP peptide derivative) No entry found Derived from the peptide ccTP Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Beta tile Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.3 μM in low-salt; MIC=0.3 μM in high-salt), Micrococcus luteus (MIC=0.5 μM in low-salt; MIC=0.7 μM in high-salt), Enterococcus faecalis (MIC=1.0 μM in low-salt; MIC=1.2 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=9.8 μM in low-salt; MIC=2.0 μM in high-salt), Pseudomonas aeruginosa (MIC=8.0 μM in low-salt; MIC=5.3 μM in high-salt), Primula vulgaris (MIC=26.7 μM in low-salt; MIC=56.2 μM in high-salt), Klebsiella oxytoca (MIC=6.1 μM in low-salt; MIC=7.8 μM in high-salt);##Fungi: Candida albicans (MIC=6.4 μM in low-salt; MIC=11.2 μM in high-salt), Candida kefyr (MIC=1.1 μM in low-salt; MIC=1.9 μM in high-salt), Candida tropicalis (MIC=2.8 μM in low-salt; MIC=4.2 μM in high-salt). [Ref.10673369] EC25=910 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18586 KWCRCVCRRGICRCRCRG 18 [Arg4,8,13]ccTP (ccTP peptide derivative) No entry found Derived from the peptide ccTP Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.7 μM in low-salt; MIC=1.3 μM in high-salt), Micrococcus luteus (MIC=0.5 μM in low-salt; MIC=0.8 μM in high-salt), Enterococcus faecalis (MIC=0.7 μM in low-salt; MIC=0.5 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=5.5 μM in low-salt; MIC=1.2 μM in high-salt), Pseudomonas aeruginosa (MIC=3.9 μM in low-salt; MIC=4.7 μM in high-salt), Primula vulgaris (MIC=16.8 μM in low-salt; MIC=55.6 μM in high-salt), Klebsiella oxytoca (MIC=2.4 μM in low-salt; MIC=5.4 μM in high-salt);##Fungi: Candida albicans (MIC=7.1 μM in low-salt; MIC=5.1 μM in high-salt), Candida kefyr (MIC=4.2 μM in low-salt; MIC=0.7 μM in high-salt), Candida tropicalis (MIC=1.9 μM in low-salt; MIC=4.8 μM in high-salt). [Ref.10673369] EC25=920 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18587 KWCRCVCRRGICRCRCRK 18 [Arg4,8,13][Lys18]ccTP (ccTP peptide derivative) No entry found Derived from the peptide ccTP Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.7 μM in low-salt; MIC=0.7 μM in high-salt), Micrococcus luteus (MIC=0.3 μM in low-salt; MIC=0.4 μM in high-salt), Enterococcus faecalis (MIC=1.4 μM in low-salt; MIC=1.2 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=6.1 μM in low-salt; MIC=1.2 μM in high-salt), Pseudomonas aeruginosa (MIC=2.0 μM in low-salt; MIC=4.7 μM in high-salt), Primula vulgaris (MIC=17.0 μM in low-salt; MIC=39.8 μM in high-salt), Klebsiella oxytoca (MIC=4.1 μM in low-salt; MIC=4.1 μM in high-salt);##Fungi: Candida albicans (MIC=10.5 μM in low-salt; MIC=5.2 μM in high-salt), Candida kefyr (MIC=1.1 μM in low-salt; MIC=0.7 μM in high-salt), Candida tropicalis (MIC=2.3 μM in low-salt; MIC=1.9 μM in high-salt). [Ref.10673369] EC25=3900 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18588 GFCRCLCRRGVCRCICTK 18 RTD No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.10673369]Gram-positive bacteria: Staphylococcus aureus (MIC=1.1 μM in low-salt; MIC=0.9 μM in high-salt), Micrococcus luteus (MIC=0.5 μM in low-salt; MIC=0.4 μM in high-salt), Enterococcus faecalis (MIC=1.2 μM in low-salt; MIC=1.2 μM in high-salt);##Gram-negative bacteria: Escherichia coli (MIC=2.0 μM in low-salt; MIC=28.4 μM in high-salt), Pseudomonas aeruginosa (MIC=2.0 μM in low-salt; MIC=5.2 μM in high-salt), Primula vulgaris (MIC=10.2 μM in low-salt; MIC=50.4 μM in high-salt), Klebsiella oxytoca (MIC=2.0 μM in low-salt; MIC=12.8 μM in high-salt);##Fungi: Candida albicans (MIC=4.0 μM in low-salt; MIC=5.2 μM in high-salt), Candida kefyr (MIC=1.8 μM in low-salt; MIC=1.2 μM in high-salt), Candida tropicalis (MIC=2.8 μM in low-salt; MIC=1.0 μM in high-salt). [Ref.10673369]EC25=2350 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. Tam JP, Lu YA, Yang JL. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework. DRAMP18589 GWLDVAKKIGKAAFNVAKNFLFNKAVNFAAKGIKKAVDLWG 42 DSE (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi.Has hemolytic activity. [Ref.22391524]Gram-positive bacterium: Staphylococcus aureus (MIC=8.9 μmol/L; MMC=13.3 μmol/L);##Gram-negative bacterium: Escherichia coli (MIC=3.3 μmol/L; MMC=13.3 μmol/L);##Fungi: Candida albicans (MIC=53.3 μmol/L; MMC=53.3 μmol/L) [Ref.22391524]HC50=0.6±0.1 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22391524 Antimicrob Agents Chemother. 2012 Jun;56(6):3004-10. Lorenzón EN, Cespedes GF, Vicente EF, Nogueira LG, Bauab TM, Castro MS, Cilli EM. Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha. DRAMP18590 GWLDVAKKIGKAAFNVAKNFL-spacer-LFNKAVNFAAKGIKKAVDLWG 42 DEP (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22391524]Gram-positive bacterium: Staphylococcus aureus (MIC=3.2 μmol/L; MMC=12.9 μmol/L);##Gram-negative bacterium: Escherichia coli (MIC=1.6 μmol/L; MMC=3.2 μmol/L);##Fungi: Candida albicans (MIC=51.7 μmol/L; MMC=51.7 μmol/L) [Ref.22391524]HC50=0.7±0.1 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22391524 Antimicrob Agents Chemother. 2012 Jun;56(6):3004-10. Lorenzón EN, Cespedes GF, Vicente EF, Nogueira LG, Bauab TM, Castro MS, Cilli EM. Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha. DRAMP18591 GWLDVAKKIGKAAFNVAKNFL-spacer-LFNKAVNFAAKGIKKAVDLWG 42 DEA (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22391524]Gram-positive bacterium: Staphylococcus aureus (MIC=12.9 μmol/L; MMC=25.9 μmol/L);##Gram-negative bacterium: Escherichia coli (MIC=6.5 μmol/L; MMC=12.9 μmol/L);##Fungi: Candida albicans (MIC=100 μmol/L; MMC<100 μmol/L) [Ref.22391524]HC50=0.8±0.1 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22391524 Antimicrob Agents Chemother. 2012 Jun;56(6):3004-10. Lorenzón EN, Cespedes GF, Vicente EF, Nogueira LG, Bauab TM, Castro MS, Cilli EM. Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha. DRAMP18592 GWLDVAKKIGKAAFNVAKNFI 21 Ctx(Ile21)-Ha (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22519531]Gram-positive bacterium: Staphylococcus aureus (MIC=1 μmol/L);##Gram-negative bacteria: Escherichia coli (MIC=4 μmol/L), Pseudomonas aeruginosa (MIC=8 μmol/L);##Fungi: Candida albicans (MIC=8 μmol/L), Candida krusei (MIC=8 μmol/L), Candida parapsilosis (MIC=4 μmol/L), Cryptococcus neoformans (MIC=8 μmol/L) [Ref.22519531]HC50=26 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22519531 Protein Pept Lett. 2012 Jun 1;19(6):596-603. Cespedes GF, Lorenzón EN, Vicente EF, Mendes-Giannini MJ, Fontes W, Castro MS, Cilli EM. Mechanism of action and relationship between structure and biological activity of Ctx-Ha: a new ceratotoxin-like peptide from Hypsiboas albopunctatus. DRAMP18593 GWLDVAKKIGKAAFNVAKNFI 21 Ctx(Ile21)-Ha-VD16 (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. D-Valine to replace L-Valine at the position 16 on the peptide Ctx(Ile21)-Ha. Has hemolytic activity. [Ref.22519531]Gram-positive bacterium: Staphylococcus aureus (MIC=2 μmol/L);##Gram-negative bacteria: Escherichia coli (MIC=4 μmol/L), Pseudomonas aeruginosa (MIC=16 μmol/L);##Fungi: Candida albicans (MIC=31 μmol/L), Candida krusei (MIC=16 μmol/L), Candida parapsilosis (MIC=31 μmol/L), Cryptococcus neoformans (MIC=31 μmol/L) [Ref.22519531]HC50=18.7 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22519531 Protein Pept Lett. 2012 Jun 1;19(6):596-603. Cespedes GF, Lorenzón EN, Vicente EF, Mendes-Giannini MJ, Fontes W, Castro MS, Cilli EM. Mechanism of action and relationship between structure and biological activity of Ctx-Ha: a new ceratotoxin-like peptide from Hypsiboas albopunctatus. DRAMP18594 GWLDVAKKIGKAAFNVAKNFI 21 Ctx(Ile21)-Ha-VD5,16 (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. D-Valine to replace L-Valine at the position 5 and 16 on the peptide Ctx(Ile21)-Ha.Has hemolytic activity. [Ref.22519531]Gram-positive bacterium: Staphylococcus aureus (MIC=64 μmol/L);##Gram-negative bacteria: Escherichia coli (MIC=16 μmol/L), Pseudomonas aeruginosa (MIC=128 μmol/L);##Fungi: Candida albicans (MIC=16 μmol/L), Candida krusei (MIC=16 μmol/L), Candida parapsilosis (MIC=31 μmol/L), Cryptococcus neoformans (MIC=31 μmol/L) [Ref.22519531]HC50=43.1 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22519531 Protein Pept Lett. 2012 Jun 1;19(6):596-603. Cespedes GF, Lorenzón EN, Vicente EF, Mendes-Giannini MJ, Fontes W, Castro MS, Cilli EM. Mechanism of action and relationship between structure and biological activity of Ctx-Ha: a new ceratotoxin-like peptide from Hypsiboas albopunctatus. DRAMP18595 GWLDVAKKKGKAAFNVAKNFI 21 Ctx(Ile21)-Ha-I9K (Ctx-Ha peptide derivative) No entry found Derived from the peptide Ctx-Ha Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. L-Lysine to replace L-Isoleucine at the position 9 on the peptide Ctx(Ile21)-Ha.Has hemolytic activity. [Ref.22519531]Gram-negative bacteria: Escherichia coli (MIC=8 μmol/L), Pseudomonas aeruginosa (MIC=32 μmol/L);##Fungi: Candida albicans (MIC=16 μmol/L), Candida krusei (MIC=31 μmol/L), Candida parapsilosis (MIC=31 μmol/L), Cryptococcus neoformans (MIC=31 μmol/L) [Ref.22519531]HC50=24.9 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22519531 Protein Pept Lett. 2012 Jun 1;19(6):596-603. Cespedes GF, Lorenzón EN, Vicente EF, Mendes-Giannini MJ, Fontes W, Castro MS, Cilli EM. Mechanism of action and relationship between structure and biological activity of Ctx-Ha: a new ceratotoxin-like peptide from Hypsiboas albopunctatus. DRAMP18596 NVWKKVLGKIIKVAK 15 LL-I/1 (Lasioglossin LL-I peptide derivative) No entry found Derived from the peptide Lasioglossin LL-I Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=1.3 μM), Staphylococcus aureus (MIC=71.6 μM);##Gram-negative bacteria: Escherichia coli (MIC=2.5 μM), Pseudomonas aeruginosa (MIC=22.7 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2102. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18597 VNWKKVLAKIIKVAK 15 LL-I/2 (Lasioglossin LL-I peptide derivative) No entry found Derived from the peptide Lasioglossin LL-I Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.6 μM), Staphylococcus aureus (MIC=7.2 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.7 μM), Pseudomonas aeruginosa (MIC=26.9 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2103. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18598 VNWKKVLKKIIKVAK 15 LL-I/3 (Lasioglossin LL-I peptide derivative) No entry found Derived from the peptide Lasioglossin LL-I Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=15.6 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.7 μM), Pseudomonas aeruginosa (MIC=19.0 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2104. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18599 VNWKKVLPKIIKVAK 15 LL-I/4 (Lasioglossin LL-I peptide derivative) No entry found Derived from the peptide Lasioglossin LL-I Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.9 μM);##Gram-negative bacteria: Escherichia coli (MIC=5.0 μM), Pseudomonas aeruginosa (MIC=100 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2105. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18600 NVWKKILGKIIKVAK 15 LL-II/1 (Lasioglossin LL-II peptide derivative) No entry found Derived from the peptide Lasioglossin LL-II Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=19.7 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.1 μM), Pseudomonas aeruginosa (MIC=23.3 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2106. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18601 VNWKKILAKIIKVAK 15 LL-II/2 (Lasioglossin LL-II peptide derivative) No entry found Derived from the peptide Lasioglossin LL-II Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.Has hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=4.3 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.7 μM), Pseudomonas aeruginosa (MIC=22.5 μM). [Ref.19591185]LC50=66.5 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2107. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18602 VNWKKILKKIIKVAK 15 LL-II/3 (Lasioglossin LL-II peptide derivative) No entry found Derived from the peptide Lasioglossin LL-II Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=15.6 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.7 μM), Pseudomonas aeruginosa (MIC=26.1 μM). [Ref.19591185]LC50=88.2 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2108. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18603 VNWKKILPKIIKVAK 15 LL-II/4 (Lasioglossin LL-II peptide derivative) No entry found Derived from the peptide Lasioglossin LL-II Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=80 μM);##Gram-negative bacteria: Escherichia coli (MIC=2.5 μM), Pseudomonas aeruginosa (MIC=100 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2109. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18604 NVWKKILGKIIKVVK 15 LL-III/1 (Lasioglossin LL-III peptide derivative) No entry found Derived from the peptide Lasioglossin LL-III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=9.0 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.4 μM), Pseudomonas aeruginosa (MIC=23.1 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2110. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18605 VNWKKILAKIIKVVK 15 LL-III/2 (Lasioglossin LL-III peptide derivative) No entry found Derived from the peptide Lasioglossin LL-III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Has hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.6 μM), Staphylococcus aureus (MIC=2.2 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.4 μM), Pseudomonas aeruginosa (MIC=27.1 μM). [Ref.19591185]LC50=55.1 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2111. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18606 VNWKKILKKIIKVVK 15 LL-III/3 (Lasioglossin LL-III peptide derivative) No entry found Derived from the peptide Lasioglossin LL-III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.Has hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.7 μM), Staphylococcus aureus (MIC=9.6 μM);##Gram-negative bacteria: Escherichia coli (MIC=0.7 μM), Pseudomonas aeruginosa (MIC=26.1 μM). [Ref.19591185]LC50=72.2 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2112. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18607 VNWKKILPKIIKVVK 15 LL-III/4 (Lasioglossin LL-III peptide derivative) No entry found Derived from the peptide Lasioglossin LL-III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.8 μM), Staphylococcus aureus (MIC=32.5 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.2 μM), Pseudomonas aeruginosa (MIC=100 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2113. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18608 VNWKKILGKIIKVVK 15 LL-III/5 (Lasioglossin LL-III peptide derivative) No entry found Derived from the peptide Lasioglossin LL-III Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.Weak hemolytic activity. PTM: C-terminal hydroxyl modification" [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=1.2 μM), Staphylococcus aureus (MIC=40 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.5 μM), Pseudomonas aeruginosa (MIC=40 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2114. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18609 VNWKKILGKIIKVVK 15 LL-Ⅲ/6 (Lasioglossin LL-Ⅲ peptide derivative) No entry found Derived from the peptide Lasioglossin LL-Ⅲ Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. PTM: C-terminal methoxy modification" [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=0.5 μM), Staphylococcus aureus (MIC=2.1 μM);##Gram-negative bacteria: Escherichia coli (MIC=1.0 μM), Pseudomonas aeruginosa (MIC=22.5 μM). [Ref.19591185]LC50=79.3 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2115. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18610 VNWKKILGKI 10 LL-Ⅲ/7 (Lasioglossin LL-Ⅲ peptide derivative) No entry found Derived from the peptide Lasioglossin LL-Ⅲ Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=4.7 μM);##Gram-negative bacteria: Escherichia coli (MIC=23.3 μM), Pseudomonas aeruginosa (MIC=75 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2116. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18611 ILGKIIKVVK 10 LL-Ⅲ/8 (Lasioglossin LL-Ⅲ peptide derivative) No entry found Derived from the peptide Lasioglossin LL-Ⅲ Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Weak hemolytic activity. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=40 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2117. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18612 KIIKVVK 7 LL-Ⅲ/10 (Lasioglossin LL-Ⅲ peptide derivative) No entry found Derived from the peptide Lasioglossin LL-Ⅲ Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria. [Ref.19591185]Gram-positive bacteria: Bacillus subtilis (MIC=100 μM). [Ref.19591185]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19591185 Chembiochem. 2009 Aug 17;10(12):2089-2119. Cerovský V, Budesínský M, Hovorka O, Cvacka J, Voburka Z, Slaninová J, Borovicková L, Fucík V, Bednárová L, Votruba I, Straka J. Lasioglossins: Three Novel Antimicrobial Peptides from the Venom of the Eusocial Bee Lasioglossum laticeps (Hymenoptera: Halictidae. DRAMP18613 VRRFGWWWGFLRR 13 TPG (Tritrpticin peptide derivative) No entry found Derived from the peptide Tritrpticin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.12207877]Gram-positive bacteria: Bacillus subtilis (MIC=16 μg/ml), Staphylococcus aureus (MIC=16 μg/ml), Staphylococcus epidermidis (MIC=8 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=32 μg/ml), Salmonella typhimurium (MIC=32 μg/ml), Pseudomonas aeruginosa (MIC=64 μg/ml);##Fungus: Candida albicans (MIC=32 μg/ml). [Ref.12207877]6% hemolysis at 25 μg/ml, 15% hemolysis at 50 μg/ml, 25% hemolysis at 100 μg/ml, 70% hemolysis at 200 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12207877 Biochem Biophys Res Commun. 2002 Sep 6;296(5):1044-50. Yang ST, Yub Shin SY, Kim YC, Kim Y, Hahm KS, Kim JI. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. DRAMP18627 KLKKLLKKWLKLLKKLLK 18 D4-K9L8W (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 12 and 16 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 4 and 8 on the peptide K9L8W. Weak hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=1 μM), Staphylococcus epidermidis (MIC=2 μM), Staphylococcus aureus (MIC=2 μM);##Gram-negative bacteria: Escherichia coli (MIC=2 μM), Pseudomonas aeruginosa (MIC=2 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50>800 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18507 FSGGNCRGFRRRCFCTK 17 SolyC (Plant defensin; tomato, plants) No entry found Belongs to the tomato defensin family Not found Tomato Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Beta sheet Not found Function: Antibacterial activity against a panel of human pathogens, including H.pylori, and displays anti-inflammatory activity in vitro. Weak hemolytic activity. [Ref.23124812]Gram-positive bacteria: Staphylococcus aureus A170 (MIC=40 μg/mL), Staphylococcus epidermidis (MIC=40 μg/mL), Listeria monocytogenes (MIC=40 μg/mL);##Gram-negative bacteria: Salmonella enterica serovar Paratyphi (MIC=15 μg/mL), Escherichia coli (MIC=15 μg/mL), Helicobacter pylori VB1 (MIC=15 μg/mL), Helicobacter pylori VB2 (MIC=10 μg/mL), Helicobacter pylori VB3 (MIC=15 μg/mL), Helicobacter pylori VB4 (MIC=12 μg/mL), Helicobacter pylori VB5 (MIC=15 μg/mL), Helicobacter pylori VB6 (MIC=10 μg/mL), Helicobacter pylori VB7 (MIC=15 μg/mL), Helicobacter pylori VB8 (MIC=10 μg/mL), Helicobacter pylori VB9 (MIC=10 μg/mL), Helicobacter pylori VB10 (MIC=15 μg/mL). [Ref.23124812]<5% hemolysis at 50 μg/mL against mouse red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23124812 J Pept Sci. 2012 Dec;18(12):755-62. Rigano MM, Romanelli A, Fulgione A, Nocerino N, D'Agostino N, Avitabile C, Frusciante L, Barone A, Capuano F, Capparelli R. A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori. DRAMP20763 DIDITGCSACKYAAGQVCTIGCSAAGGFICGLLGITIPVAGLSCLGFVEIVCTVADEYSGCGDAVAKEACNRAGLC 76 Halocin C8 (HalC8, Halocin-C8; Microhalocins, Archaeocin, Bacteriocin, Archaea, Euryarchaeota, Prokaryotes) P83716 Not found proC8 Halobacterium sp. (strain AS7092) Antimicrobial, Antibacterial Protein level Not found Not found "Function: Antibacterial activity against a wide variety of haloarchaeons. Causes cell lysis and death, possibly by disrupting the cell wall. Immunity protein HalI: Acts as an immunity protein for halocin-C8. Able to block the halocin-C8 activity by sequestering the activity of halocin-C8 through specific and direct binding. Miscellaneous: Is quite robust, as it can be desalted, boiled, subjected to organic solvents, and stored at 4 degrees Celsius for extended periods without losing activity. Induction: Increases to maximal levels upon transition from exponential to stationary phase." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12811620 Extremophiles. 2003 Oct;7(5):401-7. Li Y, Xiang H, Liu J, Zhou M, Tan H. Purification and biological characterization of halocin C8, a novel peptide antibiotic from Halobacterium strain AS7092. DRAMP20764 LQSNININTAAAVILIFNQVQVGALCAPTPVSGGGPVP 38 Halocin R1 (HalR1, Halocin-R1; Microhalocins, Archaeocin, Bacteriocin, Archaea, Euryarchaeota, Prokaryotes) No entry found Not found Not found Halobacterium sp. GN101 Antimicrobial, Antibacterial Protein level Not found Not found "Function: HalR1 is a microhalocin ( 38 amino acids ), and even more intriguing, HalR1 is 63% identical and 71% similar to HalS8 (identical residues in capitals ) . HalR1 is not cationic like typical bacteriocins and eucaryocins, it will be interesting to discover their mechanisms of action." [Ref.11114928] Archaea: Sulfolobus solfataricus (Inhibition Zone=7mm) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11938468##11114928 J Ind Microbiol Biotechnol. 2002 Jan;28(1):23-31.##J Bacteriol. 2001 Jan;183(1):287-91. O'Connor EM, Shand RF.##Haseltine C, Hill T, Montalvo-Rodriguez R, Kemper SK, Shand RF, Blum P. Halocins and sulfolobicins: the emerging story of archaeal protein and peptide antibiotics.##Secreted euryarchaeal microhalocins kill hyperthermophilic crenarchaea. DRAMP20765 DIDITGCSACKYAAGQVCTIGCSAAGGFICGLLGITIPVAGLSSLGFFVITCTTSADYYSIPDSNAAK 68 Halocin A4 (HalA4, Halocin-A4, Halocin U1; Microhalocins, Archaeocin, Bacteriocin, Archaea, Euryarchaeota, Prokaryotes) No entry found Not found Not found Haloarchaeon strain TuA4 Antimicrobial, Antibacterial Protein level Not found Not found Function: TuA4 cell lysates are not toxic for S. solfataricus, and protease (but not nuclease) treatment of the halocin A4 preparation inactivated toxicity, indicating that the A4 toxic factor must be a secreted protein. [Ref.11114928] Archaea: Sulfolobus solfataricus (Inhibition Zone=12mm) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11114928 J Bacteriol. 2001 Jan;183(1):287-91. Haseltine C, Hill T, Montalvo-Rodriguez R, Kemper SK, Shand RF, Blum P. Secreted euryarchaeal microhalocins kill hyperthermophilic crenarchaea. DRAMP18614 VRRFAWWWAFLRR 13 TPA (Tritrpticin peptide derivative) No entry found Derived from the peptide Tritrpticin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.12207877]Gram-positive bacteria: Bacillus subtilis (MIC=16 μg/ml), Staphylococcus aureus (MIC=32 μg/ml), Staphylococcus epidermidis (MIC=16 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=32 μg/ml), Salmonella typhimurium (MIC=32 μg/ml), Pseudomonas aeruginosa (MIC=64 μg/ml);##Fungus: Candida albicans (MIC=32 μg/ml). [Ref.12207877]18% hemolysis at 25 μg/ml, 30% hemolysis at 50 μg/ml, 62% hemolysis at 100 μg/ml, 95% hemolysis at 200 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12207877 Biochem Biophys Res Commun. 2002 Sep 6;296(5):1044-50. Yang ST, Yub Shin SY, Kim YC, Kim Y, Hahm KS, Kim JI. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. DRAMP18615 VRRFPFFFPFLRR 13 TWF (Tritrpticin peptide derivative) No entry found Derived from the peptide Tritrpticin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. No hemolytic activity. [Ref.12207877]Gram-positive bacteria: Bacillus subtilis (MIC=8 μg/ml), Staphylococcus aureus (MIC=16 μg/ml), Staphylococcus epidermidis (MIC=8 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=8 μg/ml), Salmonella typhimurium (MIC=8 μg/ml), Pseudomonas aeruginosa (MIC=16 μg/ml);##Fungus: Candida albicans (MIC=16 μg/ml). [Ref.12207877]Non-hemolysis at 200 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12207877 Biochem Biophys Res Commun. 2002 Sep 6;296(5):1044-50. Yang ST, Yub Shin SY, Kim YC, Kim Y, Hahm KS, Kim JI. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. DRAMP18616 RGLRRLGRKIAHGVKKYGPTVKRIKRKA 28 [K22,25,27]-SMAP-29 (SMAP-29 peptide derivative) No entry found Derived from the peptide SMAP-29 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. No hemolytic activity. [Ref.11467858]Gram-positive bacteria: [No NaCl]: Bacillus subtilis (MIC=6.0 μM), Staphylococcus aureus (MIC=2.0 μM), Micrococcus luteus (MIC=2.0 μM), Staphylococcus epidermidis (MIC=1.0 μM);##[100 mM NaCl]: Bacillus subtilis (MIC=4.0 μM), Staphylococcus aureus (MIC=1.0 μM), Micrococcus luteus (MIC=1.0 μM), Staphylococcus epidermidis (MIC=1.0 μM).##Gram-negative bacteria: [No NaCl]: Escherichia coli (MIC=6.0 μM), Salmonella typhimurium (MIC=2.0 μM), Pseudomonas aeruginosa (MIC=12.0 μM);[100 mM NaCl]: Escherichia coli (MIC=4.0 μM), Salmonella typhimurium (MIC=1.0 μM), Pseudomonas aeruginosa (MIC=4.0 μM).##Fungi: [No NaCl]: Candida albicans (MIC=2.0 μM);[100 mM NaCl]: Candida albicans (MIC=16.0 μM). [Ref.11467858]Non-hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11467858 Biochem Biophys Res Commun. 2001 Jul 27;285(4):1046-51. Shin SY, Park EJ, Yang ST, Jung HJ, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide. DRAMP18617 RGLRRLGRKIAHGVKKYGATVLRIIRIA 28 [A19]-SMAP-29 (SMAP-29 peptide derivative) No entry found Derived from the peptide SMAP-29 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.11467858]Gram-positive bacteria: [No NaCl]: Bacillus subtilis (MIC=4.0 μM), Staphylococcus aureus (MIC=2.0 μM), Micrococcus luteus (MIC=2.0 μM), Staphylococcus epidermidis (MIC=2.0 μM);##[100 mM NaCl]: Bacillus subtilis (MIC=2.0 μM), Staphylococcus aureus (MIC=1.0 μM), Micrococcus luteus (MIC=2.0 μM), Staphylococcus epidermidis (MIC=1.0 μM).##Gram-negative bacteria: [No NaCl]: Escherichia coli (MIC=4.0 μM), Salmonella typhimurium (MIC=2.0 μM), Pseudomonas aeruginosa (MIC=16.0 μM);[100 mM NaCl]: Escherichia coli (MIC=1.0 μM), Salmonella typhimurium (MIC=1.0 μM), Pseudomonas aeruginosa (MIC=4.0 μM).##Fungi: [No NaCl]: Candida albicans (MIC=2.0 μM);[100 mM NaCl]: Candida albicans (MIC=16.0 μM). [Ref.11467858]7% hemolysis at 12.5 μM, 13% hemolysis at 25 μg/ml, 28% hemolysis at 50 μg/ml, 50.4% hemolysis at 100 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11467858 Biochem Biophys Res Commun. 2001 Jul 27;285(4):1046-51. Shin SY, Park EJ, Yang ST, Jung HJ, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide. DRAMP18618 RGLRRLGRKIAHGVKKY 17 SMAP-29(1-17) (SMAP-29 peptide derivative) No entry found Derived from the peptide SMAP-29 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. No hemolytic activity. [Ref.11467858]Gram-positive bacteria: [No NaCl]: Bacillus subtilis (MIC=8.0 μM), Staphylococcus aureus (MIC=2.0 μM), Micrococcus luteus (MIC=2.0 μM), Staphylococcus epidermidis (MIC=1.0 μM);##[100 mM NaCl]: Bacillus subtilis (MIC=16.0 μM), Staphylococcus aureus (MIC=4.0 μM), Micrococcus luteus (MIC=4.0 μM), Staphylococcus epidermidis (MIC=2.0 μM).##Gram-negative bacteria: [No NaCl]: Escherichia coli (MIC=8.0 μM), Salmonella typhimurium (MIC=2.0 μM), Pseudomonas aeruginosa (MIC=8.0 μM);[100 mM NaCl]: Escherichia coli (MIC=16.0 μM), Salmonella typhimurium (MIC=8.0 μM), Pseudomonas aeruginosa (MIC=16.0 μM).##Fungi: [No NaCl]: Candida albicans (MIC=8.0 μM);[100 mM NaCl]: Candida albicans (MIC=16.0 μM). [Ref.11467858]Non-hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11467858 Biochem Biophys Res Commun. 2001 Jul 27;285(4):1046-51. Shin SY, Park EJ, Yang ST, Jung HJ, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide. DRAMP18619 RKLRRLKRKIAHKVKKY 17 [K2,7,13]-SMAP-29(1-17) (SMAP-29 peptide derivative) No entry found Derived from the peptide SMAP-29 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. No hemolytic activity. [Ref.11467858]Gram-positive bacteria: [No NaCl]: Bacillus subtilis (MIC=4.0 μM), Staphylococcus aureus (MIC=2.0 μM), Micrococcus luteus (MIC=2.0 μM), Staphylococcus epidermidis (MIC=1.0 μM);[100 mM NaCl]: Bacillus subtilis (MIC=4.0 μM), Staphylococcus aureus (MIC=2.0 μM), Micrococcus luteus (MIC=1.0 μM), Staphylococcus epidermidis (MIC=1.0 μM).##Gram-negative bacteria: [No NaCl]: Escherichia coli (MIC=3.0 μM), Salmonella typhimurium (MIC=2.0 μM), Pseudomonas aeruginosa (MIC=6.0 μM);[100 mM NaCl]: Escherichia coli (MIC=6.0 μM), Salmonella typhimurium (MIC=4.0 μM), Pseudomonas aeruginosa (MIC=3.0 μM).##Fungi: [No NaCl]: Candida albicans (MIC=8.0 μM);[100 mM NaCl]: Candida albicans (MIC=8.0 μM). [Ref.11467858]Non-hemolysis at 100 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11467858 Biochem Biophys Res Commun. 2001 Jul 27;285(4):1046-51. Shin SY, Park EJ, Yang ST, Jung HJ, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide. DRAMP18620 KKTWWKTWWTKWSQPKKKRKV 21 Pep-1-K (Pep-1 peptide derivative) No entry found Derived from the peptide Pep-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-positive bacteria. No hemolytic activity. [Ref.16945333]Gram-positive bacteria: Bacillus subtilis (KCTC 3068) (MIC=2.0 μM), Staphylococcus aureus (KCTC 1621) (MIC=2.0 μM), Staphylococcus epidermidis (KCTC 1917) (MIC=1.0 μM);##Gram-negative bacteria: Escherichia coli (KCTC 1682) (MIC=2.0 μM), Salmonella typhimurium (KCTC 1926) (MIC=1.0 μM), Pseudomonas aeruginosa (KCTC 1637) (MIC=2.0 μM);##Antibiotic-resistant bacteria: MRSA 1 (CCARM 3001) (MIC=2.0 μM), MRSA 2 (CCARM 3089) (MIC=2.0 μM), MRSA 3 (CCARM 3543) (MIC=1.0 μM), MDRPA 1 (CCARM 2092) (MIC=8.0 μM), MDRPA 2 (CCARM 2095) (MIC=8.0 μM), MDRPA 3 (CCARM 2109) (MIC=8.0 μM). [Ref.16945333]Non-hemolysis at 200 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16945333 Biochem Biophys Res Commun. 2006 Oct 20;349(2):769-74. Zhu WL, Lan H, Park IS, Kim JI, Jin HZ, Hahm KS, Shin SY. Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. DRAMP18621 FLYIVAKLLSGLL 13 Temporin-PEa (Temporin-PE peptide derivative) No entry found Derived from the peptide Temporin-PE Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria and fungi. Weak hemolytic activity. [Ref.29191658]Gram-positive bacteria: Staphylococcus aureus (MIC=1.0 μM), Methicillin-resistant Staphylococcus aureus (MIC=2.0 μM), Enterococcus faecalis (MIC=2.0 μM);##Fungus: Candida albicans (MIC=2.0 μM).##Cancer cell lines: NCI-H157 (IC50=3.398 μM), U251MG (IC50=3.520 μM), PC-3 (IC50=27.62 μM), MDA-MB-435s (IC50=9.864 μM), HMEC-1 (IC50=40.30 μM). [Ref.29191658]HC50=531.7 μM against horse red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29191658 Biochem Biophys Res Commun. 2018 Jan 22;495(4):2539-2546. Sang M, Wu Q, Xi X, Ma C, Wang L, Zhou M, Burrows JF, Chen T. Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus. DRAMP18622 FLPIVAKLLSGLLGRKKRRQRRR 23 Temporin-PEb (Temporin-PE peptide derivative) No entry found Derived from the peptide Temporin-PE Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.29191658]Gram-positive bacteria: Staphylococcus aureus (MIC=1.0 μM), Methicillin-resistant Staphylococcus aureus (MIC=2.0 μM), Enterococcus faecalis (MIC=2.0 μM);##Gram-negative bacteria: Escherichia coli (MIC=2.0 μM);##Fungus: Candida albicans (MIC=1.0 μM).##Cancer cell lines: NCI-H157 (IC50=3.464 μM), U251MG (IC50=3.087 μM), PC-3 (IC50=3.051 μM), MDA-MB-435s (IC50=3.483 μM), HMEC-1 (IC50=9.976 μM). [Ref.29191658]HC50=44.64 μM against horse red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29191658 Biochem Biophys Res Commun. 2018 Jan 22;495(4):2539-2546. Sang M, Wu Q, Xi X, Ma C, Wang L, Zhou M, Burrows JF, Chen T. Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus. DRAMP18623 INLKILARLAKKIL 14 [I5,R8] Mastoparan-L ([I5,R8] MP-L;Mastoparan-L peptide derivative) No entry found Derived from the peptide Mastoparan Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anitifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.27423268]Cytotoxicity against THP-1-derived macrophages, Weak hemolytic activity. [Ref.27423268]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=25 μM), Streptococcus pyogenes ATCC 19615 (MIC=6.25 μM), Listeria ivanovii Li 4pVS2 (MIC=50 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=6.25 μM), Klebsiella pneumoniae ATCC 13883 (MIC=6.25 μM), Acinetobacter baumannii ATCC 19606 (MIC=3 μM);##Fungi: Candida albicans ATCC 90028 (MIC=12.5 μM), Candida parapsilosis ATCC 22019 (MIC=25 μM). [Ref.27423268]LC50>200 μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27423268 Biochim Biophys Acta. 2016 Nov;1858(11):2699-2708. Irazazabal LN, Porto WF, Ribeiro SM, Casale S, Humblot V, Ladram A, Franco OL. Selective amino acid substitution reduces cytotoxicity of the antimicrobial peptide mastoparan. DRAMP18624 KLKKLLKKWLKLLKKLLK 18 K9L8W No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=4 μM), Staphylococcus epidermidis (MIC=8 μM), Staphylococcus aureus (MIC=8 μM);##Gram-negative bacteria: Escherichia coli (MIC=8 μM), Pseudomonas aeruginosa (MIC=8 μM), Salmonella typhimurium (MIC=4 μM). [Ref.20363271]HC50=14 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18625 KLKKLLKKWLKLLKKLLK 18 D3-K9L8W-1 (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 6 and 12 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 18 on the peptide K9L8W. Has hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=2 μM), Staphylococcus epidermidis (MIC=4 μM), Staphylococcus aureus (MIC=4 μM);##Gram-negative bacteria: Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=4 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50=150 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18626 KLKKLLKKWLKLLKKLLK 18 D3-K9L8W-2 (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 5 and 10 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 15 on the peptide K9L8W. Has hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=1 μM), Staphylococcus epidermidis (MIC=4 μM), Staphylococcus aureus (MIC=4 μM);##Gram-negative bacteria: Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=4 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50=116 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18628 KLKKLLKKWLKLLKKLLK 18 D6-K9L8W (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 6 and 12 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 3,15 and 18 on the peptide K9L8W, D-Tryptophan replace L-Tryptophan at the position 9 on the peptide K9L8W. Weak hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=1 μM), Staphylococcus epidermidis (MIC=4 μM), Staphylococcus aureus (MIC=2 μM);##Gram-negative bacteria: Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=2 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50>800 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18629 KLKKLLKKWLKLLKKLLK 18 D9-K9L8W-1 (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 2,6,10,12 and 16 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 4,8,14 and 18 on the peptide K9L8W. Weak hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=1 μM), Staphylococcus epidermidis (MIC=4 μM), Staphylococcus aureus (MIC=4 μM);##Gram-negative bacteria: Escherichia coli (MIC=2 μM), Pseudomonas aeruginosa (MIC=2 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50>800 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18630 KLKKLLKKWLKLLKKLLK 18 D9-K9L8W-2 (D-amino acid substitution of K9L8W) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. D-Leucine replace L-Leucine at the position 10,12,13,16 and 17 on the peptide K9L8W, D-Lysine replace L-Lysine at the position 11,14,15 and 18 on the peptide K9L8W. Has hemolytic activity. [Ref.20363271]Gram-positive bacteria: Bacillus subtilis (MIC=2 μM), Staphylococcus epidermidis (MIC=4 μM), Staphylococcus aureus (MIC=4 μM);##Gram-negative bacteria: Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=4 μM), Salmonella typhimurium (MIC=2 μM). [Ref.20363271]HC50=154 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20363271 Peptides. 2010 Jul;31(7):1251-61. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. DRAMP18631 VGHNADLQIKLSIRRLLAAGVLKQTKGVGA 30 H5(61–90) V1 (Histone H5 peptide derivative) No entry found Derived from Histone H5 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presented an orders alpha-helix structure with 84.2 % alpha-helices in 30?mM SDS Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. H5(61 [Ref.29402952] Gram-positive bacteria: Listeria monocytogenes (MIC=23.1±8.1 μg/mL);##Gram-negative bacterium: Pseudomonas aeruginosa (MIC=16±0 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29402952 Sci Rep. 2018 Feb 5;8(1):2411. Jodoin J, Hincke MT. Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides. DRAMP18632 LSIRRLLAAGVLKQTKGVGA 20 Peptide H5 (71-90) (Histone H5 peptide derivative) No entry found Derived from Histone H5 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.29402952] Gram-negative bacterium: Pseudomonas aeruginosa (MIC=26.7±14.1 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29402952 Sci Rep. 2018 Feb 5;8(1):2411. Jodoin J, Hincke MT. Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides. DRAMP18633 VGHNADLQIKLSIRRLLAAGVLKQTKGVGA 30 H5(61-90) V2 (Histone H5 peptide derivative) No entry found Derived from Histone H5 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presented an orders alpha-helix structure with 75.5 % alpha-helices in 30?mM SDS Function: Antibacterial activity against Gram-negative bacteria. H5(61 [Ref.29402952] Gram-negative bacterium: Pseudomonas aeruginosa (MIC=33.8 ± 26.3 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29402952 Sci Rep. 2018 Feb 5;8(1):2411. Jodoin J, Hincke MT. Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides. DRAMP18634 VGHNADLQIKLSIRRLLAAGVLKQTKGVGA 30 H5(61-90) V3 (Histone H5 peptide derivative) No entry found Derived from Histone H5 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presented an orders alpha-helix structure with 84.7 % alpha-helices in 30?mM SDS Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. H5(61 [Ref.29402952] Gram-positive bacteria: Listeria monocytogenes (MIC=106.7 ± 37.0 μg/mL);##Gram-negative bacterium: Pseudomonas aeruginosa (MIC=48.0 ± 32.4 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29402952 Sci Rep. 2018 Feb 5;8(1):2411. Jodoin J, Hincke MT. Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides. DRAMP18635 KLIPIASKTCPAGKNLCYKI 20 NCP-0 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Unordered structure The peptide adopts overall content of unordered secondary structure that is 67% Function: Antibacterial activity against the Gram-negative bacteria. [Ref.29364903] Gram-negative bacteria: Burkholderia cepacia ATCC 17759(MBC=50μg/ml);Moraxella catarrhalis ATCC 25238(MBC=1.6μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29364903 PLoS One. 2018 Jan 24;13(1):e0190778. Sala A, Cabassi CS, Santospirito D, Polverini E, Flisi S, Cavirani S, Taddei S. Novel Naja atra cardiotoxin 1 (CTX-1) derived antimicrobial peptides with broad spectrum activity. DRAMP18636 KLIFILSKTIPAGKNLFYKI 20 NCP-3a (CTX-1 peptide derivative) No entry found Derived from CTX-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29364903] Gram-positive bacteria: Methicillin-resistant Staphylococcus aureus ATCC 43300 (MBC=6.3 μg/ml), Staphylococcus aureus ATCC 22953 (MBC=12.5 μg/ml), Enterococcus hirae ATCC 10541 (MBC=6.3 μg/ml), Streptococcus agalactiae ATCC 13813 (MBC=3.1 μg/ml);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MBC=6.3 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MBC=25 μg/ml), Acinetobacter baumannii (ornithological, cloacal) (MBC=25 μg/ml), Acinetobacter baumannii (human, urinary) (MBC=25 μg/ml), Klebsiella pneumoniae subsp. pneumoniae (herpetological, cloacal) (MBC=50 μg/ml), Burkholderia cepacia ATCC 17759 (MBC=50 μg/ml), Moraxella catarrhalis ATCC 25238 (MBC=3.1 μg/ml);##Fungi: Candida albicans ATCC 10231 (MBC=6.3 μg/mL), Candida glabrata ATCC 90030 (MBC=25 μg/mL), Malassezia pachydermatis DSMZ 6172 (MBC=6.3 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29364903 PLoS One. 2018 Jan 24;13(1):e0190778. Sala A, Cabassi CS, Santospirito D, Polverini E, Flisi S, Cavirani S, Taddei S. Novel Naja atra cardiotoxin 1 (CTX-1) derived antimicrobial peptides with broad spectrum activity. DRAMP18637 KLILILSKTIPAGKNLFYKI 20 NCP-3b (CTX-1 peptide derivative) No entry found Derived from CTX-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29364903] Gram-positive bacteria: Methicillin-resistant Staphylococcus aureus ATCC 43300 (MBC=6.3 μg/ml), Staphylococcus aureus ATCC 22953 (MBC=50 μg/ml), Enterococcus hirae ATCC 10541 (MBC=12.5 μg/ml), Streptococcus agalactiae ATCC 13813 (MBC=12.5 μg/ml);##Gram-negative bacterium: Escherichia coli ATCC 25922 (MBC=12.5 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MBC=25 μg/ml), Acinetobacter baumannii (ornithological, cloacal) (MBC=25 μg/ml), Acinetobacter baumannii (human, urinary) (MBC=25 μg/ml), Klebsiella pneumoniae subsp. pneumoniae (herpetological, cloacal) (MBC=25 μg/ml), Burkholderia cepacia ATCC 17759 (MBC=25 μg/ml), Moraxella catarrhalis ATCC 25238 (MBC=12.5 μg/ml);##Fungi: Candida albicans ATCC 10231 (MBC=12.5 μg/mL), Candida glabrata ATCC 90030 (MBC=100 μg/mL), Malassezia pachydermatis DSMZ 6172 (MBC=25 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29364903 PLoS One. 2018 Jan 24;13(1):e0190778. Sala A, Cabassi CS, Santospirito D, Polverini E, Flisi S, Cavirani S, Taddei S. Novel Naja atra cardiotoxin 1 (CTX-1) derived antimicrobial peptides with broad spectrum activity. DRAMP18638 VYPFMWGGAYCFCDAELV 18 VT18-LV (VT18 peptide derivative) No entry found Derived from VT18 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Double-stranded Not found Function: Antibacterial activity against the Gram-positive bacteria. [Ref.29277569] Gram-positive bacteria: Streptococcus pneumoniae ATCC 700669 (MIC=207 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29277569 Biochimie. 2018 Mar;146:139-147. Yang R, Zhang G, Zhang F, Li Z, Huang C. Membrane permeabilization design of antimicrobial peptides based on chikungunya virus fusion domain scaffold and its antibacterial activity against gram-positive Streptococcus pneumoniae in respiratory infection. DRAMP18639 CKCRRRKVHGPMIRIRKK 18 CTO17 (TO17 peptide derivative) No entry found Derived from TO17 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative bacteria. [Ref.29183811] Gram-negative bacterium: Vibrio vulnificus (MIC=20 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29183811 Fish Shellfish Immunol. 2018 Jan;72:639-645. He SW, Wang GH, Yue B, Zhou S, Zhang M. TO17: A teleost antimicrobial peptide that induces degradation of bacterial nucleic acids and inhibits bacterial infection in red drum, Sciaenops ocellatus. DRAMP18640 KCRRRKVHGPMIRIRKKNL 19 TO19 (TO17 peptide derivative) No entry found Derived from TO17 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative bacteria. [Ref.29183811] Gram-negative bacterium: Vibrio vulnificus (MIC=20 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29183811 Fish Shellfish Immunol. 2018 Jan;72:639-645. He SW, Wang GH, Yue B, Zhou S, Zhang M. TO17: A teleost antimicrobial peptide that induces degradation of bacterial nucleic acids and inhibits bacterial infection in red drum, Sciaenops ocellatus. DRAMP18641 TWWRWW 6 KCM11 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Low activity against the Gram-negative strains. High activity against the Gram-positive strains [Ref.19734717] Gram-negative bacteria: Acidovorax konjaci(MEC=2.5 nM), Pseudomonas syringae pv. tomato DC3000 (MEC=5 nM), Pectobacterium carotovorum subsp. atrosepticum (MEC=5 nM), Xanthomonas albilineans (MEC=0.3 nM), Xanthomonas campestris pv. vesicatoria 833 (MEC=0.3 nM), Xanthomonas campestris pv. vesicatoria 833 pilA (MEC=0.3 nM), Xanthomonas oryzae pv. oryzae 599 (MEC=1.3 nM), Xanthomonas oryzae pv. oryzae 710 (MEC=1.3 nM), Xanthomonas oryzae pv. oryzae 090 (MEC=1.3 nM);##Gram-positive bacterium: Clavibacter michiganensis subsp. michiganensis (MEC=0.3 nM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19734717 J Microbiol Biotechnol. 2009 Aug;19(8):792-802. Choi J, Moon E. Identification of novel bioactive hexapeptides against phytopathogenic bacteria through rapid screening of a synthetic combinatorial library. DRAMP18642 KWRWIW 6 KCM12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: High activity against E. coli DH5 [Ref.19734717] Gram-negative bacteria: Acidovorax konjaci (MEC=1.3 nM), Pseudomonas syringae pv. tomato DC3000 (MEC=0.3 nM), Escherichia coli DH5α (MEC=1.3 nM), Pseudomonas putida (MEC=0.6 nM), Pectobacterium carotovorum subsp. carotovorum (MEC=5 nM), Pectobacterium carotovorum subsp. atrosepticum (MEC=0.6 nM), Xanthomonas albilineans (MEC=1.3 nM), Xanthomonas campestris pv. vesicatoria 833 (MEC=0.3 nM), Xanthomonas campestris pv. vesicatoria 833 pilA (MEC=0.3 nM), Xanthomonas oryzae pv. oryzae 599 (MEC=0.2 nM), Xanthomonas oryzae pv. oryzae 710 (MEC=0.2 nM), Xanthomonas oryzae pv. oryzae 090 (MEC=0.2 nM);##Gram-positive bacterium: Clavibacter michiganensis subsp. michiganensis (MEC=0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19734717 J Microbiol Biotechnol. 2009 Aug;19(8):792-802. Choi J, Moon E. Identification of novel bioactive hexapeptides against phytopathogenic bacteria through rapid screening of a synthetic combinatorial library. DRAMP18643 KWWWRW 6 KCM21 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: High activity against E. coli DH5 [Ref.19734717] Gram-negative bacteria: Acidovorax konjaci (MEC=0.6 nM), Pseudomonas syringae pv. tomato DC3000 (MEC=0.6 nM), Escherichia coli DH5α (MEC=1.3 nM), Pseudomonas putida (MEC=1.3 nM), Pectobacterium carotovorum subsp. carotovorum (MEC=5 nM), Pectobacterium carotovorum subsp. atrosepticum (MEC=0.6 nM), Xanthomonas albilineans (MEC=0.2 nM), Xanthomonas campestris pv. vesicatoria 833 (MEC=0.2 nM), Xanthomonas campestris pv. vesicatoria 833 pilA (MEC=0.2 nM), Xanthomonas oryzae pv. oryzae 599 (MEC=0.2 nM), Xanthomonas oryzae pv. oryzae 710 (MEC=0.3 nM), Xanthomonas oryzae pv. oryzae 090 (MEC=0.3 nM);##Gram-positive bacterium: Clavibacter michiganensis subsp. michiganensis (MEC=0.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19734717 J Microbiol Biotechnol. 2009 Aug;19(8):792-802. Choi J, Moon E. Identification of novel bioactive hexapeptides against phytopathogenic bacteria through rapid screening of a synthetic combinatorial library. DRAMP18644 WRWFIH 6 KRS22 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not foundn Function: High activity against XCV833 and CM at the high concentration [Ref.19734717] Gram-negative bacteria: Acidovorax konjaci (MEC=5 nM), Pseudomonas syringae pv. tomato DC3000 (MEC=2.5 nM), Escherichia coli DH5α (MEC=5 nM), Pectobacterium carotovorum subsp. atrosepticum (MEC=2.5 nM), Xanthomonas albilineans (MEC=2.5 nM), Xanthomonas campestris pv. vesicatoria 833 (MEC=2.5 nM), Xanthomonas campestris pv. vesicatoria 833 pilA (MEC=2.5 nM), Xanthomonas oryzae pv. oryzae 599 (MEC=0.6 nM), Xanthomonas oryzae pv. oryzae 710 (MEC=1.3 nM), Xanthomonas oryzae pv. oryzae 090 (MEC=0.3 nM);##Gram-positive bacterium: Clavibacter michiganensis subsp. michiganensis (MEC=1.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19734717 J Microbiol Biotechnol. 2009 Aug;19(8):792-802. Choi J, Moon E. Identification of novel bioactive hexapeptides against phytopathogenic bacteria through rapid screening of a synthetic combinatorial library. DRAMP18645 RKTWFW 6 PAF19 No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity against Penicillium digitatum PHI-26, Penicillium italicum PHI-1, Botrytis cinerea CECT2100. All residues of PAF19 are D-animo acids. [Ref.11976121] Fungi: Penicillium digitatum PHI-26 (MIC=60 μM, IC50=36 ± 6 μM), Penicillium italicum PHI-1 (MIC=80 μM, IC50=52 ± 5 μM), Botrytis cinerea CECT2100 (MIC=80 μM, IC50=43 ± 14 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976121 Appl Environ Microbiol. 2002 May;68(5):2453-60. López-García B, Pérez-Payá E, Marcos JF. Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library. DRAMP18646 RKWHFW 6 PAF32 No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity against Penicillium digitatum PHI-26, Penicillium italicum PHI-1, Botrytis cinerea CECT2100, Fusarium oxysporum CECT2866, Saccharomyces cerevisiae W303-1A. All residues of PAF32 are D-animo acids. [Ref.11976121] Fungi: Penicillium digitatum PHI-26 (MIC=20 μM, IC50=7 ± 1 μM), Penicillium italicum PHI-1 (MIC=20 μM, IC50=15 ± 5 μM), Botrytis cinerea CECT2100 (MIC=40 μM, IC50=19 ± 8 μM), Fusarium oxysporum CECT2866 (MIC=80 μM, IC50=56 ± 11 μM), Saccharomyces cerevisiae W303-1A (MIC>160 μM, IC50=63 ± 10 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976121 Appl Environ Microbiol. 2002 May;68(5):2453-60. López-García B, Pérez-Payá E, Marcos JF. Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library. DRAMP18647 RKWLFW 6 PAF34 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Antifungal activity against Penicillium digitatum PHI-26, Penicillium italicum PHI-1, Penicillium expansum CMP-1, Botrytis cinerea CECT2100, Saccharomyces cerevisiae W303-1A . Antibacterial activity against Escherichia coli DH5 [Ref.11976121] Fungi: Penicillium digitatum PHI-26 (MIC=40 μM, IC50=15 ± 1 μM), Penicillium italicum PHI-1 (MIC=20 μM, IC50=12 ± 4 μM), Penicillium expansum CMP-1 (MIC=160 μM, IC50> 80 μM), Botrytis cinerea CECT2100 (MIC=60 μM), Saccharomyces cerevisiae W303-1A (MIC>160 μM, IC50=52 ± 22 μM);##Gram-negative bacterium: Escherichia coli DH5α(MIC=160 μM, IC50>80 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976121 Appl Environ Microbiol. 2002 May;68(5):2453-60. López-García B, Pérez-Payá E, Marcos JF. Identification of novel hexapeptides bioactive against phytopathogenic fungi through screening of a synthetic peptide combinatorial library. DRAMP18648 FVPWFSKFLPRIL 13 [Pro3,DLeu9]TL(3) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The analogues bearing a D residue showed a reduction in the percentage of helicity compared to the corresponding L analogues in the MMs Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(3) is D-Leucine, D-Proline replace L-Proline at the position 10 on the peptide [Pro3,DLeu9]TL(2). [Ref.28863356] Gram-positive bacterium: Bacillus megaterium Bm11 (MIC=3.125μM), Staphylococcus epidermidis ATCC 12228 (MIC=25μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=50μM), Escherichia coli D21 (MIC=50μM), Pseudomonas syringae pv tabaci 1918 (MIC=50μM);##Yeasts: Candida albicans ATCC 10231 (MIC=3.125μM), Candida crusei ATCC 6258 (MIC=3.125μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-763. Merlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP18649 FQWQRNPRKVR 11 HLP6 (HLP2 peptide derivative) No entry found Derived from the peptide HLP 2 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. HLP 6 had a proline substituted for methionine in HLP 2. [Ref.9596699] Gram-negative bacteria: Escherichia coli NCTC 10418 (MIC=750 μM);##Gram-negative bacterium: Staphylococcus aureus (MIC=250 μM);##Clinical isolates: Acinetobacter sp.(MIC=10 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9596699 Infect Immun. 1998 Jun;66(6):2434-40. Chapple DS, Mason DJ, Joannou CL, Odell EW, Gant V, Evans RW. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. DRAMP18650 FQWQRNMRKVR 11 HLP7 (HLP2 peptide derivative) No entry found Derived from the peptide HLP 2 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. HLP 7 is the d form of HLP 2. [Ref.9596699] Gram-negative bacteria: Escherichia coli NCTC 8007 (MIC=18 μM), Escherichia coli NCTC 10418 (MIC=40 μM);##Gram-negative bacterium: Staphylococcus aureus (MIC=14 μM);##Clinical isolates: Acinetobacter sp. (MIC=0.3 μM), Klebsiella sp. strain 3105 (MIC=80 μM), Providencia stuartii (MIC=110 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9596699 Infect Immun. 1998 Jun;66(6):2434-40. Chapple DS, Mason DJ, Joannou CL, Odell EW, Gant V, Evans RW. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. DRAMP18651 SRSELIVHQRRC 12 Cm-p3 (Cm-p1 peptide derivative) No entry found Derived from the peptide Cm-p1 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity against Candida albicans and Trichophyton rubrum. [Ref.25921828] Fungi: Candida albicans (01U) (MIC=128 μg/ml), Candida albicans (38U) (MIC=64 μg/ml), Trichophyton rubrum (MIC=128 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25921828 FASEB J. 2015 Aug;29(8):3315-25. López-Abarrategui C, McBeth C, Mandal SM, Sun ZJ, Heffron G, Alba-Menéndez A, Migliolo L, Reyes-Acosta O, García-Villarino M, Nolasco DO, Falcão R, Cherobim MD, Dias SC, Brandt W, Wessjohann L, Starnbach M, Franco OL, Otero-González AJ. Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae). DRAMP18652 SRSELIVHQRMK 12 Cm-p4 (Cm-p1 peptide derivative) No entry found Derived from the peptide Cm-p1 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity against Candida albicans, Cryptococcus neoformans and Trichophyton rubrum. [Ref.25921828] Fungi: Candida albicans (01U) (MIC=32 μg/ml), Candida albicans (38U) (MIC=32 μg/ml), Candida parapsilosis (MIC=256 μg/ml), Trichophyton rubrum (MIC=32 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25921828 FASEB J. 2015 Aug;29(8):3315-25. López-Abarrategui C, McBeth C, Mandal SM, Sun ZJ, Heffron G, Alba-Menéndez A, Migliolo L, Reyes-Acosta O, García-Villarino M, Nolasco DO, Falcão R, Cherobim MD, Dias SC, Brandt W, Wessjohann L, Starnbach M, Franco OL, Otero-González AJ. Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae). DRAMP18653 SRSELIVHQRLF 12 Cm-p5 (Cm-p1 peptide derivative) No entry found Derived from the peptide Cm-p1 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity against Candida albicans, Candida parapsilosis, Cryptococcus neoformans, Trichophyton mentagrophytes and Trichophyton rubrum. [Ref.25921828] Fungi: Candida albicans (01U) (MIC=10 μg/ml), Candida albicans (38U) (MIC=10 μg/ml), Candida parapsilosis (MIC=32 μg/ml), Cryptococcus neoformans (L26) (MIC=64 μg/ml), Cryptococcus neoformans (L30) (MIC=64 μg/ml), Trichophyton mentagrophytes (MIC=128 μg/ml), Trichophyton rubrum (MIC=10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 25921828 FASEB J. 2015 Aug;29(8):3315-25. López-Abarrategui C, McBeth C, Mandal SM, Sun ZJ, Heffron G, Alba-Menéndez A, Migliolo L, Reyes-Acosta O, García-Villarino M, Nolasco DO, Falcão R, Cherobim MD, Dias SC, Brandt W, Wessjohann L, Starnbach M, Franco OL, Otero-González AJ. Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae). DRAMP18654 GIIKVIKSLIEQFTGK 16 dPSMα1 (PSMα1 peptide derivative; bacteriocin; staphylococcus aureus, bacteria) A9JX05, A8Z0V1, P0C7Y9, P0C7Y8, P0C7Y7, P0C7Y6, P0C7Y5, P0C7Y4, P0C7Y3 Belongs to the phenol-soluble modulin alpha peptides family. psmA1 Truncated the peptide PSMα1 (from Staphylococcus aureus) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. Stimulates the secretion of the chemotactic factor interleukin-8 (IL-8). The ensuing activation process triggers an inflammatory response in the host, thus contributing greatly to virulence. Also possesses hemolytic activity, which may contribute to the development of disease. Peptide production is higher in most prevalent community-associated MRSA strains than in hospital-associated MRSA strains. Induction: Up-regulated by agr." [Ref.22371493]Gram-positive bacteria: Staphylococcus epidermidis ATCC35984 (MIC=42 μM), Streptococcus serotype GAS M3 strain 4041-05 (MIC=11 μM). [Ref.22371493]Non-hemolytic at 10μg/mL against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22371493 J Biol Chem. 2012 Apr 20;287(17):13889-98. Gonzalez DJ, Okumura CY, Hollands A, Kersten R, Akong-Moore K, Pence MA, Malone CL, Derieux J, Moore BS, Horswill AR, Dixon JE, Dorrestein PC, Nizet V. Novel phenol-soluble modulin derivatives in community-associated methicillin-resistant Staphylococcus aureus identified through imaging mass spectrometry. DRAMP18655 VGTIIKIIKAIIDIFAK 17 dPSMα4 (PSMα4 peptide derivative; bacteriocin; staphylococcus aureus, bacteria) A9JX08, P0C827, P0C826, P0C825, P0C824, P0C823, P0C822, P0C821, P0C820 Belongs to the phenol-soluble modulin alpha peptides family. psmA4 Truncated the peptide PSMα4 (from Staphylococcus aureus) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Not found Not found "Function: Antibacterial activity against Gram-positive bacteria. Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. Stimulates the secretion of the chemotactic factor interleukin-8 (IL-8). The ensuing activation process triggers an inflammatory response in the host, thus contributing greatly to virulence. Also possesses hemolytic activity, which may contribute to the development of disease. Peptide production is higher in most prevalent community-associated MRSA strains than in hospital-associated MRSA strains. Induction: Up-regulated by agr." [Ref.22371493]Gram-positive bacteria: Streptococcus serotype GAS M3 strain 4041-05 (MIC=10 μM). [Ref.22371493]52% hemolysis at 10μg/mL against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22371493 J Biol Chem. 2012 Apr 20;287(17):13889-98. Gonzalez DJ, Okumura CY, Hollands A, Kersten R, Akong-Moore K, Pence MA, Malone CL, Derieux J, Moore BS, Horswill AR, Dixon JE, Dorrestein PC, Nizet V. Novel phenol-soluble modulin derivatives in community-associated methicillin-resistant Staphylococcus aureus identified through imaging mass spectrometry. DRAMP18656 MRTGNAD 7 Microcin 7 (Bacteriocin; Escherichia coli, Bacteria) No entry found Bacteriocin Not found Escherichia coli Antimicrobial, Antibacterial, Anti-Gram- Natural Not found Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.2861788] Gram-negative bacteria: Escherichia coli , Klebsiella pneumoniae, Salmonella typhi, Salmonella typhimurium, Salmonella sp., Shigella flexneri, Shigella sp., Proteus mirabilis No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2861788 Antimicrob Agents Chemother. 1985 May;27(5):791-7. Garcia-Bustos JF, Pezzi N, Mendez E. Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli. DRAMP18657 GDGTGPGPGP 10 Chitinase (Bacteriocin; Streptomyces violaceusniger, Bacteria) P86977 Bacteriocin Not found Streptomyces violaceusniger Antimicrobial, Antifungal Protein level Not found Not found Function: Antifungal activity aginst mycelial growth of wood rotting fungi. [Ref.22915152] Inhibits mycelial growth of wood rotting fungi: Phanerochaete chrysosporium MTCC 787 (Inhibition Zone=32.60 mm), Schizophyllum commune ITCC 3751 (Inhibition Zone=27.60 mm), Gloeophyllum trabeum MTCC 355 (Inhibition Zone=30.70 mm), Polyporus agaricans ITCC 761 (Inhibition Zone=25.70 mm),Coriolus versicolor MTCC 138 (Inhibition Zone=20.60 mm), Polystictus versicolor ITCC 13 (Inhibition Zone=16.70 mm), Postia placenta MTCC 144 (Inhibition Zone=20.60 mm), Polyporus friabilis ITCC 335 (Inhibition Zone=22.60 mm). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22915152 J Basic Microbiol. 2013 May;53(5):429-39. doi: 10.1002/jobm.201100648. Epub 2012 Aug 23. Nagpure A, Gupta RK. Purification and characterization of an extracellular chitinase from antagonistic Streptomyces violaceusniger. DRAMP18658 FLPIVAKLLSGLL 13 Temporin-PE (Edible frogs, amphibians, animals) A0A2H4WAJ8 Not found Not found Pelophylax kl.esculentus(Europe edible frog) Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-cancer, Anti-Gram- Protein level Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi.Has hemolytic activity. [Ref.29191658]Gram-positive bacteria: Staphylococcus aureus (MIC=2.0 μM), Methicillin-resistant Staphylococcus aureus (MIC=4.0 μM), Enterococcus faecalis (MIC=8.0 μM);##Gram-negative bacteria: Escherichia coli (MIC=16.0 μM);##Fungus: Candida albicans (MIC=4.0 μM).##Cancer cell lines: NCI-H157 (IC50=34.56 μM), U251MG (IC50=25.13 μM), PC-3 (IC50=38.56 μM), MDA-MB-435s (IC50=33.23 μM), HMEC-1 (IC50=58.62 μM). [Ref.29191658]HC50=39.64 μM against horse red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29191658 Biochem Biophys Res Commun. 2018 Jan 22;495(4):2539-2546. Sang M, Wu Q, Xi X, Ma C, Wang L, Zhou M, Burrows JF, Chen T. Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus. DRAMP18659 VKVGINGFGRIGRLVTRAAFHGKKVEVVAIND 32 YFGAP-OH(Yellowfin tuna GAPDH-related antimicrobial peptide; fish, animals) No entry found Not found Not found Yellowfin tuna (Thunnus albacares) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix and Beta strands One Alpha helix and two parallel Beta strands "Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacterial.Weak hemolytic activity. YFGAP-OH is the C-terminus amidated modification of YFGAP." [Ref.22771964]Gram-positive bacteria: Bacillus subtilis KCTC1021 (MIC=13.0 μg/ml), Bacillus subtilis RM125 (MIC=1.2 μg/ml), Micrococcus luteus ATCC9341 (MIC=6.5 μg/ml), Staphylococcus aureus RM4220 (MIC=125.0 μg/ml), Staphylococcus aureus KCTC1621 (MIC=11.0 μg/ml), Streptococcus iniae FP5229 (MIC=17.0 μg/ml);##Gram-negative bacteria: Escherichia coli D31 (MIC=6.2 μg/ml), Escherichia coli KCTC1116 (MIC=5.0 μg/ml), Escherichia coli ML35p (MIC=3.0 μg/ml), Enterobacter cloacae KCTC1685 (MIC=12.0 μg/ml), Pseudomonas aeroginosa KCTC2004 (MIC=3.7 μg/ml), Salmonella enterica KCTC2514 (MIC=3.1 μg/ml), Shigella flexneri KCTC2517 (MIC=5.0 μg/ml), Aeromonas hydrophila KCTC2358 (MIC=8.0 μg/ml), Vibrio parahemolyticus KCCM41664 (MIC=3.2 μg/ml) [Ref.22771964]0.4% hemolysis at 100 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22771964 Fish Shellfish Immunol. 2012 Oct;33(4):743-52. doi: 10.1016/j.fsi.2012.06.023. Seo JK, Lee MJ, Go HJ, Park TH, Park NG. Purification and characterization of YFGAP, a GAPDH-related novel antimicrobial peptide, from the skin of yellowfin tuna, Thunnus albacares. DRAMP18660 VKVGINGFGRIGRLVTRAAFHGKKVEVVAIND 32 YFGAP-NH2(Yellowfin tuna GAPDH-related antimicrobial peptide; fish, animals) No entry found Not found Not found Yellowfin tuna(Thunnus albacares) Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Not found Alpha helix and Beta strands One Alpha helix and two parallel Beta strands "Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. YFGAP-NH2 is the C-terminus free forms of YFGAP." [Ref.22771964]Gram-positive bacteria: Bacillus subtilis KCTC1021 (MIC=5.4 μg/ml), Bacillus subtilis RM125 (MIC=0.7 μg/ml), Micrococcus luteus ATCC9341 (MIC=6.0 μg/ml), Staphylococcus aureus RM4220 (MIC=34.0 μg/ml), Staphylococcus aureus KCTC1621 (MIC=3.7 μg/ml);##Gram-negative bacteria: Escherichia coli D31 (MIC=1.9 μg/ml), Escherichia coli KCTC1116 (MIC=3.3 μg/ml), Escherichia coli ML35p (MIC=0.4 μg/ml), Enterobacter cloacae KCTC1685 (MIC=3.5 μg/ml), Pseudomonas aeroginosa KCTC2004 (MIC=1.7 μg/ml), Salmonella enterica KCTC2514 (MIC=0.9 μg/ml), Shigella flexneri KCTC2517 (MIC=2.0 μg/ml), Aeromonas hydrophila KCTC2358 (MIC=3.6 μg/ml), Vibrio parahemolyticus KCCM41664 (MIC=0.9 μg/ml);##Fungi: Candida albicans KCTC7965 (MIC=125.0 μg/ml) [Ref.22771964]2.7% hemolysis at 100 μg/ml against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22771964 Fish Shellfish Immunol. 2012 Oct;33(4):743-52. doi: 10.1016/j.fsi.2012.06.023. Seo JK, Lee MJ, Go HJ, Park TH, Park NG. Purification and characterization of YFGAP, a GAPDH-related novel antimicrobial peptide, from the skin of yellowfin tuna, Thunnus albacares. DRAMP18661 GWLDVAKKIGKAAFNVAKNFL 21 Ctx-Ha (Frogs, amphibians, animals) No entry found Belongs to the Ceratotoxin family Not found Hypsiboas albopunctatus Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Not found Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.22391524]Gram-positive bacterium: Staphylococcus aureus (MIC=1.7 μmol/L; MMC=6.8 μmol/L);##Gram-negative bacterium: Escherichia coli (MIC=3.4 μmol/L; MMC=3.4 μmol/L);##Fungi: Candida albicans (MIC=54.6 μmol/L; MMC<100 μmol/L) [Ref.22391524]HC50=37.3±1.4 μmol/L against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22391524 Antimicrob Agents Chemother. 2012 Jun;56(6):3004-10. Lorenzón EN, Cespedes GF, Vicente EF, Nogueira LG, Bauab TM, Castro MS, Cilli EM. Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha. DRAMP18662 LLAGLAANFLPKIFCKITRKC 21 Brevinin 21 (Brevinin-1E truncated peptide 21; Frogs, amphibians, animals) No entry found Derived from the peptide Brevinin-1E Not found Rana esculenta Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Not found Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.9748603]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC=12.5 μg/ml), Methicillin resistant Staphylococcus aureus (MIC=25 μg/ml), Micrococcus luteus ATCC 9341 (MIC=6.25 μg/ml);##Gram-negative bacteria:Escherichia coli ATCC 2592 (MIC=12.5 μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=12.5 μg/ml);##Fungus: Candida albicans ATCC 36232 (MIC=6.25 μg/ml). [Ref.9748603]HD50=77 μg/ml(oxidized); HD50=110 μg/ml(reduced) against mouse red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9748603 Biochim Biophys Acta. 1998 Sep 8;1387(1-2):239-48. Kwon MY, Hong SY, Lee KH. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. DRAMP18663 GLAANFLPKIFCKITRKC 18 Brevinin 18 (Brevinin-1E truncated peptide 18; Frogs, amphibians, animals) No entry found Derived from the peptide Brevinin-1E Not found Rana esculenta Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Not found Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Has hemolytic activity. [Ref.9748603]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC=25 μg/ml), Methicillin resistant Staphylococcus aureus (MIC=100 μg/ml), Micrococcus luteus ATCC 9341 (MIC=12.5 μg/ml);##Gram-negative bacteria:Escherichia coli ATCC 2592 (MIC=25 μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=12.5 μg/ml);##Fungus: Candida albicans ATCC 36232 (MIC=25 μg/ml). [Ref.9748603]HD50=146 μg/ml(oxidized); HD50=230 μg/ml(reduced) against mouse red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9748603 Biochim Biophys Acta. 1998 Sep 8;1387(1-2):239-48. Kwon MY, Hong SY, Lee KH. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. DRAMP18664 ANFLPKIFCKITRKC 15 Brevinin 15 (Brevinin-1E truncated peptide 15; Frogs, amphibians, animals) No entry found Derived from the peptide Brevinin-1E Not found Rana esculenta Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Not found Alpha helix Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.9748603]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC=100 μg/ml), Micrococcus luteus ATCC 9341 (MIC=25 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 2592 (MIC=50 μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=50 μg/ml);##Fungus: Candida albicans ATCC 36232 (MIC=50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9748603 Biochim Biophys Acta. 1998 Sep 8;1387(1-2):239-48. Kwon MY, Hong SY, Lee KH. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. DRAMP18665 INLKALAALAKKIL 14 Mastoparan-L (MP-L; insects, arthropods, invertebrates, animals) P01514 Belongs to the tetradecapeptide family Not found Vespula lewisii (Korean yellow-jacket isp) (Vespula flaviceps lewisii) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found 1D7N resolved by NMR. "Function: Mast cell degranulating peptide. Activates G proteins that couple to phospholipase C. May be able to switch from an in-plane to a transmembrane orientation in lipid bilayers. Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Has hemolytic activity. PTM: Leucine amide at the position 14. Tissue specificity: Expressed by the venom gland." [Ref.27423268]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=12.5 μM), Enterococcus faecalis ATCC 29212 (MIC=25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=25 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=50 μM), Klebsiella pneumoniae ATCC 13883 (MIC=12.5 μM), Acinetobacter baumannii ATCC 19606 (MIC=2.7 μM) [Ref.27423268]40% hemolysis at 10μM against rat red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27423268 Biochim Biophys Acta. 2016 Nov;1858(11):2699-2708. Irazazabal LN, Porto WF, Ribeiro SM, Casale S, Humblot V, Ladram A, Franco OL. Selective amino acid substitution reduces cytotoxicity of the antimicrobial peptide mastoparan. DRAMP18666 GLGSVFGRLARILGRVIPKV 20 P1 (Pilosulin-1 1-20; Ant, insects, arthropods, invertebrates, animals) Q07932 Derived from the peptide Pilosulin-1, Belongs to the pilosulin family. Not found Myrmecia pilosula (Jumper ant) Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal, Anti-Gram- Protein level Alpha helix Not found 5X3L resolved by NMR. "Function: Has strong cytotoxic and hemolytic activities. Is more potent against mononuclear leukocytes than against granulocytes. Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. Adopts an alpha-helical structure. Allergenic properties: Causes an allergic reaction in human. Binds to IgE." [Ref.15639237]Gram-positive bacteria: Staphylococcus aureus 710A (MIC=4 μM), Bacillus megaterium BM11 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli ML-35 (MIC=2 μM), Pseudomonas aeruginosa ATCC27853 (MIC=8 μM), Salmonella typhimurium ATCC14028 (MIC=8 μM).##Drug resistant clinical isolates: Staphylococcus simulans 22 (MIC=2 μM), Micrococcus luteus (MIC=0.5 μM), Enterococcus spp. I-11305b (MIC=2 μM), Enterococcus spp. I-11054 (MIC=2 μM), Staphylococcus haemolyticus I-10925 (MIC=2 μM), Staphylococcus epidermidis LT1324 (MIC=2 μM), Staphylococcus aureus 5185 (MIC=2 μM), Staphylococcus aureus I-11574 (MIC=2 μM), Staphylococcus aureus LT1338 (MIC=3 μM), Staphylococcus aureus T1334 (MIC=1.5 μM), Citrobacter freundii I-11090 (MIC=2 μM), Klebsiella pneumoniae I-10910 (MIC=2 μM), Escherichia coli I-11276b (MIC=4 μM), Escherichia coli O-19592 (MIC=2 μM), Stenotrophomonas maltophilia O-16451 (MIC=2 μM), Stenotrophomonas maltophilia I-10717 (MIC=2 μM), Pseudomonas aeruginosa 4991 (MIC=4 μM), Pseudomonas aeruginosa I-10968 (MIC=4 μM), Candida albicans I-11301 (MIC=4 μM). [Ref.15639237]20% hemolysis at 10μM, 100% hemolysis at 100μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15639237 Arch Biochem Biophys. 2005 Feb 15;434(2):358-64. Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A. Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin. DRAMP18667 KETWWETWWTEWSQPKKKRKV 21 Pep-1 No entry found Not found Not found Derived from the nuclear localization sequence of simian virus 40 large T antigen and from reverse t Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria.No hemolytic activity. [Ref.16945333]Gram-positive bacteria: Bacillus subtilis (KCTC 3068) (MIC=8.0 μM), Staphylococcus aureus (KCTC 1621) (MIC=64.0 μM), Staphylococcus epidermidis (KCTC 1917) (MIC=64.0 μM);##Gram-negative bacteria: Escherichia coli (KCTC 1682) (MIC=32.0 μM);##Antibiotic-resistant bacteria: MDRPA 1 (CCARM 2092) (MIC=32.0 μM), MDRPA 3 (CCARM 2109) (MIC=32.0 μM). [Ref.16945333]Non-hemolysis at 200 μM against human red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16945333 Biochem Biophys Res Commun. 2006 Oct 20;349(2):769-74. Zhu WL, Lan H, Park IS, Kim JI, Jin HZ, Hahm KS, Shin SY. Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. DRAMP18668 PSVQGAAAQLTADVKK 16 AI-hemocidins 1 (Hb-1 truncated peptide) No entry found Belongs to truncated Hb-1 Not found Arca inflata Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against the Gram-negative bacteria. [Ref.28661457] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=47.35 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=47.35 μM), Pseudomonas aeruginosa clinical isolate (MIC=47.35 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28661457 Mar Drugs. 2017 Jun 29;15(7). pii: E205. Li C, Zhu J, Wang Y, Chen Y, Song L, Zheng W, Li J, Yu R. Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata DRAMP18669 ISAAEFGKINGPIKK 15 AI-hemocidins 3 (Hb-1 truncated peptide) No entry found Belongs to truncated Hb-1 Not found Arca inflata Antimicrobial, Antibacterial, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against the Gram-negative bacteria. [Ref.28661457] Gram-negative bacterium: Pseudomonas aeruginosa ATCC 27853 (MIC=95.37 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28661457 Mar Drugs. 2017 Jun 29;15(7). pii: E205. Li C, Zhu J, Wang Y, Chen Y, Song L, Zheng W, Li J, Yu R. Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata DRAMP18670 VLASKNFGDK 10 AI-hemocidins 4 (Hb-1 truncated peptide) No entry found Belongs to truncated Hb-1 Not found Arca inflata Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Antibacterial activity against the Gram-positive bacteria. [Ref.28661457] Gram-positive bacterium: Bacillus subtilis ATCC 6633 (MIC=69.55 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28661457 Mar Drugs. 2017 Jun 29;15(7). pii: E205. Li C, Zhu J, Wang Y, Chen Y, Song L, Zheng W, Li J, Yu R. Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata DRAMP18671 KCRRRKVHGPMIRIRKK 17 TO17 (TFPI-1 C-terminal peptide) No entry found Belongs to the TFPI-1 C-terminal peptide Not found Red drum (Sciaenops ocellatus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29183811] Gram-positive bacteria: Micrococcus luteus (MIC=9 μM; MBC=18 μM), Staphylococcus aureus (MIC=4 μM; MBC=8 μM);##Gram-negative bacterium: Vibrio vulnificus (MIC= 80 μM; MBC=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 29183811 Fish Shellfish Immunol. 2018 Jan;72:639-645. He SW, Wang GH, Yue B, Zhou S, Zhang M. TO17: A teleost antimicrobial peptide that induces degradation of bacterial nucleic acids and inhibits bacterial infection in red drum, Sciaenops ocellatus. DRAMP18672 APPPGLSAGV 10 Peptide 7 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18673 ELVRKNVDHLSTPDVLELV 19 Peptide 3 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18674 SPPNQPSIMTFDYAKTNK 18 Peptide 2 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18675 SLPPTLEEEFNMKKMG 16 Peptide 4 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18676 SPPSEQLGKSFNF 13 Peptide 5 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18677 SPPPGESKVDMSFNYALSNPAQ 22 Peptide 6 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18678 APPPGYAMESDSFS 14 Peptide 8 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18679 FPPPGESAVDMSFFYALSNP 20 Peptide 9 (Mollusca/molluscs/mollusks, invertebrates, animals) No entry found Not found Not found Marine snail Rapana venosa Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-positive and Gram-negative bacterium. [Ref.21703315] Gram-positive bacterium: Staphylococcus aureus;##Gram-negative bacterium: Klebsiella pneumoniae No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 21703315 Peptides. 2011 Jul;32(7):1477-83. Dolashka P, Moshtanska V, Borisova V, Dolashki A, Stevanovic S, Dimanov T, Voelter W. Antimicrobial proline-rich peptides from the hemolymph of marine snail Rapana venosa. DRAMP18680 GIADILKGLL 10 Ctry2146 (Scorpions, animals) P0DMF1 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tryznai (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18681 LLGGLLQSLL 10 Ctry2346 (Scorpions, animals) P0DMF2 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tryznai (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E-01% and 1.E+00% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18682 GILDAITGLL 10 Ctry2606 (Scorpions, animals) P0DMF4 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tryznai (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E-03% and 1.E-02% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18683 YIRDFITRRPPFGNI 15 Ctri9194 (Scorpions, animals) P0DMF5 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18684 GILDALTGIL 10 Ctri9293 (Scorpions, animals) P0DMF6 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18685 GVVDTLKNLLMGLL 14 Ctri9594 (Scorpions, animals) P0DMF7 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E-01% and 1.E+00% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18686 FLFNVIPHAINATASLIKK 19 Ctri9610 (Scorpions, animals) P0DME2 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E-01% and 1.E+00% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18687 FLVGILPRMRGFITPFLKKVR 21 Ctri10033 (Scorpions, animals) P0DME4 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18688 FLWSLIPSAISAVTSLIKK 19 Ctri10036 (Scorpions, animals) P0DME3 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18689 FDLGGLIKGVVDLF 14 Ctri10261 (Scorpions, animals) P0DMF8 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Chaerilus tricostatus (Scorpion) Antimicrobial, Antiviral Not found Not found Not found "Function: Shows a low ability to inhibit hepatitis C virus (HCV) infection in Huh7.5.1 cells. Tissue specificity: Expressed by the venom gland." [Ref.23415044] The HCV RNA level is screened that between 1.E+00% and 1.E+01% of control(IFNα.2a) in Huh7.5.1 cells. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP18690 LRPAVIRPKGK 11 Hyposin-HA1 (Frogs, amphibians, animals) P84954 Belongs to the Hyposins family Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-13. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP18691 LRPAFIRPKGK 11 Hyposin-HA2 (Frogs, amphibians, animals) P84955 Belongs to the Hyposins family Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-13. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP18692 LGPALITRKPLKGKP 15 Hyposin-HA5 (Frogs, amphibians, animals) P84958 Belongs to the Hyposins family Not found Phyllomedusa azurea (Orange-legged monkey frog) (Phyllomedusa hypochondrialis azurea) Antimicrobial Protein level Not found Not found "Function: Has antimicrobial activity. Tissue specificity: Expressed by the skin glands." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17696382 J Proteome Res. 2007 Sep;6(9):3604-13. Thompson AH, Bjourson AJ, Orr DF, Shaw C, McClean S. Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins. DRAMP18693 RPKPQQFFGLM 11 Substance P (Mammals, animals) P67932, P67933 Belongs to the tachykinin family. TAC1 Not found Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Substance P possesses direct antimicrobial activity. Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.12074933]Gram-negative bacteria: Escherichia coli (MIC=0.06%), Proteus vulgaris (MIC=0.13%), Pseudomonas aeruginosa (MIC=0.13%) ;##Gram-positive bacteria: Staphylococcus aureus (MIC=0.007%), Enterococcus faecalis (MIC=0.13%);##Yeast: Candida albicans (MIC=0.25%) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12074933 Life Sci. 2002 Jul 5;71(7):747-50. Kowalska K, Carr DB, Lipkowski AW. Direct antimicrobial properties of substance P. DRAMP18694 RPKPQQWFWLM 11 substance P antagonist (Mammals, animals) No entry found Not found Not found Not found Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.12074933]Gram-negative bacteria: Escherichia coli (MIC=0.13%), Proteus vulgaris (MIC=0.13%), Pseudomonas aeruginosa (MIC=0.13%) ;##Gram-positive bacteria: Staphylococcus aureus (MIC=0.13%), Enterococcus faecalis (MIC=0.13%);##Yeast: Candida albicans (MIC=0.03%). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12074933 Life Sci. 2002 Jul 5;71(7):747-50. Kowalska K, Carr DB, Lipkowski AW. Direct antimicrobial properties of substance P. DRAMP18695 KHFGKDSNFPF 11 Venom peptide 1 (Scorpions, animals) P86825 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short ant Not found Tityus serrulatus (Brazilian scorpion) Antimicrobial, Antibacterial Protein level Not found Not found "Function: May be an antibacterial peptide. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18718845 Toxicon. 2008 Oct;52(5):611-8. Rates B, Ferraz KK, Borges MH, Richardson M, De Lima ME, Pimenta AM. Tityus serrulatus venom peptidomics: assessing venom peptide diversity. DRAMP18696 FQWQRNMRKVRGPPVS 16 HLP1 (Lactotransferrin truncated peptide) P02788, A0A161I202 Belongs to the Lactotransferrin LTF Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. HLP 1 corresponded to the loop region of human lactoferricin (residues 20 to 35). [Ref.9596699] Gram-negative bacteria: Escherichia coli NCTC 8007 (MIC=500 μM), Escherichia coli NCTC 10418 (MIC=500μM);##Gram-positive bacterium: Staphylococcus aureus (MIC=500 μM);##Clinical isolates: Acinetobacter sp.(MIC=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9596699 Infect Immun. 1998 Jun;66(6):2434-40. Chapple DS, Mason DJ, Joannou CL, Odell EW, Gant V, Evans RW. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. DRAMP18697 FQWQRNMRKVR 11 HLP2 (Lactotransferrin truncated peptide) P02788, A0A161I202 Belongs to the Lactotransferrin Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against Gram-negative bacteria and Gram-positive bacteria. HLP 2 corresponded to the alpha-helical region of the loop in its native conformation (residues 20 to 30). [Ref.9596699] Gram-negative bacteria: Escherichia coli NCTC 8007 (MIC=290 μM), Escherichia coli NCTC 10418 (MIC=579 μM);##Gram-positive bacterium: Staphylococcus aureus (MIC=14 μM);##Clinical isolates: Acinetobacter sp. (MIC=0.86 μM), Enterobacter aerogenes (MIC=290 μM), Klebsiella sp. strain 3105 (MIC=290 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9596699 Infect Immun. 1998 Jun;66(6):2434-40. Chapple DS, Mason DJ, Joannou CL, Odell EW, Gant V, Evans RW. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. DRAMP18698 AERVGAGAPVYL 12 Histone H2A (Trouts, fish, animals) P02264 Belongs to the histone H2A family. Not found Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Protein level Not found Not found "Function: The secreted form has antibacterial activity against Gram-positive bacteria and antifungal activity against Saccharomyces cerevisiae. Tissue specificity: Expressed and secreted by skin epithelium." [Ref.12164782] Gram positive bacteria: Aerococcus viridans (MIC=0.08-0.15 µM), Bacillus subtilis (MIC=0.6-1.2 µM), Micrococcus luteus (MIC=0.6-1.2 µM), Planococcus citreus (MIC=0.08-0.15 µM), Renibacterium salmoninarum (MIC=0.15-0.3 µM);##Fungi: Saccharomyces cerevisiae (MIC=0.3-0.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12164782 Biochem J. 2002 Dec 1;368(Pt 2):611-20. Fernandes JMO., Kemp GD., Molle MG., Smith VJ.2002 Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. DRAMP18699 FLGGLLASLLGKI 13 Pleurain-B1 (Frogs, amphibians, animals) B5L1B2, B5L1B4, B5L1B6, B5L1B3 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli(MIC=25 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=3.1 μg/ml), Bacillus subtilis (MIC=3.1 μg/ml);##Yeast: Candida albicans (MIC=1.6μg /ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18700 YPELQQDLIARLL 13 Pleurain-C1 (Frogs, amphibians, animals) B5L1A8 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 μg/ml), Bacillus subtilis (MIC=3.1 μg/ml);##Yeast: Candida albicans(MIC=25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18701 FRSGILKLASKIPSVLCAVLKNC 23 Pleurain-D4 (Frogs, amphibians, animals) B5L1I4 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 μg/ml), Bacillus subtilis (MIC=50 μg/ml);##Yeast: Candida albicans(MIC=25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18702 AKAWGIPPHVIPQIVPVRIRPLCGNV 26 Pleurain-E1 (Frogs, amphibians, animals) B5L1I5 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=25 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6..3 μg/ml)##Yeast: Candida albicans (MIC=25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18703 GFWDSVKEGLKNAAVTILNKIKCKISECPPA 31 Pleurain-G1 (Frogs, amphibians, animals) B5L1I8 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=50 μg/ml), Bacillus subtilis (MIC=100 μg/ml);##Yeast: Candida albicans(MIC=12.5 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18704 FIPGLRRLFATVVPTVVCAINKLPPG 26 Pleurain-J1 (Frogs, amphibians, animals) B5L1L0 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=12.5 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 μg/ml), Bacillus subtilis (MIC=50 μg/ml);##Yeast: Candida albicans(MIC=6.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18705 GFFDRIKALTKNVTLELLNTITCKLPVTPP 30 Pleurain-N1 (Frogs, amphibians, animals) B5L1L8 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=50 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 μg/ml);##Yeast: Candida albicans (MIC=12.5 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18706 CVHWMTNTARTACIAP 16 Pleurain-R1 (Frogs, amphibians, animals) No entry found Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Rana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675]Gram-negative bacterium: Escherichia coli (MIC=100 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=25 μg/ml), Bacillus subtilis (MIC=100 μg/ml);##Yeast: Candida albicans(MIC=50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP18707 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRPL 60 BACTENECIN 7 (bac 7, Pro-rich; bovine cathelicidin, cattle, ruminant, mammals, animals) P19661 Belongs to the cathelicidin family. CATHL3 Bos taurus (Bovine neutrophils) Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Not found Rich Not found 4JWC resolved by NMR "Function: Antibacterial activity against an array of gram-negative and gram-positive bacteria. PTM: Elastase is responsible for its maturation." [Ref.2777377] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=12 µg/ml in Murller-Hinton, MIC=50 µg/ml in Iso-Sensitest), Salmonella typhimurium LT2 (MIC=12 µg/ml in Murller-Hinton, MIC=200 µg/ml in Iso-Sensitest), Salmonella typhimurium ATCC 14028 (MIC=25 µg/ml in Murller-Hinton, MIC=100 µg/ml in Iso-Sensitest), Klebsiella pneumoniae ATCC 13883 (MIC=12 µg/ml in Murller-Hinton, MIC=200 µg/ml in Iso-Sensitest), Enterobacter cloacae ATCC 13047 (MIC=25 µg/ml in Murller-Hinton, MIC=200 µg/ml in Iso-Sensitest), Pseudomonas aeruginosa ATCC 7700 (MIC=50 µg/ml in Murller-Hinton);##Gram-positive bacterium: Staphylococcus epidermidis ATCC 12228 (MIC=200 µg/ml in Murller-Hinton, MIC=200 µg/ml in Iso-Sensitest). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2777377 Infect Immun. 1989 Oct;57(10): 3142-6. Gennaro R, Skerlavaj B, Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. DRAMP18708 ALWMTLLKKVLKAAAKAALNAVLVGANA 28 Dermaseptin-S4 (DRS-S4, DS4; frog, amphibians, animals) P80280 Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfami Not found Phyllomedusa sauvagei (Sauvage's leaf frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found 2DD6 resolved by NMR Function: Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1. Probably acts by disturbing membrane functions with its amphipathic structure. Binds to healthy erythrocytes (this binding is receptor independent), and has strong hemolytic activity. Does not bind to P.falciparum infected erythrocytes, but accumulates within the parasite. Kills the parasite, and only at high concentrations has a hemolytic activity on the host cell. [Swiss_Prot Entry P80280]Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1 [Swiss_Prot Entry P80280]Strong hemolytic activity Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8306981 Eur. J. Biochem. 1994; 219:145-154. Mor A, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. DRAMP18709 INLKALAALAKKIL 14 Mastoparan (MP; insects, arthropods, invertebrates, animals) P01514 Not found Not found Vespula flaviceps lewisii (Korean yellow-jacket isp) Antimicrobial, Antibacterial, Cell degranulating Not found Helix Not found 1D7N resolved by NMR Function: Antibacterial and cell degranulating activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 540362 Chem Pharm Bull (Tokyo). 1979 Aug;27(8):1942-4 Hirai Y, Yasuhara T, Yoshida H, Nakajima T, Fujino M, Kitada C. A new mast cell degranulating peptide mastoparan in the venom of Vespula lewisii DRAMP18710 VTCDLLSFKGQVNDSACAANCLSLGKAGGHCEKVGCICRKTSFKDLWDKRF 51 Royalisin (Insects, arthropods, invertebrates, animals) No entry found Not found Not found Apis mellifera L. (royal jelly honeybee) Antimicrobial, Antibacterial, Anti-Gram+ Protein level Bridge High content of cysteine residues and a compact structure owing to intramolecular disulfide cross-linking. Function: Antibacteria activity against Gram-positive bacteria. [Ref.2358464] Gram-positive bacteria: Bifidobacterium adolescentis ATCC15703 (MIC=15 µM at concentration of 1%, MIC=43 µM at concentration of 10%, MIC=59 µM at concentration of 100%), Bifidobacterium bifidum ATCC15606 (MIC=91 µM at concentration of 100%), Bifidobacterium breve ATCC15700 (MIC=67 µM at concentration of 10%, MIC=87 µM at concentration of 100%), Bifidobacterium infantis ATCC15697 (MIC=20 µM at concentration of 10%, MIC=71 µM at concentration of 100%), Bifidobacterium longum ATCC15707 (MIC=29 µM at concentration of 1%, MIC=81 µM at concentration of 10%, MIC=81 µM at concentration of 100%), Clostridium perfringens ATCC13124 (MIC=75 µM at concentration of 100%), Corynebacterium pyogenes (MIC=31 µM at concentration of 10%, MIC=96 µM at concentration of 100%), Eubacterium aerofacience (MIC=17 µM at concentration of 100%), Lactobacillus acidophilus ATCC314 (MIC=44 µM at concentration of 100%), Lactobacillus acidophilus ATCC4356 (MIC=47 µM at concentration of 100%), Lactobacillus bulgaricus ATCC11841 (MIC=21 µM at concentration of 1%, MIC=87 µM at concentration of 10%, MIC=84 µM at concentration of 100%), Lactobacillus helveticus ss. jugurti (MIC=33 µM at concentration of 1%, MIC=90 µM at concentration of 10%, MIC=72 µM at concentration of 100%), Lactobacillus lactis ATCC7830 (MIC=59 µM at concentration of 1%, MIC=90 µM at concentration of 10%, MIC=88 µM at concentration of 100%), Lactobacillus leichmannii ATCC7830 (MIC=14 µM at concentration of 1%, MIC=88 µM at concentration of 10%, MIC=89 µM at concentration of 100%), Leuconostoc cremoris ATCC19254 (MIC=16 µM at concentration of 1%, MIC=84 µM at concentration of 10%, MIC=88 µM at concentration of 100%), Stapjylococcus aureus SC-D (MIC=17 µM at concentration of 1%, MIC=22 µM at concentration of 10%, MIC=82 µM at concentration of 100%), Streptococcus cremoris SCR-812 (MIC=10 µM at concentration of 1%, MIC=18 µM at concentration of 10%, MIC=83 µM at concentration of 100%), Streptococcus thermophilus ATCC19258 (MIC=9 µM at concentration of 1%, MIC=14 µM at concentration of 10%, MIC=86 µM at concentration of 100%). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2358464 J. Biol. Chem. 1990; 265:11333-11337 Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kaishima T, Kobayashi K. A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. DRAMP18711 GRKSDCFRKNGFCAFLKCPYLTLISGLCSFHLC 33 Chicken Heterophil Peptide 2 (CHP-2, avian beta-defensin, birds, animals) P80390 Belongs to the beta-defensin family. Not found Gallus gallus (Chicken) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found Function: Has bactericidal activity. Potent activity against E.coli ML-35, L.monocytogenes EGD and C.albicans. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 7964174 J. Leukoc. Biol. 1994; 56: 661-665. Evans EW, Beach GG, Wunderlich J, Harmon BG. Isolation of antimicrobial peptides from avian heterophils. DRAMP18712 GFGKAFHSVSNFAKKHKTA 19 Styelin A (Tunicate, invertebrates, animals) P81469 Belongs to the Cecropins family. Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Helix Not found "Function: Bactericidal against several Gram-positive and Gram-negative bacteria. Tissue specificity: Hemocytes and pharyngeal tissues." [Ref.9467865] Gram positive bacteria: Listeria monocytogenes EGD (MIC=2 µg/ml), Staphylococcus aureus 930918-3 (MIC=6 µg/ml), Enterococcus faecalis 94.132 (MIC=2 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa MR 3007 (MIC=4 µg/ml), Escherichia coli ML-35p (MIC=2.7 µg/ml), Salmonella typhimurium 14028S (MIC=5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9467865 Comp. Biochem. Physiol. 1997; 118:515-521 Lee IH, Cho Y, Lehrer RI. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. DRAMP18713 GFGPAFHSVSNFAKKHKTA 19 Styelin B (Tunicate, invertebrates, animals) P81470 Belongs to the Cecropins family. Not found Styela clava (Sea squirt) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Helix Not found "Function: Bactericidal against several Gram-positive and Gram-negative bacteria. Tissue specificity: Hemocytes and pharyngeal tissues." [Ref.9467865] Gram positive bacteria: Listeria monocytogenes EGD (MIC=2 µg/ml), Staphylococcus aureus 930918-3 (MIC=6 µg/ml), Enterococcus faecalis 94.132 (MIC=2 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa MR 3007 (MIC=4.5 µg/ml), Escherichia coli ML-35p (MIC=2.7 µg/ml), Salmonella typhimurium 14028S (MIC=5 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9467865 Comp. Biochem. Physiol. 1997; 118:515-521 Lee IH, Cho Y, Lehrer RI. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. DRAMP18714 IIGGR 5 Cathepsin G(1-5) (Human, primates, mammals, animals) No entry found Belongs to the Cathepsin G N-terminal 1-5 truncted peptide. Not found Homo sapiens Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Bactericidal activity against Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2116408 J Biol Chem. 1990 Aug 15;265(23):13584-8. Bangalore N, Travis J, Onunka VC, Pohl J, Shafer WM. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. DRAMP18715 HPQYNQR 7 Cathepsin G(77-83) (Human, primates, mammals, animals) No entry found Belongs to the Cathepsin G 77-83 truncted peptide. Not found Homo sapiens Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Bactericidal activity against Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2116408 J Biol Chem. 1990 Aug 15;265(23):13584-8. Bangalore N, Travis J, Onunka VC, Pohl J, Shafer WM. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. DRAMP18716 PDPAKTAPKKGSKKAVTKA 19 Histone H2B-1(HLP-1) (fish, animals) P81903 Belongs to the histone H2B family. Not found Ictalurus punctatus (Channel catfish) (Silurus punctatus) Antimicrobial, Antibacterial, Anti-Gram- Protein level The nucleosome is a histone octamer Not found "Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Has broad-spectrum antimicrobial and antibacterial activity. It is important in the antimicrobial defenses of fish skin and possesses strong activity against saprolegnia, the most common fungal infection in fish. It is also inhibitory to fish bacterial pathogens, such as aeromonas hydrophila, vibrio alginolyticus and Escherichia coli D31. PTM: Monoubiquitination at the C-terminal Lys gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. Phosphorylated during apoptosis; which facilitates apoptotic chromatin condensation. " [Ref.9645227] Gram negative bacteria: Escherichia coli (MIC=0.37±0.023 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9645227 Cell. Mol. Life Sci. 1998; 54:467-475 Robinette D., Wada S., Arroll T., Levy MG., Miller WL., Noga EJ. Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins. DRAMP18717 EFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS 37 Charybdotoxin (Yellow scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals) No entry found Not found Not found Leiurus quinquestriatus hebraeus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Combine Helix and Beta structure Not found 2CRD resolved by NMR Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.15118082]Gram-positive bacteria: Bacillus subtilis (Inhibition zone=4 mm completely inhibit in PH5.5, Inhibition zone=7 mm incompletely inhibit and Inhibition zone=6 mm in PH7.5 completely inhibit at 10 μg/well), Staphylococcus aureus (Inhibition zone=3 mm incompletely inhibit in PH5.5, Inhibition zone=6 mm incompletely inhibit and Inhibition zone=1 mm completely inhibit in PH7.5 at 10 μg/well);##Gram-negative bacteria: Escherichia coli (Inhibition zone=2 mm incompletely inhibit in PH5.5, Inhibition zone=8 mm incompletely inhibit in PH7.5 at 10 μg/well);##Fungi: Candida albicans (Inhibition zone=13 mm completely inhibit in PH5.5, Inhibition zone=15 mm in PH7.5 completely inhibit at 10 μg/well). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15118082 Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Yount NY, Yeaman MR. Multidimensional signatures in antimicrobial peptides. DRAMP18718 GDDDDDD 7 SAAP fraction 2 (Surfactant-associated anionic peptides; Asp-rich; sheep, ruminant, mammals, animals) No entry found Not found Not found Ovis aries Antimicrobial, Antibacterial, Anti-Gram- Protein level Rich Not found Function: Antibacterial activity against negative bacteria. No amidation at the C-terminus [Ref.8552650] Gram-negative bacterium: Pasteurella haemolytica (MBC50=0.04 mM in Zn-saline, MBC50=11.49 mM in Test buffer; Peptide/surfactant mixture MBC50=0.05 mM in Zn-saline, MBC50=6.44 mM in Test buffer; Peptide/serum mixture MBC50=0.05 mM in Zn-saline, MBC50=10.38 mM in Test buffer; Peptide/surfactant/serum mixture MBC50=0.06 mM in Zn-saline, MBC50=5.93 mM in Test buffer). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8552650 Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):412-6. Brogden KA, de Lucca AJ, Bland J, Elliott S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. DRAMP18719 DDDDDDD 7 SAAP fraction 3 (Surfactant-associated anionic peptides; Asp-rich; sheep, ruminant, mammals, animals) No entry found Not found Not found Ovis aries Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Rich Not found Function: Antibacterial activity against Gram positive and negative bacteria. No amidation at the C-terminus [Ref.8552650] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MBC50=1.21 mM in Zn-saline), Streptococcus faecalis ATCC 29213 (MBC50=1.39 mM in Zn-saline);##Gram-negative bacteria: Escherichia coli ATCC 12795 (MBC50=0.64 mM in Zn-saline), Klebsiella pneumoniae ATCC 10031 (MBC50=0.62 mM in Zn-saline), Pasteurella haemolytica (MBC50=0.02 mM in Zn-saline, MBC50=8.52 mM in Test buffer; Peptide/surfactant mixture MBC50=0.01 mM in Zn-saline, MBC50=4.43 mM in Test buffer; Peptide/serum mixture MBC50=0.02 mM in Zn-saline, MBC50=4.95 mM in Test buffer; Peptide/surfactant/serum mixture MBC50=0.03 mM in Zn-saline, MBC50=2.79 mM in Test buffer). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8552650 Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):412-6. Brogden KA, de Lucca AJ, Bland J, Elliott S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. DRAMP18720 GADDDDD 7 SAAP fraction 6 (Surfactant-associated anionic peptides; Asp-rich; sheep, ruminant, mammals, animals) No entry found Not found Not found Ovis aries Antimicrobial, Antibacterial, Anti-Gram- Protein level Rich Not found Function: Antibacterial activity against negative bacteria. No amidation at the C-terminus [Ref.8552650] Gram-negative bacterium: Pasteurella haemolytica (MBC50=0.02 mM in Zn-saline, MBC50=10.10 mM in Test buffer; Peptide/surfactant mixture MBC50=0.04 mM in Zn-saline, MBC50=5.18 mM in Test buffer; Peptide/serum mixture MBC50=0.04 mM in Zn-saline, MBC50=5.59 mM in Test buffer; Peptide/surfactant/serum mixture MBC50=0.04 mM in Zn-saline, MBC50=4.75 mM in Test buffer). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 8552650 Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):412-6. Brogden KA, de Lucca AJ, Bland J, Elliott S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. DRAMP18721 GWKIGKKLEHHGQNIRDGLISAGPAVFAVGQAATIYAAAK 40 Hinnavin I (Hin I; insects, arthropods, invertebrates, animals) No entry found Belongs to the Cecropins family. Not found Artogeia rapae (cabbage butterfly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Hinnavin 1 is heat stable; its activity is retained after 60 min incubation at 100 DC, being effective against Gram negative and/or Gram positive bacteria. Hinnavin I and lysozyme 2 showed a powerful synergistic effect on the inhibition of bacterial growth. [Ref.9339895] Gram-positive bacteria: Bacillus subtilis (Inhibition zone=3.0 mm), Bacillus megaterium Bm11 (Inhibition zone=5.0 mm), Bacillus thuringiensis (Inhibition zone=3.0 mm);##Gram-negative bacteria: Escherichia coli (Inhibition zone=7.0 mm), Escherichia coli D21 (Inhibition zone=7.1 mm), Enterobacter cloacae (Inhibition zone=6.0 mm);##Fungi: Candida albicans (Inhibition zone=3.0 mm), Aspergillus niger (Inhibition zone=3.0 mm). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membranes 9339895 Mol Cells. 1997 Aug 31;7(4):509-13 Bang IS, Son SY, Yoe SM. Hinnavin I, an antibacterial peptide from cabbage butterfly, Artogeia rapae. DRAMP18722 AKKFGKAFVGEIM 13 MA (Magainin 2 (9-21) truncated peptide) P11006 Belongs to truncated magainin 2. magainins Xenopus laevis (African clawed frog) Antimicrobial, Antibacterial, Anti-Gram- Not found Alpha helix Not found Function: Antibacterial activity against the Gram-negative bacteria. [Ref.28178190] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=32 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). pii: E339. Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP18723 KWKLFKKI 8 CE (Cecropin A (1 P01507 Belongs to truncated Cecropin A. Not found Hyalophora cecropia (Cecropia moth) Antimicrobial, Antibacterial, Anti-Gram- Not found random coil Not found Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. [Ref.28178190] Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=64 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). pii: E339. Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP18724 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK 69 Oncorhyncin III (Oncorhyncin-3, histone-derived; fish, animals) P02315 Belongs to the HMGN family. Not found Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Oncorhyncin III has antibacterial activity against Gram-positive and Gram-negative bacteria at submicromolar concentrations. Non-histone protein that probably binds to the inner side of nucleosomal DNA, altering the association between the DNA and the nucleosome octamer. [Ref.12713443] Gram-positive bacteria: Aerococcus viridans (MIC=0.06-0.12 μM), Bacillus subtilis (MIC=0.25-0.5 μM), Micrococcus luteus (MIC=0.12-0.25 μM), Planococcus citerus (MIC=0.06-0.12 μM);##Gram-negative bacteria: Aeromonas hydrophila (MIC>0.5 μM), Aeromonas salmonicida (MIC>0.5 μM), Escherichia coli (MIC=0.25-0.5 μM), Listonella anguillarum (MIC=0.25-0.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12713443 Biochem 2003; 373 (Pt 2): 621-628 Fernandes JM., Saint N, Kemp GD, Smith VJ. Oncorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss. DRAMP02518 KRFKKFFKKLKNSVKKRAKKFFKKPKVIGVTFPF 34 NA-CATH No entry found Not found Not found Naja atra Antimicrobial, Antibacterial, Anti-Gram- Not found Alpha helix, random coil NA-CATH has previously been shown to be random coil in water or buffer and Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.28089718] Gram-negative bacteria: Acinetobacter baumannii ATCC 9955 (MIC=10μg/ml), Acinetobacter baumannii ATCC BAA-1794 (MIC=10μg/ml), Escherichia coli ATCC 51659 (MIC=21μg/ml), K. pneumoniae ATCC 33495 (MIC=5.2μg/ml), K. pneumoniae ATCC BAA-1705 (MIC=5.2μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=10μg/ml), Pseudomonas aeruginosa ATCC BAA-2110 (MIC=10μg/ml) [Ref.28089718] 0% hemolysis at 300μg/ml against sheep red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 28089718 Dev Comp Immunol. 2017 May;70:135-144. Barksdale SM, Hrifko EJ, van Hoek ML. Cathelicidin antimicrobial peptide from Alligator mississippiensis has antibacterial activity against multi-drug resistant Acinetobacter baumanii and Klebsiella pneumoniae DRAMP03714 FLGALWNVAKSVF 13 VmCT1 I0DEB3 Belongs to the scorpion NDBP 5 family Not found Vaejovis mexicanus smithi (Scorpion) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix, random coil the peptide showed a coiled structure in water, zwitterionic lipid vesicles (POPC and POPC:DOPE) and negatively charge lipid vesicle (POPC:POPG) the analogs tend to adopt helical structures. Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria, antifungal activity. Has hemolytic activity. [Ref.27912176] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=3.12 μmol/L), Bacillus subtilis ATCC 6633 (MIC=25μmol/L), Staphylococcus epidermidis ATCC 12228 (MIC=3.12μmol/L);##Gram-negative bacterium: Pseudomonas aeruginosa ATCC 27853 (MIC=0.78μmol/L), Escherichia coli D31 (MIC=3.12μmol/L), Serratia marcescens ATCC 4112 (MIC=1.56μmol/L), Enterobacter cloacae β-12 (MIC=25μmol/L), Micrococcus luteus A270 (MIC=1.56μmol/L);##Fungi: Candida albicans MDM8 (MIC=12.5μmol/L), Candida tropicalis IOC 4560 (MIC=6.25μmol/L), Candida parapsilosis IOC 4564 (MIC=25μmol/L), Aspergillus niger (MIC=25μmol/L), Cladosporium herbarum ATCC 26362 (MIC=50μmol/L), Cryptococcus neoformans (MIC=3.12μmol/L) [Ref.27912176] 10% hemolysis at 1.99μmol/L against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity DRAMP03645 LVQRGRFGRFLRKIRRFRPKVTITIQGSARFG 32 fowlicidin-2 No entry found Not found CATHL2 Gallus gallus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not foundn 2GDL Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. Has hemolytic activity. [Ref.27698732] Gram-positive bacterium:Staphylococcus aureus ATCC 29213 (MIC=4µM);##Gram-negative bacterium:Escherichia coli ATCC 25922 (MIC=1µM), Pseudomonas aeruginosa ATCC 27853 (MIC=4µM), Salmonella typhimurium C77-31 (MIC=2µM) [Ref.27698732] 15% hemolysis at 10µM,40% hemolysis at 80µM,60% hemolysis at 200µM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 27698732 Exp Ther Med. 2016 Oct;12(4):2324-2330. Xing LW, Tian SX, Gao W, Yang N, Qu P, Liu D, Jiao J, Wang J, Feng XJ. Recombinant expression and biological characterization of the antimicrobial peptide fowlicidin-2 in Pichia pastoris. DRAMP20766 GEILCNLCTGLINTLENLLTTKGADKVKDYISSLCNKASGFIATLCTKVLDFGIDKLIQLIEDKVDANAICAKIHAC 77 Pore-forming peptide ameobapore A(Amoeba peptide, AP-A; Parasite, amoebozoa, protozoa, protists) P34095 Belongs to the amoebapore (amoebapore) family Not found Entamoeba histolytica Antimicrobial, Antibacterial, Anti-Gram+, Antibiotic Protein level Alpha helix Not found 1OF9 resolved by NMR. Function: Forms pores in the cytoplasmic membrane of host cells. Has antibacterial activity against M.luteus, no activity against E.coli. Implicated in the cytolytic activity of the parasite. [Ref.7715451] Gram-positive bacterium: Micrococcus luteus (MIC=2 μM, MBC=5 μM).##[Ref.11948186]Gram-positive bacterium: B. subtilis (100% permeabilized bacteria: 5 nM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Disulfide bonds between Cys5 and Cys77, Cys8 and Cys71, Cys35 and Cys46 Not included yet Not included yet Not found 1881907##7715451##11948186 Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7659-63.##Mol Microbiol. 1994 Dec;14(5):895-904.##J Biol Chem. 2002 Jun 21;277(25):22353-60. Leippe M, Ebel S, Schoenberger OL, Horstmann RD, üller-Eberhard HJ.##Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ.##Herbst R, Ott C, Jacobs T, Marti T, Marciano-Cabral F, Leippe M. Pore-forming peptide of pathogenic Entamoeba histolytica.##Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes.##Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. DRAMP20767 GAILCNLCKDTVKLVENLLTVDGAQAVRQYIDNLCGKASGFLGTLCEKILSFGVDELVKLIENHVDPVVVCEKIHAC 77 Pore-forming peptide ameobapore B (Parasite, amoebozoa, protozoa, protists) Q24824 Belongs to the amoebapore (amoebapore) family Not found Entamoeba histolytica Antimicrobial, Antibacterial, Anti-Gram+, Antibiotic Protein level Alpha helix Not found Function: Forms pores in the cytoplasmic membrane of host cells. Has antibacterial activity against M.luteus, no activity against E.coli. Implicated in the cytolytic activity of the parasite. [Ref.7715451] Gram-positive bacterium: Micrococcus luteus (MIC=5 μM, MBC=5 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Disulfide bonds between Cys5 and Cys77, Cys8 and Cys71, Cys35 and Cys46 Not included yet Not included yet Not found 7715451 Mol Microbiol. 1994 Dec;14(5):895-904. Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. DRAMP20768 IPVLCPVCTSLVGKLIDLVLGGAVDKVTDYLETLCAKADGLVETLCTKIVSYGIDKLIEKILEGGSAKLICGLIHAC 77 Pore-forming peptide ameobapore C (EH-APP; Parasite, amoebozoa, protozoa, protists) Q24825 Belongs to the amoebapore (amoebapore) family Not found Entamoeba histolytica Antimicrobial, Antibacterial, Anti-Gram+, Antibiotic Protein level Alpha helix Not found Function: Forms pores in the cytoplasmic membrane of host cells. Has antibacterial activity against M.luteus, no activity against E.coli. Implicated in the cytolytic activity of the parasite. [Ref.7715451] Gram-positive bacterium: Micrococcus luteus (MIC=5 μM, MBC=10 μM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Disulfide bonds between Cys5 and Cys77, Cys8 and Cys71, Cys35 and Cys46 Not included yet Not included yet Not found 7715451 Mol Microbiol. 1994 Dec;14(5):895-904. Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. DRAMP20769 DAECEICKFVIQQVEAFIESNHSQAEIQKELNKLCSSVPSIFTQTCLSIARMVPYIIKKLEEHNSPGQVCQGLHLCKSS 78 Naegleriapore A (NP-A; parasite, amoebozoa; protozoa, protists) Q95X03 Not found NP-A Naegleria fowleri (Brain eating amoeba) Antimicrobial, Antibacterial, Anti-Gram+ Protein predicted Not found Not found No comments found on DRAMP database [Ref.11948186] Gram-positive bacterium: B. subtilis (100% permeabilized bacteria: 158 nM) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11948186 J Biol Chem. 2002 Jun 21;277(25):22353-60. Herbst R, Ott C, Jacobs T, Marti T, Marciano-Cabral F, Leippe M. Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. DRAMP20770 SVIGCEICEWLVATAEGFVNKTKPQIEQELLQICAKLGPYEQICDQLVLMELPDIIDQIIAKEPPAIVCSQVKICNGSAMAVAA 84 Naegleriapore B (NP-B; parasite, amoebozoa, protozoa, protists) Q95X02 Not found NP-B Naegleria fowleri (Brain eating amoeba) Not found Protein predicted Not found Not found No comments found on DRAMP database No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11948186 J Biol Chem. 2002 Jun 21;277(25):22353-60. Herbst R, Ott C, Jacobs T, Marti T, Marciano-Cabral F, Leippe M. Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. DRAMP20771 GKCSVLKKVACAAAIAGAVAACGGIDLPCVLAALKAAEGCASCFCEDHCHGVCKDLHLC 59 Acanthaporin (parasite, amoebozoa, protozoa, protists) I3NI56 Not found Not found Acanthamoeba culbertsoni Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found 2LRD, 2LRE resolved by NMR. Function: Acanthaporin is antimicrobially active against several Gram-positive and Gram-negative bacteria at pH 5.2 but is inactive at pH 7.4, reflecting a pH-dependent activity of the protein. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23143413 Nat Chem Biol. 2013 Jan;9(1):37-42. Michalek M, Sönnichsen FD, Wechselberger R, Dingley AJ, Hung CW, Kopp A, Wienk H, Simanski M, Herbst R, Lorenzen I, Marciano-Cabral F, Gelhaus C, Gutsmann T, Tholey A, Grötzinger J, Leippe M. Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba. DRAMP20772 PPHKKKLAVYPVFLFYLFLSWFSLIV 26 cPcAMP1/26 (ciliate, Protists) No entry found Not found Pcamp1 Paramecium caudatum Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: cPcAMP1/26 is capable of markedly killing A. hydrophila and S. aureus (p < 0.05) [Ref.26883426] cPcAMP1/26 is capable of markedly killing A. hydrophila and S. aureus (p < 0.05), with the bactericidal rates being 27.7%, 31.7% and 40.1% as well as 34.4%, 47.4% and 49.2%, respectively [Ref.26883426] cPcAMP1/26 showed little hemolytic activity towards human erythrocytes at 100 μg/ml Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 26883426 Dev Comp Immunol. 2016 Jul;60:53-65. Cui P, Dong Y, Li Z, Zhang Y, Zhang S. Identification and functional characterization of an uncharacterized antimicrobial peptide from a ciliate Paramecium caudatum. DRAMP20775 FLGFLKNLF 9 Ctry2459-WT (Ctry2459, scorpions,animals) P0DMF3 Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family. Not found Chaerilus tryznai (Scorpion) Antimicrobial, Antiviral Protein level Not found Not found Function: Inhibit hepatitis C virus(HCV) infection via inactivating infectious viral particle. However, it cannot suppress established infection because of the poor cellular uptake and restriction of endosomes. [Ref.23415044] Virus: Hepatitis C virus (EC50=1.84 μg/ml).##Cytotoxic: Huh7.5.1 cells (CC50=79.8 μg/ml) [Ref.23415044] HC50 = 137.9 μg/ml against human red blood cells. Linear Free Free L [Ref.23415044] CC50=79.8 μg/ml against Huh7.5.1 cells. Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP20776 IGGYCSWLRL 10 HaA4 (beetles,insects,animals) No entry found Not found Not found Harmonia axyridis (Multicolored Asian lady beetle) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria. HaA4 is proved to have more potent activity against Staphylococcus epidermidis, M. luteus, and Pseudomonas syringae. [Ref.23124352] Gram-negative bacteria: Escherichia coli KACC 13821 (MIC=32 microM), Klebsiella pneumoniae KACC 11402 (MIC<64 microM), Pseudomonas aeruginosa KACC 10259 (MIC<64 microM), Pseudomonas syringae KACC 10659 (MIC=2 microM)；## Gram-positive bacteria: Staphylococcus aureus KACC 13257 (MIC<64 microM), MR Staphylococcus aureus CCARM 3001(MIC=32 microM), Enterococcus faecalis KACC 13807 (MIC=16 microM), Enterococcus hirae KACC 16328 ( MIC=32 microM), Staphylococcus epidermidis KACC 13234 (MIC=8 microM), Micrococcus luteus KACC 10488 (MIC = 4 microM), Streptococcus pyogenes KACC 11956 (MIC=32 microM) [Ref.23124352] In the hemolytic assay, HaA4 peptide evidenced no hemolytic activity against mouse red blood cells, even at high concentrations, and thus suggesting that the peptide may not be detrimental to eukaryotic cells. Linear Free Amidation L [Ref.23124352] The cytotoxicity is not found in a dose dependent manner. Not found 23124352 J Microbiol Biotechnol. 2012 Nov;22(11):1588-90. Kim IW, Lee JH, Park HY, Kwon YN, Yun EY, Nam SH, Kim SR, Ahn MY, Hwang JS. Characterization and cDNA cloning of a defensin-like peptide, harmoniasin, from Harmonia axyridis. DRAMP20777 KRFKKFFRKLKKSVKKRAKEFFKKPRVIGVSIPF 34 Cath-BF No entry found Derived from three-finger toxin Not found Bungarus fasciatus (Banded krait) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29392557] Gram-positive bacteria: MRSA PS-2 (MIC=64 μg/ml);##Gram-negative bacteria, MRSA PS-7 (MIC=64 μg/ml), MRSA PS-18 (MIC=64 μg/ml), MRSA PS-45 (MIC=64 μg/ml), MRSA PS-46 (MIC=128 μg/ml), MRSA PS-50 (MIC=64 μg/ml), MRSA PS-59 (MIC=128 μg/ml), MRSA PS-70 (MIC=32 μg/ml), MRSA PS-84 (MIC=128 μg/ml), MRSA PS-106 (MIC=128 μg/ml), MRSA PS-131 (MIC=64 μg/ml), MRSA PS-139 (MIC=64 μg/ml), MRSA PS-162 (MIC=64 μg/ml), MRSA PS-165 (MIC=32 μg/ml), Staphylococcus aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=256 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli ATCC 51446 (MIC=16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=32 μg/ml), Klebsiella pneumoniae ATCC 13883 (MIC=4 μg/ml) [Ref.29392557] 5% haemolysis at 1.0 μg/ml, 5% haemolysis at 2.0 μg/ml, 5% haemolysis at 4.0 μg/ml, 5% haemolysis at 8.0 μg/ml, 7% haemolysis at 16.0 μg/ml, 9% haemolysis at 31.2 μg/ml, 13% haemolysis at 62.5 μg/ml, 17% haemolysis at 125.0 μg/ml, 19% haemolysis at 250.0 μg/ml, 23% haemolysis at 500.0 μg/ml, 24% haemolysis at 1000.0 μg/ml against human red blood cells Linear Free Free L [Ref.29392557] The cell viability of HUVEC at the peptide concentration of 35.5 μg/ml, 71 μg/ml and 113 μg/ml is 127%, 100% and 76%. ##The cell viability of H9c2 at the peptide concentration of 35.5, 71, and 113 μg/ml is 132, 100, and 80%. Not found 29392557 J Microbiol. 2018 Feb;56(2):128-137. Tajbakhsh M, Karimi A, Tohidpour A, Abbasi N, Fallah F, Akhavan MM. The antimicrobial potential of a new derivative of cathelicidin from Bungarus fasciatus against methicillin-resistant Staphylococcus aureus. DRAMP20778 FFFLSRIF 8 Temporin-SHf (frogs,amphibians,animals) No entry found Belongs to the Temporin family Not found Pelophylax saharica(Sahara frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Once bound parallel to the microbial membrane surface, it folds into a non-amphipathic hydrophobic Function: Antibacterial activity against the Gram-negative bacteria (Escherichia coli ATCC 25922, Escherichia coli ATCC 35218, Escherichia coli D21, Escherichia coli ML-35p, Pseudomonas aeruginosa ATCC 27853) and Gram-positive bacteria (Staphylococcus aureus ATCC 25923, E. faecalis ATCC 29212, Bacillus megaterium. Antifungal activity) [Ref.20308076] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=25 μM); Escherichia coli ATCC 35218(MIC>200 μM); Escherichia coli D21(MIC=100 μM); Escherichia coli ML-35p(MIC=30 μM); Pseudomonas aeruginosa ATCC 27853(MIC>200 μM);## Gram-positive bacteria: Staphylococcus aureus ATCC 25923(MIC=12.5 μM); E. faecalis ATCC 29212(MIC=50 μM); Bacillus megaterium(MIC=3 μM);## Yeasts: Candida albicans ATCC 90028(MIC=50 μM); C. parapsilosis ATCC 22019(MIC=50 μM); S. cerevisiae(MIC=12.5 μM);## Fungus(MIC>200 μM) [Ref.20308076] Temporin-SHf is not cytotoxic against human erythrocytes (LC50 = 200 μm), with a hemolytic activity detected only at peptide concentration far above the MIC values determined for the sensitive strains (3–50 μm) Linear Free Amidation L [Ref.20308076] No cytotoxicity information found Not found 20308076 J Biol Chem. 2010 May 28;285(22):16880-92. Abbassi F, Lequin O, Piesse C, Goasdou Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide. DRAMP20779 GMWSKILGHLIR 12 Halictine 1 (bees,insects,animals) No entry found Not found Not found Halictus sexcinctus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Exhibits potent antimicrobial activity against the Gram-positive and Gram-negative bacteria as well as noticeable hemolytic activity. [Ref.20198492] Gram-negative bacteria: Escherichia coli(MIC=3.8 μM), Pseudomonas aeruginosa(MIC=45.0 μM);## Gram-positive bacteria: Bacillus subtilis(MIC=0.8 μM), Staphylococcus aureus(MIC=7.7 μM) [Ref.20198492] LC50=82μM against rat red blood cells Linear Free Amidation L [Ref.20198492] No cytotoxicity information found Not found 20198492 Amino Acids. 2010 Aug;39(3):763-75. Monincová L, Budesínskμ M, Slaninová J, Hovorka O, Cvacka J, Voburka Z, Fucík V, Borovicková L, Bednárová L, Straka J, Cerovskμ V. Novel antimicrobial peptides from the venom of the eusocial bee Halictus sexcinctus (Hymenoptera: Halictidae) and their analogs. DRAMP20780 GKWMSLLKHILK 12 Halictine 2 (bees,insects,animals) No entry found Not found Not found Halictus sexcinctus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Exhibits potent antimicrobial activity against the Gram-positive and Gram-negative bacteria as well as noticeable hemolytic activity. [Ref.20198492] Gram-negative bacteria: Escherichia coli(MIC=2.5μM), Pseudomonas aeruginosa(MIC=42.1);## Gram-positive bacteria: Bacillus subtilis(MIC=1.0μM), Staphylococcus aureus(MIC=8.1μM) [Ref.20198492] LC50=78.1μM against rat red blood cells Linear Free Amidation L [Ref.20198492] No cytotoxicity information found Not found 20198492 Amino Acids. 2010 Aug;39(3):763-75. Monincová L, Budesínskμ M, Slaninová J, Hovorka O, Cvacka J, Voburka Z, Fucík V, Borovicková L, Bednárová L, Straka J, Cerovskμ V. Novel antimicrobial peptides from the venom of the eusocial bee Halictus sexcinctus (Hymenoptera: Halictidae) and their analogs. DRAMP20781 LNWGAILKHIIK 12 Panurgine 1(bees,insects,animals) C0HL84 Not found Not found Panurgus calcaratus(communal bee) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria, antifungal activity, and low hemolytic activity against human erythrocytes. [Ref.23483218] Gram-negative bacteria: Escherichia coli(MIC=3.7μM), Pseudomonas aeruginosa(MIC=51.7μM) ;## Gram-positive bacteria: Micrococcus luteus(MIC=1.5μM), Bacillus subtilis(MIC=1.3μM), Staphylococcus aureus(MIC=10.6μM) ;## Yeast: Candida albicans(MIC=7.3μM) [Ref.23483218] LC50=119μM against rat red blood cells Linear Free Amidation L [Ref.23483218] No cytotoxicity information found Not found 23483218 Amino Acids. 2013 Jul;45(1):143-57. Čujová S, Slaninová J, Monincová L, Fuμík V, Bednárová L, μtokrová J, Hovorka O, Voburka Z, Straka J, μeμovskμ V. Panurgines, novel antimicrobial peptides from the venom of communal bee Panurgus calcaratus (Hymenoptera: Andrenidae). DRAMP20782 FLSGILKLAFKIPSVLCAVLKNC 23 Pleurain-D1 (Frogs,amphibians,animals) B5L1C5, B5L1D1, B5L1C3, B5L1C9, B5L1C2, B5L1D4 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Nidirana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675] Gram-negative bacteria: Escherichia coli (MIC=25 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 μg/ml), Bacillus subtilis (MIC=50 μg/ml);##Yeast: Candida albicans(MIC=25 μg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.19028675] No cytotoxicity information found Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP20783 GLLDSVKEGLKKVAGQLLDTLKCKISGCTPA 31 Pleurain-M1 (Frogs,amphibians,animals) B5L1L3 Belongs to the frog skin active peptide (FSAP) family. Pleurain subfamily. Not found Nidirana pleuraden (Yunnan pond frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria and fungi. [Ref.19028675] Gram-negative bacteria: Escherichia coli (MIC=6.3 μg/ml);##Gram-positive bacteria: Staphylococcus aureus (MIC=6.3 μg/ml), Bacillus subtilis (MIC=25 μg/ml);##Yeast: Candida albicans(MIC=12.5 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.19028675] No cytotoxicity information found Not found 19028675 Mol Cell Proteomics. 2009 Mar;8(3):571-83. Yang H, Wang X, Liu X, Wu J, Liu C, Gong W, Zhao Z, Hong J, Lin D, Wang Y, Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. DRAMP20784 FLKGCWTKWYSLKPKCPF 18 Megin 1 No entry found Not found Not found Amphibian skin Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found The peptide contains an intra-molecular di-sulfide bridge Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27114317] Gram-negative bacteria: Escherichia coli (ATCC 25922)(MIC=25μg/mL);B. dysenteriae(MIC=3μg/mL);##Gram-positive bacteria:Staphylococcus aureus (ATCC 2592)(MIC=6.25μg/mL);Bacillus subtilis (ATCC 6633)(MIC=3μg/mL) ;##Fungi:C.albicans (ATCC 2002)(MIC=50μg/mL) [Ref.27114317] Human red blood cells: 2.3% hemolysis at 25μg/ml; 5.6% hemolysis at 50μg/ml; 18.7% hemolysis at 100μg/ml; 29.5% hemolysis at 200μg/ml. Rabbit red blood cells :3.1% hemolysis at 25μg/ml; 7.3% hemolysis at 50μg/ml; 20.5% hemolysis at 100μg/ml; 32.9% hemolysis at 200μg/ml Cyclic Free Amidation Disulfide bond between Cys5 and Cys16 L No cytotoxicity information found Not found 27114317 Chin J Nat Med. 2016 Apr;14(4):294-298. Yang HL, Shen ZQ, Liu X, Kong Y. Two novel antimicrobial peptides from skin venoms of spadefoot toad Megophrys minor. DRAMP20785 FFVLKFLLKWAGKVGLEHLACKFKNWC 27 Megin 2 No entry found Not found Not found Amphibian skin Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found The peptide contains an intra-molecular di-sulfide bridge Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27114317] Gram-negative bacteria: Escherichia coli (ATCC 25922)(MIC=6.25μg/mL);B. dysenteriae(MIC=1.5μg/mL);##Gram-positive bacteria:Staphylococcus aureus (ATCC 2592)(MIC=12.5μg/mL);Bacillus subtilis (ATCC 6633)(MIC=1.5μg/mL) ;##Fungi:C.albicans (ATCC 2002)(MIC=12.5μg/mL) [Ref.27114317] Human red blood cells: 3.9% hemolysis at 25μg/ml; 13.7% hemolysis at 50μg/ml; 27.7% hemolysis at 100μg/ml; 45.3% hemolysis at 200μg/ml;Rabbit red blood cells: 5.6% hemolysis at 25μg/ml; 15.2% hemolysis at 50μg/ml; 36.2% hemolysis at 100μg/ml; 50.3% hemolysis at 200 μg/ml Cyclic Free Free Disulfide bond between Cys21 and Cys27. L No cytotoxicity information found Not found 27114317 Chin J Nat Med. 2016 Apr;14(4):294-298. Yang HL, Shen ZQ, Liu X, Kong Y. Two novel antimicrobial peptides from skin venoms of spadefoot toad Megophrys minor. DRAMP20786 RRLRPRRPRLPRPRPRPRPRPR 22 mini-ChBac7.5N alpha No entry found Not found Not found Capra hircus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27795854] Gram-negative bacteria: E.coli (ML35p)(MIC=0.3 ± 0.1μM without NaCl;MIC=1.5 ± 0.2μM 100 mM NaCl;MIC=1μM Broth microdilution assay);E.coli (ATCC 25922)(MIC=0.6 ± 0.1μM without NaCl;MIC=0.9 ± 0.2μM 100 mM NaCl;MIC=2μM Broth microdilution assay);E.coli (M17)(MIC=0.5 ± 0.1μM without NaCl;MIC=0.8 ± 0.1μM 100 mM NaCl;MIC=2μM Broth microdilution assay);Pseudomonas aeruginosa (ATCC 27853)(MIC=1.1 ± 0.4μM without NaCl;MIC=3.7 ± 1.2μM 100 mM NaCl;MIC=2μM Broth microdilution assay);Pseudomonas aeruginosa clinical isolate(MIC=2μM Broth microdilution assay);Klebsiella spp. clinical isolate(MIC=4μM Broth microdilution assay);Acinetobacter baumannii clinical isolate(MIC=2μM Broth microdilution assay);##Gram-positive bacteria:Listeria monocytogenes (EGD)(MIC=0.2 ± 0.1μM without NaCl;MIC=1.0 ± 0.2μM 100 mM NaCl;MIC=2μM Broth microdilution assay);Micrococcus luteus CIP A270(MIC=1μM Broth microdilution assay);Staphylococcus aureus (710A)(MIC=0.7 ± 0.2μM without NaCl;MIC> 50μM 100 mM NaCl;MIC>64μM Broth microdilution assay);Staphylococcus aureus (ATCC 25923)(MIC>64μM Broth microdilution assay);MRSA (ATCC 33591)(MIC=0.7 ± 0.2μM without NaCl;MIC> 50μM 100 mM NaCl;MIC>64μM Broth microdilution assay);Staphylococcus intermedius clin. isolate(MIC>64μM Broth microdilution assay);##Fungi:Candida albicans (820)(MIC=0.3 ± 0.1μM without NaCl;MIC> 50μM 100 mM NaCl;MIC=64μM Broth microdilution assay);Candida parapsilosis clinical isolate(MIC>64μM Broth microdilution assay) [Ref.27818338] No hemolytic activity Linear Free Free L [Ref.27795854] The cytotoxicity values of the experimental samples are not significantly different from the values of the control samples over the entire range of concentrations:1-30 μM against various types of cultured human cells: namly, reythroleukemi Not found 27795854 Acta Naturae. 2016 Jul-Sep;8(3):136-146. Shamova OV, Orlov DS, Zharkova MS, Balandin SV, Yamschikova EV, Knappe D, Hoffmann R, Kokryakov VN, Ovchinnikova TV. Minibactenecins ChBac7.N DRAMP20787 RRLRPRRPRLPRPRPRPRPRP 21 mini-ChBac7.5N beta No entry found Not found Not found Capra hircus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27795854] Gram-negative bacteria:E.coli (ML35p)(MIC=0.3 ± 0.1μM without NaCl;MIC=1.4 ± 0.2μM 100 mM NaCl;MIC=1μM Broth microdilution assay);E.coli (ATCC 25922)(MIC=0.5 ± 0.2μM without NaCl;MIC=0.8 ± 0.2μM 100 mM NaCl;MIC=2μM Broth microdilution assay);E.coli (M17)(MIC=0.5 ± 0.1μM without NaCl;MIC=0.9 ± 0.2μM 100 mM NaCl;MIC=1μM Broth microdilution assay);Pseudomonas aeruginosa (ATCC 27853)(MIC=1.0 ± 0.3μM without NaCl;MIC=3.2 ± 0.8μM 100 mM NaCl;MIC=2μM Broth microdilution assay);Pseudomonas aeruginosa clinical isolate(MIC=2μM Broth microdilution assay);Klebsiella spp. clinical isolate(MIC=4μM Broth microdilution assay);Acinetobacter baumannii clinical isolate(MIC=4μM Broth microdilution assay);##Gram-positive bacteria:Listeria monocytogenes (EGD)(MIC=0.2 ± 0.1μM without NaCl;MIC=0.9 ± 0.2μM 100 mM NaCl;MIC=2μM Broth microdilution assay);Micrococcus luteus CIP A270(MIC=1μM Broth microdilution assay);Staphylococcus aureus (710A)(MIC=0.6 ± 0.1μM without NaCl;MIC> 50μM 100 mM NaCl;MIC>64μM Broth microdilution assay);Staphylococcus aureus (ATCC 25923)(MIC>64μM Broth microdilution assay);MRSA (ATCC 33591)(MIC=0.5 ± 0.1μM without NaCl;MIC> 50μM 100 mM NaCl;MIC>64μM Broth microdilution assay);Staphylococcus intermedius clin. isolate(MIC>64μM Broth microdilution assay);##Fungi:Candida albicans (820)(MIC=0.3 ± 0.1μM without NaCl;MIC> 50μM 100 mM NaCl;MIC=64μM Broth microdilution assay);Candida parapsilosis clinical isolate(MIC>64μM Broth microdilution assay) [Ref.27818338] No hemolytic activity Linear Free Free L [Ref.27795854] The cytotoxicity values of the experimental samples are not significantly different from the values of the control samples over the entire range of concentrations:1-30 μM against various types of cultured human cells: namly, reythroleukemi Not found 27795854 Acta Naturae. 2016 Jul-Sep;8(3):136-146. Shamova OV, Orlov DS, Zharkova MS, Balandin SV, Yamschikova EV, Knappe D, Hoffmann R, Kokryakov VN, Ovchinnikova TV. Minibactenecins ChBac7.N DRAMP20788 QGVRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKCCRSW 42 Bovine neutrophil Beta-defensin 3 (BNBD-3; cattle, ruminant, mammals; animals) P46161 Belongs to the beta-defensin family DEFB3 Bos taurus (Bovine) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Antibacterial against Escherichia coli ML35 and Staphylococcus aureus 502A. Tissue specificity: Neutrophilic granules." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a N-terminal glutamine Free Disulfide bonds between Cys24 and Cys53, Cys31 and Cys46, Cys36 and Cys54 L No cytotoxicity information found Not found 8454635 J. Biol. Chem. 1993; 268:6641-6648. Selsted ME, Tang Y-Q, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP20789 GPLSCGRNGGVCIPIRCPVPNRQIGTCFGRPVKCCRSW 38 Bovine neutrophil Beta-defensin 12 (BNBD-12; cattle, ruminant, mammals; animals) P46170 Belongs to the beta-defensin family DEFB12 Bos taurus (Bovine) Antimicrobial, Antibacterial Protein level Bridge Not found 1BNB resolved by NMR "Function: Antibacterial against Escherichia coli ML35 and Staphylococcus aureus 511A. Tissue specificity: Neutrophilic granules." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys5 and Cys34, Cys12 and Cys27, Cys17 and Cys35 L No cytotoxicity information found Not found 8454635 J. Biol. Chem. 1993; 268:6641-6648. Selsted ME, Tang Y-Q, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. DRAMP20790 KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKALG 36 Cecropin B (Insects, arthropods, invertebrates, animals) P01508 Belongs to the cecropin family. Not found Hyalophora cecropia (Cecropia moth) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against several Gram-positive and Gram-negative bacteria. [Ref.7019715] Gram-positive bacteria: Bacillus megaterium Bm11 (Inhibition zone=10.0 mm), Bacillus subtilis (Inhibition zone=7.2 mm);##Gram-negative bacteria: Escherichia coli K12 D31 (Inhibition zone=12.5 mm), Serratia marcescens Db1108 (Inhibition zone=7.2 mm), Pseudomonas aeruginosa OT97 (Inhibition zone=9.7 mm), Xenorhabdus nematophilus Xn21 (Inhibition zone=10.0 mm). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation (Leu35) PMID:3857578 L [Ref.7019715] No cytotoxicity information found Not found 7019715 Nature. 1981 Jul 16;292(5820):246-8. Steiner H, Hultmark D, Engstr?m A, Bennich H, Boman HG. Sequence and specificity of two antibacterial proteins involved in insect immunity DRAMP20791 GGLKKLGKKLEGVGKRVFKASEKALPVAVGIKALGK 36 Cecropin A1 (insects, arthropods, invertebrates, animals) P81417 Not found CECA1 Aedes albopictus (Asian tiger mosquito) Antimicrobial, Antibacterial Protein level Alpha helix Not found Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.9712710] No cytotoxicity information found Not found 9712710 Biochem. Biophys. Res. Commun. 1998 Aug; 249(2):410-415. Sun D, Eccleston ER, Fallon AM. Peptide sequence of an antibiotic cecropin from the vector mosquito, Aedes albopictus. DRAMP20792 GLFVGVLAKVAAHVVPAIAEHF 22 Maculatin 1.1 (Frog, amphibians, animals) P82066 Not found Not found Litoria genimaculata (Green-eyed tree frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Helix Not found 2MMJ resolved by NMR "Function: Maculatin-1.1 shows significant antibacterial activity against Gram-positive bacteria, less against Gram-negative bacteria. Maculatin-1.1.1 is inactive. Tissue specificity: Expressed by the skin dorsal glands." [Ref.9620615] Gram positive bacteria: Bacillus cereus (MIC=50 μg/ml), Leuconostoc lactis (MIC=25 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=12.5 μg/ml), Staphylococcus aureus (MIC=6-12.5 μg/ml), Staphylococcus epidermidis (MIC=12.5 μg/ml), Streptococcus faecalis (MIC=25 μg/ml), Streptococcus uberis (MIC=3 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=100 μg/ml), Pasteurella multocida (MIC=100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.9620615] No cytotoxicity information found Not found 9620615 J. Pept. Sci. 1998 Apr; 4(2): 111-115. Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC. The maculatin peptide from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1 DRAMP20793 GLFVGLAKVAAHNNPAIAEHFQA 23 Maculatin 1.2 (Frog, amphibians, animals) P82067 Not found Not found Litoria genimaculata (Green-eyed tree frog) Antimicrobial, Antibacterial, Anti-Gram+ Not found Helix Not found "Function: Antibacterial activity against Staphylococcus aureus and Streptococcus uberis. Tissue specificity: Expressed by the skin dorsal glands." [Ref.9620615] Gram positive bacteria: Staphylococcus aureus (MIC=50 μg/ml), Streptococcus uberis (MIC=6 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.9620615] No cytotoxicity information found Not found 9620615 J. Pept. Sci. 1998 Apr; 4(2): 111-115. Rozek T, Waugh RJ, Steinborner ST, Bowie JH, Tyler MJ, Wallace JC. The maculatin peptide from the skin glands of the tree frog Litoria genimaculata. A comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1 DRAMP20794 LFCKRGTCHFGRCPSHLIKV 20 Turkey Heterophil Peptide 2 (THP-2; avian beta-defensin, birds, animals) P80392 Belongs to the beta-defensin family. Not found Meleagris gallopavo (Wild turkey) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Antibacterial activity against the Gram-positive bacterium Staphylococcus aureus. Lacks antibacterial activity against the Gram-negative bacterium Escherichia coli K-12. Tissue specificity: Expressed in circulating heterophil granulocytes and bone marrow (at protein level)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.7964174] No cytotoxicity information found Not found 7964174 J. Leukoc. Biol. 1994 Nov; 56: 661-665. Evans EW, Beach GG, Wunderlich J, Harmon BG. Isolation of antimicrobial peptides from avian heterophils. DRAMP20795 XTCESPSHKFKGPCATNRNCES 22 So-D1 (S. oleracea defensin 1; spinach defensins, plants) P81572 Belongs to the DEFL family. Group II subfamily. Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial Protein level Bridge Not found Function: Antimicrobial peptide. Active against Gram-positive and Gram-negative bacteria pathogens. [Ref.9762899] Gram-positive bacterium: Clavibacter michiganensis (EC50=1 μM);##Gram-negative bacterium: Ralstonia solanacearum (EC50=15 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.9762899] No cytotoxicity information found Not found 9762899 FEBS Lett. 1998 Sep 18;435(2-3): 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP20796 GIFSNMYXRTPAGYFRGPXGYXXN 24 So-D6 (S. oleracea defensin 6, spinach defensins; plants) P81567 Belongs to the DEFL family. Group II subfamily. Not found Spinacia oleracea (Spinach) Antimicrobial, Antibacterial Protein level Bridge Not found "Function: Antimicrobial activity against Fungi, Gram-positive and Gram-negative bacteria. Tissue specificity: Distributed in the epidermal cell layer of leaves and in the subepidermal layer region of stems. Not in roots. Developmental stage: Present throughout the life of the leaf." [Ref.9762899] Gram-positive bacterium: Clavibacter michiganensis (EC50=1 μM);##Gram-negative bacterium: Ralstonia solanacearum (EC50=6 μM);##Fusarium solani (EC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.9762899] No cytotoxicity information found Not found 9762899 FEBS Lett. 1998 Sep 18;435(2-3): 159-162. Segura A, Moreno M, Molina A, Garcia-Olmedo F Novel defensin subfamily from spinach (Spinacia oleracea). DRAMP20797 GVIDAAKKVVNVLKNLF 17 Uperin 3.6 (Toad, amphibians, animals) P82043 Belongs to the frog skin active peptide (FSAP) family. Uperin subfamily. Not found Uperoleia mjobergii (Australian toadlet) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found "Function: Antibacterial activity against B.cereus, L.lactis, L.innocua, M.luteus, S.aureus, S.epidermidis and S.uberis. Tissue specificity: Expressed by the skin dorsal glands. Mass spectrometry: Molecular mass is 1826 Da from positions 1 - 17. Determined by FAB." [Ref.10461748] Gram positive bacteria: Bacillus cereus (MIC=25 μg/ml), Leuconostoc lactis (MIC=3 μg/ml), Listeria innocua (MIC=50 μg/ml), Micrococcus luteus (MIC=50 μg/ml), Staphylococcus aureus (MIC=25 μg/ml), Staphylococcus epidermidis (MIC=12 μg/ml), Streptococcus uberis (MIC=12 μg/ml);##Gram-negative bacterium: Pasteurella haemolytica (MIC=25 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.10461748] No cytotoxicity information found Not found 10461748 J Pept Res. 1999 Aug;54(2):137-45. Chia BC, Carver JA, Mulhern TD, Bowie JH The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii. DRAMP20798 QGVRNSQSCRRNKGICVPIRCPGSMRQIGTCLGAQVKCCRRK 42 Lingual antimicrobial peptide (LAP, beta defensin, cattle, ruminant, animals) Q28880 Belongs to the beta-defensin family. LAP/TAP subfamily. LAP Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Bridge Not found "Function: Shows a broad spectrum of antibacterial and antifungal activities. Tissue specificity: In many of the exposed epithelial surfaces including conjunctivae, bronchi, colon, urinary tract and trachea. Developmental stage: Not found in fetus." [Ref.7886453] Gram-positive bacterium: Staphylococcus aureus 29213 (MIC=63-125 μg/ml);##Gram-negative bacteria: Escherichia coli D31 (MIC=16-32 μg/ml), Pseudomonas aeruginosa 27853 (MIC=63-125 μg/ml);##Fungi: Candida albicans 14053 (MIC=32-63 μg/ml), Candida tropicalis 13803 (MIC=16-32 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys9 and Cys38, Cys16 and Cys31, Cys21 and Cys39. L [Ref.7886453] No cytotoxicity information found Not found 7886453 Science. 1995 Mar 17; 267(5204):1645-1648 Schonwetter BS., Stolzenberg ED., Zasloff MA. Epithelial antibiotics induced at sites of inflammation. DRAMP20799 GCWSTVLGGLKKFAKGGLEAIVNPK 25 XT-2 (frog, amphibians, animals) No entry found Belongs to the Pipidae family. Not found Xenopus tropicalis (Diploid clawed frog, Africa) Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix Not found Function: Antibacterial activity against the Gram-negative bacteria (Escherichia coli). [Ref.11738090] Gram-negative bacteria: Escherichia coli (MIC=8μM). [Ref.11738090] HC50 is not determined against human red blood cells. Linear Free Free L [Ref.11738090] No cytotoxicity information found Not found 11738090 Biochim Biophys Acta 2001 Nov 26;1550(1):81-9. Ali MF, Soto A, Knoop FC, Conlon JM. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). DRAMP20800 KKKKPLFGLFFGLF 14 the K4 peptide (synthetic; Phe-rich >25%) No entry found Not found Not found the APD database-aided design. Antimicrobial, Antibacterial, Anti-Gram- Not found Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Have Hemolytic activity against rabbit erythrocytes. Have Cytotoxicity activity on CHO-K1 cells, the peptide is slightly cytotoxic at 160 [Ref.19573572] Gram-negative bacteria: Escherichia coli (MIC=40-80 μg/ml or 24-48 μM), Vibrio alginolyticus (MIC=10-20 μg/ml or 6-12 μM), Vibrio harveyi (MIC=5-10 μg/ml or 3-6 μM). [Ref.19573572] No significant hemolytic activity is observed at 10 and 40 μg/ml. Slight hemolysis (6.65%) is shown at 160 μg/ml. Linear Free Free L [Ref.19573572] The cell viability of CHO-K1 cells is 127%, 123%,78% and 10% at peptide concentrations of 10 μg/ml, 40 μg/ml, 160 μg/ml and 640 μg/ml Not found 19573572 Peptides. 2009 Sep;30(9):1608-12 Duval E, Zatylny C, Laurencin M, Baudy-Floc'h M, Henry J. KKKKPLFGLFFGLF: a cationic peptide designed to exert antibacterial activity DRAMP20801 GFGCPNNYQCHRHCKSIPGRCGGYCGGWHRLPCTCYRC 38 Mussel Defensin MGD-1 (Mediterranean mussel defensin 1; mollusca/molluscs/mollusks, invertebrates, animals) P80571 Belongs to the invertebrate defensin family. Type 2 subfamily. FH3 Mytilus galloprovincialis (Mediterranean mussel) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Combine Helix and Beta structure The signature of MGD-1 is that of the arthropod defensins which range in length from 34 to 51 amino acid residues with 6 conserved cysteines engaged in three intramolecular disulfide bridges. They are characterized by the presence of a flexible amino-terminal loop, a central amphipathic 1FJN resolved by NMR Function: Active against both Gram-positive and Gram-negative bacteria but is not cytotoxic towards human erythrocytes or protozoa. [Ref.8925841] Gram-positive bacteria: Micrococcus luteus (MIC=0.08 μg/ml);##Gram-negative bacteria: Escherichia coli (MIC=6.4 μg/ml), Vibrio alginolyticus (MIC=6.4 μg/ml), Vibrio splendidus (MIC=1.6 μg/ml), Vibrio P1 (MIC=6.4 μg/ml). [Ref.8925841] The plasma is capable of causing 20% of the total hemolysis. Cyclic Free Amidation Disulfide bonds between Cys4 and Cys25, Cys10 and Cys33, Cys14 and Cys35, Cys21 and Cys38. Hydroxylation of Trp28 (3hydroxytryptophan) L [Ref.8925841] The protozoan P. marinus is not killed by pure peptide, even at a concentration of 16 μg/ml. Cell membranes 8925841 Eur J Biochem. 1996 Aug 15;240(1):302-6. Hubert F, Noel T, Roch P. A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis) DRAMP20802 GLGSVLGKALKIGANLL 17 CPF-AM1 (caerulein precursor fragment-AM1, frogs, amphibians, animals) No entry found Belongs to the CPF family. Not found Xenopus amieti (skin secretions, Africa) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.20226221] Gram-positive bacteria: Staphylococcus aureus (MIC>200μM) ;##Gram-negative bacteria: Escherichia coli (MIC>200μM). [Ref.20226221] LC50>200μM against human red blood cells Linear Free Amidation L [Ref.20226221] No cytotoxicity information found Cell membranes 20226221 Peptides. 2010 Jun;31(6):989-94. Conlon JM, Al-Ghaferi N, Ahmed E, Meetani MA, Leprince J, Nielsen PF. Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae). DRAMP20803 FFRNLWKGAKAAFRAGHAAWRA 22 moronecidin-like peptide No entry found Not found Not found Hippocampus comes Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix The peptide is Schiffer Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria; antifungal activity. [Ref.30039186] Gram-positive bacteria:Staphylococcus aureus ATCC 25923 (MIC=3.12 μg/ml),Staphylococcus epidermidis ATCC 1435 (MIC=1.56 μg/ml),Staphylococcus aureus MRSA (MIC=3.12 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.25 μg/ml), Pseudomonas aeruginosa ATCC10662 (MIC=50 μg/ml),Acinetobacter baumannii clinical isolate (MIC=6.25 μg/ml);##Fungi:Candida albicans clinical isolate (MIC=6.25 μg/ml), Candida tropicalis clinical isolate (MIC=6.25 μg/ml) [Ref.30039186] 50% hemolysis at 87.5μg/ml,25% hemolysis at 50μg/ml,60% hemolysis at 100μg/ml against human red cells Linear Free Amidation L [Ref.30039186] No cytotoxicity information found Not found 30039186 Mar Biotechnol (NY). 2018 Dec;20(6):718-728. Mohammadi M, Taheri B, Momenzadeh N, Salarinia R, Nabipour I, Farshadzadeh Z, Bargahi A. Identification and Characterization of Novel Antimicrobial Peptide from Hippocampus comes by In Silico and Experimental Studies DRAMP20804 DLRDSWKVIGSDKK 14 AI-hemocidins 2 (Hb-1 truncated peptide) No entry found Belongs to truncated Hb-1 Not found Arca inflata Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil Peptides displayed random coil conformations in PBS, the spectra of AI-hemocidin 2 featured an Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria. [Ref.28661457] Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=45.54 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=91.08 μM), Pseudomonas aeruginosa clinical isolate (MIC=91.08 μM);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=22.77 μM), Bacillus subtilis ATCC 6633 (MIC=182.16 μM). [Ref.28661457] 10.27 ± 0.42% hemolysis at 500 μg/mL against murine red blood cells. Linear Free Free L [Ref.28661457] The cell viability of HEK293 at the peptide concentration of 250 μg/ml is 88.18±9.48%. IC50 > 1000 μg/ml against HEK293 cells. Not found 28661457 Mar Drugs. 2017 Jun 29;15(7). Li C, Zhu J, Wang Y, Chen Y, Song L, Zheng W, Li J, Yu R. Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata DRAMP20805 FSTKTRNWFSEHFKKVKEKLKDTFA 25 Apo5 APOC164-88 No entry found Not found Not found American alligator Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix,beta-sheet,beta-turn,random coil Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.27542832] Gram-positive bacteria:Staphylococcus aureus ATCC BAA-1718 (EC50=4.96μg/ml), Staphylococcus aureus ATCC 33592 (EC50=0.0680μg/ml);##Gram-negative bacteria:Escherichia coli ATCC 4157 (EC50=19.7μg/ml), Escherichia coli ATCC 51659 (EC50=13.9μg/ml), Pseudomonas aeruginosa PAO1 (EC50=0.0878μg/ml), Pseudomonas aeruginosa ATCC BAA-2110 (EC50=0.467μg/ml), Acinetobacter baumannii ATCC 9955 (EC50=0.644μg/ml), Acinetobacter baumannii ATCC BAA-1794 (EC50=0.234μg/ml) [Ref.27542832] Not hemolytic to sheep red blood cells. Linear Free Free L [Ref.27542832] The cell proliferation of A549 human lung epithelial cells is 175%, 170%, 145%, 173% and 120% at peptide concentrations of 1 μg/ml, 10 μg/ml, 25 μg/ml, 50 μg/ml, 100 μg/ml Not found 27542832 BMC Microbiol. 2016 Aug 19;16(1):189. Barksdale SM, Hrifko EJ, Chung EM, van Hoek ML. Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii DRAMP20806 KTRNWFSEHFKKVKEKLKDTFA 22 Apo6 APOC167-88 No entry found Not found Not found American alligator Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix,beta-sheet,beta-turn,random coil Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.27542832] Gram-positive bacteria:Staphylococcus aureus ATCC BAA-1718 (EC50=2.31μg/ml), Staphylococcus aureus ATCC 33592 (EC50=0.883μg/ml);##Gram-negative bacteria:Escherichia coli ATCC 4157 (EC50=3.85μg/ml), Escherichia coli ATCC 51659 (EC50=9.07μg/ml), Pseudomonas aeruginosa PAO1 (EC50=1.17μg/ml), Pseudomonas aeruginosa ATCC BAA-2110 (EC50=0.130μg/ml), Acinetobacter baumannii ATCC 9955 (EC50=0.233μg/ml), Acinetobacter baumannii ATCC BAA-1794 (EC50=0.126μg/ml) [Ref.27542832] Not hemolytic to sheep red blood cells. Linear Free Free L [Ref.27542832] The cell proliferation of A549 human lung epithelial cells is 190%, 167%, 150%, 135% and 144% at peptide concentrations of 1 μg/ml, 10 μg/ml, 25 μg/ml, 50 μg/ml, 100 μg/ml Not found 27542832 BMC Microbiol. 2016 Aug 19;16(1):189. Barksdale SM, Hrifko EJ, Chung EM, van Hoek ML. Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii DRAMP20807 PPPVIKFNRPFLMWIVERDTRSILFMGKIVNPKAP 35 A1P394-428 No entry found Not found Not found American alligator Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Alpha helix,beta-sheet,beta-turn,random coil A1P is primarily random coil with two anti-parallel Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.27542832] Gram-positive bacteria:Staphylococcus aureus ATCC BAA-1718 (EC50=36.5μg/ml), Staphylococcus aureus ATCC 33592 (EC50=2.68μg/ml);##Gram-negative bacteria:Escherichia coli ATCC 4157 (EC50=9.2μg/ml), Escherichia coli ATCC 51659 (EC50=2.51μg/ml), Pseudomonas aeruginosa PAO1 (EC50=38.6μg/ml), Acinetobacter baumannii ATCC 9955 (EC50=24.0μg/ml), Acinetobacter baumannii ATCC BAA-1794 (EC50=2.36μg/ml) [Ref.27542832] Not hemolytic to sheep red blood cells. Linear Free Free L [Ref.27542832] The cell proliferation of A549 human lung epithelial cells is 170%, 180%, 182%, 180% and 180% at peptide concentrations of 1 μg/ml, 10 μg/ml, 25 μg/ml, 50 μg/ml, 100 μg/ml Not found 27542832 BMC Microbiol. 2016 Aug 19;16(1):189. Barksdale SM, Hrifko EJ, Chung EM, van Hoek ML. Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii DRAMP20808 RRLRKKTRKRLKKIGKVLKWI 21 RI21 (PMAP-36 peptide derivative) No entry found Derived from PMAP-36 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and Fungi.. [Ref.27251456] Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=4 μM, MBC=4 μM), Staphylococcus aureus 25923 (MIC=4 μM, MBC=4 μM), Staphylococcus epidermidis 12228 (MIC=4 μM, MBC=8 μM), Bacillus subtilis 63501 (MIC=1 μM, MBC=4 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=2 μM, MBC=8 μM), Escherichia coli EC183 (MIC=1 μM, MBC=2 μM), Escherichia coli 1005 (MIC=2 μM, MBC=2 μM), Salmonella typhimurium C77-31 (MIC=1 μM, MBC=2 μM);##Fungi: Candida albicans 2.2086 (MIC=8 μM, MFC=16 μM), Candida albicans CA276 (MIC=8 μM, MFC=32 μM), Candida tropicalis 2.1975 (MIC=1 μM, MFC=2 μM), Candida krusei 2.1857 (MIC=2 μM, MFC=4 μM). [Ref.27251456] 5% hemolysis at 32 μM, MHC=32 μM against human red blood cells. Linear Free Amidation L [Ref.27251456] No cytotoxicity information found Not found 27251456 Sci Rep. 2016 Jun 2;6:27258. Lyu Y, Yang Y, Lyu X, Dong N, Shan A. Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. DRAMP20809 RKKTRKRLKKIGKVLKWI 18 RI18 (PMAP-36 peptide derivative) No entry found Derived from PMAP-36 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and Fungi.. [Ref.27251456] Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=4 μM, MBC=4 μM), Staphylococcus aureus 25923 (MIC=8 μM, MBC=8 μM), Staphylococcus epidermidis 12228 (MIC=4 μM, MBC=16 μM), Bacillus subtilis 63501 (MIC=1 μM, MBC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=2 μM, MBC=4 μM), Escherichia coli EC183 (MIC=1 μM, MBC=2 μM), Escherichia coli 1005 (MIC=2 μM, MBC=4 μM), Salmonella typhimurium C77-31 (MIC=2 μM, MBC=4 μM);##Fungi: Candida albicans 2.2086 (MIC=16 μM, MFC=32 μM), Candida albicans CA276 (MIC=8 μM, MFC=16 μM), Candida tropicalis 2.1975 (MIC=2 μM, MFC=4 μM), Candida krusei 2.1857 (MIC=4 μM, MFC=8 μM). [Ref.27251456] 5% hemolysis at 128 μM, MHC=128 μM against human red blood cells. Linear Free Amidation L [Ref.27251456] No cytotoxicity information found Not found 27251456 Sci Rep. 2016 Jun 2;6:27258. Lyu Y, Yang Y, Lyu X, Dong N, Shan A. Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. DRAMP20810 TRKRLKKIGKVLKWI 15 TI15 (PMAP-36 peptide derivative) No entry found Derived from PMAP-36 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and Fungi.. [Ref.27251456] Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=32 μM, MBC=128 μM), Staphylococcus aureus 25923 (MIC=32 μM, MBC=128 μM), Staphylococcus epidermidis 12228 (MIC=32 μM, MBC=64 μM), Bacillus subtilis 63501 (MIC=2 μM, MBC=4 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=8 μM, MBC=16 μM), Escherichia coli EC183 (MIC=2 μM, MBC=4 μM), Escherichia coli 1005 (MIC=4 μM, MBC=8 μM), Salmonella typhimurium C77-31 (MIC=8 μM, MBC=32 μM);##Fungi: Candida albicans 2.2086 (MIC=64 μM, MFC=64 μM), Candida albicans CA276 (MIC=128 μM, MFC=128 μM), Candida tropicalis 2.1975 (MIC=2 μM, MFC=4 μM), Candida krusei 2.1857 (MIC=8 μM, MFC=16 μM). [Ref.27251456] Non-hemolysis upto 128 μM, MHC>128 μM against human red blood cells. Linear Free Amidation L [Ref.27251456] No cytotoxicity information found Not found 27251456 Sci Rep. 2016 Jun 2;6:27258. Lyu Y, Yang Y, Lyu X, Dong N, Shan A. Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. DRAMP20811 RLKKIGKVLKWI 12 RI12 (PMAP-36 peptide derivative) No entry found Derived from PMAP-36 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and Fungi.. [Ref.27251456] Gram-positive bacteria: Staphylococcus aureus 29213 (MIC=64 μM, MBC=128 μM), Staphylococcus aureus 25923 (MIC=128 μM, MBC=128 μM), Staphylococcus epidermidis 12228 (MIC=64 μM, MBC=64 μM), Bacillus subtilis 63501 (MIC=2 μM, MBC=8 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=8 μM, MBC=32 μM), Escherichia coli EC183 (MIC=2 μM, MBC=4 μM), Escherichia coli 1005 (MIC=16 μM, MBC=32 μM), Salmonella typhimurium C77-31 (MIC=8 μM, MBC=32 μM);##Fungi: Candida albicans 2.2086 (MIC=128 μM, MFC=128 μM), Candida albicans CA276 (MIC=128 μM, MFC=128 μM), Candida tropicalis 2.1975 (MIC=8 μM, MFC=8 μM), Candida krusei 2.1857 (MIC=16 μM, MFC=16 μM). [Ref.27251456] Non-hemolysis upto 128 μM, MHC>128 μM against human red blood cells. Linear Free Amidation L [Ref.27251456] No cytotoxicity information found Not found 27251456 Sci Rep. 2016 Jun 2;6:27258. Lyu Y, Yang Y, Lyu X, Dong N, Shan A. Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. DRAMP20812 GILGKLWKGVKSIF 14 K8 No entry found Belongs to the Hp1404 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26952110] Gram-positive bacteria:Staphylococcus aureus AB94004 (MIC=6.25μg/mL), Staphylococcus aureus ATCC6538 (MIC=6.25μg/mL), Staphylococcus aureus ATCC25923 (MIC=12.5μg/mL), Staphylococcus aureus MRSA P1381 (MIC=6.25μg/mL), Staphylococcus aureus MRSA P1374 (MIC=6.25μg/mL);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=25μg/mL), Escherichia coli ATCC25922 (MIC=100μg/mL), Pseudomonas aeruginosa AB93066 (MIC=50μg/mL), Pseudomonas aeruginosa ATCC9027 (MIC=25μg/mL) [Ref.26952110] 2% hemolysis at 50μg/mL, 20% hemolysis at 100μg/mL, 45% hemolysis at 200μg/mL, 65% hemolysis at 400μg/mL against human red blood cells Linear Free Amidation L [Ref.26952110] No cytotoxicity information found Not found 26952110 Appl Microbiol Biotechnol. 2016 Jun;100(11):5069-77. Li Z, Liu G, Meng L, Yu W, Xu X, Li W, Wu Y, Cao Z. K1K8: an Hp1404-derived antibacterial peptide DRAMP20813 LILGKLWKGVKSIF 14 L1K8 No entry found Belongs to the Hp1404 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26952110] Gram-positive bacteria:Staphylococcus aureus AB94004 (MIC=12.5μg/mL), Staphylococcus aureus ATCC6538 (MIC=12.5μg/mL), Staphylococcus aureus ATCC25923 (MIC=12.5μg/mL), Staphylococcus aureus MRSA P1381 (MIC=25μg/mL), Staphylococcus aureus MRSA P1374 (MIC=6.25μg/mL);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=50μg/mL), Escherichia coli ATCC25922 (MIC=100μg/mL), Pseudomonas aeruginosa AB93066 (MIC=100μg/mL), Pseudomonas aeruginosa ATCC9027 (MIC=25μg/mL) [Ref.26952110] 2% hemolysis at 200μg/mL, 10% hemolysis at 400μg/mL against human red blood cells Linear Free Amidation L [Ref.26952110] No cytotoxicity information found Not found 26952110 Appl Microbiol Biotechnol. 2016 Jun;100(11):5069-77. Li Z, Liu G, Meng L, Yu W, Xu X, Li W, Wu Y, Cao Z. K1K8: an Hp1404-derived antibacterial peptide DRAMP20814 SILGKLWKGVKSIF 14 S1K8 No entry found Belongs to the Hp1404 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26952110] Gram-positive bacteria:Staphylococcus aureus AB94004 (MIC=6.25μg/mL), Staphylococcus aureus ATCC6538 (MIC=6.25μg/mL), Staphylococcus aureus ATCC25923 (MIC=6.25μg/mL), Staphylococcus aureus MRSA P1381 (MIC=12.5μg/mL), Staphylococcus aureus MRSA P1374 (MIC=6.25μg/mL);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=25μg/mL), Escherichia coli ATCC25922 (MIC=50μg/mL), Pseudomonas aeruginosa AB93066 (MIC=50μg/mL), Pseudomonas aeruginosa ATCC9027 (MIC=25μg/mL) [Ref.26952110] 15% hemolysis at 200μg/mL, 45% hemolysis at 400μg/mL against human red blood cells Linear Free Amidation L [Ref.26952110] No cytotoxicity information found Not found 26952110 Appl Microbiol Biotechnol. 2016 Jun;100(11):5069-77. Li Z, Liu G, Meng L, Yu W, Xu X, Li W, Wu Y, Cao Z. K1K8: an Hp1404-derived antibacterial peptide DRAMP20815 FILGKLWKGVKSIF 14 F1K8 No entry found Belongs to the Hp1404 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26952110] Gram-positive bacteria:Staphylococcus aureus AB94004 (MIC=6.25μg/mL), Staphylococcus aureus ATCC6538 (MIC=6.25μg/mL), Staphylococcus aureus ATCC25923 (MIC=6.25μg/mL), Staphylococcus aureus MRSA P1381 (MIC=12.5μg/mL), Staphylococcus aureus MRSA P1374 (MIC=12.5μg/mL);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=25μg/mL), Escherichia coli ATCC25922 (MIC=50μg/mL), Pseudomonas aeruginosa AB93066 (MIC=50μg/mL), Pseudomonas aeruginosa ATCC9027 (MIC=50μg/mL) [Ref.26952110] 2% hemolysis at 100μg/mL, 35% hemolysis at 200μg/mL, 70% hemolysis at 400μg/mL against human red blood cells Linear Free Amidation L [Ref.26952110] No cytotoxicity information found Not found 26952110 Appl Microbiol Biotechnol. 2016 Jun;100(11):5069-77. Li Z, Liu G, Meng L, Yu W, Xu X, Li W, Wu Y, Cao Z. K1K8: an Hp1404-derived antibacterial peptide DRAMP20816 KILGKLWKGVKSIF 14 K1K8 No entry found Belongs to the Hp1404 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26952110] Gram-positive bacteria:Staphylococcus aureus AB94004 (MIC=6.25μg/mL), Staphylococcus aureus ATCC6538 (MIC=12.5μg/mL), Staphylococcus aureus ATCC25923 (MIC=12.5μg/mL), Staphylococcus aureus MRSA P1381 (MIC=6.25μg/mL), Staphylococcus aureus MRSA P1374 (MIC=6.25μg/mL);##Gram-negative bacteria: Escherichia coli AB94012 (MIC=25μg/mL), Escherichia coli ATCC25922 (MIC=50μg/mL), Pseudomonas aeruginosa AB93066 (MIC=50μg/mL), Pseudomonas aeruginosa ATCC9027 (MIC=50μg/mL) [Ref.26952110] 10% hemolysis at 400μg/mL against human red blood cells Linear Free Amidation L [Ref.26952110] The cell vaibility of HFF cell lines is 100%, 108%, 105% and 38% at peptide concentrations of 0 μg/ml, 50 μg/ml, 100 μg/ml and 200 μg/ml. ##The cell viability of HEK293T cell lines is 105%, 125%, 101% and 21% at peptide concentrations of Not found 26952110 Appl Microbiol Biotechnol. 2016 Jun;100(11):5069-77. Li Z, Liu G, Meng L, Yu W, Xu X, Li W, Wu Y, Cao Z. K1K8: an Hp1404-derived antibacterial peptide DRAMP20817 RRLIRLILRLLR 12 RR12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26795535] Gram-positive bacteria:Bacillus subtilis lab strain (MIC=8μM), Staphylococcus aureus ATCC25923 (MIC=8μM), Streptococcus pyogenes ATCC19615 (MIC=12.5μM), Enterococcus feacalis ATCC29212 (MIC=10μM);##Gram-negative bacteria:Escherichia coli lab strain (MIC=8μM), Pseudomonas aeruginosa ATCC27853 (MIC=12.5μM), Klebsiella pneumoniae ATCC13883 (MIC=8μM), Salmonella enterica ATCC14028 (MIC=10μM) [Ref.26795535] 4% hemolysis at 25μM, 10% hemolysis at 50μM, 32% hemolysis at 100μM against mice red cells Linear Free Amidation L [Ref.26849911] No cytotoxicity information found Not found 26849911 Biopolymers. 2016 May;106(3):345-56. Mohanram H, Bhattacharjya S. Salt-resistant short antimicrobial peptides DRAMP20818 RRLIWLILRLLR 12 RR12Wpolar No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26795535] Gram-positive bacteria:Bacillus subtilis lab strain (MIC=4μM), Staphylococcus aureus ATCC25923 (MIC=4μM), Streptococcus pyogenes ATCC19615 (MIC=4μM), Enterococcus feacalis ATCC29212 (MIC=8μM);##Gram-negative bacteria:Escherichia coli lab strain (MIC=8μM), Pseudomonas aeruginosa ATCC27853 (MIC=10μM), Klebsiella pneumoniae ATCC13883 (MIC=4μM), Salmonella enterica ATCC14028 (MIC=10μM) [Ref.26795535] 5% hemolysis at 5 μM, 12% hemolysis at 10 μM, 32% hemolysis at 25 μM, 60% hemolysis at 50 μM, 78% hemolysis at 100 μM against mice red cells Linear Free Amidation L [Ref.26849911] No cytotoxicity information found Not found 26849911 Biopolymers. 2016 May;106(3):345-56. Mohanram H, Bhattacharjya S. Salt-resistant short antimicrobial peptides DRAMP20819 RRLIRLWLRLLR 12 RR12Whydro No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.26795535] Gram-positive bacteria:Bacillus subtilis lab strain (MIC=4μM), Staphylococcus aureus ATCC25923 (MIC=8μM), Streptococcus pyogenes ATCC19615 (MIC=8μM), Enterococcus feacalis ATCC29212 (MIC=8μM);##Gram-negative bacteria:Escherichia coli lab strain (MIC=4μM), Pseudomonas aeruginosa ATCC27853 (MIC=10μM), Klebsiella pneumoniae ATCC13883 (MIC=4μM), Salmonella enterica ATCC14028 (MIC=8μM) [Ref.26795535] 2% hemolysis at 25 μM, 5% hemolysis at 50μM, 18% hemolysis at 100μM against mice red cells Linear Free Amidation L [Ref.26849911] No cytotoxicity information found Not found 26849911 Biopolymers. 2016 May;106(3):345-56. Mohanram H, Bhattacharjya S. Salt-resistant short antimicrobial peptides DRAMP20820 FRIRVRV 7 FV7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28178190] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=64 μM), Streptococcus Faecalis ATCC 29212 (MIC=32 μM), Bacillus subtilis CMCC 63501 (MIC=16 μM), Staphylococcus epidermidis ATCC 12228 (MIC=32 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16 μM), Escherichia coli UB 1005 (MIC=32 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μM), Pseudomonas aeruginosa PAO1 (MIC=32 μM), Salmonella typhimurium ATCC 14028 (MIC=16 μM), Salmonella typhimurium ATCC 7731 (MIC=32 μM). [Ref.28178190] 3% hemolysis at 128 μM against human red cells Linear Free Amidation L [Ref.28178190] No cytotoxicity information found Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP20821 FRIRVRVFKRIVQRIKDFLR 20 FV-LL (FV7 and LL(LL-37,(17-29)) hybrid peptide) No entry found FV7 and LL(LL-37,(17-29)) hybrid peptide Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, random coil The hybrid peptide displayed an unordered conformation in phosphate buffer. Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28178190] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2 μM), Streptococcus Faecalis ATCC 29212 (MIC=4 μM), Bacillus subtilis CMCC 63501 (MIC=4 μM), Staphylococcus epidermidis ATCC 12228 (MIC=1 μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=1 μM), Escherichia coli UB 1005 (MIC=4 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=4 μM), Pseudomonas aeruginosa PAO1 (MIC=2 μM), Salmonella typhimurium ATCC 14028 (MIC=2 μM), Salmonella typhimurium ATCC 7731 (MIC=2 μM). [Ref.28178190] 2% hemolysis at 128 μM against human red cells Linear Free Amidation L [Ref.28178190] No cytotoxicity information found Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP20822 FRIRVRVAKKFGKAFVGEIM 20 FV-MA (FV7 and MA(Magainin 2 (9-21)) hybrid peptide) No entry found FV7 and MA(Magainin 2 (9-21)) hybrid peptide Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, random coil The hybrid peptide displayed an unordered conformation in phosphate buffer. Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28178190] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=8 μM), Streptococcus Faecalis ATCC 29212 (MIC=16 μM), Bacillus subtilis CMCC 63501 (MIC=4 μM), Staphylococcus epidermidis ATCC 12228 (MIC=8 μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=8 μM), Escherichia coli UB 1005 (MIC=8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μM), Pseudomonas aeruginosa PAO1 (MIC=2 μM), Salmonella typhimurium ATCC 14028 (MIC=4 μM), Salmonella typhimurium ATCC 7731 (MIC=4 μM). [Ref.28178190] 1% hemolysis at 2 μM, 8% hemolysis at 4 μM, 10% hemolysis at 8 μM, 15% hemolysis at 16 μM, 20% hemolysis at 32 μM, 37% hemolysis at 64 μM, 55% hemolysis at 128 μM against human red cells Linear Free Amidation L [Ref.28178190] No cytotoxicity information found Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP20823 FRIRVRVKWKLFKKI 15 FV-CE (FV7 and CE(Cecropin A (1 No entry found FV7 and CE(Cecropin A (1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil The hybrid peptide displayed an unordered conformation in phosphate buffer. Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28178190] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=8 μM), Streptococcus Faecalis ATCC 29212 (MIC=1 μM), Bacillus subtilis CMCC 63501 (MIC=1 μM), Staphylococcus epidermidis ATCC 12228 (MIC=0.5 μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=2 μM), Escherichia coli UB 1005 (MIC=2 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=2 μM), Pseudomonas aeruginosa PAO1 (MIC=2 μM), Salmonella typhimurium ATCC 14028 (MIC=4 μM), Salmonella typhimurium ATCC 7731 (MIC=4 μM). [Ref.28178190] 1% hemolysis at 2 μM, 5% hemolysis at 128 μM against human red cells Linear Free Amidation L [Ref.28178190] No cytotoxicity information found Not found 28178190 Int J Mol Sci. 2017 Feb 6;18(2). Tan T, Wu D, Li W, Zheng X, Li W, Shan A. High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7 DRAMP20824 GLFKKLRRKIKKGFKKIFKRLPPIGVGVSIPLAGKR 36 AM-CATH36 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, random coil NA-CATH has previously been shown to be random coil in water or buffer and Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28089718] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=21μg/ml), Staphylococcus aureus ATCC 33592 (MIC=21μg/ml);##Gram-negative bacteria:Acinetobacter baumannii ATCC 9955 (MIC=5.2μg/ml), Acinetobacter baumannii ATCC BAA-1794 (MIC=5.2μg/ml), Escherichia coli ATCC 4157 (MIC=140μg/ml), K. pneumoniae ATCC 33495 (MIC=5.2μg/ml), K. pneumoniae ATCC BAA-1705 (MIC=5.6μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=5.2μg/ml), Pseudomonas aeruginosa ATCC BAA-2110 (MIC=5.2μg/ml) [Ref.28089718] 0% hemolysis at 300μg/ml against sheep red cells Linear Free Free L [Ref.28089718] The survival rate of A549 human lung epithelial cells is 124% at a peptide concentration of 300 μg/ml Not found 28089718 Dev Comp Immunol. 2017 May;70:135-144. Barksdale SM, Hrifko EJ, van Hoek ML. Cathelicidin antimicrobial peptide from Alligator mississippiensis has antibacterial activity against multi-drug resistant Acinetobacter baumanii and Klebsiella pneumoniae DRAMP20825 KIKKGFKKIFKRLPPIGVGVSIPLAGKR 28 AM-CATH28 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix, random coil NA-CATH has previously been shown to be random coil in water or buffer and Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28089718] Gram-negative bacteria:Acinetobacter baumannii ATCC 9955 (MIC=28μg/ml), Acinetobacter baumannii ATCC BAA-1794 (MIC=10μg/ml), K. pneumoniae ATCC 33495 (MIC=5.6μg/ml), K. pneumoniae ATCC BAA-1705 (MIC=28μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=21μg/ml) [Ref.28089718] 1% hemolysis at 300μg/ml against sheep red cells Linear Free Free L [Ref.28089718] The survival rate of A549 human lung epithelial cells is 122% at a peptide concentration of 300 μg/ml Not found 28089718 Dev Comp Immunol. 2017 May;70:135-144. Barksdale SM, Hrifko EJ, van Hoek ML. Cathelicidin antimicrobial peptide from Alligator mississippiensis has antibacterial activity against multi-drug resistant Acinetobacter baumanii and Klebsiella pneumoniae DRAMP20826 GLFKKLRRKIKKGFKKIFKRL 21 AM-CATH21 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, random coil NA-CATH has previously been shown to be random coil in water or buffer and Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28089718] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=28μg/ml), Staphylococcus aureus ATCC 33592 (MIC=28μg/ml);##Gram-negative bacteria:Acinetobacter baumannii ATCC 9955 (MIC=42μg/ml), Acinetobacter baumannii ATCC BAA-1794 (MIC=10μg/ml), Escherichia coli ATCC 4157 (MIC=21μg/ml), Escherichia coli ATCC 51659 (MIC=140μg/ml), K. pneumoniae ATCC 33495 (MIC=5.2μg/ml), K. pneumoniae ATCC BAA-1705 (MIC=28μg/ml), Pseudomonas aeruginosa ATCC 9027 (MIC=10μg/ml), Pseudomonas aeruginosa ATCC BAA-2110 (MIC=42μg/ml) [Ref.28089718] 0.5% hemolysis at 300μg/ml against sheep red cells Linear Free Free L [Ref.28089718] The survival rate of A549 human lung epithelial cells is 113% at a peptide concentration of 300 μg/ml Not found 28089718 Dev Comp Immunol. 2017 May;70:135-144. Barksdale SM, Hrifko EJ, van Hoek ML. Cathelicidin antimicrobial peptide from Alligator mississippiensis has antibacterial activity against multi-drug resistant Acinetobacter baumanii and Klebsiella pneumoniae DRAMP20827 FLPIVGLLKSLLK 13 TB_L1FK No entry found Derived from TB Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria,antifungal activity. [Ref.28443279] Gram-positive bacteria: S.aureus ATCC 33591 (MIC=6μM), Staphylococcus epidermidis (MIC=1.5μM);##Gram-negative bacteria: Klebsiella pneumoniae ATCC BAA-1706 (MIC=6μM), Pseudomonas aeruginosa ATCC 27853 (MIC=6μM) [Ref.28443279] 8% hemolysis at 48μM, 38% hemolysis at 96μM against human red cells Linear Free Amidation L [Ref.28443279] IC50 = 52 μM against PBMCs. ##IC50 = 59 μM against A549 cells Not found 28443279 Front Chem. 2017 Apr 11;5:24 Grassi L, Maisetta G, Maccari G, Esin S, Batoni G. Analogs of the Frog-skin Antimicrobial Peptide Temporin 1Tb Exhibit a Wider Spectrum of Activity and a Stronger Antibiofilm Potential as Compared to the Parental Peptide DRAMP20828 KKLLPIVANLLKSLL 15 TB_KKG6A No entry found Derived from TB Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria,antifungal activity. [Ref.28443279] Gram-positive bacteria: S.aureus ATCC 33591 (MIC=1.5μM), Staphylococcus epidermidis (MIC=1.5μM);##Gram-negative bacteria: Klebsiella pneumoniae ATCC BAA-1706 (MIC=3μM), Pseudomonas aeruginosa ATCC 27853 (MIC=3μM) [Ref.28443279] 11% hemolysis at 48μM, 55% hemolysis at 96μM against human red cells Linear Free Amidation L [Ref.28443279] IC50 = 49 μM against PBMCs. ##IC50 = 16 μM against A549 cells Not found 28443279 Front Chem. 2017 Apr 11;5:24 Grassi L, Maisetta G, Maccari G, Esin S, Batoni G. Analogs of the Frog-skin Antimicrobial Peptide Temporin 1Tb Exhibit a Wider Spectrum of Activity and a Stronger Antibiofilm Potential as Compared to the Parental Peptide DRAMP20829 RWKIFKKIERVGQNVRDGIIKAGPAIQVLGTAKALGK 37 ABP-dHC-Cecropin A No entry found Derived from dHC Not found Synthetic construct Anti-Cancer Synthetic Alpha helix ABP-dHC-Cecropin A and its analog adopt a well-defined Function: Anticancer activity against the human leukemia cells [Ref.28347740] Cancer cell lines: Leukemia cell lines K562 (IC50=349.5μM), Leukemia cell lines U937 (IC50=303.2μM), Leukemia cell lines THP-1 (IC50=228.5μM) [Ref.28347740] 0% hemolysis at 0μM, 1% hemolysis at 800μM against human red cells Linear Free Free L [Ref.28347740] IC50 = 349.5 μM and CI = [304.0, 399.0] μM against K562 cells. ## IC50 = 303.2 μM and CI =[291.2, 315.3] μM against U937 cells. IC50 = 228.5 μM and CI = [199.1, 258.0] μM against THP-1 cells. The CI is the Confidence Interval of 90%. Not found 28347740 Eur J Pharmacol. 2017 May 15;803:138-147. Sang M, Zhang J, Zhuge Q Selective cytotoxicity of the antibacterial peptide ABP-dHC-Cecropin A and its analog towards leukemia cells DRAMP20830 RWKIFKKIERVGQNVRDGIIKAGKAIQVLGTAKALGK 37 ABP-dHC-Cecropin A-K No entry found Derived from dHC Not found Synthetic construct Anti-Cancer Synthetic Alpha helix ABP-dHC-Cecropin A and its analog adopt a well-defined Function: Anticancer activity against the human leukemia cells [Ref.28347740] Cancer cell lines: Leukemia cell lines K562 (IC50=184.9μM), Leukemia cell lines U937 (IC50=223.9μM), Leukemia cell lines THP-1 (IC50=196.1μM) [Ref.28347740] 0% hemolysis at 0μM, 1% hemolysis at 800μM against human red cells Linear Free Free L [Ref.28347740] IC50 = 184.9 μM and CI = [185.3, 191.0] μM against K562 cells. ## IC50 = 223.9 μM and CI =[211.4, 236.5] μM against U937 cells. IC50 = 196.1 μM and CI = [170.2, 222.1] μM against THP-1 cells. The CI is the Confidence Interval of 90%. Not found 28347740 Eur J Pharmacol. 2017 May 15;803:138-147. Sang M, Zhang J, Zhuge Q Selective cytotoxicity of the antibacterial peptide ABP-dHC-Cecropin A and its analog towards leukemia cells DRAMP20831 ILGKLWEGLKSLF 13 IsCT1L1 No entry found Belongs to the scorpion NDBP 5 family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.28657596] Gram-positive bacteria:Staphylococcus aureus (MIC=50μg/mL);##Gram-negative bacteria: S. typhimurium (MIC=100μg/mL), Escherichia coli (MIC=50μg/mL) [Ref.28657596] 1% hemolysis at 10 μg/ml, 78% hemolysis at 50 μg/ml, 90% hemolysis at 100 μg/ml against human red cells Linear Free Amidation L [Ref.28657596] No cytotoxicity information found Not found 28657596 Antibiotics (Basel). 2017 Jun 28;6(3). de la Salud Bea R, Petraglia AF, Ascuitto MR, Buck QM. Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides DRAMP20832 IDWKKLLNAAKQIL 14 Polybia-MP1S-D8N No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria, position 6 and 10 are cross-linked residues connected by the oct-4-enyl hydrocarbon staple [Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC=0.8μM), Staphylococcus aureus (MIC=0.8μM), Staphylococcus epidermidis (MIC=37.5μM);##Gram-negative bacteria:Escherichia coli (MIC=50μM), Shigella dysenteriae (MIC=100μM), Klebsiella pneumoniae (MIC=37.5μM) [Ref.29075946] 16.3% hemolysis at 12.5μM, 37.8% hemolysis at 25μM against human red cells Cyclic Free Amidation The oct-4-enyl hydrocarbon staple between Leu6 and Ala10 L [Ref.29075946] No cytotoxicity information found Not found 29075946 Arch Pharm Res. 2017 Dec;40(12):1414-1421. Luong HX, Kim DH, Lee BJ, Kim YW Antimicrobial activity and stability of stapled helices of polybia-MP1 DRAMP20833 FVPWFSKFLGRIL 13 [Pro3,DLeu9]TL(1) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix The analogues bearing a D residue shows a reduction in the percentage of helicity compared to the corresponding L analogues in the MMs Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(1) is D-Leucine. [Ref.28863356] Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3.125μM), Staphylococcus aureus Cowan I (MIC=12.5μM), Staphylococcus epidermidis ATCC 12228 (MIC=6.25μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=12.5μM), Escherichia coli D21 (MIC=12.5μM), Pseudomonas syringae pv tabaci 1918 (MIC=12.5μM), Pseudomonas aeruginosa ATCC 2785 (MIC=50μM);##Yeasts: Candida albicans ATCC 10231 (MIC=3.125μM), Candida crusei ATCC 6258 (3.125μM). [Ref.28863356] 21±4% hemolysis at 50μM, 7±3% hemolysis at 25μM, 6±3% hemolysis at 12.5μM, 3±2% hemolysis at 6.25μM, 1±1% hemolysis at 3.125μM against human red blood cells.##20.63 ± 2.66% cytotoxic effect at 12.5μM, 57.52 ± 3.99% cytotoxic effect at 25μM, 91.58 ± 3.85% cytotoxic effect at 50 μM on HaCaT cells. Linear Free Amidation Mixed (D-Leu9) [Ref.28863356] The cytotoxic effects of the peptide are 20.63±2.66%, 57.52±3.99% and 91.58±3.85% at 12.5, 25 and 50 μM Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-761. Merlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP20834 RWQWRWQWR 9 PLS No entry found Not found Not found Not found Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria [Ref.29551999] Gram-negative bacteria:E. faecalis-sensitive strain (MIC=25.6 μM),Staphylococcus aureus-sensitive strain (MIC=34.9 μM),,Staphylococcus aureus-resistant strain (MIC=25.0 μM);##Gram-positive bacteria:Klebsiella pneumoniaae-sensitive strain (MIC=30.7 μM),Klebsiella pneumoniaae-resistant strain (MIC=26.2 μM),Pseudomonas aeruginosa-sensitive strain (MIC=99.7 μM),Pseudomonas aeruginosa-resistant strain (MIC=107.2 μM) [Ref.29551999] 24.8% hemolysis at 100μM,50% hemolysis at >100μM against human red cells Linear Free Free L [Ref.29551999] No cytotoxicity information found Not found 29551999 Front Microbiol. 2018 Mar 2;9:329. Vega SC, Mart Design, Synthesis and Evaluation of Branched RRWQWR-Based Peptides as Antibacterial Agents against Clinically Relevant Gram-Positive and Gram-Negative Pathogens DRAMP20835 ALAGTIIAGASLTFQVLDKVLEELGKVSRK 30 StII1-30 StII peptide derivative No entry found Not found Not found Synthetic construct Candidacidal Synthetic Alpha helix The peptide at low concentration exists in a random coil conformation.Increasing the peptide concentration up to 300 Function: Antibacterial activity against the candida No MICs found in DRAMP database [Ref.29359791] HC50=42.5μM against human red blood cells Linear Free Free L [Ref.29359791] No cytotoxicity information found Not found 29359791 Biopolymers. 2018 Jan 23. Lima de Oliveira A, Maffud Cilli E, Ros U, Crusca E Jr, Lanio ME, Alvarez C, Schreier S, Aguiar Pertinhez T, Spisni A. Insights on the structure-activity relationship of peptides derived from Sticholysin II. DRAMP20836 VLDKVLEELGKVSRKIAVGI 20 StII16-35 StII peptide derivative No entry found Not found Not found Synthetic construct Candidacidal Synthetic Random coil conformation The peptide displays a random coil conformation up to 1 mM and does not show any structure concentration Function: Antibacterial activity against the candida No MICs found in DRAMP database [Ref.29359791] HC50=128μM against human red blood cells Linear Free Free L [Ref.29359791] No cytotoxicity information found Not found 29359791 Biopolymers. 2018 Jan 23. Lima de Oliveira A, Maffud Cilli E, Ros U, Crusca E Jr, Lanio ME, Alvarez C, Schreier S, Aguiar Pertinhez T, Spisni A. Insights on the structure-activity relationship of peptides derived from Sticholysin II. DRAMP20837 KRVKRFKKFFRKIKKGFRKIFKKTKIFIGGT 31 Pb-CATH1 Python bivittatus antimicrobial peptides peptide derivative No entry found Derived from cathelicidin family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive [Ref.28630199]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=2μg/ml);Pseudomonas aeruginosa (ATCC 27853)(MIC=3μg/ml);S. typhimurium (ATCC 14028)(MIC=1.5μg/ml);##Gram-positive bacteria:Staphylococcus aureus (ATCC 29213)(MIC>128μg/ml);B. cereus (ATCC 10876)(MIC=46μg/ml) [Ref.28630199] 0% hemolysis at 4μg/ml against human red blood cell; 1.4 ± 0.4% hemolysis at 8μg/ml against human red blood cell; 5.1 ± 0.5% hemolysis at 16μg/ml against human red blood cell;7.3 ± 0.6% hemolysis at 32μg/ml against human red blood cell; 12.2 ± 0.7% hemolysis at 64μg/ml against human red blood cell Linear Free Free L [Ref.28630199] No cytotoxicity information found Not found 28630199 Antimicrob Agents Chemother. 2017 Aug 24;61(9). Kim D, Soundrarajan N, Lee J, Cho HS, Choi M, Cha SY, Ahn B, Jeon H, Le MT, Song H, Kim JH, Park C. Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity. DRAMP20838 TRSRWRRFIRGAGRFARRYGWRIAL 25 Pb-CATH4 bivittatus antimicrobial peptides peptide derivative No entry found Derived from cathelicidin family Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix The peptide adopts arginine content of this peptide is 37.5%, and it contains two tryptophan residues (8.3%) Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria [Ref.28630199]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=1μg/ml);Pseudomonas aeruginosa (ATCC 27853)(MIC=3μg/ml);S. typhimurium (ATCC 14028)(MIC=0.5μg/ml);##Gram-positive bacteria:Staphylococcus aureus (ATCC 29213)(MIC>128μg/ml);B. cereus (ATCC 10876)(MIC=10μg/ml);##Clinical isolates:Escherichia coli(MIC=4.7μg/ml);K. pneumoniae(MIC=1.18μg/ml) [Ref.28630199] 0% hemolysis at 4μg/ml against human red blood cell; 1.4 ± 0.4% hemolysis at 8μg/ml against human red blood cell; 5.1 ± 0.5% hemolysis at 16μg/ml against human red blood cell;7.3 ± 0.6% hemolysis at 32μg/ml against human red blood cell; 12.2 ± 0.7% hemolysis at 64μg/ml against human red blood cell Linear Free Free L [Ref.28630199] The cell viability of Pk15(pig kidney fibroblasts) is 103.8%, 124.6%, 94.7%,55.2% and 53.9% at peptide concentrations of 5, 10, 20, 30 and 64 μg/ml. ##The cell viability of HaCaT(human keratinocytes) is 106.9%, 94.6%, 66.2%, 58.1% and 51. Not found 28630199 Antimicrob Agents Chemother. 2017 Aug 24;61(9). Kim D, Soundrarajan N, Lee J, Cho HS, Choi M, Cha SY, Ahn B, Jeon H, Le MT, Song H, Kim JH, Park C. Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity. DRAMP20839 GFVALLKKLPLILKHLH 17 Xylopin C0HKQ5 Not found Not found Xylocopa appendiculata circumvolans Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Linear cationic alpha-helical Not found Function: Antimicrobial and mast cell degranulating peptide which probably acts by forming pores in membranes (PubMed:28546807, PubMed:28855917). Active against both Gram-negative and Gram-positive bacterial strains as well as against yeasts (PubMed:28546807, PubMed:28855917). Has leishmanicidal activity (IC50=25uM)(PubMed:28855917). Has little hemolytic activity (PubMed:28546807, PubMed:28855917) [Ref.28855917]Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=15.0μM);Micrococcus luteus (ATCC 10240)(MIC=1.9μM);Bacillus subtilis (ATCC 6633)(MIC=3.75μM);Streptococcus pyogenes (CS)(MIC=3.75μM);Streptococcus agalactiae (CS)(MIC=3.75μM);Enterococcus. faecalis (CS)(MIC=15.0μM);##Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=3.75μM);Pseudomonas aeruginosa (ATCC 27853)(MIC=7.5μM);Stenotrophomonas maltophilia (ATCC 13637)(MIC=3.75μM);Shigella boydii (CS)(MIC=3.75μM);Klebsiella pneumoniae (CS)(MIC=7.5μM);Serratia marcescens (CS)(MIC=7.5μM);Enterobacter cloacae (CS)(MIC=7.5μM);Proteus mirabilis (CS)(MIC>30μM);Morganella morgannii (CS)(MIC=30μM);Acinetobacter baumanii/calcoaceticus (CS)(MIC=3.75μM) ;##Yeasts:Candida albicans (ATCC 90112)(MIC=7.5μM);Sacharomyces cerevisae(MIC=3.75μM) [Ref.28855917]IC50=25uM against human red blood cells Linear Free Amidation L [Ref.28855917] No cytotoxicity information found Not found 28855917 J Venom Anim Toxins Incl Trop Dis. 2017 Aug 29;23:40. Kazuma K, Ando K, Nihei KI, Wang X, Rangel M, Franzolin MR, Mori-Yasumoto K, Sekita S, Kadowaki M, Satake M, Konno K. Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans. DRAMP20840 PDRAIDTYRTSPVADQRYNA 20 SLAY-C1 No entry found Synthetic construct Non-antibacterial Synthetic form Unknown Not mentioned Function: Non-antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC > 128 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC > 128 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] No hemolytic activity information found. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP20841 SKVWRHWRRFWHRAHRLH 18 C1b No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts an low alpha-helical content when dissolved in water. However, the peptides displayed 3.23 Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=6.25μM);Pseudomonas aeruginosa(MIC=1.56μM);##Gram-positive bacteria:Staphylococcus aureus(MIC=3.13μM);B. cereus(MIC=3.13μM);S. lactis(MIC=3.13μM);E. faecalis (MIC=1.56μM);E. faecium(MIC=3.13μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-1b analogues. DRAMP20842 SKVWRHWRRFW 11 C1b(1-11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=12.5μM);Pseudomonas aeruginosa(MIC=3.13μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 6.25μM);B. cereus(MIC=6.25μM);S. lactis(MIC=6.25μM);E. faecalis (MIC=6.25μM);E. faecium(MIC=6.25μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-2b analogues. DRAMP20843 SKVWRHWRRFWHR 13 C1b(1-13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts 41.93% alpha-helical Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=6.25μM);Pseudomonas aeruginosa(MIC=3.13μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 3.13μM);B. cereus(MIC=1.56μM);S. lactis(MIC=3.13μM);E. faecalis (MIC=3.13μM);E. faecium(MIC=6.25μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-3b analogues. DRAMP20844 VWRHWRRFWHR 11 C1b(3-13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts 53.49% alpha-helical Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=6.25μM);Pseudomonas aeruginosa(MIC=3.13μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 3.13μM);B. cereus(MIC=3.13μM);S. lactis(MIC=6.25μM);E. faecalis (MIC=3.13μM);E. faecium(MIC=3.13μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-4b analogues. DRAMP20845 VWRHWRRFW 9 C1b(3-11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=25μM);Pseudomonas aeruginosa(MIC=50μM);##Gram-positive bacteria:Staphylococcus aureus(MIC=25μM);B. cereus(MIC=50μM);S. lactis(MIC=100μM);E. faecalis (MIC=100μM);E. faecium(MIC=50μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-6b analogues. DRAMP20846 VWRHWRRFWH 10 C1b(3-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=50μM);Pseudomonas aeruginosa(MIC=12.5μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 12.25μM);B. cereus(MIC=6.25μM);S. lactis(MIC=12.25μM);E. faecalis (MIC=12.25μM);E. faecium(MIC=6.25μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-7b analogues. DRAMP20847 WRHWRRFWHR 10 C1b(4-13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts 65.69% alpha-helical Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=25μM);Pseudomonas aeruginosa(MIC=3.13μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 50μM);B. cereus(MIC=6.25μM);S. lactis(MIC=6.25μM);E. faecalis (MIC=3.13μM);E. faecium(MIC=6.25μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-8b analogues. DRAMP20848 VWRKWRRFW 9 [K4]C1b(3-11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=6.25μM);Pseudomonas aeruginosa(MIC=6.25μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 6.25μM);B. cereus(MIC=6.25μM);S. lactis(MIC=3.13μM);E. faecalis (MIC=3.13μM);E. faecium(MIC=3.13μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-9b analogues. DRAMP20849 VWRRWRRFW 9 [R4]C1b(3-11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts 3.23% alpha-helical Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=12.5μM);Pseudomonas aeruginosa(MIC=6.25μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 12.25μM);B. cereus(MIC=6.25μM);S. lactis(MIC=12.25μM);E. faecalis (MIC=12.25μM);E. faecium(MIC=12.5μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-10b analogues. DRAMP20850 VWRKWRRFWKR 11 [K4,K10]C1b(3-13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=3.13μM);Pseudomonas aeruginosa(MIC=1.56μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 6.25μM);B. cereus(MIC=3.13μM);S. lactis(MIC=6.25μM);E. faecalis (MIC=6.25μM);E. faecium(MIC=6.25μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-11b analogues. DRAMP20851 VWRRWRRFWRR 11 [R4,R10]C1b(3-13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Random coil conformation The peptide adopts 70.2% alpha-helical Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27060618]Gram-negative bacteria:Escherichia coli(MIC=3.13μM);Pseudomonas aeruginosa(MIC=3.13μM);##Gram-positive bacteria:Staphylococcus aureus(MIC= 3.13μM);B. cereus(MIC=3.13μM);S. lactis(MIC=3.13μM);E. faecalis (MIC=1.56μM);E. faecium(MIC=1.56μM) [Ref.27060618] HC50>500μM against human red blood cells Linear Free Free L [Ref.27060618] No cytotoxicity information found Not found 27060618 Acta Biomater. 2016 Jun;37:59-68. Dong W, Dong Z, Mao X, Sun Y, Li F, Shang D. Structure-activity analysis and biological studies of chensinin-12b analogues. DRAMP20852 ONNRPVYIPRPRPPHPRL 18 Api137 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=2μg/mL);K. pneumoniae (DSM 681)(MIC=16μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=256μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>256μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>256μg/mL);Rat cardiomyocytes(IC50>0.6g/L);HEK293 cells(IC50>0.6g/L);HeLa cells(IC50>0.6g/L) [Ref.27243004] 0.4 ± 0.5% hemolysis at 0.1 g/L; 1.0 ± 0.2% hemolysis at 0.6 g/L against human red blood cells Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] IC50 > 0.6 g/L against Rat cardiomyocytes. ##IC50 > 0.6g/L against HEK293. ##IC50 > 0.6g/L against HeLa. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20853 OIORPVYOPRPRPPHPRL 18 Api755 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=8μg/mL);K. pneumoniae (DSM 681)(MIC=8μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=16μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>64μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>16μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>128μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>128μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] No cytotoxicity information found. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20854 OWORPVYOPRPRPPHPRL 18 Api760 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=8μg/mL);K. pneumoniae (DSM 681)(MIC=8μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=16μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>32μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>8μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>128μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>128μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] No cytotoxicity information found. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20855 OWOWORPVYOPRPRPPHPRL 20 Api793 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=8μg/mL);K. pneumoniae (DSM 681)(MIC=16μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=16μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>16μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>8μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>64μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>64μg/mL);Rat cardiomyocytes(IC50>0.6g/L);HEK293 cells(IC50=0.64 ± 0.05g/L);HeLa cells(IC50=0.64 ± 0.05g/L) [Ref.27243004] 1.3 ± 0.4% hemolysis at 0.1 g/L; 1.6 ± 0.5% hemolysis at 0.6 g/L against human red blood cells Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] IC50 > 0.6 g/L against Rat cardiomyocytes.## IC50 = 0.64 ± 0.05 g/L against HEK293. IC50 = 0.64 ± 0.15 g/L against HeLa. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20856 OWOWOWORPVYOPRPRPPHPRL 22 Api794 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria; highly active against Pseudomonas aeruginosa in vitro [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=16μg/mL);K. pneumoniae (DSM 681)(MIC=32μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=16μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>16μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>16μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>32μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>128μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>16μg/mL);Rat cardiomyocytes(IC50>0.6g/L);HEK293 cells(IC50>0.6g/L);HeLa cells(IC50>0.6g/L) [Ref.27243004] 1.7 ± 0.2% hemolysis at 0.1 g/L; 1.9 ± 0.3% hemolysis at 0.6 g/L against human red blood cells Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] IC50 > 0.6 g/L against Rat cardiomyocytes.## IC50 = 0.28 ± 0.03 g/L against HEK293. IC50 = 0.23 ± 0.09 g/L against HeLa. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20857 OIOIORPVYOPRPRPPHPRL 20 Api795 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria; highly active against Pseudomonas aeruginosa in vitro [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=8μg/mL);K. pneumoniae (DSM 681)(MIC=8μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=8μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>16μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>8μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>32μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>256μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>128μg/mL);Rat cardiomyocytes(IC50>0.6g/L);HEK293 cells(IC50>0.6g/L);HeLa cells(IC50>0.6g/L) [Ref.27243004] 0.8 ± 0.4% hemolysis at 0.1 g/L; 0.0 ± 0.7% hemolysis at 0.6 g/L against human red blood cells Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] IC50 > 0.6 g/L against Rat cardiomyocytes.## IC50 > 0.6g/L against HEK293. IC50 > 0.6g/L against HeLa. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20858 OIOIOIORPVYOPRPRPPHPRL 22 Api796 apidaecin petide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.27243004]Gram-negative bacteria: Escherichia coli (ATCC 25922 )(MIC=8μg/mL);K. pneumoniae (DSM 681)(MIC=16μg/mL);##Gram-positive bacteria:50% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC=8μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>16μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>16μg/mL);##Gram-positive bacteria:100% MHB:Pseudomonas aeruginosa(DSM 1117)(MIC>64μg/mL);Pseudomonas aeruginosa(DSM 3227)(MIC>128μg/mL);Pseudomonas aeruginosa(DSM 9644)(MIC>128μg/mL);Rat cardiomyocytes(IC50>0.6g/L);HEK293 cells(IC50>0.6g/L);HeLa cells(IC50>0.6g/L) [Ref.27243004] 0.8 ± 0.2% hemolysis at 0.1 g/L;μ0.1 ± 0.8 % hemolysis at 0.6 g/L against human red blood cells Linear Guanidation (Orn1 conjugated with N,N,N′,N′-tetramethylguanidino) Free The 'O' in sequence is Ornithine L [Ref.27243004] IC50 > 0.6 g/L against Rat cardiomyocytes.## IC50 > 0.6g/L against HEK293. IC50 > 0.6g/L against HeLa. Not found 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Sch?fer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa. DRAMP20859 KFRTRRSKSSSNGGRKGSKG 20 TT(1-24) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. TT(1 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=32μM);A. salmonicida (ATCC 33658)(MIC=32-16μM);Y. ruckeri (NCIMB 1315)(MIC=32μM);V. anguillarum (ATCC 43305 With addition of 2% NaCl)(MIC>32μM);A. hydrophila (ATCC 7966)(MIC>32μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=64μM);L. garvieae (ATCC 49156)(MIC=16-8μM) [Ref.27818338] No hemolytic activity to human Linear Free Free L [Ref.27818338] No cytotoxicity information found Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins. DRAMP20860 KFRTRRSKSSSNGGRKGSKGGSKGRPGSGSSIAGA 35 TT(1-35) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. TT(1 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=4μM);A. salmonicida (ATCC 33658)(MIC=2μM);Y. ruckeri (NCIMB 1315)(MIC=8μM);V. anguillarum (ATCC 43305 With addition of 2% NaCl)(MIC>32μM);A. hydrophila (ATCC 7966)(MIC>32μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=16-8μM);L. garvieae (ATCC 49156)(MIC=1μM) [Ref.27818338] No hemolytic activity to human;No hemolytic activity to trout Linear Free Free L [Ref.27818338] The cell viability of RTG-2 cells is 106%, 117%, 126% and 121.5% at peptide concentrations of 0.25, 1, 4, and 8 μM. Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins. DRAMP20861 KIRTRRSOARKOSRGNGGGIROPGGGIRLGGGSLIGR 37 STF(1-37) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. The peptides inhibit the growth of V. anguillarum or A. hydrophila (MIC >32 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=2μM);A. salmonicida (ATCC 33658)(MIC=8-4μM);Y. ruckeri (NCIMB 1315)(MIC=16μM);V. anguillarum (ATCC 43305 With addition of 2% NaCl)(MIC>32μM);A. hydrophila (ATCC 7966)(MIC>32μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=16-8μM);L. garvieae (ATCC 49156)(MIC=8μM) [Ref.27818338] No hemolytic activity to human;No hemolytic activity to trout Cyclic Free Free Disulfide bond between Cys12 and Cys22. L [Ref.27818338] The cell viability of RTG-2 cells is 108%, 112%, 117% and 118% at peptide concentrations of 0.25, 1, 4, and 8 μM. Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins. DRAMP20862 RRGKDSGGPKMGRKNSKGGWRGRPGSGRPGFGSGI 39 rtCATH2(5-40) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria.The peptides inhibit the growth of V. anguillarum or A. hydrophila (MIC >32 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=16μM);A. salmonicida (ATCC 33658)(MIC=16μM);Y. ruckeri (NCIMB 1315)(MIC=16μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=64μM) [Ref.27818338] No hemolytic activity to human Linear Free Free L [Ref.27818338] No cytotoxicity information found Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins. DRAMP20863 KIRTRRGKDSGGPKMGRKNSKGGWRGRPGSGSRPGFGSGI 42 rtCATH2(1-40) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. The peptides inhibit the growth of V. anguillarum or A. hydrophila (MIC >32 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=4μM);A. salmonicida (ATCC 33658)(MIC=8-4μM);Y. ruckeri (NCIMB 1315)(MIC=16μM);V. anguillarum (ATCC 43305 With addition of 2% NaCl)(MIC>32μM);A. hydrophila (ATCC 7966)(MIC>32μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=16-8μM);L. garvieae (ATCC 49156)(MIC=16-8μM) [Ref.27818338] No hemolytic activity to human;No hemolytic activity to trout Linear Free Free L [Ref.27818338] The cell viability of RTG-2 cells is 112.5%, 105%, 107%, 94% at peptide concentrations of 0.25, 1, 4, and 8 μM. Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins. DRAMP20864 KFRSNGRHGSGSRLGGGSLIGRPGGGS 27 SF(18-45) No entry found Derived from Cathelicidins Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Unconventional feature Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. SF(18 [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=16μM);A. salmonicida (ATCC 33658)(MIC=64μM);Y. ruckeri (NCIMB 1315)(MIC=32μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=64μM) [Ref.27818338] No hemolytic activity to human Linear Free Free L [Ref.27818338] No cytotoxicity information found Not found 27818338 Fish Shellfish Immunol. 2016 Dec;59:456-468. D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M. DRAMP20865 (RRWQWR)2-K-(Ahx) 14 the dimeric RRWQWR motif peptide molecule No entry found Derived from bovine LfcinB6 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29984236] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=14 μg/ml; MBC=110 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=55 μg/ml; MBC=110 μg/ml);##Gram-negative bacteria: Klebsiella pneumoniae ATCC 13883 (MIC=27 μg/ml; MBC=55 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=27 μg/ml; MBC=220 μg/ml) [Ref.29984236] 0% hemolysis at 5 μM, 1% hemolysis at 12 μM, 2% hemolysis at 22 μM, 2% hemolysis at 50 μM, 4% hemolysis at 100 μM against human red blood cells Branched Free Amidation L [Ref.29984236] No cytotoxicity information found Not found 29984236 Biomed Res Int. 2018 Jun 10;2018:5252891 Sandra C. Vega Chaparro, J. Tatiana Valencia Salguero, Diana A. Martínez Baquero, Jaiver E. Rosas Pérez. Effect of Polyvalence on the Antibacterial Activity of a Synthetic Peptide Derived from Bovine Lactoferricin against Healthcare-Associated Infectious Pathogens. DRAMP20866 (RRWQWR)4-K2-(Ahx)2-C2 30 the tetrameric RRWQWR motif peptide molecule No entry found Derived from bovine LfcinB6 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29984236] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=29 μg/ml; MBC=57 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=57 μg/ml; MBC=57 μg/ml);##Gram-negative bacteria: Klebsiella pneumoniae ATCC 13883 (MIC=29 μg/ml; MBC=115 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=57 μg/ml; MBC=115 μg/ml) [Ref.29984236] 5% haemolysis at 5 μM, 10% haemolysis at 12 μM, 10% haemolysis at 22 μM, 0% haemolysis at 50 μM, 2% haemolysis at 100 μM against human red blood cells Branched Free Amidation Disulfide bond which links two dimeric motif peptides L [Ref.29984237] No cytotoxicity information found Not found 29984236 Biomed Res Int. 2018 Jun 10;2018:5252891 Sandra C. Vega Chaparro, J. Tatiana Valencia Salguero, Diana A. Martínez Baquero, Jaiver E. Rosas Pérez. Effect of Polyvalence on the Antibacterial Activity of a Synthetic Peptide Derived from Bovine Lactoferricin against Healthcare-Associated Infectious Pathogens. DRAMP20867 RWQWRWQWR 9 the palindromic RRWQWR motif peptide molecule No entry found Derived from bovine LfcinB6 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29984236] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=74 μg/ml; MBC=148 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=9 μg/ml; MBC=74 μg/ml);##Gram-negative bacteria: Klebsiella pneumoniae ATCC 13883 (MIC=74 μg/ml; MBC=148 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=74 μg/ml; MBC=148 μg/ml) [Ref.29984236] 0% haemolysis at 5 μM, 1% haemolysis at 12 μM, 0% haemolysis at 22 μM, 5% haemolysis at 50 μM, 25% haemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.29984238] No cytotoxicity information found Not found 29984236 Biomed Res Int. 2018 Jun 10;2018:5252891 Sandra C. Vega Chaparro, J. Tatiana Valencia Salguero, Diana A. Martínez Baquero, Jaiver E. Rosas Pérez. Effect of Polyvalence on the Antibacterial Activity of a Synthetic Peptide Derived from Bovine Lactoferricin against Healthcare-Associated Infectious Pathogens. DRAMP20868 KFKKLFKKLSPVIGKEFKRIVERIKRFLR 29 H4 No entry found Derived from BMAP-27 and OP-145 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix The peptide adopts a conformational structure with 90 % alpha helix. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29910626] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=20 μM), Staphylococcus aureus ATCC 33591 (MIC=10 μM), Staphylococcus aureus ATCC 43300 (MIC=10 μM), Staphylococcus aureus ATCC BAA41 (MIC=10 μM), Enterococcus faecalis ATCC 19433 (MIC=15 μM), Enterococcus faecalis ATCC BAA2365 (MIC=5 μM), Staphylococcus epidermidis ATCC 12228 (MIC=10 μM), Enterococcus faecium ATCC BAA2316 (MIC=5 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=10 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=20 μM), Acinetobacter baumannii ATCC 19606 (MIC=10 μM), Klebsiella pneumoniae ATCC 13883 (MIC=2.5 μM), Pseudomonas aeruginosa ATCC BAA2114 (MIC=25 μM), Escherichia coli ATCC BAA2452 (MIC=10 μM) [Ref.29910626] 0% haemolysis at 5 μM, 0% haemolysis at 10 μM, 0% haemolysis at 25 μM, 0% haemolysis at 40 μM, 0% haemolysis at 55 μM, 0% haemolysis at 75 μM, 0% haemolysis at 80 μM, 2.1% haemolysis at 100 μM against human red blood cells Linear Free Free L [Ref.29910626] IC50 = 61.9±0.18 μM against HEK293.## IC50 = 64.9±1.01 μM against Vero. Not found 29910626 Infect Drug Resist. 2018 Jun 1;11:835-847. Almaaytah A, Qaoud MT, Abualhaijaa A, Al-Balas Q, Alzoubi KH. Hybridization and antibiotic synergism as a tool for reducing the cytotoxicity of antimicrobial peptides. DRAMP20869 GLLKRIKTL 9 Pal-ano-9 (Pal-anoplin peptide derivative) No entry found Derived from the peptide Pal-anoplin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. The peptide is palmitoylated. [Ref.29614317] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=0.406 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.406 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=3.25 μg/mL). [Ref.29614317] HC50=18.92μg/mL against human red blood cells Linear Acylation (Gly1 conjugated with a palmitoyl group) Amidation L [Ref.29614317] No cytotoxicity information found Not found 29614317 Peptides. 2018 Jun;104:7-14. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG. Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin. DRAMP20870 GLLKRIKT 8 Pal-ano-8 (Pal-anoplin peptide derivative) No entry found Derived from the peptide Pal-anoplin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Random coil Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. The peptide is palmitoylated. [Ref.29614317] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=1.63 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.25 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=26 μg/mL). [Ref.29614317] HC50=33.74μg/mL against human red blood cells Linear Acylation (Gly1 conjugated with a palmitoyl group) Amidation L [Ref.29614318] No cytotoxicity information found Not found 29614317 Peptides. 2018 Jun;104:7-14. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG. Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin. DRAMP20871 GLLKRIK 7 Pal-ano-7 (Pal-anoplin peptide derivative) No entry found Derived from the peptide Pal-anoplin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Random coil Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. The peptide is palmitoylated. [Ref.29614317] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=0.813 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1.63 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=13 μg/mL). [Ref.29614317] HC50=37.70μg/mL against human red blood cells Linear Acylation (Gly1 conjugated with a palmitoyl group) Amidation L [Ref.29614319] No cytotoxicity information found Not found 29614317 Peptides. 2018 Jun;104:7-14. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG. Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin. DRAMP20872 GLLKRI 6 Pal-ano-6 (Pal-anoplin peptide derivative) No entry found Derived from the peptide Pal-anoplin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. The peptide is palmitoylated. [Ref.29614317] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=0.61 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3.25 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=1.63 μg/mL). [Ref.29614317] HC50=7.51μg/mL against human red blood cells Linear Acylation (Gly1 conjugated with a palmitoyl group) Amidation L [Ref.29614320] No cytotoxicity information found Not found 29614317 Peptides. 2018 Jun;104:7-14. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG. Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin. DRAMP20873 GLLKR 5 Pal-ano-5 (Pal-anoplin peptide derivative) No entry found Derived from the peptide Pal-anoplin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Random coil Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. The peptide is palmitoylated. [Ref.29614317] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=3.25 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=6.5 μg/mL);##Fungi: Candida albicans ATCC 10231 (MIC=13 μg/mL). [Ref.29614317] HC50= 66.12μg/mL against human red blood cells Linear Acylation (Gly1 conjugated with a palmitoyl group) Amidation L [Ref.29614321] No cytotoxicity information found Not found 29614317 Peptides. 2018 Jun;104:7-14. Salas RL, Garcia JKDL, Miranda ACR, Rivera WL, Nellas RB, Sabido PMG. Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin. DRAMP20874 SKVWRHWRRFWHRAHRKL 18 Chensinin-1b No entry found Derived from chensinin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, beta sheet and Random coil The peptide adopts a random coil structure in water and presents an ordered alpha-helix structure with 11.96 % beta-strands and 28.06 % alpha-helices in TFE solution Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Anticancer activities against HeLa cervical carcinoma and MCF-7 breast carcinoma. [Ref.29549839] Gram-positive bacteria: Staphylococcus aureus (MIC=3.13 μM), Bacillus cereus (MIC=3.13 μM), Streptococcus lactis (MIC=3.13 μM), Enterococcus faecalis (MIC=1.56 μM), Enterococcus faecium (MIC=3.13 μM);##Gram-negative bacteria: Escherichia coli (MIC=6.25 μM), Pseudomonas aeruginosa (MIC=1.56 μM);##cancer cells: HeLa cervical carcinoma (IC50=113.10μ±μ4.10 μM), MCF-7 breast carcinoma (IC50=51.85μ±μ0.88 μM) [Ref.29549839] HC50>500 μM against human red blood cells Linear Free Free L [Ref.29549839] No cytotoxicity information found Cell membrane (disrupted the bacterial cell membranes through a 29549839 Eur J Med Chem. 2018 Apr 25;150:546-558. Dong W, Liu Z, Sun L, Wang C, Guan Y, Mao X, Shang D. Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails. DRAMP20875 SKVWRHWRRFWHRAHRKL 18 OA-C1b No entry found Derived from Chensinin-1b Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presents an ordered alpha-helix structure with 12.88 % beta-strands and 47.36 % alpha-helices in TFE solution Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Anticancer activities against HeLa cervical carcinoma, A375 melanoma and MCF-7 breast carcinoma. The peptide is a lipopeptide with CH3(CH2)6CO-. [Ref.29549839] Gram-positive bacteria: Staphylococcus aureus (MIC=3.13 μM), Bacillus cereus (MIC=1.56 μM), Streptococcus lactis (MIC=1.56 μM), Enterococcus faecalis (MIC=1.56 μM), Enterococcus faecium (MIC=1.56 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.13 μM), Pseudomonas aeruginosa (MIC=1.56 μM);##cancer cells: HeLa cervical carcinoma (IC50=23.86μ±μ0.95 μM), A375 melanoma (IC50=50.97μ±μ1.45 μM), MCF-7 breast carcinoma (IC50=34.94μ±μ2.99 μM) [Ref.29549839] HC50>500 μM against human red blood cells Linear Acylation (Ser1 conjugated with octanoic acid) Free L [Ref.29549839] No cytotoxicity information found Not found 29549839 Eur J Med Chem. 2018 Apr 25;150:546-558. Dong W, Liu Z, Sun L, Wang C, Guan Y, Mao X, Shang D. Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails. DRAMP20876 SKVWRHWRRFWHRAHRKL 18 LA-C1b No entry found Derived from Chensinin-1b Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presents an ordered alpha-helix structure with 6.31 % beta-strands and 32.16 % alpha-helices in TFE solution Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Anticancer activities against HeLa cervical carcinoma, A375 melanoma and MCF-7 breast carcinoma. The peptide is a lipopeptide with CH3(CH2)6CO-. [Ref.29549839] Gram-positive bacteria: Staphylococcus aureus (MIC=3.13 μM), Bacillus cereus (MIC=3.13 μM), Streptococcus lactis (MIC=3.13 μM), Enterococcus faecalis (MIC=1.56 μM), Enterococcus faecium (MIC=3.13 μM);##Gram-negative bacteria: Escherichia coli (MIC=6.25 μM), Pseudomonas aeruginosa (MIC=1.56 μM);##cancer cells: HeLa cervical carcinoma (IC50=20.38μ±μ0.28 μM), A375 melanoma (IC50=21.25μ±μ1.51 μM), MCF-7 breast carcinoma (IC50=25.77μ±μ2.02 μM) [Ref.29549839] HC50>500 μM against human red blood cells Linear Acylation (Ser1 conjugated with lauric acid) Free L [Ref.29549839] No cytotoxicity information found Not found 29549839 Eur J Med Chem. 2018 Apr 25;150:546-558. Dong W, Liu Z, Sun L, Wang C, Guan Y, Mao X, Shang D. Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails. DRAMP20877 SKVWRHWRRFWHRAHRKL 18 PA-C1b No entry found Derived from Chensinin-1b Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix, Random coil The peptide adopts a random coil structure in water and presents an ordered alpha-helix structure with 12.88 % beta-strands and 22.67 % alpha-helices in TFE solution Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Anticancer activities against HeLa cervical carcinoma, A375 melanoma and MCF-7 breast carcinoma. The peptide is a lipopeptide with CH3(CH2)6CO-. [Ref.29549839] Gram-positive bacteria: Staphylococcus aureus (MIC=12.5 μM), Bacillus cereus (MIC=6.25 μM), Streptococcus lactis (MIC=3.13 μM), Enterococcus faecalis (MIC= 3.13 μM), Enterococcus faecium (MIC= 6.25 μM);##Gram-negative bacteria: Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=6.25 μM);##cancer cells: HeLa cervical carcinoma (IC50=21.04μ±μ0.18 μM), A375 melanoma (IC50=18.15μ±μ0.21 μM), MCF-7 breast carcinoma (IC50=20.63μ±μ0.47 μM) [Ref.29549839] HC50>500 μM against human red blood cells Linear Acylation (Ser1 conjugated with palmitic acid) Free L [Ref.29549839] No cytotoxicity information found Not found 29549839 Eur J Med Chem. 2018 Apr 25;150:546-558. Dong W, Liu Z, Sun L, Wang C, Guan Y, Mao X, Shang D. Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails. DRAMP20878 MGFGCPEDEYECHNHCKNSVGCRGGYCDAGTLRQRCTCYGCNQKGRSIQE 50 rVpDef No entry found Derived from VpDef ATGGGTTTTGGTTGTCCAGA Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29524591] Gram-positive bacteria: Listeria monocytogenes ATCC 21633 (MIC=75 μg/ml), Bacillu subtilis Lzz-133 (MIC=95 μg/ml), Staphylococcus aureus ATCC 25923 (MIC=120 μg/ml);##Gram-negative bacteria: Escherichia coli O157 ATCC 35150 (MIC=50 μg/ml), Eschericha coli ATCC 10305 (MIC=75 μg/ml), Salmonella enterica ATCC 10467 (MIC=120 μg/ml) [Ref.29524591] 0% haemolysis at 30 μg/ml, 0% haemolysis at 60 μg/ml, 0% haemolysis at 90 μg/ml, 0% haemolysis at 115 μg/ml, 0.2% haemolysis at 145 μg/ml, 1.5% haemolysis at 175 μg/ml against rabbit red blood cells Linear Free Free L [Ref.29524591] No cytotoxicity information found Not found 29524591 Protein Expr Purif. 2018 Jul;147:78-84. Meng DM, Lv YJ, Zhao JF, Liu QY, Shi LY, Wang JP, Yang YH, Fan ZC. Efficient production of a recombinant Venerupis philippinarum defensin (VpDef) in Pichia pastoris and characterization of its antibacterial activity and stability. DRAMP20879 KWKIFKKIEKVGRNVRDGIIKAGPAVQVVGQATSIAK 37 DAN1 A0A212EJN7 Belongs to the cecropin family. KGM_210268 Danaus plexippus (monarch butterfly) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Random coil Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29501691] Gram-positive bacteria: Bacillus subtilis (MIC=131.3μ±μ46.1 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC=4.9μ±μ2.3 μg/mL), Pseudomonas aeruginosa (MIC=7μ±μ0.8 μg/mL), Klebsiella pneumoniae (MIC=16.2μ±μ1.9 μg/mL) [Ref.29501691] 0% haemolysis at 10 μg/ml, 0% haemolysis at 25 μg/ml, 0% haemolysis at 50 μg/ml, 0% haemolysis at 100 μg/ml, 0% haemolysis at 200 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.29501691] No cytotoxicity information found Not found 29501691 Peptides. 2018 May;103:26-30. doi: 10.1016/j.peptides.2018.01.017. Duwadi D, Shrestha A, Yilma B, Kozlovski I, Sa-Eed M, Dahal N, Jukosky J. Identification and screening of potent antimicrobial peptides in arthropod genomes. DRAMP20880 RWKFLKKIEKVGRKVRDGVIKAGPAVGVVGQATSIYK 37 DAN2 A0A212F3T6 Belongs to the cecropin family. KGM_210265 Monarch butterfly (Danaus plexippus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Random coil Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29501691] Gram-positive bacteria: Bacillus subtilis (MIC=50μ±μ19 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC=2.1μ±μ0.7 μg/mL), Pseudomonas aeruginosa (MIC=5μ±μ2.5 μg/mL), Klebsiella pneumoniae (MIC=4.3μ±μ1.4 μg/mL);##Fungi: Candida albicans (MIC=72.5μ±μ35.2 μg/mL) [Ref.29501691] 0% haemolysis at 10 μg/ml, 0% haemolysis at 25 μg/ml, 0% haemolysis at 50 μg/ml, 0% haemolysis at 100 μg/ml, 0% haemolysis at 200 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.29501691] No cytotoxicity information found Not found 29501691 Peptides. 2018 May;103:26-30. doi: 10.1016/j.peptides.2018.01.017. Duwadi D, Shrestha A, Yilma B, Kozlovski I, Sa-Eed M, Dahal N, Jukosky J. Identification and screening of potent antimicrobial peptides in arthropod genomes. DRAMP20881 VTCDLLSAEAKGVKVNHAACAAHCLLKRKRGGYCNKRRICVCRN 44 HOLO1 D6X2G2 Derived from defensin-like peptides Not found Red flour beetle (Tribolium castaneum) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity against Candida albicans. [Ref.29501691] Gram-positive bacteria: Staphylococcus aureus (MIC=13.2μ±μ1.8 μg/mL), Bacillus subtilis (MIC=6μ±μ1.8 μg/mL);##Fungi: Candida albicans (MIC=4.6μ±μ1.1 μg/mL) [Ref.29501691] 0% haemolysis at 10 μg/ml, 0% haemolysis at 25 μg/ml, 0% haemolysis at 50 μg/ml, 0% haemolysis at 100 μg/ml, 0% haemolysis at 200 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.29501691] No cytotoxicity information found Not found 29501691 Peptides. 2018 May;103:26-30. doi: 10.1016/j.peptides.2018.01.017. Duwadi D, Shrestha A, Yilma B, Kozlovski I, Sa-Eed M, Dahal N, Jukosky J. Identification and screening of potent antimicrobial peptides in arthropod genomes. DRAMP20882 ATCDLLSASTPWGSLNHSACAAHCLTKRYKGGRCRNGICRCRR 43 LOUDEF1 E0VPU4 Derived from defensin-like peptides 8233460 Phum_PHUM365 Human body louse (Pediculhumanus humanus) Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity Candida albicans. [Ref.29501691] Gram-positive bacteria: Staphylococcus aureus (MIC=35μ±μ1.3 μg/mL), Bacillus subtilis (MIC=7μ±μ1.6 μg/mL);##Fungi: Candida albicans (MIC= 19.1μ±μ9.6 μg/mL) [Ref.29501691] 0% haemolysis at 10 μg/ml, 0% haemolysis at 25 μg/ml, 0% haemolysis at 50 μg/ml, 0% haemolysis at 100 μg/ml, 0% haemolysis at 200 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.29501691] No cytotoxicity information found Not found 29501691 Peptides. 2018 May;103:26-30. Duwadi D, Shrestha A, Yilma B, Kozlovski I, Sa-Eed M, Dahal N, Jukosky J. Identification and screening of potent antimicrobial peptides in arthropod genomes. DRAMP20883 KRFKKFFRKLKKSVKKRKKEFKKKPRVIKVSIPF 34 Cath-A No entry found Derived from three-finger toxin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29392557] Gram-positive bacteria: MRSA PS-2 (MIC=64 μg/ml);##Gram-negative bacteria, MRSA PS-7 (MIC=64 μg/ml), MRSA PS-18 (MIC=32 μg/ml), MRSA PS-45 (MIC=32 μg/ml), MRSA PS-46 (MIC=32 μg/ml), MRSA PS-50 (MIC=32 μg/ml), MRSA PS-59 (MIC=64 μg/ml), MRSA PS-70 (MIC=32 μg/ml), MRSA PS-84 (MIC=128 μg/ml), MRSA PS-106 (MIC=32 μg/ml), MRSA PS-131 (MIC=128 μg/ml), MRSA PS-139 (MIC=32 μg/ml), MRSA PS-162 (MIC=128 μg/ml), MRSA PS-165 (MIC=32 μg/ml), Staphylococcus aureus ATCC 25923 (MIC=32 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=128 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli ATCC 51446 (MIC=16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=64 μg/ml), Klebsiella pneumoniae ATCC 13883 (MIC=16 μg/ml) [Ref.29392557] 0% haemolysis at 1.0 μg/ml, 0% haemolysis at 2.0 μg/ml, 0% haemolysis at 4.0 μg/ml, 0% haemolysis at 8.0 μg/ml, 0% haemolysis at 16.0 μg/ml, 0% haemolysis at 31.2 μg/ml, 2% haemolysis at 62.5 μg/ml, 4% haemolysis at 125.0 μg/ml, 15% haemolysis at 250.0 μg/ml, 23% haemolysis at 500.0 μg/ml, 53% haemolysis at 1000.0 μg/ml against human red blood cells Linear Free Free L [Ref.29392557] The cell viability of HUVEC is 132%, 99% and 79% at peptide concentrations of 35.5, 71 and 113 μg/ml .## The cell viability of H9c2is 129%, 97%, and 80% at peptide concentrations of 35.5, 71, and 113 μg/ml . Not found 29392557 J Microbiol. 2018 Feb;56(2):128-137. Tajbakhsh M, Karimi A, Tohidpour A, Abbasi N, Fallah F, Akhavan MM. The antimicrobial potential of a new derivative of cathelicidin from Bungarus fasciatus against methicillin-resistant Staphylococcus aureus. DRAMP20884 KRFKKFFRKLKKSVKKRKKEFKKKPRVIGVSIPF 34 Cath-B No entry found Derived from three-finger toxin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29392557] Gram-positive bacteria: MRSA PS-2 (MIC=256 μg/ml);##Gram-negative bacteria, MRSA PS-7 (MIC=32 μg/ml), MRSA PS-18 (MIC=128 μg/ml), MRSA PS-45 (MIC=64 μg/ml), MRSA PS-46 (MIC=128 μg/ml), MRSA PS-50 (MIC=128 μg/ml), MRSA PS-59 (MIC=32 μg/ml), MRSA PS-84 (MIC=128 μg/ml), MRSA PS-131 (MIC=64 μg/ml), MRSA PS-139 (MIC=64 μg/ml), MRSA PS-162 (MIC=256 μg/ml), MRSA PS-165 (MIC=128 μg/ml), Staphylococcus aureus ATCC 25923 (MIC=32 μg/ml), Staphylococcus aureus ATCC 33591 (MIC=256 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 μg/ml), Escherichia coli ATCC 51446 (MIC=8 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=32 μg/ml), Klebsiella pneumoniae ATCC 13883 (MIC=8 μg/ml) [Ref.29392557] 0% haemolysis at 1.0 μg/ml, 0% haemolysis at 2.0 μg/ml, 0% haemolysis at 4.0 μg/ml, 0% haemolysis at 8.0 μg/ml, 3% haemolysis at 16.0 μg/ml, 3% haemolysis at 31.2 μg/ml, 3% haemolysis at 62.5 μg/ml, 3% haemolysis at 125.0 μg/ml, 3% haemolysis at 250.0 μg/ml, 4% haemolysis at 500.0 μg/ml, 5% haemolysis at 1000.0 μg/ml against human red blood cells Linear Free Free L [Ref.29392557] The cell viability of HUVEC is 118%, 100% and 75% at peptide concentrations of 35.5 μg/ml, 71 μg/ml and 113 μg/ml.## The cell viability of H9c2 is 123%, 97%, and 88% at peptide concentrations of 35.5, 71, and 113 μg/ml. Not found 29392557 J Microbiol. 2018 Feb;56(2):128-137. Tajbakhsh M, Karimi A, Tohidpour A, Abbasi N, Fallah F, Akhavan MM. The antimicrobial potential of a new derivative of cathelicidin from Bungarus fasciatus against methicillin-resistant Staphylococcus aureus. DRAMP20885 ILKKLWEGVKSI 12 Hp1404-T1a No entry found Derived from Hp1404 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and adopts a random coil conformation in the presence of all liposome types . Function: Antibacterial activity against the Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa 431 (MIC=25 μM), Pseudomonas aeruginosa 434 (MIC=25 μM), Pseudomonas aeruginosa 3399 (MIC=25 μM), Pseudomonas aeruginosa 3592 (MIC=12.5 μM), Pseudomonas aeruginosa 3904 (MIC=25 μM), Pseudomonas aeruginosa 4891 (MIC=25 μM), Pseudomonas aeruginosa 671973 (MIC=25 μM) [Ref.29379033] Hp1404-T1a does not induce substantial hemolysis, even at the high tested concentration (200μμM) against mouse red blood cells Linear Free Amidation L [Ref.29379033] No cytotoxicity information found Lipopolysaccharide (LPS)-binding 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20886 ILKKLLEGVKSI 12 Hp1404-T1b No entry found Derived from Hp1404 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and adopts a random coil conformation in the presence of all liposome types . Function: Antibacterial activity against the Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa 434 (MIC=25 μM), Pseudomonas aeruginosa 3592 (MIC=25 μM) [Ref.29379033] Hp1404-T1b does not induce substantial hemolysis, even at the high tested concentration (200μμM) against mouse red blood cells Linear Free Amidation L [Ref.29379033] No cytotoxicity information found Lipopolysaccharide (LPS)-binding 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20887 KLIPILSKTIPAGKNLFYKI 20 NCP-2 (CTX-1 peptide derivative) No entry found Derived from CTX-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The peptide adopts a conformational structure with 20 % alpha helix, 25 % beta sheet and 35 % random coil in the presence of DMPE-DMPG mixed vesicles. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29364903] Gram-positive bacteria: Staphylococcus aureus ATCC 22953 (MBC=50 μg/ml), Streptococcus agalactiae ATCC 13813 (MBC=12.5 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MBC=12.5 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MBC=12.5 μg/ml), Acinetobacter baumannii (herpetological, cloacal) (MBC=1.6 μg/ml), Acinetobacter baumannii (ornithological, cloacal) (MBC=50 μg/ml), Acinetobacter baumannii (human, urinary) (MBC=1.6 μg/ml), Moraxella catarrhalis ATCC 25238 (MBC=1.6 μg/ml);##Fungi: Candida albicans ATCC 10231 (MBC=50 μg/mL), Malassezia pachydermatis DSMZ 6172 (MBC=6.3 μg/mL) [Ref.29364903] 2% haemolysis at 12.5 μg/ml, 8% haemolysis at 100.0 μg/ml against sheep red blood cells Linear Free Free L [Ref.29364903] The cell death rate of Madin-Darby Bovine Kidney(MDBK) cells is 3 % and 5% at peptide concentrations of 12.5 and 100 μg/ml Not found 29364903 PLoS One. 2018 Jan 24;13(1):e0190778. Sala A, Cabassi CS, Santospirito D, Polverini E, Flisi S, Cavirani S, Taddei S. Novel Naja atra cardiotoxin 1 (CTX-1) derived antimicrobial peptides with broad spectrum activity. DRAMP20888 KLIWILSKTIPAGKNLFYKI 20 NCP-3 (CTX-1 peptide derivative) No entry found Derived from CTX-1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The peptide adopts a conformational structure with 43 % beta sheet and 35 % random coil in the presence of DMPE-DMPG mixed vesicles. Function: Antimicrobial activity against the Gram-positive bacteria, Gram-negative bacteria and fungi. NCP-3 completely inhibits the viral activity of BoHV-1 on MDBK cells at the concentration of 25 [Ref.29364903] Gram-positive bacteria: Methicillin-resistant Staphylococcus aureus ATCC 43300 (MBC=6.3 μg/ml), Staphylococcus aureus ATCC 22953 (MBC=1.6 μg/ml), Enterococcus hirae ATCC 10541 (MBC=1.6 μg/ml), Streptococcus agalactiae ATCC 13813 (MBC=1.6 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MBC=12.5 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MBC=12.5 μg/ml), Acinetobacter baumannii (herpetological, cloacal) (MBC=1.6 μg/ml), Acinetobacter baumannii (ornithological, cloacal) (MBC=6.3 μg/ml), Acinetobacter baumannii (human, urinary) (MBC=1.6 μg/ml), Klebsiella pneumoniae subsp. pneumoniae (herpetological, cloacal) (MBC=50 μg/ml), Enterobacter cloacae (herpetological, cloacal) (MBC=25 μg/ml), Burkholderia cepacia ATCC 17759 (MBC=50 μg/ml), Moraxella catarrhalis ATCC 25238 (MBC=1.6 μg/ml);##Fungi: Candida albicans ATCC 10231 (MBC=12.5 μg/mL), Candida glabrata ATCC 90030 (MBC=50 μg/mL), Malassezia pachydermatis DSMZ 6172 (MBC=6.3 μg/mL). [Ref.29364903] 3% haemolysis at 12.5 μg/ml, 9% haemolysis at 100.0 μg/ml against sheep red blood cells Linear Free Free L [Ref.29364903] The cell death rate of Madin-Darby Bovine Kidney(MDBK) cells is 3 % and 7% at peptide concentrations of 12.5 and 100 μg/ml Not found 29364903 PLoS One. 2018 Jan 24;13(1):e0190778. Sala A, Cabassi CS, Santospirito D, Polverini E, Flisi S, Cavirani S, Taddei S. Novel Naja atra cardiotoxin 1 (CTX-1) derived antimicrobial peptides with broad spectrum activity. DRAMP20889 VYPFMWGGAYCFCKAKLV 18 VT18-KKLV (VT18 peptide derivative) No entry found Derived from VT18 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Double-stranded Not found Function: Antibacterial activity against the Gram-positive bacteria. [Ref.29277569] Gram-positive bacteria: Streptococcus pneumoniae ATCC 700669 (MIC=52 μg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=105 μg/ml), Streptococcus pneumoniae ATCC 700677 (MIC=76 μg/ml) [Ref.29277569] 0.5% hemolysis at 5 μg/ml, 1.0% hemolysis at 10μg/ml, 2.0% hemolysis at 20 μg/ml, 2.5% hemolysis at 50 μg/ml, 3.0% hemolysis at 100 μg/ml, 5.0% hemolysis at 250 μg/ml, 7.0% hemolysis at 500 μg/ml against human red blood cells Linear Free Amidation L [Ref.29277569] The cell viability of NL-20 normal lung cell line is not affected (<20%) below 50 μg/ml.## The cell viability of NL-20 is 82%, 44%, 17% and 13% at peptide concentrations of 50, 100, 250 and 500 μg/ml. Not found 29277569 Biochimie. 2018 Mar;146:139-147. Yang R, Zhang G, Zhang F, Li Z, Huang C. Membrane permeabilization design of antimicrobial peptides based on chikungunya virus fusion domain scaffold and its antibacterial activity against gram-positive Streptococcus pneumoniae in respiratory infection. DRAMP20890 VYPFCWGGAYAFCKAKLV 18 VT18-CAKKLV (VT18 peptide derivative) No entry found Derived from VT18 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Double-stranded Not found Function: Antibacterial activity against the Gram-positive bacteria. [Ref.29277569] Gram-positive bacteria: Streptococcus pneumoniae ATCC 700669 (MIC=58 μg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=90 μg/ml), Streptococcus pneumoniae ATCC 700677 (MIC=72 μg/ml) [Ref.29277569] 0.5% hemolysis at 5 μg/ml, 1.0% hemolysis at 10μg/ml, 1.5% hemolysis at 20 μg/ml, 2.0% hemolysis at 50 μg/ml, 3.8% hemolysis at 100 μg/ml, 4.5% hemolysis at 250 μg/ml, 6.8% hemolysis at 500 μg/ml against human red blood cells Linear Free Amidation L [Ref.29277569] The cell viability of NL-20 normal lung cell line is not affected (<20%) below 50 μg/ml.## The cell viability of NL-20 is 86%, 48%, 19% and 11% at peptide concentrations of 50, 100, 250 and 500 μg/ml. Not found 29277569 Biochimie. 2018 Mar;146:139-147. Yang R, Zhang G, Zhang F, Li Z, Huang C. Membrane permeabilization design of antimicrobial peptides based on chikungunya virus fusion domain scaffold and its antibacterial activity against gram-positive Streptococcus pneumoniae in respiratory infection. DRAMP20891 VYPFCWGGAYAFCKAKLV 18 cVT18-CAKKLV (VT18 peptide derivative) No entry found Derived from VT18 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Double-stranded Not found Function: Antibacterial activity against the Gram-positive bacteria. The positions 4 and 13 of cVT18-CAKKLV have a disulfide bond to form a cyclic peptide. [Ref.29277569] Gram-positive bacteria: Streptococcus pneumoniae ATCC 700669 (MIC=35 μg/ml), Streptococcus pneumoniae ATCC 49619 (MIC=67 μg/ml), Streptococcus pneumoniae ATCC 700677 (MIC=49 μg/ml) [Ref.29277569] 0.5% hemolysis at 5 μg/ml, 0.5% hemolysis at 10 μg/ml, 0.6% hemolysis at 20 μg/ml, 1.0% hemolysis at 50 μg/ml, 1.9% hemolysis at 100 μg/ml, 2.5% hemolysis at 250 μg/ml, 3.5% hemolysis at 500 μg/ml against human red blood cell Cyclic Free Amidation Disulfide bond between Cys5 and Cys13. L [Ref.29277569] The cell viability of NL-20 normal lung cell line is not affected (<20%) below 50 μg/ml.## The cell viability of NL-20 is 81%, 73%, 34% and 19% at peptide concentrations of 50, 100, 250 and 500 μg/ml. Not found 29277569 Biochimie. 2018 Mar;146:139-147. Yang R, Zhang G, Zhang F, Li Z, Huang C. Membrane permeabilization design of antimicrobial peptides based on chikungunya virus fusion domain scaffold and its antibacterial activity against gram-positive Streptococcus pneumoniae in respiratory infection. DRAMP20892 FIAAIIGGLFSAGKAIHRLIRRRRR 25 H3A/H4A No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=32 μg/ml; MBC=32 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=128 μg/ml; MBC=256 μg/ml);##Fungi: Candida albicans (MIC=512 μg/ml; MBC=512 μg/ml) [Ref.29040295] 7% haemolysis at 1.56 μg/ml, 10% haemolysis at 3.13 μg/ml, 70% haemolysis at 6.25 μg/ml, 95% haemolysis at 12.50 μg/ml, 98% haemolysis at 25.00 μg/ml, 100% haemolysis at 50.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20893 FIHHIIGGLFSAGKAAHRLIRRRRR 25 I16A No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=64 μg/ml; MBC=128 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=64 μg/ml; MBC=512 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 10% haemolysis at 6.25 μg/ml, 20% haemolysis at 12.50 μg/ml, 35% haemolysis at 25.00 μg/ml, 80% haemolysis at 50.00 μg/ml, 95% haemolysis at 100.00 μg/ml, 100% haemolysis at 200.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20894 FIHHIIGGLFSAGKAIHRHHRRRRR 25 L19H/I20H No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=128 μg/ml; MBC=512 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 10% haemolysis at 6.25 μg/ml, 13% haemolysis at 12.50 μg/ml, 16% haemolysis at 25.00 μg/ml, 40% haemolysis at 50.00 μg/ml, 85% haemolysis at 100.00 μg/ml, 100% haemolysis at 200.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20895 AAHHIIGGLFSAGKAIHRLIRRRRR 25 F1A/I2A No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found 5H2S Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=128 μg/ml; MBC=256 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC=256 μg/ml);##Fungi: Candida albicans (MIC=64 μg/ml; MBC=128 μg/ml) [Ref.29040295] 10% haemolysis at 12.50 μg/ml, 15% haemolysis at 25.00 μg/ml, 30% haemolysis at 50.00 μg/ml, 90% haemolysis at 100.00 μg/ml, 95% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20896 FIHHIIGGAASAGKAIHRLIRRRRR 25 L9A/F10A No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity. [Ref.29040295] Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 5% haemolysis at 25.00 μg/ml, 10% haemolysis at 50.00 μg/ml, 30% haemolysis at 100.00 μg/ml, 95% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml, 100% haemolysis at 800.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20897 FIHHIIGGLFSAGKARHRLIRRRRR 25 I16R No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity. [Ref.29040295] Fungi: Candida albicans (MIC=128 μg/ml; MBC=256 μg/ml) [Ref.29040295] 10% haemolysis at 25.00 μg/ml, 20% haemolysis at 50.00 μg/ml, 30% haemolysis at 100.00 μg/ml, 75% haemolysis at 200.00 μg/ml, 95% haemolysis at 400.00 μg/ml, 100% haemolysis at 800.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20898 FIHHIIGGLFSAGKAEHRLIRRRRR 25 I16E No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antifungal Synthetic Not found Not found Function: Antifungal activity. [Ref.29040295] Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 5% haemolysis at 25.00 μg/ml, 15% haemolysis at 50.00 μg/ml, 40% haemolysis at 100.00 μg/ml, 65% haemolysis at 200.00 μg/ml, 85% haemolysis at 400.00 μg/ml, 90% haemolysis at 800.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20899 FIHHAAGGLFSAGKAIHRLIRRRRR 25 I5A/I6A No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-negative bacteria: Pseudomonas aeruginosa (MIC=512 μg/ml; MBC=512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 5% haemolysis at 25.00 μg/ml, 7% haemolysis at 50.00 μg/ml, 10% haemolysis at 100.00 μg/ml, 40% haemolysis at 200.00 μg/ml, 80% haemolysis at 400.00 μg/ml, 100% haemolysis at 800.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20900 FIHHIIGGLFSIGKIIHRLIRRRRR 25 A12I/A15I No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=16 μg/ml; MBC=64 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=64 μg/ml; MBC=256 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=512 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 0% haemolysis at 0.20 μg/ml, 5% haemolysis at 0.39 μg/ml, 25% haemolysis at 0.78 μg/ml, 85% haemolysis at 1.56 μg/ml, 95% haemolysis at 3.13 μg/ml, 100% haemolysis at 6.25 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20901 FIHHIIGGLFSVGKHIHRLIRRRRR 25 A12V/A15H No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=16 μg/ml; MBC=16 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=32 μg/ml; MBC=64 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=128 μg/ml; MBC=128 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 0% haemolysis at 0.78 μg/ml, 10% haemolysis at 1.56 μg/ml, 55% haemolysis at 3.13 μg/ml, 85% haemolysis at 6.25 μg/ml, 98% haemolysis at 12.50 μg/ml, 100% haemolysis at 25.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20902 FIHHIIGGLFSVGKHIHSLIHRRRR 25 VHSH No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Not found Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=16 μg/ml; MBC=16 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=16 μg/ml; MBC=32 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 5% haemolysis at 1.56 μg/ml, 5% haemolysis at 3.13 μg/ml, 10% haemolysis at 6.25 μg/ml, 35% haemolysis at 12.50 μg/ml, 55% haemolysis at 25.00 μg/ml, 85% haemolysis at 50.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20903 FIHHIIGGLFSAGKAIHRLIRRR 23 dC2 No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=16 μg/ml; MBC=32 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=32 μg/ml; MBC=32 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=512 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 2% haemolysis at 3.13 μg/ml, 5% haemolysis at 6.25 μg/ml, 25% haemolysis at 12.50 μg/ml, 65% haemolysis at 25.00 μg/ml, 90% haemolysis at 50.00 μg/ml, 100% haemolysis at 100.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20904 FIHHIIGGLFSAGKAIHSLIHRRRR 25 R18S/R21H No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=32 μg/ml; MBC=64 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=32 μg/ml; MBC=32 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC=512 μg/ml);##Fungi: Candida albicans (MIC=256 μg/ml; MBC=512 μg/ml) [Ref.29040295] 8% haemolysis at 6.25 μg/ml, 10% haemolysis at 12.50 μg/ml, 15% haemolysis at 25.00 μg/ml, 40% haemolysis at 50.00 μg/ml, 80% haemolysis at 100.00 μg/ml, 100% haemolysis at 200.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20905 FIHHIIGGLFSAGKAIHRLIR 21 dC4 No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=64 μg/ml; MBC=128 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=256 μg/ml; MBC=256 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=256 μg/ml) [Ref.29040295] 5% haemolysis at 12.50 μg/ml, 10% haemolysis at 25.00 μg/ml, 45% haemolysis at 50.00 μg/ml, 80% haemolysis at 100.00 μg/ml, 100% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20906 HHIIGGLFSAGKAIHRLIRRRRR 23 dN2 No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=512 μg/ml; MBC=512 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=512 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml) [Ref.29040295] 5% haemolysis at 12.50 μg/ml, 5% haemolysis at 25.00 μg/ml, 20% haemolysis at 50.00 μg/ml, 65% haemolysis at 100.00 μg/ml, 90% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20907 IIGGLFSAGKAIHRLIRRRRR 21 dN4 No entry found Derived from TP4 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=128 μg/ml; MBC=128 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=64 μg/ml; MBC=256 μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC>512 μg/ml);##Fungi: Candida albicans (MIC=64 μg/ml; MBC=128 μg/ml) [Ref.29040295] 10% haemolysis haemolysis at 12.50 μg/ml, 12% haemolysis haemolysis at 25.00 μg/ml, 20% haemolysis haemolysis at 50.00 μg/ml, 35% haemolysis haemolysis at 100.00 μg/ml, 75% haemolysis haemolysis at 200.00 μg/ml, 100% haemolysis haemolysis at 400.00 μg/ml, 100% haemolysis haemolysis at 800.00 μg/ml against mouse red blood cells Linear Free Free L [Ref.29040295] No cytotoxicity information found Not found 29040295 PLoS One. 2017 Oct 17;12(10):e0186442. Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD. Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. DRAMP20908 FLHFLHHLF 9 Ctry2459-H3 (Ctry2459 peptide derivative, His-rich) No entry found Derived from the peptide Ctry2459 Not found Synthetic construct(from a scorpion venom peptide library) Antimicrobial, Antiviral Synthetic Not found Not found Function: Inhibits hepatitis C virus(HCV) infection via inactivating infectious viral particle. However, it cannot suppress established infection because of the poor cellular uptake and restriction of endosomes. [Ref.23415044] Virus: Hepatitis C virus ( EC50 = 0.85 μg/ml ).##Cytotoxic: Huh7.5.1 cells (CC50>500 μg/ml) [Ref.23415044] HC50 = 416.4 μg/ml against human red blood cells. Linear Free Amidation L [Ref.23415044] CC50>500 μg/ml against Huh7.5.1 cells Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP20909 FLGFLHHLF 9 Ctry2459-H2 (Ctry2459 peptide derivative, His-rich) No entry found Derived from the peptide Ctry2460 Not found Synthetic construct( from a scorpion venom peptide library) Antimicrobial, Antiviral Synthetic Not found Not found Function: Inhibits hepatitis C virus(HCV) infection via inactivating infectious viral particle. However, it cannot suppress established infection because of the poor cellular uptake and restriction of endosomes. [Ref.23415044] Virus: Hepatitis C virus ( EC50 = 1.08 μg/ml ).##Cytotoxic: Huh7.5.1 cells (CC50>500 μg/ml) [Ref.23415044] HC50 = 203.3 μg/ml against human red blood cells. Linear Free Amidation L [Ref.23415044] CC50>500 μg/ml against Huh7.5.1 cells Not found 23415044 Biomaterials. 2013 Apr;34(13):3511-22. Hong W, Zhang R, Di Z, He Y, Zhao Z, Hu J, Wu Y, Li W, Cao Z. Design of histidine-rich peptides with enhanced bioavailability and inhibitory activity against hepatitis C virus. DRAMP20910 FLGGLIKPWWPWRR 14 RN7-IN7(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=31.25μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=62.5μg/ml), Acinetobacter baumanii ATCC 15308(MIC=125μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=31.25-62.5μg/ml), Staphylococcus aureus ATCC 25923(MIC=31.25μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=31.25μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] The hemolytic activities of RN7-IN7 is 0.0% at 15.62μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 62.5 μg/ml. The cell viability of NL-20 is 95%, 92% and 6% at peptide concentrations of 62.5, 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected( Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20911 CMSTRGDQARKICE 14 Sm-AMP-X2 U4N938 Belongs to the sm-amp-x Stellaria media (Common chickweed) Antimicrobial, Antifungal protein level Not found Not found Function: The mature peptide has antifungal activities [Ref.24081691] Fungus: Alternaria alternata(IC50>32.0μM), Aspergillus niger(IC50=16.9±1.9μM), Bipolaris sorokiniana(IC50>32.0μM), Botrytis cinerea(IC50>32.0μM), Fusarium oxysporum(IC50=25.0±3.0μM), Fusarium solani(IC50=22.5±3.1μM), Phytophthora infestans(IC50>32.0μM), Pythium ultimum(IC50>32.0μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys1 and Cys13 L [Ref.24081691] No cytotoxicity information found Not found 24081691 Plant Mol Biol. 2014 Jan;84(1-2):189-202. doi: 10.1007/s11103-013-0127-z. Epub 2013 Oct 1. Slavokhotova AA, Rogozhin EA, Musolyamov AK, Andreev YA, Oparin PB, Berkut AA, Vassilevski AA, Egorov TA, Grishin EV, Odintsova TI. Novel antifungal DRAMP20912 FLGGLIKKWPWWPWRR 16 RN7-IN9(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=7.81μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=31.25μg/ml), Acinetobacter baumanii ATCC 15308(MIC=31.25μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=7.81–15.62μg/ml), Staphylococcus aureus ATCC 25923(MIC=7.81μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=7.81μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] The hemolytic activities of RN7-IN7 is 0.0% at 15.62μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 31.25 μg/ml. The cell viability of NL-20 is 51%, 13% and 7% at peptide concentrations of 62.5, 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20913 AIHDILKYGKPS 12 Myxinidin (G1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC =10 microM), S. Salmonella typhimurium (MIC =3 microM), Klebsiella pneumoniae (MIC >50 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 3%, 5% and 10% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20914 GAHDILKYGKPS 12 Myxinidin (I2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC >50 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =30 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 6%, 6.6% and 15.5% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20915 GIADILKYGKPS 12 Myxinidin (H3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC =15 microM), S. Salmonella typhimurium (MIC =10 microM), Klebsiella pneumoniae (MIC =30 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =20 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 4.9%,12% and 20% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20916 GIHAILKYGKPS 12 Myxinidin (D4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC =30 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =5 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 10%, 29.9% and 34.9% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20917 GIHDALKYGKPS 12 Myxinidin (I5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =20 microM), Pseudomonas aeruginosa (MIC =10 microM), S. Salmonella typhimurium (MIC =4 microM), Klebsiella pneumoniae (MIC =20 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =20 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 4%, 11.7% and 20% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M1, Finamore E2, Mignogna E2, Falanga A3, Nicoletti GF4, Pedone C3, Morelli G3, Leone M5, Galdiero M6, Galdiero S7. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20918 GIHDIAKYGKPS 12 Myxinidin (L6) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC =20 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =5 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 8%, 19.9% and 29.9% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20919 GIHDILAYGKPS 12 Myxinidin (K7) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.2495783[Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =15 microM), Pseudomonas aeruginosa (MIC =15 microM), S. Salmonella typhimurium (MIC =15 microM), Klebsiella pneumoniae (MIC =20 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 2%, 5.7% and 14% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20920 GIHDILKAGKPS 12 Myxinidin (Y8) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =20 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC =20 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 3% and 10% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20921 GIHDILKYAKPS 12 Myxinidin (G9) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative[Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =5 microM), Pseudomonas aeruginosa (MIC =15 microM), S. Salmonella typhimurium (MIC =10 microM), Klebsiella pneumoniae (MIC =10 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 0.7%, 4.9% and 15% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20922 GIHDILKYGAPS 12 Myxinidin (K10) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =15 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC =10 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =20 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 2%, 7% and 12% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20923 GIHDILKYGKAS 12 Myxinidin (P11) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC =30 microM), S. Salmonella typhimurium (MIC =10 microM), Klebsiella pneumoniae (MIC =30 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 4.9%, 12% and 9.9% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20924 GIHDILKYGKPA 12 Myxinidin (S12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC >50 microM), Pseudomonas aeruginosa (MIC >50 microM), S. Salmonella typhimurium (MIC >50 microM), Klebsiella pneumoniae (MIC =30 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC >50 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] The toxicity of the peptide against Vero cells is 0.7%, 0.7%, 7%, 14.9% and 19.9% at peptide concentrations of 1, 20, 50, 100 and 200 μM. Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20925 GIRDILKYGKPS 12 MH3R No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-nagative and Gram-positive bacteria. [Ref.24957834] Gram-negative bacteria: Escherichia coli (MIC =5 microM), Pseudomonas aeruginosa (MIC =20 microM), S. Salmonella typhimurium (MIC =5 microM), Klebsiella pneumoniae (MIC =5 microM) ;## Gram-positive bacteria: Staphylococcus aureus (MIC =10 microM) [Ref.24957834] Some peptides at 50 μM led to about 10% hemolysis against human red blood cells, but in general, negligible hemolytic activity is observed even at 100 μM and 200 μM peptide. Linear Free Amidation L [Ref.24957834] No cytotoxicity information found Not found 24957834 Antimicrob Agents Chemother. 2014 Sep;58(9):5280-90. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, Morelli G, Leone M, Galdiero M, Galdiero S. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. DRAMP20926 LLPWKWPWWKWRR 13 IN1(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=31.25μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=31.25μg/ml), Acinetobacter baumanii ATCC 15308(MIC>250μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=31.25–62.5μg/ml), Staphylococcus aureus ATCC 25923(MIC=31.25μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=31.25μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] The hemolytic activities of IN1 is 3.6% at 250μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 62.5 μg/ml. The cell viability of NL-20 is 37% and 17% at peptide concentrations of 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected (<10%) bel Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20927 RRPWRWPWWPWRR 13 IN2(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=31.25μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=31.25μg/ml), Acinetobacter baumanii ATCC 15308(MIC>250μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=31.25–62.5μg/ml), Staphylococcus aureus ATCC 25923(MIC=31.25μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=31.25μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] IN2 showed 15.39% hemolytic activity at concentration of 250μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 62.5 μg/ml. The cell viability of NL-20 is 40% and 19% at peptide concentrations of 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected (<10%) bel Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20928 RRPWRWPRWPWRR 13 IN3(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=31.25μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=31.25μg/ml), Acinetobacter baumanii ATCC 15308(MIC>250μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=62.5μg/ml), Staphylococcus aureus ATCC 25923(MIC=31.25μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=62.5μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] The hemolytic activities of IN3 is 2.39% at 250μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 62.5 μg/ml. The cell viability of NL-20 is 93% and 26% at peptide concentrations of 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected (<10%) bel Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20929 FLGGLIKWWPWRR 13 RN7-IN6(designed based on indolicidin and ranalexin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Exhibits antimicrobial activity against the Gram-positive and Gram-negative bacteria. [Ref.26046345] Gram-negative bacteria: Escherichia coli ATCC 25922(MIC=7.81μg/ml), Pseudomonas aeruginosa ATCC 15442(MIC=31.25μg/ml), Acinetobacter baumanii ATCC 15308(MIC>31.25μg/ml), citrobacter spp(MIC>250μg/ml), Klebsiella pneumoniae(MIC>250μg/ml) ;## Gram-positive bacteria: Streptococcus pneumoniae(30 clinical isolates)(MIC=7.81–15.62μg/ml), Staphylococcus aureus ATCC 25923(MIC=7.81μg/ml), Methicillin resistant Staphylococcus aureus (MRSA)(MIC=7.81μg/ml), Enterococcus cloacae(MIC>250μg/ml), [Ref.26046345] The hemolytic activities of RN7-IN6 is 0.0% at 15.62μg/ml against human RBCs. Linear Free Amidation L [Ref.26046345] The cell viability of NL-20 cell line is not affected (<10%) below 31.25 μg/ml. The cell viability of NL-20 is 70%, 6% and 8% at peptide concentrations of 62.5, 125 and 250 μg/ml.## The cell viability of WRL-68 cell line is not affected Not found 26046345 PLoS One. 2015 Jun 5;10(6):e0128532. Jindal HM, Le CF, Mohd Yusof MY, Velayuthan RD, Lee VS, Zain SM, Isa DM, Sekaran SD. Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae. DRAMP20930 KKLFKKILKYLA 12 BP100-Ala-NH-C16H33 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29750913] Gram-negative bacteria:Escherichia coli(ATCC 25922)(MIC=16μM);##Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=8μM);Bacillus subtilis(PY79)(MIC=8μM) [Ref.29750913] C50 =6.3μM against human red blood cells Linear Free Amidation and Acylation (-NH-C₁₆H₃₃, conjugated with a n‑hexadecyl acyl chain) L [Ref.29750913] No cytotoxicity information found Not found 29750913 Biochim Biophys Acta. 2018 Aug;1860(8):1502-1516. Carretero GPB, Saraiva GKV, Cauz ACG, Rodrigues MA, Kiyota S, Riske KA, Dos Santos AA, Pinatto-Botelho MF, Bemquerer MP, Gueiros-Filho FJ, Chaimovich H, Schreier S, Cuccovia IM. Synthesis, biophysical and functional studies of two BP101 analogues modified by a hydrophobic chain and a cyclic peptide. DRAMP20932 GILGKLWEGVKSIF 14 Hp1404 No entry found Melittin Not found Heterometrus petersii Antimicrobial, Antibacterial, Anti-Gram- Protein level Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and the presence of PE:PG and PC:CH liposomes, adopts a random coil conformation when mixed with PC:CH:SM liposomes. Function: Antibacterial activity against Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=12.5 μM), Pseudomonas aeruginosa 138 (MIC=12.5 μM), Pseudomonas aeruginosa 431 (MIC=12.5 μM), Pseudomonas aeruginosa 434 (MIC=12.5 μM), Pseudomonas aeruginosa 557 (MIC=6.25 μM), Pseudomonas aeruginosa 559 (MIC=25 μM), Pseudomonas aeruginosa 778 (MIC=12.5 μM), Pseudomonas aeruginosa 1034 (MIC=6.25 μM), Pseudomonas aeruginosa 1162 (MIC=12.5 μM), Pseudomonas aeruginosa 3290 (MIC=12.5 μM), Pseudomonas aeruginosa 3399 (MIC=6.25 μM), Pseudomonas aeruginosa 3543 (MIC=6.25 μM), Pseudomonas aeruginosa 3592 (MIC=6.25 μM), Pseudomonas aeruginosa 3904 (MIC=6.25 μM), Pseudomonas aeruginosa 4007 (MIC=25 μM), Pseudomonas aeruginosa 4319 (MIC=12.5 μM), Pseudomonas aeruginosa 4891 (MIC=6.25 μM), Pseudomonas aeruginosa 5018 (MIC=12.5 μM), Pseudomonas aeruginosa 671973 (MIC=3.13 μM) [Ref.29379033]Hemolysis 2% at 12.5 μM against mouse red blood cell, hemolysis 11% at 25.0 μM against mouse red blood cell, hemolysis 55% at 50.0 μM against mouse red blood cell, hemolysis 92% at 100.0 μM against mouse red blood cell, hemolysis 100% at 200.0 μM against mouse red blood cell Linear Free Amidation L [Ref.29379033] The cell survial against HaCaT cells is 85%, 26%, 5% and 6% at peptide concentrations of 25, 50, 100 and 200 μM Lipopolysaccharide (LPS)-binding 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20933 FFSLIPSLVGGLISAFK 17 Stigmurin No entry found Derived from scorpion venom peptide Not found Tityus stigmurus Antimicrobial, Antibacterial, Anti-Gram+, Antifungal, Antiparasitic, Antiproliferative Transcript level Alpha helix Not found Function: Antibacterial activity against the Gram-positive bacteria. Antifungal activity against yeasts.Antiparasitic Activity against epimastigote forms of Trypanosoma cruzi. Antiproliferative Activity against HeLa cells. [Ref.29670004] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=9.38 μM), Staphylococcus epidermidis ATCC 122225 (MIC=9.38 μM);##yeasts: Candida albicans ATCC 90028 (MIC=37.5 μM);##Stigmurin inhibit 90% of the epimastigote forms of Trypanosoma cruzi growth at 25 ?M;##HeLa cell line: IC50=7.98 μM [Ref.29670004]Hemolysis 0% at 1.17 μM, hemolysis 1% at 2.34 μM, hemolysis 1% at 4.69 μM, hemolysis 0% at 9.38 μM, hemolysis 1% at 18.75 μM, hemolysis 1% at 37.50 μM, hemolysis 3% at 75.00 μM against human red blood cell Linear Free Amidation L [Ref.29670004] The cell viability of HeLa cell lines is 56%, 66%, 66%, 81%, 78%, 66% and 30% at peptide concentrations of 2, 4, 8, 10, 15, 20 and 40 μM. ##The cell viability of 3T3 cell lines is 81%, 63%, 51%, 29%, 27%, 19% and 15% at peptide concentra Not found 29670004 Toxins (Basel). 2018 Apr 18;10(4). pii: E161. Parente AMS, Daniele-Silva A, Furtado AA, Melo MA, Lacerda AF, Queiroz M, Moreno C, Santos E, Rocha HAO, Barbosa EG, Carvalho E, Silva-Júnior AA, Silva MS, Fernandes-Pedrosa MF. Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity. DRAMP20934 MNFNKFFVLFALIMVAVVGQSEAGWLKKLGKKIERVGQHTRDATIQTIGVAQQAVNVAATLKG 63 Lucilin Peptide D7RT24 Cecropins ATGAATTTTAATAAATTTTT L. eximia maggots Antimicrobial, Antibacterial, Anti-Gram-, Wound-healing Transcript level Alpha helix Not found Function: Antibacterial activity against the Gram-negative bacteria. Immunomodulatory activity. Decreasing the TNF-alpha production in PBMCs and inducing cellular migration in human keratinocytes. [Ref.29890152] Gram-negative bacteria: Escherichia coli DH10B (MIC=7.8 μg/ml; MBC=7.8 μg/ml), Escherichia coli ESBL (MIC=15.6 μg/ml; MBC=15.6 μg/ml), Enterobacter cloacae (MIC=125 μg/ml; MBC=125 μg/ml) [Ref.29890152]Hemolysis 0% at 0.24 μg/ml, hemolysis 0% at 0.49 μg/ml, hemolysis 0% at 0.98 μg/ml, hemolysis 0% at 1.95 μg/ml, hemolysis 0% at 3.91 μg/ml, hemolysis 0% at 7.81 μg/ml, hemolysis 0% at 15.60 μg/ml, hemolysis 0% at 31.00 μg/ml, hemolysis 0% at 63.00 μg/ml, hemolysis 0% at 125.00 μg/ml, hemolysis 0% at 250.00 μg/ml against human red blood cell Linear Free Free L [Ref.29890152] The peptide did not show cytotoxic activities against Vero cells. ##The peptide showed a toxic concentration from 62.5 μg/ml with IC50 of 58.30 μg/ml against PBMCs Not found 29890152 Bioorg Med Chem Lett. 2012 Jun 15;22(12):4185-8. Téllez GA, Zapata JA, Toro LJ, Henao DC, Bedoya JP, Rivera JD, Trujillo JV, Rivas-Santiago B, Hoyos RO, Castano JC. Identification, Characterization, Immunolocalization, and Biological Activity of Lucilin Peptide. DRAMP20935 GFGMALKLLKKVL 13 Macropin 1(solitary bee, insects, animals) C0HL98 Not found Not found Macropis fulvipes (Solitary bee) (Megilla fulvipes) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix,random coil Not found [Ref.24616110] Antimicrobial peptide active against Gram-positive bacteria like B.subtilis, S.aureus and L.monocytogenes as well as against Gram-negative bacteria like E.coli and P.aeruginosa with minimum inhibitory concentrations (MIC) between 1.3 ?M and 35 ?M.Active against fungus C.albicans (MIC=6.3 ?M).Has little hemolytic activity . Adopts an alpha-helical structure in a membrane mimic environment. [Ref.29185466] Acts by disrupting membranes and bacterial cell wall structures.Binds to peptidoglycan and lipopolysaccharide (LPS) [Ref.24616110] Gram-negative bacteria: Escherichia coli(MIC=3.0 μM), Pseudomonas aeruginosa(MIC=35.0 μM);## Gram-positive bacteria: Bacillus subtilis (MIC=1.3 μM), Staphylococcus aureus(MIC=3.7 μM);## Fungus: Candida albicans (MIC=6.3 μM). ##[Ref.29185466]Gram-positive bacteria:Staphylococcus aureus ATCC 25923 (MIC=3.13 μM), Staphylococcus aureus ATCC 29213 (MIC=3.13 μM), Listeria monocytogenes KCTC 3710 (MIC=25 μM);##Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=6.25 μM), Pseudomonas aeruginosa ATCC 15692 (MIC=6.25 μM), Escherichia coli ATCC 25922 (MIC=6.25 μM) [Ref.24616110] LC50=160 μM against human red blood cells. ##[Ref.29185466]5% hemolysis at 25 μM against red blood cells, 93% hemolysis at 50 μM against red blood cells Linear Free Amidation L [Ref.29185466] In HaCaT cells, Macropin produced cell survival rates of 82% and 41% at peptide concentrations of 25 and 50 μM.## In Raw cells, Macropin produce cell survival rates of 41% and 0% at peptide concentrations of 25 and 50 μM. Not found 24616110##29185466 J Pept Sci. 2014 Jun;20(6):375-84. doi: 10.1002/psc.2625. Epub 2014 Mar 11.## Sci Rep. 2017 Nov 29;7(1):16580. doi: 10.1038/s41598-017-16784-6. Monincová L, Veverka V, Slaninová J, Buděšínský M, Fučík V, Bednárová L, Straka J, Ceřovský V.## Ko SJ, Kim MK, Bang JK, Seo CH, Luchian T, Park Y. Structure-activity study of macropin, a novel antimicrobial peptide from the venom of solitary bee Macropis fulvipes (Hymenoptera: Melittidae).## Macropis fulvipes Venom component Macropin Exerts its Antibacterial and Anti-Biofilm Properties by Damaging the Plasma Membranes of Drug Resistant Bacteria. DRAMP20936 RVKRFKKFFRKIKKGFRKIFKKTKIFIG 28 ΔPb-CATH1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. [Ref.28630199] Gram-positive bacteria: Staphylococcus aureus (ATCC 29213)(MIC>128 μg/ml); B. cereus ATCC 10876 (MIC=46 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=3 μg/ml), S. typhimurium ATCC 14028 (MIC=1.5 μg/ml) [Ref.28630199]1.4 ± 0.4% hemolysis at 8 μg/ml, 5.1 ± 0.5% hemolysis at 16 μg/ml, 7.3 ± 0.6% hemolysis at 32 μg/ml, 12.2 ± 0.7% hemolysis at 64 μg/ml against chicken red blood cells Linear Free Free L [Ref.28630199] No cytotoxicity information found Not found 28630199 Antimicrob Agents Chemother. 2017 Aug 24;61(9). pii: e00530-17. Kim D, Soundrarajan N, Lee J, Cho HS, Choi M, Cha SY, Ahn B, Jeon H, Le MT, Song H, Kim JH, Park C. Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity DRAMP20937 HRVKRNGFRKFMRRLKKFFAGG 22 Pb-CATH3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. [Ref.28630199] Gram-positive bacteria: B. cereus ATCC 10876 (MIC=32 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=3 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μg/ml), S. typhimurium ATCC 14028 (MIC=2 μg/ml);##Clinical isolates: Escherichia coli (4.7 μg/ml), K. pneumoniae (1.18 μg/ml) [Ref.28630199]0% hemolysis at 8 μg/ml, 1.7 ± 0.5% hemolysis at 16 μg/ml, 3.1 ± 0.5% hemolysis at 32 μg/ml, 4.0 ± 0.2% hemolysis at 64 μg/ml against chicken red blood cells Linear Free Free L [Ref.28630199] No cytotoxicity information found Not found 28630199 Antimicrob Agents Chemother. 2017 Aug 24;61(9). pii: e00530-17. Kim D, Soundrarajan N, Lee J, Cho HS, Choi M, Cha SY, Ahn B, Jeon H, Le MT, Song H, Kim JH, Park C. Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity DRAMP20938 RLLRKFFRKLKKSV 14 Cbf-14 No entry found Belongs to cathelicidin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix,beta-sheet,beta-turn,random coil The percentages of possible occurring conformations involved helix, beta, turn and random are also quantified in various solutions Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. [Ref.28522372]Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=64 μg/ml), Staphylococcus aureus (MIC=32 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=32 μg/ml), Escherichia coli (MIC=32 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa (MIC=32 μg/ml);##Yeasts: Candida albicans ATCC 10231 (MIC=64 μg/ml), Candida albicans (MIC=64 μg/ml) [Ref.28522372]2% hemolysis at 800 μg/ml against mice red blood cells Linear Free Free L The percentages of possible occurring conformations involved helix, beta, turn and random are also quantified in various solutions Not found 28522372 Eur J Pharm Sci. 2017 Jul 15;105:169-177. Kang W, Liu H, Ma L, Wang M, Wei S, Sun P, Jiang M, Guo M, Zhou C, Dou J. Effective antimicrobial activity of a peptide mutant Cbf-14-2 against penicillin-resistant bacteria based on its unnatural amino acids DRAMP20939 RLLRKFFRKLKKSV 14 D-Cbf-14 No entry found Belongs to cathelicidin Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic Alpha helix,beta-sheet,beta-turn,random coil The percentages of possible occurring conformations involved helix, beta, turn and random are also quantified in various solutions Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria. All amino acids in the sequence are D-type. [Ref.28522372] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=64 μg/ml), Staphylococcus aureus (MIC=32 μg/ml);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=32 μg/ml), Escherichia coli (MIC=32 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μg/ml), Pseudomonas aeruginosa (MIC=64 μg/ml);##Yeasts: Candida albicans ATCC 10231 (MIC=64 μg/ml), Candida albicans (MIC=64 μg/ml) [Ref.28522372]1% hemolysis at 800 μg/ml against mice red blood cells Linear Free Free D [Ref.28522372] In mice spleen cells, the peptide produced cell viability of 97% at 800 μg/ml Not found 28522372 Eur J Pharm Sci. 2017 Jul 15;105:169-182. Kang W, Liu H, Ma L, Wang M, Wei S, Sun P, Jiang M, Guo M, Zhou C, Dou J. Effective antimicrobial activity of a peptide mutant Cbf-14-3 against penicillin-resistant bacteria based on its unnatural amino acids DRAMP20940 IDWKKLLDAAKKIL 14 Polybia-MP1S-Q12K No entry found Derived from Polybia-MP1 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic Alpha helix The peptide adopts a conformational structure with 81.8% alpha helix in the aqueous solution. Function: Antibacterial activity against the Gram-positive bacteria, position 6 and 10 are cross-linked residues connected by the oct-4-enyl hydrocarbon staple [Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC=0.8 μM), Staphylococcus aureus (MIC=1.2 μM), Staphylococcus epidermidis (MIC=50 μM) [Ref.29075946]9.6% hemolysis at 12.5μM,13.9% hemolysis at 25μM against human red blood cells Cyclic Free Amidation The oct-4-enyl hydrocarbon staple between Leu6 and Ala10 L [Ref.29075946] No cytotoxicity information found Not found 29075946 Arch Pharm Res. 2017 Dec;40(12):1414-1422. Luong HX, Kim DH, Lee BJ, Kim YW Antimicrobial activity and stability of stapled helices of polybia-MP1 DRAMP20941 FVPWFSKFLKRIL 13 [Pro3,DLeu9]TL(8) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The analogues bearing a D residue showed a reduction in the percentage of helicity compared to the corresponding L analogues in the MMs Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(8) is D-Leucine, L-Lysine replace L-Proline at the position 10 on the peptide [Pro3,DLeu9]TL(2). [Ref.28863356] Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3.125μM), Staphylococcus aureus Cowan I (MIC=6.25μM), Staphylococcus epidermidis ATCC 12228 (MIC=3.125μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=3.125μM), Escherichia coli D21 (MIC=12.5μM), Pseudomonas syringae pv tabaci 1918 (MIC=6.25μM), Pseudomonas aeruginosa ATCC 2785 (MIC=12.5μM);##Yeasts: Candida albicans ATCC 10231 (MIC=1.56μM), Candida crusei ATCC 6258 (MIC=1.56μM) [Ref.28863356]49.30 ± 2.88% cytotoxic effect at 12.5 μM, 66.86 ± 2.81% cytotoxic effect at 25 μM, 96.79 ± 1.24% cytotoxic effect at 50 μM on HaCaT cells. Linear Free Amidation Mixed (D-Leu9) [Ref.28863356] The cytotoxic effect is 49.30±2.88%, 66.86±2.81% and 96.79±1.24% at peptide concentrations of 12.5, 25 and 50 μM Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-761. Merlino F, Carotenuto A, Casciaro B, MartorMerlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP20942 FVPWFSKFLKRIL 13 [Pro3,DLeu9]TL(9) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The analogues bearing a D residue showed a reduction in the percentage of helicity compared to the corresponding L analogues in the MMs Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(9) is D-Leucine, D-Lysine replace L-Proline at the position 10 on the peptide [Pro3,DLeu9]TL(2). [Ref.28863356] Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3.125 μM), Staphylococcus aureus Cowan I (MIC=12.5 μM), Staphylococcus epidermidis ATCC 12228 (MIC=3.125 μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=6.25 μM), Escherichia coli D21 (MIC=12.5 μM), Pseudomonas syringae pv tabaci 1918 (MIC=12.5 μM), Pseudomonas aeruginosa ATCC 2785 (MIC=12.5 μM);##Yeasts: Candida albicans ATCC 10231 (MIC=1.56 μM), Candida crusei ATCC 6258 (MIC=1.56 μM) [Ref.28863356]7±4% hemolysis at 50 μM, 5±3% hemolysis at 25 μM, 5±2% hemolysis at 12.5 μM, 1±2% hemolysis at 6.25 μM, 0±1% hemolysis at 3.125 μM against human red blood cells. ##28.22 ± 3.52% cytotoxic effect at 25 μM, 87.9 ± 1.07% cytotoxic effect at 50 μM on HaCaT cells. Linear Free Amidation Mixed (D-Leu9, D-Lys10) [Ref.28863356] The cytotoxic effect is 0%, 28.22±3.52% and 87.9±1.07% at 12.5, 25 and 50 μM Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-761. Merlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP20943 FVPWFSKFLWRIL 13 [Pro3,DLeu9]TL(10) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix A distorted (type IV) Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(8) is D-Leucine, L-Tryptophan replace L-Proline at the position 10 on the peptide [Pro3,DLeu9]TL(2). [Ref.28863356] Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=1.56 μM), Staphylococcus aureus Cowan I (MIC=3.125 μM), Staphylococcus epidermidis ATCC 12228 (MIC=1.56 μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=3.125 μM), Escherichia coli D21 (MIC=25 μM), Pseudomonas syringae pv tabaci 1918 (MIC=1.56 μM);##Yeasts: Candida albicans ATCC 10231 (MIC=3.125 μM), Candida crusei ATCC 6258 (MIC=3.125 μM) [Ref.28863356]37±1% hemolysis at 50μM, 20±3% hemolysis at 25μM, 7±1% hemolysis at 12.5μM, 4±2% hemolysis at 6.25μM, 2±1% hemolysis at 3.125μM against human red blood cells.##32.1 ± 2.21% cytotoxic effect at 25μM, 89.3 ± 0.8% cytotoxic effect at 50 μM on HaCaT cells. Linear Free Amidation Mixed (D-Leu9) [Ref.28863356] The cytotoxic effect is 0%, 32.1±2.21% and 89.3±0.8% at 12.5, 25 and 50 μM Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-761. Merlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP20944 FVPWFSKFLWRIL 13 [Pro3,DLeu9]TL(11) (Temporin L peptide derivative) No entry found Derived from Temporin L Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The analogues bearing a D residue showed a reduction in the percentage of helicity compared to the corresponding L analogues in the MMs Function: Antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteria and Fungi. The position 9 of [Pro3,DLeu9]TL(10) is D-Leucine, D-Tryptophan replace L-Proline at the position 10 on the peptide [Pro3,DLeu9]TL(2). [Ref.28863356] Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3.125μM), Staphylococcus aureus Cowan I (MIC=3.125μM), Staphylococcus epidermidis ATCC 12228 (MIC=1.56μM);##Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MIC=3.125μM), Escherichia coli D21 (MIC=25μM), Pseudomonas syringae pv tabaci 1918 (MIC=3.125μM), Pseudomonas aeruginosa ATCC 2785 (MIC=50μM);##Yeasts: Candida albicans ATCC 10231 (MIC=3.125μM),Candida crusei ATCC 6258 (MIC=3.125μM) [Ref.28863356]19.21 ± 1.44% cytotoxic effect at 12.5μM, 35.34 ± 5.99% cytotoxic effect at 25μM, 96.77 ± 0.81% cytotoxic effect at 50 μM on HaCaT cells. Linear Free Amidation Mixed (D-Leu9, D-Trp10) [Ref.28863356] The cytotoxic effect is 19.21±1.44%, 35.34±5.99% and 96.77±0.81% at 12.5, 25 and 50 μM Not found 28863356 Eur J Med Chem. 2017 Oct 20;139:750-761. Merlino F, Carotenuto A, Casciaro B, Martora F, Loffredo MR, Di Grazia A, Yousif AM, Brancaccio D, Palomba L, Novellino E, Galdiero M, Iovene MR, Mangoni ML, Grieco P. Glycine-replaced derivatives of [Pro3,DLeu9]TL, a temporin L analogue: Evaluation of antimicrobial, cytotoxic and hemolytic activities DRAMP20945 KWKLFKKIFKRIVQRIKDFLRN 22 Recombinant Cecropin A (1–8)–LL37 (17–30) (C–L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria [Ref.29925795] Gram-negative bacteria: Escherichia coli CVCC 245 (MIC=7.2 ± 0.14 μg/mL);##Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2.2 ± 0.05 μg/mL),L. mono. CVCC 1599 (MIC=2.1 ± 0.03 μg/mL) [Ref.29925795] 50% hemolysis at 221 ± 3.45μg/ml against sheep red blood cells Linear Free Free L [Ref.29925795] No cytotoxicity information found Not found 29925795 Molecules. 2018 Jun 20;23(6). pii: E1491. Wei X, Wu R, Zhang L, Ahmad B, Si D, Zhang R. Expression, Purification, and Characterization of a Novel Hybrid Peptide with Potent Antibacterial Activity DRAMP20946 TRSRWRRFIRGAGRFARRYGWRIA 24 ΔPb-CATH4 bivittatus antimicrobial peptides peptide derivative No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Not found Not found Function: Antibacterial activity against the Gram-negative and Gram-negative bacteria. It is tested against the clinically isolated antibiotic resistance strains Escherichia coli and Klebsiella pneumoniae,which showed complete resistance particularly toward ampicillin and to a lesser extent with gentamicin [Ref.28630199] Gram-negative bacteria: Escherichia coli (ATCC 25922)(MIC=1μg/ml);Pseudomonas aeruginosa (ATCC 27853)(MIC=3μg/ml);S. typhimurium (ATCC 14028)(MIC=0.5μg/ml);##Gram-positive bacteria: Staphylococcus aureus (ATCC 29213)(MIC>128μg/ml);B. cereus (ATCC 10876)(MIC=10μg/ml);##Clinical isolates:Escherichia coli(MIC=4.7μg/ml);K. pneumoniae(MIC=1.18μg/ml) [Ref.28630199]Hemolysis 0% at 4μg/ml against human red blood cell;Hemolysis 1.2 ± 0.3% at 8μg/ml against human red blood cell;Hemolysis 3.2 ± 0.4% at 16μg/ml against human red blood cell;Hemolysis 6.5 ± 0.4% at 32μg/ml against human red blood cell;Hemolysis 10.7 ± 0.2% at 64μg/ml against human red blood cell Linear Free Free L [Ref.28630199] No cytotoxicity information found Not found 28630199 Antimicrob Agents Chemother. 2017 Aug 24;61(9). pii: e00530-17. Kim D, Soundrarajan N, Lee J, Cho HS, Choi M, Cha SY, Ahn B, Jeon H, Le MT, Song H, Kim JH, Park C. Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity. DRAMP20947 FLKALWNVAKSVF 13 [K]3-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 6 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.10 in water;0.60 in TFE/Water;0.98 in POPC;0.52 in POPC:POPG;1 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It presented higher or equivalent antimicrobial activity when compared to VmCT1. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=1.56μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=0.78μmol/L);Escherichia coli (D31)(MIC=1.56μmol/L);Serratia marcescens (ATCC 4112)(MIC=1.56μmol/L);Enterobacter cloacae (beta-12)(MIC=6.25μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=0.78μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=3.12μmol/L);Bacillus subtilis (ATCC 6633)(MIC=6.25μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=3.12μmol/L);##Fungi: Candida albicans MDM8(MIC=3.12μmol/L);Candida tropicalis (IOC 4560)(MIC=3.12μmol/L);Candida parapsilosis (IOC 4564)(MIC=6.25μmol/L);##Aspergillus niger(MIC=12.5μmol/L);##Cladosporium herbarum (ATCC 26362)(MIC=25μmol/L);##Cryptococcus neoformans(MIC=3.12μmol/L) [Ref.27912176] MHC=1.60 μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20948 FLGALWKVAKSVF 13 [K]7-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 7 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.04 in water;0.43 in TFE/Water;0.80 in POPC;0.63 in POPC:POPG;0.88 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It presented higher or equivalent antimicrobial activity when compared to VmCT2. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=1.56μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=0.39μmol/L);Escherichia coli (D31)(MIC=1.56μmol/L);Serratia marcescens (ATCC 4112)(MIC=0.78μmol/L);Enterobacter cloacae (beta-12)(MIC=6.25μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=1.56μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=1.56μmol/L);Bacillus subtilis (ATCC 6633)(MIC=3.12μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=1.56μmol/L);##Fungi: Candida albicans MDM8(MIC=1.56μmol/L);Candida tropicalis (IOC 4560)(MIC=1.56μmol/L);Candida parapsilosis (IOC 4564)(MIC=1.56μmol/L);##Aspergillus niger(MIC=6.25μmol/L);##Cladosporium herbarum (ATCC 26362)(MIC=12.5μmol/L);##Cryptococcus neoformans(MIC=1.56μmol/L) [Ref.27912176] MHC=1.60μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20949 FLGALWNVAKKVF 13 [K]11-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 8 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.02 in water;0.27 in TFE/Water;0.56 in POPC;0.50 in POPC:POPG;0.76 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It presented higher or equivalent antimicrobial activity when compared to VmCT3. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=1.56μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=0.39μmol/L);Escherichia coli (D31)(MIC=1.56μmol/L);Serratia marcescens (ATCC 4112)(MIC=0.78μmol/L);Enterobacter cloacae (beta-12)(MIC=6.25μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=1.56μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=1.56μmol/L);Bacillus subtilis (ATCC 6633)(MIC=6.25μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=1.56μmol/L);##Fungi: Candida albicans MDM8(MIC=1.56μmol/L);Candida tropicalis (IOC 4560)(MIC=3.12μmol/L);Candida parapsilosis (IOC 4564)(MIC=6.25μmol/L);##Aspergillus niger(MIC=6.25μmol/L);##Cladosporium herbarum (ATCC 26362)(MIC=6.25μmol/L);##Cryptococcus neoformans(MIC=1.56μmol/L) [Ref.27912176] MHC=1.60μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20950 FLGELWNVAKSVF 13 [E]4-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 9 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.02 in water;0.15 in TFE/Water;0.17 in POPC;0.20 in POPC:POPG;0.24 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi. It showed a diminished antimicrobial activity against all the microorganisms tested, besides that it did not present activity at the range of concentrations analyzed against Escherichia coli SBS 363, E. cloacae, Bacillus subtilis, C. parapsilosis, A. niger and C. herbarum. [Ref.27912176] Gram-negative bacteria: Pseudomonas aeruginosa (ATCC 27853)(MIC=3.12μmol/L);Escherichia coli (D31)(MIC=50μmol/L);Serratia marcescens (ATCC 4112)(MIC=3.12μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=25μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=50μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=50μmol/L);##Fungi:Candida albicans MDM8(MIC=50μmol/L);Candida tropicalis (IOC 4560)(MIC=12.5μmol/L);##Cryptococcus neoformans(MIC=12.5μmol/L) [Ref.27912176] MHC=25μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20951 FLGALWEVAKSVF 13 [E]7-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 10 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.04 in water;0.24 in TFE/Water;0.57 in POPC;0.44 in POPC:POPG;0.64 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It analog presented a reduction or similar antimicrobial activity when compared to model molecule, this analog had an increase on activity against Escherichia coli SBS 363, Bacillus subtilis and C. herbarum. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=1.56μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=0.78μmol/L);Escherichia coli (D31)(MIC=1.56μmol/L);Serratia marcescens (ATCC 4112)(MIC=1.56μmol/L);Enterobacter cloacae (beta-12)(MIC=25μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=1.56μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=6.25μmol/L);Bacillus subtilis (ATCC 6633)(MIC=12.5μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=6.25μmol/L);##Fungi: Candida albicans MDM8(MIC=12.5μmol/L);Candida tropicalis (IOC 4560)(MIC=12.5μmol/L);Candida parapsilosis (IOC 4564)(MIC=50μmol/L);##Aspergillus niger(MIC=25μmol/L);##Cladosporium herbarum (ATCC 26362)(MIC=25μmol/L);##Cryptococcus neoformans(MIC=6.25μmol/L) [Ref.27912176] MHC=1.60μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20952 FLGALWNVWKSVF 13 [W]9-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 11 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.02 in water;0.11 in TFE/Water;0.30 in POPC;0.11 in POPC:POPG;0.24 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It antimicrobial activities are increased or preserved when compared to VmCT1. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=1.56μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=0.78μmol/L);Escherichia coli (D31)(MIC=1.56μmol/L);Serratia marcescens (ATCC 4112)(MIC=1.56μmol/L);Enterobacter cloacae (beta-12)(MIC=6.52μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=1.56μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=6.25μmol/L);Bacillus subtilis (ATCC 6633)(MIC=3.12μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=1.56μmol/L);##Fungi: Candida albicans MDM8(MIC=6.25μmol/L);Candida tropicalis (IOC 4560)(MIC=50μmol/L);Candida parapsilosis (IOC 4564)(MIC=50μmol/L);##Aspergillus niger(MIC=50μmol/L);##Cladosporium herbarum (ATCC 26362)(MIC=50μmol/L);##Cryptococcus neoformans(MIC=3.12μmol/L) [Ref.27912176]MHC=1.60μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20953 FLGELWNVWKSVF 13 [E]4[W]9-VmCT1-NH2 VmCT1 petide derivative No entry found Belongs to the scorpion NDBP 12 family Not found Synthetic construct Antimicrobial, Antibacterial Synthetic Helical structures The peptide adopts Helical fraction 0.01 in water;0.11 in TFE/Water;0.24 in POPC;0.14 in POPC:POPG;0.23 in POPC:DOPE; Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria and fungi.It analog displayed a reduction in the antimicrobial activity, being the exceptions Escherichia coli SBS 363, Bacillus subtilis and Candida albicans. [Ref.27912176] Gram-negative bacteria: Escherichia coli (SBS 363)(MIC=12.5μmol/L);Pseudomonas aeruginosa (ATCC 27853)(MIC=3.12μmol/L);Escherichia coli (D31)(MIC=6.25μmol/L);Serratia marcescens (ATCC 4112)(MIC=3.12μmol/L);Enterobacter cloacae (beta-12)(MIC=50μmol/L);##Gram-positive bacteria: Micrococcus luteus (A270)(MIC=3.12μmol/L);Staphylococcus aureus (ATCC 29213)(MIC=12.5μmol/L);Bacillus subtilis (ATCC 6633)(MIC=12.5μmol/L);Staphylococcus epidermidis (ATCC 12228)(MIC=6.25μmol/L);##Fungi: Candida albicans MDM8(MIC=6.25μmol/L);Candida tropicalis (IOC 4560)(MIC=12.5μmol/L);##Cryptococcus neoformans(MIC=6.25μmol/L) [Ref.27912176] MHC=1.60μmol/L against human red blood cells Linear Free Amidation L [Ref.27912176] No cytotoxicity information found Not found 27912176 Eur J Med Chem. 2017 Jan 27;126:456-463. Pedron CN, Torres MT, Lima JADS, Silva PI, Silva FD, Oliveira VX. Novel designed VmCT1 analogs with increased antimicrobial activity. DRAMP20955 LGDFFRKSKEKIGKEFKRIVQRIKDFLRNLAKRHHGYKRKFH 42 L31-P113 No entry found Derived from LL-37 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The peptide adopts a conformational structure with 80 % alpha helix. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29859288] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=25 ± 0 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16.6 ± 7.2 μM);##Fungi: Candida albicans ATCC 90028 (MIC=166.6 ± 57.7 μg/mL) [Ref.29859288] Hemolysis 12.0 ± 0.7% at 500 μg/ml against human red blood cells Linear Free Free L [Ref.29859288] No cytotoxicity information found Not found 29859288 Gene. 2018 May 30. pii: S0378-1119(18)30617-6. Wanmakok M, Orrapin S, Intorasoot A, Intorasoot S. Expression in Escherichia coli of novel recombinant hybrid antimicrobial peptide AL32-P113 with enhanced antimicrobial activity in vitro. DRAMP20956 ALGDFFRKSKEKIGKEFKRIVQRIKDFLRNLAKRHHGYKRKFHLEY 46 AL32-P113 No entry found Derived from LL-37 and Hst-5 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic Alpha helix The peptide adopts a conformational structure with 81 % alpha helix. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. [Ref.29859288] Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=66.6 ± 28.8 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=41.6 ± 14.4 μM), Extended-spectrum beta-lactamase producing Escherichia coli (MIC=41.6 ± 14.4 μg/mL), New Delhi metallo-bata-lactamase-1 producing Acinetobacter baumannii (MIC=20.8 ± 7.2 μg/mL);##Fungi: Candida albicans ATCC 90028 (MIC=166.6 ± 57.7 μg/mL) [Ref.29859288] Hemolysis 10.4 ± 2.2% at 500 μg/ml against human red blood cells Linear Free Free L [Ref.29859288] No cytotoxicity information found Not found 29859288 Gene. 2018 May 30. pii: S0378-1119(18)30617-6. Wanmakok M, Orrapin S, Intorasoot A, Intorasoot S. Expression in Escherichia coli of novel recombinant hybrid antimicrobial peptide AL32-P113 with enhanced antimicrobial activity in vitro. DRAMP20957 FFSLIPKLVKGLISAFK 17 StigA6 No entry found Derived from scorpion venom peptide Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiparasitic, Antiproliferative Synthetic Alpha helix The peptide adopts helical conformation with some random structure at the N- and C-terminals. In sodium phosphate buffer (PBS) and water they have a predominantly random structure, but in 20 mM sodium dodecyl sulfate (SDS) and 2,2,2-trifluoroethanol (TFE) they have a typical alpha-helix structure. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity against yeasts.Antiparasitic Activity against epimastigote forms of Trypanosoma cruzi. Antiproliferative Activity against HeLa cells. [Ref.29670004] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2.34 μM), Staphylococcus epidermidis ATCC 122225 (MIC=9.38 μM), Enterococcus faecalis ATCC 4028 (MIC=1.17 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=4.69 μM), Enterobacter cloacae ATCC 13047 (MIC=18.75 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=9.38 μM);##yeasts: Candida albicans ATCC 90028 (MIC=9.38 μM), Candida krusei ATCC 6258 (MIC=37.5 μM), Candida glabrata ATCC 90030 (MIC=18.75 μM);##StigA6 inhibit 100% of the epimastigote forms of Trypanosoma cruzi growth at 2.5 µM;##HeLa cell line: IC50=14.01 µM [Ref.29670004] Hemolysis 0% at 1.17 μM, hemolysis 2% at 2.34 μM, hemolysis 15% at 4.69 μM, hemolysis 27% at 9.38 μM, hemolysis 30% at 18.75 μM, hemolysis 30% at 37.50 μM, hemolysis 27% at 75.00 μM against human red blood cells Linear Free Amidation L [Ref.29670004] The cell viability of HeLa cell lines is 19%, 15%, 11%, 29%, 9%, 13% and 8% at peptide concentrations of 2, 4, 8, 10, 15, 20 and 40 μM. ##The cell viability of 3T3 cell lines is 81%, 73%, 69%, 61%, 51%, 20% and 15% at peptide concentrati Not found 29670004 Toxins (Basel). 2018 Apr 18;10(4). pii: E161. Parente AMS, Daniele-Silva A, Furtado AA, Melo MA, Lacerda AF, Queiroz M, Moreno C, Santos E, Rocha HAO, Barbosa EG, Carvalho E, Silva-Júnior AA, Silva MS, Fernandes-Pedrosa MF. Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity. DRAMP20958 FFKLIPKLVKGLISAFK 17 StigA16 No entry found Derived from scorpion venom peptide Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiparasitic, Antiproliferative Synthetic Alpha helix The peptide adopts helical conformation with some random structure at the N- and C-terminals. In sodium phosphate buffer (PBS) and water they have a predominantly random structure, but in 20 mM sodium dodecyl sulfate (SDS) and 2,2,2-trifluoroethanol (TFE) they have a typical alpha-helix structure. Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity against yeasts.Antiparasitic Activity against epimastigote forms of Trypanosoma cruzi. Antiproliferative Activity against HeLa cells. [Ref.29670004] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2.34 μM), Staphylococcus epidermidis ATCC 122225 (MIC=9.38 μM), Enterococcus faecalis ATCC 4028 (MIC=1.17 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2.34 μM), Enterobacter cloacae ATCC 13047 (MIC=9.38 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=1.17 μM);##yeasts: Candida albicans ATCC 90028 (MIC=4.69 μM), Candida krusei ATCC 6258 (MIC=9.38 μM), Candida glabrata ATCC 90030 (MIC=9.38 μM);##StigA16 inhibit 100% of the epimastigote forms of Trypanosoma cruzi growth at 2.5 µM;##HeLa cell line: IC50=13.01 µM [Ref.29670004] Hemolysis 0% at 1.17 [Ref.29670004] Hemolysis 0% at 1.17 μM, hemolysis 2% at 2.34 μM, hemolysis 10% at 4.69 μM, hemolysis 20% at 9.38 μM, hemolysis 35% at 18.75 μM, hemolysis 37% at 37.50 μM, hemolysis 40% at 75.00 μM against human red blood cells Linear Free Amidation L [Ref.29670004] The cell viability of HeLa cell lines is 15%, 21%, 16%, 9%, 8%, 10% and 11% at peptide concentrations of 2, 4, 8, 10, 15, 20 and 40 μM. ##The cell viability of 3T3 cell lines is 69%, 77%, 62%, 47%, 21%, 15% and 15% at peptide concentratio Not found 29670004 Toxins (Basel). 2018 Apr 18;10(4). pii: E161. Parente AMS, Daniele-Silva A, Furtado AA, Melo MA, Lacerda AF, Queiroz M, Moreno C, Santos E, Rocha HAO, Barbosa EG, Carvalho E, Silva-Júnior AA, Silva MS, Fernandes-Pedrosa MF. Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity. DRAMP20959 ILKKLLKGVKSI 12 Hp1404-T1c No entry found Derived from Hp1404 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and adopts a random coil conformation in the presence of all liposome types . Function: Antibacterial activity against Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=3.13 μM), Pseudomonas aeruginosa 138 (MIC=25 μM), Pseudomonas aeruginosa 431 (MIC=12.5 μM), Pseudomonas aeruginosa 434 (MIC=6.25 μM), Pseudomonas aeruginosa 557 (MIC=25 μM), Pseudomonas aeruginosa 559 (MIC=25 μM), Pseudomonas aeruginosa 778 (MIC=6.25 μM), Pseudomonas aeruginosa 1034 (MIC=6.25 μM), Pseudomonas aeruginosa 1162 (MIC=3.13 μM), Pseudomonas aeruginosa 3399 (MIC=3.13 μM), Pseudomonas aeruginosa 3592 (MIC=6.25 μM), Pseudomonas aeruginosa 3904 (MIC=6.25 μM), Pseudomonas aeruginosa 4007 (MIC=12.5 μM), Pseudomonas aeruginosa 4319 (MIC=6.25 μM), Pseudomonas aeruginosa 4891 (MIC=6.25 μM), Pseudomonas aeruginosa 5018 (MIC=3.13 μM), Pseudomonas aeruginosa 671973 (MIC=6.25 μM) [Ref.29379033] Hp1404-T1c does not induce substantial hemolysis, even at the high tested concentration (200 μM) against mouse red blood cells Linear Free Amidation L [Ref.29379033] The cell survial against HaCaT cells is 100%, 70%, 66% and 53% at peptide concentrations of 25, 50, 100 and 200 μM Lipopolysaccharide (LPS)-binding and entering bacterial cells and interact with their DNA 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20960 ILKKLLKKVKSI 12 Hp1404-T1d No entry found Derived from Hp1404 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and adopts a random coil conformation in the presence of all liposome types . Function: Antibacterial activity against Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=1.56 μM), Pseudomonas aeruginosa 138 (MIC=12.5 μM), Pseudomonas aeruginosa 431 (MIC=3.13 μM), Pseudomonas aeruginosa 434 (MIC=3.13 μM), Pseudomonas aeruginosa 557 (MIC=3.13 μM), Pseudomonas aeruginosa 559 (MIC=12.5 μM), Pseudomonas aeruginosa 778 (MIC=3.13 μM), Pseudomonas aeruginosa 1034 (MIC=3.13 μM), Pseudomonas aeruginosa 1162 (MIC=1.56 μM), Pseudomonas aeruginosa 3290 (MIC=6.25 μM), Pseudomonas aeruginosa 3399 (MIC=1.56 μM), Pseudomonas aeruginosa 3543 (MIC=25 μM), Pseudomonas aeruginosa 3592 (MIC=3.13 μM), Pseudomonas aeruginosa 3904 (MIC=6.25 μM), Pseudomonas aeruginosa 4007 (MIC=6.25 μM), Pseudomonas aeruginosa 4319 (MIC=3.13 μM), Pseudomonas aeruginosa 4891 (MIC=3.13 μM), Pseudomonas aeruginosa 5018 (MIC=1.56 μM), Pseudomonas aeruginosa 671973 (MIC=1.56 μM) [Ref.29379033] Hp1404-T1d does not induce substantial hemolysis, even at the high tested concentration (200 μM) against mouse red blood cells Linear Free Amidation L [Ref.29379033] The cell survial against HaCaT cells is 58%, 48%, 52% and 34% at peptide concentrations of 25, 50, 100 and 200 μM Lipopolysaccharide (LPS)-binding 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20961 ILKKLLKKVKKI 12 Hp1404-T1e No entry found Derived from Hp1404 Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic Alpha helix The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and adopts a random coil conformation in the presence of all liposome types . Function: Antibacterial activity against Gram-negative bacteria. [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=1.56 μM), Pseudomonas aeruginosa 138 (MIC=6.25 μM), Pseudomonas aeruginosa 431 (MIC=3.13 μM), Pseudomonas aeruginosa 434 (MIC=3.13 μM), Pseudomonas aeruginosa 557 (MIC=3.13 μM), Pseudomonas aeruginosa 559 (MIC=6.25 μM), Pseudomonas aeruginosa 778 (MIC= 1.56 μM), Pseudomonas aeruginosa 1034 (MIC= 1.56 μM), Pseudomonas aeruginosa 1162 (MIC=1.56 μM), Pseudomonas aeruginosa 3290 (MIC=6.25 μM), Pseudomonas aeruginosa 3399 (MIC=0.78 μM), Pseudomonas aeruginosa 3543 (MIC=12.5 μM), Pseudomonas aeruginosa 3592 (MIC=1.56 μM), Pseudomonas aeruginosa 3904 (MIC=3.13 μM), Pseudomonas aeruginosa 4007 (MIC=3.13 μM), Pseudomonas aeruginosa 4319 (MIC=3.13 μM), Pseudomonas aeruginosa 4891 (MIC=1.56 μM), Pseudomonas aeruginosa 5018 (MIC=1.56 μM), Pseudomonas aeruginosa 671973 (MIC=1.56 μM) [Ref.29379033] Hp1404-T1e does not induce substantial hemolysis, even at the high tested concentration (200 μM) against mouse red blood cells Linear Free Amidation L [Ref.29379033] The cell survial against HaCaT cells is 100%, 100%, 100%, 99% at peptide concentrations of 25, 50, 100 and 200 μM Lipopolysaccharide (LPS)-binding and entering bacterial cells and interact with their DNA 29379033 Sci Rep. 2018 Jan 29;8(1):1763. Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y. Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa. DRAMP20963 LRLKKYKVPQL 11 Cp1 alpha s1-casein peptide derivative No entry found Derived from bovine alpha S1-casein Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, low hemolytic and toxic effects Synthetic Unordered conformation Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29783753] Gram-negative bacteria: Escherichia coli (ATCC 25922)(MIC=64μM);Escherichia coli (UB1005)(MIC=128μM);Salmonella pullorum (C7913)(MIC=256μM);Salmonella enterica subsp enterica (CMCC 50071)(MIC=256μM);##Gram-positive bacteria: Staphylococcus aureus (ATCC 29213)(MIC=640μM);L. monocytogenes (CMCC 54004)(MIC=64μM) [Ref.2978375]Hemolysis 0% at 16μM;Hemolysis 23.54% at 512μM against human red blood cells Linear Free Amidation L [Ref.29783753] In 293 cells, The peptide had no cytotoxic activity at concentrations of 1-512 μM. The cell survival rates are 100%, 96%, 98%, 105%, 104%, 112%, 116%, 114% and 103% at concentrations of 1, 2, 4, 8, 16, 32, 64, 128, 256, 512 μM Not found 29783753 Molecules. 2018 May 19;23(5). pii: E1220. Hou J, Liu Z, Cao S, Wang H, Jiang C, Hussain MA, Pang S Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine DRAMP20964 KWKLFKKIFKRIVQRIKDFLRN 22 Synthesized Cecropin A (1–8)–LL37 (17–30) (C–L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against the Gram-positive and Gram-negative bacteria. [Ref.29920061] Gram-negative bacteria: Escherichia coli (CVCC 245)(MIC=7.0 ± 0.21μg/mL);##Gram-positive bacteria: Staphylococcus aureus (ATCC 25923)(MIC=2.0 ± 0.02μg/mL );L. mono. (CVCC 1599)(MIC=2.2 ± 0.05μg/mL) [Ref.29920061]HC50 =219 ± 2.98μg/mL against sheep erythrocyte cells Linear Free Free L [Ref.29925795] No cytotoxicity information found Not found 29920061 Molecules. 2018 Jun 20;23(6). pii: E1491. Wei X, Wu R, Zhang L, Ahmad B, Si D, Zhang R. Expression, Purification, and Characterization of a Novel Hybrid Peptide with Potent Antibacterial Activity. DRAMP20965 MNKVKEWIKYLKSLFSM 17 LPcin-YK3 (bovine cathelicidin, cattle, ruminant, mammals, animals) No entry found Not found Not found Bovine Lactophoricin Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Random coil, alpha helix LPcin-YK3 peptide is a random coil in aqueous solution and forms an Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.30021422] Gram-positive bacteria : Streptococcus mutans KCCM 40105 (MIC=1.25 μg/ml), Propionibacteria acnes KCCM 41747 (MIC=1.25 μg/ml), Staphylococcus aureus KCTC 1621 (MIC=0.62 μg/ml);##Gram-negative bacteria : Porphyromonas gingvalis KCTC 5352 (MIC=0.62 μg/ml), Escherichia coli KCCM 41290 (MIC=1.25 μg/ml);##Fungi : Candida albicans KCTC 17712 (MIC=10.0 μg/ml) [Ref.30021422] 0% hemolysis at 40 μg/ml against mouse red blood cell Linear Free Free L [Ref.30021422] No cytotoxicity information found Not found 30021422 J Microbiol Biotechnol.?2018 Aug 28;28(8):1299-1309. doi: 10.4014/jmb.1805.05001. Ji-Sun Kim,Ji-Ho Jeong, Jang-Hee Cho,Dong-Hee Lee and Yongae Kim Antimicrobial Activity of Antimicrobial Peptide LPcin-YK3 Derived from Bovine Lactophoricin DRAMP20966 GLTRLFSVIK 10 andricin B (Andrias davidianus, Amphibians, Animals) No entry found Not found Not found Andrias davidianus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Random coil The residues Lys and Arg possess the positive charge, and charge-induced folding may influence the structure. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae, Aspergillus niger [Ref.29130500]Gram-positive bacteria : Bacillus subtilis CICC 10034 (MIC=32 μg/ml, 33.4 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml), Staphylococcus aureus CICC10306 (MIC=16 μg/ml, 16.7 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml), Staphylococcus aureus CICC 10384 (MIC=16 μg/ml, 16.7 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml), Listeria innocua CICC 10417 (MIC=32 μg/ml, 33.4 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml);##Gram-negative bacteria : Escherichia coli CICC10293 (MIC=16 μg/ml, 16.7 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml), Pseudomonas aeruginosa CICC 21636 (MIC=8 μg/ml, 8.3 μMol/ml;MBC=16 μg/ml, 16.7 μMol/ml), Serratia marcescens ATCC 4112 (MIC=8 μg/ml, 8.3 μMol/ml;MBC=16 μg/ml, 16.7 μMol/ml), Enterobacter cloacae CICC 21539 (MIC=16 μg/ml, 16.7 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml), Salmonella paratyphi CICC 10437 (MIC=32 μg/ml, 33.4 μMol/ml;MBC=32 μg/ml, 33.4 μMol/ml);##Fungi : Aspergillus niger CICC 2124 (MIC=64 μg/ml, 66.8 μMol/ml;MBC=64 μg/ml, 66.8 μMol/ml), Candida albicans CICC 1965 (MIC=32 μg/ml, 33.4 μMol/ml;MBC=64 μg/ml, 66.8 μMol/ml), Saccharomyces cerevisiae CICC 1002 (MIC=64 μg/ml, 66.8 μMol/ml;MBC=64 μg/ml, 66.8 μMol/ml) [Ref.29130500] 0% hemolysis at 64 μg/ml , 0.5% hemolysis at 128 μg/ml , 2% hemolysis at 256 μg/ml , 13% hemolysis at 512 μg/ml against human red blood cells Linear Free Free L [Ref.29130500] No cytotoxicity information found Not found 29130500 Lett Appl Microbiol.?2018 Jan;66(1):38-43. doi: 10.1111/lam.12823. J. Pei, Z. Feng,T. Ren,H. Sun,H. Han,W. Jin,J. Dang and Y. Tao Purifification, characterization and application of a novel antimicrobial peptide from Andrias davidianus blood DRAMP20967 AIGHCLGATL 10 andricin 01 (Andrias davidianus, Amphibians, Animals) No entry found Not found Not found Andrias davidianus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28461043] Gram-positive bacteria : Bacillus subtilis CICC 10034 (MIC=32 μg/ml;MBC=32 μg/ml), Bacillus megaterium CICC 10448 (MIC=8 μg/ml;MBC=16 μg/ml), Staphylococcus aureus CICC 10306 (MIC=32 μg/ml;MBC=32 μg/ml), Staphylococcus aureus CICC 10384 (MIC=32 μg/ml;MBC=32 μg/ml), Listeria innocua CICC 10417 (MIC=32 μg/ml;MBC=32 μg/ml);##Gram-negative bacteria : Escherichia coli CICC 10293 (MIC=8 μg/ml;MBC=16 μg/ml), Escherichia coli CGMCC 3373 (MIC=8 μg/ml;MBC=16 μg/ml), Escherichia coli CICC 10302 (MIC=8 μg/ml;MBC=16 μg/ml), Escherichia coli CICC 10300 (MIC=8 μg/ml;MBC=16 μg/ml), Pseudomonas aeruginosa CICC 21636 (MIC=4 μg/ml;MBC=8 μg/ml), Alcaligenes faecalis ATCC 8750 (MIC=8 μg/ml;MBC=16 μg/ml), Serratia marcescens ATCC 4112 (MIC=8 μg/ml;MBC=8 μg/ml), Enterobacter cloacae CICC 21539 (MIC=4 μg/ml;MBC=8 μg/ml), Salmonella Paratyphi CICC 10437 (MIC=8 μg/ml;MBC=16 μg/ml) [Ref.28461043] 0% hemolysis at 25 μg/ml , 0% hemolysis at 50 μg/ml , 4.3 ± 0.16% hemolysis at 100 μg/ml , 16.3 ± 2.16% hemolysis at 200 μg/ml against human hepatocyte cell line and human renal epithelial cells;0% hemolysis at 0–50 μg/ml against human red blood cells Linear Free Free L [Ref.28461043] The cell viability of HL-7702 cells is 100.0±0.30%, 100.5±0.52%, 86.8±2.10% and 52.1±1.81% at peptide concentrations of 25, 50, 100 and 200 μg/ml. ##The cell viability of HREpiC cells is 100.1±0.20%, 103.1±1.20%, 82.3±1.84% and 50.3±2.05% Not found 28461043 Int J Antimicrob Agents.?2017 Jul;50(1):41-46. doi: 10.1016/j.ijantimicag.2017.02.013. Jinjin Pei, Lei Jiang Antimicrobial peptide from mucus of Andrias davidianus: screening and purification by magnetic cell membrane separation technique DRAMP20968 MMRVMRRKTKVIWEKKDFIGLYSID 25 Catesbeianin-1 (Ranidae, Anura, Amphibia, Animals) C5IAX4 Not found Not found Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Alpha helix Catesbeianin-1 is an amphi pathic a-helix and that the helical wheel is divided into two parts, namely, a hydrophobic face and a hydro philic face. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28258530] Gram-positive bacteria : Staphylococcus aureus ATCC 25923 (MIC=3.1 μg/ml;MBC=6.3 μg/ml), B. subtilis ATCC6633 (MIC=25 μg/ml;MBC=50 μg/ml), Streptococcus suis CVCC606 (MIC=3.1 μg/ml;MBC=12.5 μg/ml), Listeria monocytogenes ATCC19115 (MIC=12.5 μg/ml;MBC=25 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=3.1 μg/ml;MBC=12.5 μg/ml), Pseudomonas aeruginosa ATCC227853 (MIC=12.5 μg/ml;MBC=25 μg/ml), Salmonella spp. CVCC 3377 (MIC=6.3 μg/ml;MBC=25 μg/ml), Klebsiella pneumoniae H507 (MIC=25 μg/ml;MBC=100 μg/ml) [Ref.28258530] 0% hemolysis at 0 μg/ml , hemolysis 3% at 25 μg/ml , 7% hemolysis at 50 μg/ml , 8% hemolysis at 100 μg/ml , 35% hemolysis at 200 μg/ml , 50% hemolysis at 300 μg/ml , 85% hemolysis at 400 μg/ml , 95% hemolysis at 500 μg/ml against human red blood cells Linear Free Free L [Ref.28258530] The cell viability of HEK293T cells is 102%, 103%, 103%, 100%, 98% and 85% at peptide concentrations of 0, 20, 40, 60, 80 and 100 μg/ml. ##The cell viability of HL-7200 cells is 107%, 106%, 99%, 95% and 88% at peptide concentrations of 0, Not found 28258530 Biotechnol Lett. 2017 Jun;39(6):897-903. doi: 10.1007/s10529-017-2312-7. Huihui Xu . Yang Zhang . Xin Feng . Kunyuan Tie . Yuan Cao . Wenyu Han Catesbeianin-1, a novel antimicrobial peptide isolatedfrom the skin of Lithobates catesbeianus (American bullfrog) DRAMP20969 KLLKHKLLVTLA 12 HJH-1 (bovine cathelicidin, cattle, ruminant, mammals, animals) No entry found Not found Not found Bovine Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.30110916]Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=25 μg/ml), Clinical Staphylococcus aureus (MIC=25 μg/ml), ;##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=12.5 μg/ml), Clinical Escherichia coli (MIC=25 μg/ml), Salmonella pullorum CVCC3533 (MIC=6.25 μg/ml), Clinical Salmonella (MIC=6.25 μg/ml);##Fungi : Candida albicans ATCC 90029 (MIC=50 μg/ml) [Ref.30110916] 8% hemolysis at 50 μg/ml , 12% hemolysis at 100 μg/ml , 16% hemolysis at 200 μg/ml , 17% hemolysis at 300 μg/ml , 18% hemolysis at 400 μg/ml against rabbit red blood cells Linear Free Free L [Ref.30110916] No cytotoxicity information found Not found 30110916 Molecules. 2018 Aug 14;23(8). pii: E2026. doi: 10.3390/molecules23082026. Qing Wang, Yanzhao Xu, Mengmeng Dong, Bolin Hang, Yawei Sun, Lei Wang,Yongqiang Wang, Jianhe Hu, and Wenju Zhang HJH-1, a Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity Antimicrobial Peptide DRAMP20970 VNFKLLSHSLLVTLASHL 18 P3 (bovine cathelicidin, cattle, ruminant, mammals, animals) P01966 Belongs to the globin family. HBA Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.25753638] Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=25 μg/ml), Clinical Staphylococcus aureus (MIC=12.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=12.5 μg/ml), Clinical Escherichia coli (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain (MIC=25 μg/ml);##Fungi : Candida albicans Clinical strain (MIC=25 μg/ml), Candida albicans ATCC 90029 (MIC=50 μg/ml) [Ref.25753638] 3% hemolysis at 50 μg/ml , 5% hemolysis at 100 μg/ml , 7% hemolysis at 200 μg/ml , 7.5% hemolysis at 300 μg/ml , 8% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.25753638] The cell viability of HaCaT cell lines is 93% and 94% at peptide concentrations of 200 and 400 μg/ml. In kumning mice, the LD50 of P3 is 160 mg/kg for i.p. injection, while the LD50 of PMB(served as a control) is 50 mg/kg. No mortality w Not found 25753638 Antimicrob Agents Chemother. 2015 May;59(5):2835-41. doi: 10.1128/AAC.04932-14. Qinghua Zhang, Yanzhao Xu, Qing Wang, Bolin Hang, Yawei Sun, Xiaoxiao Wei, Jianhe Hu Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model DRAMP20971 KLLSHSLLVTLA 12 JH-0 (Derived from P3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25753638]Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=6.25 μg/ml), Clinical Staphylococcus aureus (MIC=6.25 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=6.25 μg/ml), Clinical Escherichia coli (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain (MIC=6.25 μg/ml) [Ref.25753638] 2.5% hemolysis at 50 μg/ml , 4% hemolysis at 100 μg/ml , 5% hemolysis at 200 μg/ml , 6% hemolysis at 300 μg/ml , 7% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.25753638] The cell viability of HaCaT cell lines is 88% and 85% at peptide concentrations of 200 and 400 μg/ml. In Kunming mice, the LD50 of JH-0 is 120 mg/kg for i.p. injection, while the LD50 of PMB(served as a control) is 50 mg/kg. No mortalit Not found 25753638 Antimicrob Agents Chemother. 2015 May;59(5):2835-41. doi: 10.1128/AAC.04932-14. Qinghua Zhang, Yanzhao Xu, Qing Wang, Bolin Hang, Yawei Sun, Xiaoxiao Wei, Jianhe Hu Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model DRAMP20972 KLLRHRLLVTLA 12 JH-1 (Derived from P3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25753638] Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=6.25 μg/ml), Clinical Staphylococcus aureus (MIC=6.25 μg/ml), ;##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=3.125 μg/ml), Clinical Escherichia coli (MIC=6.25 μg/ml), Pseudomonas aeruginosa clinical strain (MIC=12.5 μg/ml) [Ref.25753638] 2% hemolysis at 50 μg/ml , 2.5% hemolysis at 100 μg/ml , 2.5% hemolysis at 200 μg/ml , 3% hemolysis at 300 μg/ml , 4% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.25753638] The cell viability of HaCaT cell lines is 84% and 80% at peptide concentrations of 200 and 400 μg/ml. In Kunming mice, the LD50 of JH-1 is 94 mg/kg for i.p. injection, while the LD50 of PMB(served as a control) is 50 mg/kg. No mortality Not found 25753638 Antimicrob Agents Chemother. 2015 May;59(5):2835-41. doi: 10.1128/AAC.04932-14. Qinghua Zhang, Yanzhao Xu, Qing Wang, Bolin Hang, Yawei Sun, Xiaoxiao Wei, Jianhe Hu Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model DRAMP20973 VRFKLLSHSLLVTLASHL 18 JH-2 (Derived from P3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.25753638] Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=12.5 μg/ml), Clinical Staphylococcus aureus (MIC=6.25 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=6.25 μg/ml), Clinical Escherichia coli (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain (MIC=6.25 μg/ml);##Fungi : Candida albicans ATCC 90029 (MIC=25 μg/ml), Candida albicans Clinical strain (MIC=25 μg/ml) [Ref.25753638] 2% hemolysis at 50 [Ref.25753638] 2% hemolysis at 50 μg/ml , 2.5% hemolysis at 100 μg/ml , 3.5% hemolysis at 200 μg/ml , 4% hemolysis at 300 μg/ml , 4% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.25753638] The cell viability of HaCaT cell lines is 88% and 84% at peptide concentrations of 200 and 400 μg/ml. In Kunming mice, the LD50 of JH-2 is 133 mg/kg for i.p. injection, while the LD50 of PMB(served as a control) is 50 mg/kg. no mortality Not found 25753638 Antimicrob Agents Chemother. 2015 May;59(5):2835-41. doi: 10.1128/AAC.04932-14. Qinghua Zhang, Yanzhao Xu, Qing Wang, Bolin Hang, Yawei Sun, Xiaoxiao Wei, Jianhe Hu Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model DRAMP20974 RRFKLLSHSLLVTLASHL 18 JH-3 (Derived from P3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.25753638]Gram-positive bacteria : Staphylococcus aureus ATCC29213 (MIC=6.25 μg/ml), Clinical Staphylococcus aureus (MIC=3.125 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC25922 (MIC=3.125 μg/ml), Clinical Escherichia coli (MIC=3.125 μg/ml), Pseudomonas aeruginosa clinical strain (MIC=6.25 μg/ml);##Fungi : Candida albicans ATCC 90029 (MIC=12.5 μg/ml), Candida albicans Clinical strain (MIC=6.25 μg/ml) [Ref.25753638] 8% hemolysis at 50 μg/ml , 13% hemolysis at 100 μg/ml , 17% hemolysis at 200 μg/ml , 18% hemolysis at 300 μg/ml , 18.5% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.25753638] The cell viability of HaCaT cell lines is 86% and 86% at peptide concentrations of 200 and 400 μg/ml. In Kunming mice, the LD50 of JH-3 is 180 mg/kg for i.p. injection, , while the LD50 of PMB(served as a control) is 50 mg/kg. No mortali Not found 25753638 Antimicrob Agents Chemother. 2015 May;59(5):2835-41. doi: 10.1128/AAC.04932-14. Qinghua Zhang, Yanzhao Xu, Qing Wang, Bolin Hang, Yawei Sun, Xiaoxiao Wei, Jianhe Hu Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model DRAMP20975 KFFKKLKKAVKKGFKKFAKV 20 OH-CM6 (Derived from OH-CATH30) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.22491685] Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=12.5 μg/ml), Staphylococcuss aureus ATCC 43300 MRSA (MIC=3.125 μg/ml), Staphylococcuss aureus clinical strain 1 (MIC=6.25 μg/ml), Staphylococcuss aureus clinical strain 2 (MIC=3.125 μg/ml), Staphylococcuss aureus clinical strain 3 (MIC=12.5 μg/ml), Enterococcus faecalis ATCC 29212 (MIC=25 μg/ml) ;##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=12.5 μg/ml), Escherichia coli ML-35p (MIC=6.25 μg/ml), Escherichia coli clinical strain 1 (MIC=12.5 μg/ml), Escherichia coli clinical strain 2 (MIC=3.125 μg/ml), Escherichia coli clinical strain 3 (MIC=1.56 μg/ml), Escherichia coli clinical strain 4 (MIC=12.5 μg/ml), Escherichia coli clinical strain 5 (MIC=6.25 μg/ml), Escherichia coli clinical strain 6 (MIC=3.125 μg/ml), Enterobacter cloacae ATCC 13047 (MIC>100 μg/ml), Enterobacter cloacae clinical strain (MIC>100 μg/ml), Enterobacter aerogenes clinical strain (MIC>100 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=12.5 μg/ml), Pseudomonas aeruginosa PA 01 (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain 1 (MIC=12.5 μg/ml), Pseudomonas aeruginosa clinical strain 2 (MIC=6.25 μg/ml), Haemophilus influenzae ATCC 49247 (MIC=3.125 μg/ml), Haemophilus influenzae ATCC 49766 (MIC=6.25 μg/ml), Klebsiella pneumoniae ATCC 13883 (MIC=6.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MIC=3.125 μg/ml) ;##Fungi : Candida albicans ATCC 2002 (MIC>200 μg/ml), Candida albicans clinical strain (MIC>200 μg/ml) [Ref.22491685] 13% hemolysis at 100 μg/ml , 17% hemolysis at 200 μg/ml , 18% hemolysis at 300 μg/ml , 18.5% hemolysis at 400 μg/ml against human red blood cells Linear Free Free L [Ref.22491685] The cell viability of HaCaT cell lines is 76%, 62% and 53% at peptide concentrations of 50, 100, 200 μg/ml. In Kunming mice, the LD50 of OH-CATH30 is 120 mg/kg for i.p. injection, while those of pexiganan(control 1) and PMB(control 2) are Not found 22491685 Antimicrob Agents Chemother. 2012 Jun;56(6):3309-17. doi: 10.1128/AAC.06304-11. Sheng-An Li, Wen-Hui Lee, and Yun Zhang Efficacy of OH-CATH30 and Its Analogs against Drug-ResistantBacteria In Vitro and in Mouse Models DRAMP20976 RKYVRFLHRWVKYFRAYL 18 "adevonin (Derived from Adenanthera pavonina trypsin inhibitor (ApTI)) inhibitor (ApTI))" No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Adevonin showed that its secondary structure varies according to the environment, acquiring Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.30570384]Gram-positive bacteria : Staphylococcus aureus ATCC 80958 (MIC=7.35 μM);##Gram-negative bacteria : Escherichia coli ATCC 35218 (MIC=7.35 μM), Klebsiella oxytoca ATCC 13182 (MIC=1.84 μM), Klebsiella pneumoniae ATCC 70603 (MIC=3.67 μM), Serratia marcesens ATCC 13880 (MIC=1.84 μM), Klebsiella pneumoniae KpC+ 001825971 (MIC=25.6 μM) [Ref.30570384] 0% hemolysis at 43.75 μM , 72.5% hemolysis at 175 μM , 77% hemolysis at 350 μg/ml against human type O erythrocytes Linear Free Free L [Ref.30570384] In fibroblasts, a significant reduction of cell viability, of 25% on average, is observed in each time interval(24,48 and 72h) in the highest peptide concentration(10 μM) Not found 30570384 Pathog Glob Health.?2018 Dec;112(8):438-447. doi: 10.1080/20477724.2018.1559489. Mayara S. Rodrigues, Caio F. R. de Oliveira, Luís H. O. Almeida, Simone M.Neto, Ana Paula A. Boleti, Edson L. dos Santos, Marlon H. Cardoso, Suzana,M. Ribeiro, Octávio L. Franco, Fernando S. Rodrigues, Alexandre J. Macedo,Flávia R. Brust & Maria Lígia R. Macedo Adevonin, a novel synthetic antimicrobial peptide designed from the Adenanthera pavonina trypsin inhibitor (ApTI) sequence DRAMP20977 WLLKRWKKLL 10 Anoplin-1 (Derived from Anoplin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25316570]Gram-positive bacteria : Staphylococcus aureus (MIC=32 μg/ml), bacillus subtilis (MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC=64 μg/ml), Peudomonas eruginosa (MIC=8 μg/ml) [Ref.25316570] 0% hemolysis at 100 μg/ml , 1% hemolysis at 200 μg/ml against mice red blood cells Linear Free Amidation L [Ref.25316570] No cytotoxicity information found Not found 25316570 J Pept Sci. 2014 Dec;20(12):945-51. doi: 10.1002/psc.2705. Yang Wang, Jianbo Chen, Xin Zheng, Xiaoli Yang, Panpan Ma,Ying Cai,Bangzhi Zhangb,and Yuan Chen Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity DRAMP20978 wllkrwkkll 10 Anoplin-2 (Derived from Anoplin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25316570]Gram-positive bacteria : Staphylococcus aureus (MIC=16 μg/ml), bacillus subtilis (MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC=16 μg/ml), Peudomonas eruginosa (MIC=8 μg/ml) [Ref.25316570] 0% hemolysis at 25 μg/ml , 1% hemolysis at 50 μg/ml , 0% hemolysis at 100 μg/ml , 0.5% hemolysis at 200 μg/ml against mice red blood cells Linear Free Amidation D [Ref.25316570] No cytotoxicity information found Not found 25316570 J Pept Sci. 2014 Dec;20(12):945-51. doi: 10.1002/psc.2705. Yang Wang, Jianbo Chen, Xin Zheng, Xiaoli Yang, Panpan Ma,Ying Cai,Bangzhi Zhangb,and Yuan Chen Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity DRAMP20979 KLLKWWKKLL 10 Anoplin-3 (Derived from Anoplin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25316570]Gram-positive bacteria : Staphylococcus aureus (MIC=16 μg/ml), bacillus subtilis (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC=16 μg/ml), Peudomonas eruginosa (MIC=8 μg/ml) [Ref.25316570] 0% hemolysis at 12.5 μg/ml , 0.5% hemolysis at 25 μg/ml , 0.5% hemolysis at 50 μg/ml , 4% hemolysis at 100 μg/ml , 14% hemolysis at 200 μg/ml against mice red blood cells Linear Free Amidation L [Ref.25316570] No cytotoxicity information found Not found 25316570 J Pept Sci. 2014 Dec;20(12):945-51. doi: 10.1002/psc.2705. Yang Wang, Jianbo Chen, Xin Zheng, Xiaoli Yang, Panpan Ma,Ying Cai,Bangzhi Zhangb,and Yuan Chen Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity DRAMP20980 kllkwwkkll 10 Anoplin-4 (Derived from Anoplin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25316570]Gram-positive bacteria : Staphylococcus aureus (MIC=8 μg/ml), bacillus subtilis (MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC=8 μg/ml), Peudomonas eruginosa (MIC=8 μg/ml) [Ref.25316570] 0.5% hemolysis at 12.5 μg/ml , 0.5% hemolysis at 25 μg/ml , 2% hemolysis at 50 μg/ml , 1% hemolysis at 100 μg/ml , 4% hemolysis at 200 μg/ml against mice red blood cells Linear Free Amidation D [Ref.25316570] No cytotoxicity information found Not found 25316570 J Pept Sci. 2014 Dec;20(12):945-51. doi: 10.1002/psc.2705. Yang Wang, Jianbo Chen, Xin Zheng, Xiaoli Yang, Panpan Ma,Ying Cai,Bangzhi Zhangb,and Yuan Chen Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity DRAMP20981 GFGSLLGKALRLGANVL 17 CPF-C1 (Frogs, Amphibians, Animals) No entry found Not found Not found Tetraploid frog Xenopus clivii Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Not found Random coil, alpha helix CPF-C1 revealed a random coil structure in PBS, displayed typical Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=4 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=32 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=32 μg/ml), Pseudomonas aeruginosa 2760 (MIC=128 μg/ml), Pseudomonas aeruginosa 9132 (MIC=64 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=4 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 32 μg/ml , 5% hemolysis at 64 μg/ml , 7% hemolysis at 128 μg/ml , 15% hemolysis at 256 μg/ml , 57% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation L [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20982 KFWSLLKKALRLWANVL 17 CPF-1 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix CPF-1 displayed typical Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=32 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=32 μg/ml), Pseudomonas aeruginosa 2760 (MIC=32 μg/ml), Pseudomonas aeruginosa 9132 (MIC=64 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=8 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 0 μg/ml , 5% hemolysis at 4 μg/ml , 8% hemolysis at 8 μg/ml , 20% hemolysis at 16 μg/ml , 35% hemolysis at 32 μg/ml , 58% hemolysis at 64 μg/ml , 70% hemolysis at 128 μg/ml , 78% hemolysis at 256 μg/ml , 80% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation L [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20983 kFwSLLkKALRLwANVL 17 CPF-2 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix CPF-2 displayed typical Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=8 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μg/ml), Pseudomonas aeruginosa 2760 (MIC=16 μg/ml), Pseudomonas aeruginosa 9132 (MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 4 μg/ml , 5% hemolysis at 8 μg/ml , 8% hemolysis at 16 μg/ml , 24% hemolysis at 32 μg/ml , 48% hemolysis at 64 μg/ml , 68% hemolysis at 128 μg/ml , 85% hemolysis at 256 μg/ml , 90% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Lys1, D-Trp3, D-Lys7, D-Trp13) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20984 KFWKLLKKALRLWAKVL 17 CPF-3 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix CPF-3 displayed typical Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=16 μg/ml), Pseudomonas aeruginosa 9132 (MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 256 μg/ml , 5% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation L [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20985 kFWKlLKkAlrLWAkVL 17 CPF-4 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=16 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=16 μg/ml), Escherichia coli 850 (MIC=8 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=8 μg/ml), Pseudomonas aeruginosa 9132 (MIC=32 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 32 μg/ml , 5% hemolysis at 64 μg/ml , 8% hemolysis at 128 μg/ml , 10% hemolysis at 256 μg/ml , 25% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Lys1, D-Leu5, D-Lys8, D-Leu10, D-Arg11, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20986 kFwKLLkKALrLwAkVL 17 CPF-5 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=8 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=8 μg/ml), Pseudomonas aeruginosa 9132 (MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=8 μg/ml), Acinetobacter baumannii 2982 (MIC=8 μg/ml), Acinetobacter baumannii 4956 (MIC=8 μg/ml) [Ref.28371431] 0% hemolysis at 16 μg/ml , 5% hemolysis at 32 μg/ml , 10% hemolysis at 64 μg/ml , 20% hemolysis at 128 μg/ml , 40% hemolysis at 256 μg/ml , 37% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Lys1, D-Trp3, D-Lys7, D-Arg11, D-Trp13, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20987 lFwKLLlKAlrLwAkVL 17 CPF-6 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=16 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=16 μg/ml), Pseudomonas aeruginosa 9132 (MIC=64 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC8=μg/ml), Acinetobacter baumannii 2982 (MIC=8 μg/ml), Acinetobacter baumannii 4956 (MIC=8 μg/ml) [Ref.28371431] 0% hemolysis at 4 μg/ml , 3% hemolysis at 8 μg/ml , 17.5% hemolysis at 16 μg/ml , 45% hemolysis at 32 μg/ml , 70% hemolysis at 64 μg/ml , 80% hemolysis at 128 μg/ml , 85% hemolysis at 256 μg/ml , 90% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Leu1, D-Trp3, D-Leu7, D-Leu10, D-Arg11, D-Trp13, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20988 WFKKLLKKALRLWKKVL 17 CPF-7 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix CPF-7 displayed typical Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=16 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=16 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=16 μg/ml), Pseudomonas aeruginosa 9132 (MIC=32 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=8 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431] 0% hemolysis at 4 [Ref.28371431] 0% hemolysis at 4 μg/ml , 5% hemolysis at 8 μg/ml , 23% hemolysis at 16 μg/ml , 50% hemolysis at 32 μg/ml , 70% hemolysis at 64 μg/ml , 95% hemolysis at 128 μg/ml , 90% hemolysis at 256 μg/ml , 100% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation L [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20989 wFKKlLKkAlrLWKkVL 17 CPF-8 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μg/ml), Staphylococcuss aureus 725 (MIC=8 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=8 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μg/ml), Pseudomonas aeruginosa 2760 (MIC=8 μg/ml), Pseudomonas aeruginosa 9132 (MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=8 μg/ml), Acinetobacter baumannii 2982 (MIC=8 μg/ml), Acinetobacter baumannii 4956 (MIC=8 μg/ml) [Ref.28371431]13% hemolysis at 4 μg/ml , 5% hemolysis at 8 μg/ml , 0% hemolysis at 16 μg/ml , 0% hemolysis at 32 μg/ml , 0% hemolysis at 64 μg/ml , 0% hemolysis at 128 μg/ml , 0% hemolysis at 256 μg/ml , 0% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Trp1, D-Leu5, D-Lys8, D-Leu10, D-Arg11, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20990 kFwKLLkKAlrLwKkVL 17 CPF-9 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=16 μg/ml), Staphylococcuss aureus 794 (MIC=8 μg/ml), Staphylococcuss aureus 936 (MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μg/ml), Escherichia coli 780 (MIC=8 μg/ml), Escherichia coli 804 (MIC=8 μg/ml), Escherichia coli 850 (MIC=8 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μg/ml), Pseudomonas aeruginosa 2760 (MIC=8 μg/ml), Pseudomonas aeruginosa 9132 (MIC=64 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=8 μg/ml), Acinetobacter baumannii 1980 (MIC=8 μg/ml), Acinetobacter baumannii 2982 (MIC=8 μg/ml), Acinetobacter baumannii 4956 (MIC=8 μg/ml) [Ref.28371431]0% hemolysis at 256 μg/ml , 5% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Lys1, D-Trp3, D-Lys7, D-Leu10, D-Arg11, D-Trp13, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20991 wFwKLLwKAlrLwWkVL 17 CPF-10 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μg/ml), Staphylococcuss aureus 725 (MIC=16 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=32 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=32 μg/ml), Pseudomonas aeruginosa 2760 (MIC=16 μg/ml), Pseudomonas aeruginosa 9132 (MIC=256 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=16 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431]0% hemolysis at 4 μg/ml , 5% hemolysis at 8 μg/ml , 21% hemolysis at 16 μg/ml , 40% hemolysis at 32 μg/ml , 56% hemolysis at 64 μg/ml , 65% hemolysis at 128 μg/ml , 73% hemolysis at 256 μg/ml , 85% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Trp1, D-Trp3, D-Trp7, D-Leu10, D-Arg11, D-Trp13, D-Lys15) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20992 lLKkAlrLWKkVL 13 CPF-11 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=64 μg/ml), Staphylococcuss aureus 725 (MIC=32 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=64 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=32 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=16 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=16 μg/ml), Pseudomonas aeruginosa 2760 (MIC=8 μg/ml), Pseudomonas aeruginosa 9132 (MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=128 μg/ml), Acinetobacter baumannii 1980 (MIC=64 μg/ml), Acinetobacter baumannii 2982 (MIC=64 μg/ml), Acinetobacter baumannii 4956 (MIC=32 μg/ml) [Ref.28371431]2% hemolysis at 4 μg/ml , 3% hemolysis at 8 μg/ml , 1% hemolysis at 16 μg/ml , 0% hemolysis at 32 μg/ml , 0% hemolysis at 64 μg/ml , 0% hemolysis at 128 μg/ml , 10% hemolysis at 256 μg/ml , 20% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Leu1, D-Lys4, D-Leu6, D-Arg7, D-Lys11) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20993 LLwKAlrLwWkVL 13 CPF-12 (Derived from CPF-C1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28371431]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μg/ml), Staphylococcuss aureus 725 (MIC=16 μg/ml), Staphylococcuss aureus 794 (MIC=16 μg/ml), Staphylococcuss aureus 936 (MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=16 μg/ml), Escherichia coli 780 (MIC=16 μg/ml), Escherichia coli 804 (MIC=32 μg/ml), Escherichia coli 850 (MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=64 μg/ml), Pseudomonas aeruginosa 2760 (MIC=64 μg/ml), Pseudomonas aeruginosa 9132 (MIC>256 μg/ml), Acinetobacter baumannii ATCC 19606 (MIC=16 μg/ml), Acinetobacter baumannii 1980 (MIC=16 μg/ml), Acinetobacter baumannii 2982 (MIC=16 μg/ml), Acinetobacter baumannii 4956 (MIC=16 μg/ml) [Ref.28371431]0% hemolysis at 4 μg/ml , 3% hemolysis at 8 μg/ml , 0% hemolysis at 16 μg/ml , 0% hemolysis at 32 μg/ml , 0% hemolysis at 64 μg/ml , 3% hemolysis at 128 μg/ml , 8% hemolysis at 256 μg/ml , 38% hemolysis at 512 μg/ml against human red blood cells Linear Free Amidation Mixed(D-Trp3, D-Leu6, D-Arg7, D-Trp9, D-Lys11) [Ref.28371431] No cytotoxicity information found Not found 28371431 Chem Biol Drug Des. 2017 Nov;90(5):690-702. doi: 10.1111/cbdd.12988. Junqiu Xie,Qian Zhao,Sisi Li,Zhibin Yan,Jing Li,Yao Li,Lingyun Mou,Bangzhi Zhang,Wenle Yang,Xiaokang Miao,Xianxing Jiang,and Rui Wang Novel Antimicrobial Peptide CPF-C1 Analogs with Superior Stabilities and Activities against Multidrug-Resistant Bacteria DRAMP20994 GLLKFIKKLL 10 anoplin analog 4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida parapsilosis [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=15 μg/ml), Bacillus subtilis DELTA (MIC=30 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=300 μg/ml), Zymomonas mobilis 10988 (MIC=7 μg/ml);##Fungi : Candida parapsilosis (MIC=40 μg/ml) [Ref.27862650]0% hemolysis at 55μg/ml , 7% hemolysis at 100μg/ml , 17% hemolysis at 200μg/ml , 24% hemolysis at 300 μg/ml , 33% hemolysis at 400μg/ml , 35% hemolysis at 500 μg/ml against human red blood cells Linear Free Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP20995 KLLKFIKKLL 10 anoplin analog 5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida parapsilosis [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=15 μg/ml), Bacillus subtilis DELTA (MIC=40 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=400 μg/ml), Zymomonas mobilis 10988 (MIC=10 μg/ml);##Fungi : Candida parapsilosis (MIC=30 μg/ml) [Ref.27862650]0% hemolysis at 100 μg/ml , 4% hemolysis at 200 μg/ml , 11% hemolysis at 300 μg/ml , 13% hemolysis at 400 μg/ml , 15% hemolysis at 500 μg/ml against human red blood cells Linear Free Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP20996 RLLKFIKKLL 10 anoplin analog 6 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida parapsilosis [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=20 μg/ml), Bacillus subtilis DELTA (MIC=40 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=400 μg/ml), Zymomonas mobilis 10988 (MIC=10 μg/ml);##Fungi : Candida parapsilosis (MIC=30 μg/ml) [Ref.27862650]0% hemolysis at 300 μg/ml , 3% hemolysis at 400 μg/ml , 12% hemolysis at 500 μg/ml against human red blood cells Linear Free Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP20997 GLLKFIKKLL 10 anoplin analog 7 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=30 μg/ml), Pseudomonas aeruginosa PAO (MIC=5 μg/ml), Zymomonas mobilis 10988 (MIC=5 μg/ml) [Ref.27862650]3% hemolysis at 100 μg/ml , 5% hemolysis at 200 μg/ml , 9% hemolysis at 300 μg/ml , 8% hemolysis at 400 μg/ml , 7% hemolysis at 500 μg/ml against human red blood cells Linear Acylation (Conjugated with octanoic acid) Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP20998 GLLKFIKKLL 10 anoplin analog 8 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=30 μg/ml), Pseudomonas aeruginosa PAO (MIC=5 μg/ml), Zymomonas mobilis 10988 (MIC=5 μg/ml) [Ref.27862650]10% hemolysis at 50 μg/ml , 12% hemolysis at 100 μg/ml , 10% hemolysis at 400 μg/ml , 11% hemolysis at 500 μg/ml against human red blood cells Linear Acylation (Conjugated with decanoic acid) Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP20999 GLLKFIKKLL 10 anoplin analog 9 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27862650]Gram-positive bacteria : Mycobacteria smegmatis mc2 155 (MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli DH5a (MIC=40 μg/ml), Pseudomonas aeruginosa PAO (MIC=5 μg/ml), Zymomonas mobilis 10988 (MIC=30 μg/ml) [Ref.27862650]10% hemolysis at 50 μg/ml , 12% hemolysis at 100 μg/ml , 10% hemolysis at 400 μg/ml , 11% hemolysis at 500 μg/ml against human red blood cells Linear Acylation (Conjugated with dodecanoic acid) Amidation L [Ref.27862650] No cytotoxicity information found Not found 27862650 J Pept Sci. 2016 Nov;22(11-12):731-736. doi: 10.1002/psc.2939. Kostas Chionis, Dimitrios Krikorian, Anna-Irini Koukkou, Maria Sakarellos-Daitsiotis and Eugenia Panou-Pomonis Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin DRAMP21000 GCRRLCYKQRCVTYCRGR 18 cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=32 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=4 μM), Escherichia coli CGSC 5167 (MIC=0.06 μM), Klebsiella pneumoniae ATCC 700603 (MIC=4-8 μM), Acinetobacter baumannii ATCC 19606 (MIC=1-2 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=1-4 μM), Helicobacter pylori ATCC 43504 (MIC= μM);##Fungi : Candida albicans ATCC 90028 (MIC=4-8 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5-1 μM) [Ref.28741926] 5% hemolysis at 0.03 μM , 0% hemolysis at 1.1 μM , 10% hemolysis at 17 μM , 50% hemolysis at 100μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bond between Cys2 and Cys15,Cys6 and Cys11. L [Ref.28741926] CC50 = 39.8 ± 1.0 μM against CRL-1739, CC50 = 2.9 ± 0.1 μM against MM96L, CC50 = 71.7 ± 9.2 μM against HFF-1, CC50 > 64 μM against HeLa, CC50 = 15.3 ± 1.4 μM against MCF-7, CC50 = 2.7 ± 0.1 μM against K-562, CC50 = 12.7 ± 1.1 μM PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21001 GCRRLCWKQRCVTYCRGR 18 [Y7W]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=1-2 μM) [Ref.28741926] 35.1-55.5% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 23.3 ± 0.4 μM against CRL-1739, CC50 = 5.1 ± 0.3 μM against MM96L, CC50 = 39.7 ± 3.8 μM against HFF-1, CC50 > 64 μM against HeLa, CC50 = 3.9 ± 0.2 μM against K-562. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21002 GCRRLCYKQRCVTWCRGR 18 [Y14W]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=1-2 μM) [Ref.28741926] 46.1-55.5% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 30.3 ± 1.1 μM against CRL-1739, CC50 = 4.0 ± 0.1 μM against MM96L, CC50 = 68.4 ± 9.6 μM against HFF-1, CC50 = 50.4 ± 2.4 μM against HeLa, CC50 = 2.7 ± 0.1 μM against K-562. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21003 GCRRLCYRQRCVTYCRGR 18 [K8R]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=1-2 μM) [Ref.28741926] 34.8-54.8% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 29.4 ± 1.1 μM against CRL-1739, CC50 = 5.0 ± 0.3 μM against MM96L, CC50 = 34.5 ± 3.6 μM against HFF-1, CC50 = 39.4 ± 2.6 μM against HeLa, CC50 = 3.1 ± 0.1 μM against K-562. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21004 GCRRLCWRQRCVTWCRGR 18 [Y7W, K8R, Y14W]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=1 μM) [Ref.28741926] 42-49.8% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 31.6 ± 1.3 μM against CRL-1739, CC50 = 5.4 ± 0.3 μM against MM96L, CC50 = 31.3 ± 2.6 μM against HFF-1, CC50 = 41.0 ± 4.2 μM against HeLa, CC50 = 15.1 ± 1.4 μM against MCF-7, CC50 = 3.9 ± 0.1 μM against K-562. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21005 GCRALCYKQRCVTYCRGA 18 [R4A, R18A]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=32 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=8 μM), Escherichia coli CGSC 5167 (MIC=0.5-1 μM), Klebsiella pneumoniae ATCC 700603 (MIC=32 μM), Acinetobacter baumannii ATCC 19606 (MIC=8-16 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μM), Helicobacter pylori ATCC 43504 (MIC>80 μM);##Fungi : Candida albicans ATCC 90028 (MIC=32 μM), Cryptococcus neoformans ATCC 208821 (MIC=8-16 μM) [Ref.28741926] 0% hemolysis at 17 μM , 3% hemolysis at 35 μM , 30-48.6% hemolysis at 64 μM , 40% hemolysis at 100 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 > 64 μM against CRL-1739, CC50 = 10.3 ± 1.1 μM against MM96L, CC50 = 51.2 ± 4.0 μM against HFF-1, CC50 > 64 μM against HeLa, CC50 = 48.4 ± 0.7 μM against MCF-7, CC50 = 11.5 ± 0.6 μM against K-562, CC50 = 34.1 ± 3.9 μM against HL-60;CC50=30.8 ± 2.5μM against PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21006 KCRRLCYRQRCVTYCRGR 18 [G1K, K8R]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=2 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=0.5-1 μM), Escherichia coli CGSC 5167 (MIC<0.015 μM), Klebsiella pneumoniae ATCC 700603 (MIC=8 μM), Acinetobacter baumannii ATCC 19606 (MIC=1-2 μM), Pseudomonas aeruginosa ATCC 27853 (MIC<0.25 μM), Helicobacter pylori ATCC 43504 (MIC>80 μM);##Fungi : Candida albicans ATCC 90028 (MIC=2 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.125-0.25 μM) [Ref.28741926] 0% hemolysis at 0.5 μM , 2.5% hemolysis at 0.6 μM , 20% hemolysis at 8 μM , 43.3-56.9% hemolysis at 64 μM , 50% hemolysis at 100 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 19.5 ± 0.5 μM against CRL-1739, CC50 = 1.7 ± 0.1 μM against MM96L, CC50 = 9.0 ± 0.5 μM against HFF-1, CC50 = 44.2 ± 2.2μM against HeLa, CC50 = 6.7 ± 0.7 μM against MCF-7, CC50 = 2.1 ± 0.2 μM against K-562, CC50 = 9.0 ± 1.1μM against HL-60;CC50=5.1 ± 0.3μM against PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21007 GURRLUYKQRUVTYURGR 18 [C/U]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=4-8 μM), Escherichia coli CGSC 5167 (MIC=0.03-0.06 μM), Klebsiella pneumoniae ATCC 700603 (MIC=8-16 μM), Acinetobacter baumannii ATCC 19606 (MIC=4 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=2-4 μM), Helicobacter pylori ATCC 43504 (MIC>80 μM);##Fungi : Candida albicans ATCC 90028 (MIC=4-8 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5-1 μM) [Ref.28741926] 32.3-33.3% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between SeCys2 and SeCys15, SeCys6 and SeCys11. The 'U' in sequence is SelenoCys. L [Ref.28741926] CC50 = 51.0 ± 4.6 μM against CRL-1739, CC50 = 4.6 ± 0.2 μM against MM96L, CC50 = 15.6 ± 3.6 μM against HFF-1, CC50 > 64 μM against HeLa, CC50 = 37.5 ± 3.3 μM against MCF-7, CC50 = 1.4 ± 0.2 μM against K-562, CC50 = 38.5 ± 4.8 μM against HL-60;CC50=15.5 ± 0.8μM against PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21008 GCRRWCYKQRCVTYCRGR 18 [L5W]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8-16 μM) [Ref.28741926] 36.8-43.4% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 18.3 ± 1.4 μM against CRL-1739, CC50 = 4.0 ± 0.1 μM against MM96L, CC50 = 25.0 ± 2.9 μM against HFF-1, CC50 = 17.1 ± 0.7 μM against HeLa, CC50 = 1.0 ± 0.1 μM against K-562. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21009 GCRRLCYKQRCVTYCRGpPR 20 [D-P L-P]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=4 μM), Klebsiella pneumoniae ATCC 700603 (MIC=1-4 μM), Acinetobacter baumannii ATCC 19606 (MIC=1-4 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=4 μM);##Fungi : Candida albicans ATCC 90028 (MIC=8 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5-1 μM) [Ref.28741926] 41.5-44.9% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 22.5 ± 3.3 μM against CRL-1739, CC50 = 3.0 ± 0.1 μM against MM96L, CC50 = 14.9 ± 0.8 μM against HFF-1, CC50 = 51.5 ± 3.9 μM against HeLa, CC50 = 3.9 ± 0.2 μM against K-562, CC50 = 14.1 ± 0.9 μM against PBMCs Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21010 KCRRYCYRQRCVTYCRGR 18 [G1K, L5Y, K8R]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=0.5-1 μM), Klebsiella pneumoniae ATCC 700603 (MIC=4-8 μM), Acinetobacter baumannii ATCC 19606 (MIC=1-2 μM), Pseudomonas aeruginosa ATCC 27853 (MIC<0.25-0.5 μM);##Fungi : Candida albicans ATCC 90028 (MIC=4 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5 μM) [Ref.28741926] 20.6-32% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys2 and Cys15, Cys6 and Cys11. L [Ref.28741926] CC50 = 26.5 ± 2.4 μM against CRL-1739, CC50 = 2.0 ± 0.1 μM against MM96L, CC50 = 14.7 ± 1.5 μM against HFF-1, CC50 = 20.9 ± 1.4 μM against HeLa, CC50 = 15.2 ± 1.9 μM against MCF-7, CC50 = 1.3 ± 0.1 μM against K-562, CC50 = 15.7 ±1.1μM against HL-60;CC50=10.4 ± 1.0μM against PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21011 KURRYUYRQRUVTYURGR 18 [C/U, G1K, L5Y, K8R]cGm (Derived from Gm) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28741926]Gram-positive bacteria : Staphylococcuss aureus ATCC 25923 (MIC=8 μM);##Gram-negative bacteria : Escherichia coli ATCC 25922 (MIC=1-2 μM), Klebsiella pneumoniae ATCC 700603 (MIC=4-16 μM), Acinetobacter baumannii ATCC 19606 (MIC=1-2 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=1 μM);##Fungi : Candida albicans ATCC 90028 (MIC=4 μM), Cryptococcus neoformans ATCC 208821 (MIC=0.5-1 μM) [Ref.28741926] 17.8-24% hemolysis at 64 μM against human red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between SeCys2 and SeCys15, SeCys6 and SeCys11. The 'U' in sequence is SelenoCys. L [Ref.28741926] CC50 = 46.2 ± 7.6 μM against CRL-1739, CC50 = 2.3 ± 0.2 μM against MM96L, CC50 = 30.8 ± 2.0 μM against HFF-1, CC50 = 36.2 ± 2.8 μM against HeLa, CC50 = 29.0 ± 3.7 μM against MCF-7, CC50 = 6.4 ± 0.6 μM against K-562, CC50 = 33.3 ±7.4μM against HL-60;CC50=9.5 ± 0.5μM against PBMCs. Not found 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. doi: 10.1021/acschembio.7b00459.? Sonia Troeira Henriques, Nicole Lawrence, Stephanie Chaousis, Anjaneya S. Ravipati, Olivier Cheneval,Aurelie H. Benfield, Alysha G. Elliott, Angela Maria Kavanagh, Matthew A. Cooper, Lai Yue Chan,Yen-Hua Huang, and David J. Craik Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP21012 KILRGVCKKIMRTFLRRISKDILTGKK 27 NK-2 (Mammals, Animals) No entry found Not found Not found Mammal Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Not found Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.29043494]Gram-positive bacteria : Staphylococcus aureus (MIC=2 μM), Staphylococcus epidermidis (MIC=2 μM);##Gram-negative bacteria : Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=8 μM) [Ref.29043494] 2.5% hemolysis at 10 μg/ml , 8% hemolysis at 25 μg/ml , 22% hemolysis at 50 μg/ml , 32.5% hemolysis at 75 μg/ml , 36% hemolysis at 150 μg/ml , 38% hemolysis at 300 μg/ml against human red blood cells Linear Free Amidation L [Ref.29043494] IC50 = 25.1 μM against NK-2. ##IC50 = 8.4 μM against EJ. ##IC50 = 4.1 μM against PC-3. ##IC50 = 10.1 μM against T24. ##IC50 = 13.7 μM against HL-60. ##The proliferation inhibition activity on K562 is not significant. Not found 29043494 Probiotics Antimicrob Proteins. 2018 Mar;10(1):118-127. doi: 10.1007/s12602-017-9335-1. Jiexi Yan & Xiaolei Liang & Chang Liu & Yuemei Cheng & Lanxia Zhou & Kairong Wang & Li Zhao Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2 DRAMP21013 KILRGVCKKIMRPFLRRISKDILTGKK 27 NK-pro (Derived from NK-2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29043494]Gram-positive bacteria : Staphylococcus aureus (MIC=4 μM), Staphylococcus epidermidis (MIC=4 μM);##Gram-negative bacteria : Escherichia coli (MIC=4 μM), Pseudomonas aeruginosa (MIC=16 μM) [Ref.29043494] 0.3% hemolysis at 10 μg/ml , 2% hemolysis at 25 μg/ml , 5.5% hemolysis at 50 μg/ml , 8% hemolysis at 75 μg/ml , 15% hemolysis at 150 μg/ml , 28% hemolysis at 300 μg/ml against human red blood cells Linear Free Amidation L [Ref.29043494] IC50 = 43.7 μM against NK-2. ##IC50 = 23.3 μM against EJ. ##IC50 = 9.3 μM against PC-3. ##IC50 = 33.0 μM against T24. ##IC50 = 26.1 μM against HL-60. ####The proliferation inhibition activity on K562 is not significant. Not found 29043494 Probiotics Antimicrob Proteins. 2018 Mar;10(1):118-127. doi: 10.1007/s12602-017-9335-1. Jiexi Yan & Xiaolei Liang & Chang Liu & Yuemei Cheng & Lanxia Zhou & Kairong Wang & Li Zhao Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2 DRAMP21014 KILPGVCKKIMRPFLRRISKDILTGKK 27 NK-dpro (Derived from NK-2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antitumor Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29043494]Gram-positive bacteria : Staphylococcus aureus (MIC=8 μM), Staphylococcus epidermidis (MIC=8 μM);##Gram-negative bacteria : Escherichia coli (MIC=8 μM), Pseudomonas aeruginosa (MIC=32 μM) [Ref.29043494] 0% hemolysis at 10 μg/ml , 2% hemolysis at 25 μg/ml , 3% hemolysis at 50 μg/ml , 4.5% hemolysis at 75 μg/ml , 10% hemolysis at 150 μg/ml , 20% hemolysis at 300 μg/ml against human red blood cells Linear Free Amidation L [Ref.29043494] IC50 = 32.5 μM against NK-2. ##IC50 = 28.7 μM against EJ. ##IC50 = 9.6 μM against PC-3. ##IC50 = 39.6 μM against T24. ##IC50 = 48.4 μM against HL-60. ##The proliferation inhibition activity on K562 is not significant. Not found 29043494 Probiotics Antimicrob Proteins. 2018 Mar;10(1):118-127. doi: 10.1007/s12602-017-9335-1. Jiexi Yan & Xiaolei Liang & Chang Liu & Yuemei Cheng & Lanxia Zhou & Kairong Wang & Li Zhao Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2 DRAMP21015 RIGSILGALAKGLPTLISWIKNR 23 A (A1R) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=6.25 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=6.25 μM), Klebsiella pneumoniae (MIC=12.5 μM) [Ref.27271216] 100% hemolysis at 20μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 82%, 40%, 8%, 2% and almost 0% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21016 AIGSILGRLAKGLPTLISWIKNR 23 A (A8R) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=3.13 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=12.5 μM) [Ref.27271216] 80% hemolysis at 20 μM , 100% hemolysis at 40 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 97%, 58%, 10%, 2% and almost 0% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21017 AIGSILGALAKGLPTLKSWIKNR 23 A (I17K) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=50 μM), Staphylococcus epidermidis (MIC=12.5 μM), Bacillus subtilis (MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli (MIC=25 μM), Pseudomonas aeruginosa (MIC=25 μM), Klebsiella pneumoniae (MIC=50 μM) [Ref.27271216] 5% hemolysis at 20 μM , 13% hemolysis at 40 μM , 20% hemolysis at 60 μM , 30% hemolysis at 80 μM , 35% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 98%, 92%, 53%, 34% and 7.9% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21018 AIGSILGALAKGLPTLRSWIKNR 23 A (I17R) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=25 μM), Staphylococcus epidermidis (MIC=6.25 μM), Bacillus subtilis (MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=25 μM) [Ref.27271216] 10% hemolysis at 20 μM , 15% hemolysis at 40 μM , 20% hemolysis at 60 μM , 30% hemolysis at 80 μM , 35% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 85%, 68%, 21% and 6.6% at peptide concentrations of 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21019 RIGSILGRLAKGLPTLISWIKNR 23 A (A1R, A8R) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=12.5 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli (MIC=6.25 μM), Pseudomonas aeruginosa (MIC=6.25 μM), Klebsiella pneumoniae (MIC=6.25 μM) [Ref.27271216] 58% hemolysis at 20 μM , 80% hemolysis at 40 μM , 100% hemolysis at 60 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 92%, 80%, 29%, 1% and almost 0% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21020 RIGSILGALAKGLPTLKSWIKNR 23 A (A1R, I17K) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=100 μM), Staphylococcus epidermidis (MIC=6.25 μM), Bacillus subtilis (MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli (MIC=25 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=25 μM) [Ref.27271216] 2% hemolysis at 20 μM , 5% hemolysis at 40 μM , 10% hemolysis at 60 μM , 20% hemolysis at 80 μM , 30% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 95%, 92%, 60%, 33% and 24% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji DRAMP21021 AIGSILGRLAKGLPTLKSWIKNR 23 A (A8R, I17K) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=100 μM), Staphylococcus epidermidis (MIC=6.25 μM), Bacillus subtilis (MIC=12.5 μM);##Gram-negative bacteria : Escherichia coli (MIC=25 μM), Pseudomonas aeruginosa (MIC=25 μM), Klebsiella pneumoniae (MIC=25 μM) [Ref.27271216] 2% hemolysis at 20 [Ref.27271216] 2% hemolysis at 20 μM , 5% hemolysis at 40 μM , 10% hemolysis at 60 μM , 20% hemolysis at 80 μM , 30% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 100%, 99%, 92%, 64% and 21.1% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM. Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21022 RIGSILGRLAKGLPTLKSWIKNR 23 A (A1R, A8R, I17K) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=100 μM), Staphylococcus epidermidis (MIC=6.25 μM), Bacillus subtilis (MIC=12.5 μM);##Gram-negative bacteria : Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=12.5 μM) [Ref.27271216] 0% hemolysis at 40 μM , 1% hemolysis at 60 μM , 2% hemolysis at 80 μM , 2% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 96%, 95%, 92%, 68% and 31.4% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21023 RIGSILGRLAKGLPTLRSWIKNR 23 A (A1R, A8R, I17R) (Derived from AR-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27271216]Gram-positive bacteria : Staphylococcuss aureus (MIC=100 μM), Staphylococcus epidermidis (MIC=3.13 μM), Bacillus subtilis (MIC=12.5 μM);##Gram-negative bacteria : Escherichia coli (MIC=12.5 μM), Pseudomonas aeruginosa (MIC=12.5 μM), Klebsiella pneumoniae (MIC=12.5 μM) [Ref.27271216] 4% hemolysis at 40 μM , 10% hemolysis at 60 μM , 15% hemolysis at 80 μM , 20% hemolysis at 100 μM against human red blood cells Linear Free Amidation L [Ref.27271216] In L929 cells, the cell viability is 92%, 92%, 80%, 60% and 12% at peptide concentrations of 3.12, 6.25, 12.5, 25 and 50 μM Not found 27271216 Sci Rep. 2016 Jun 8;6:27394. doi: 10.1038/srep27394. Shi-KunZhang, Jin-wen Song, FengGong, Su-Bo Li, Hong-Yu Chang, Hui-MinXie, Hong-WeiGao, Ying-XiaTan & Shou-Ping Ji Design of an α-helical antimicrobial peptide with improved cell selective and potent anti-biofilm activity DRAMP21024 FFSLIPSLVGGLISAFK 17 Stigmurin (Tityus, Scorpionida, Arachnida) No entry found Not found Not found Scorpion Tityus stigmurus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida glabrata, Candida krusei [Ref.30709056]Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=9.4 μM), Staphylococcus epidermidis (ATCC 12228)(MIC=9.4 μM), Enterococcus faecalis (ATCC 4028)(MIC>150 μM);##Gram-negative bacteria : Pseudomonas aeruginosa (ATCC 27853)(MIC>150 μM), Escherichia coli (ATCC 25922)(MIC>150 μM), Enterobacter cloacae (ATCC 13047)(MIC>150 μM);##Fungi : Candida albicans (ATCC 90028)(MIC=37.5 μM), Candida glabrata (ATCC 90030)(MIC>150 μM), Candida krusei (ATCC 6258)(MIC>150 μM) [Ref.30709056] 7% hemolysis at 1.2 μg/ml , 4% hemolysis at 2.3 μg/ml , 2% hemolysis at 4.7 μg/ml , 0% hemolysis at 9.4 μg/ml , 3% hemolysis at 18.8 μg/ml , 2% hemolysis at 37.5 μg/ml , 3% hemolysis at 75 μg/ml , 5% hemolysis at 150 μg/ml against human red blood cells Linear Free Amidation L [Ref.30709056] No cytotoxicity information found. Not found 30709056 Int J Mol Sci. 2019 Jan 31;20(3). pii: E623. doi: 10.3390/ijms20030623. Bruno Amorim-Carmo , Alessandra Daniele-Silva , Adriana M. S. Parente ,Allanny A. Furtado , Eneas Carvalho , Johny W. F. Oliveira , Elizabeth C. G. Santos , Marcelo S. Silva , Sérgio R. B. Silva , Arnóbio A. Silva-Júnior , Norberto K. Monteiro and Matheus F. Fernandes-Pedrosa Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin DRAMP21025 FFSLIPSLVKKLIKAFK 17 StigA25 (Derived from Stigmurin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida glabrata, Candida krusei [Ref.30709056]Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=1.2 μM), Staphylococcus epidermidis (ATCC 12228)(MIC=2.3 μM), Enterococcus faecalis (ATCC 4028)(MIC=4.7 μM);##Gram-negative bacteria : Pseudomonas aeruginosa (ATCC 27853)(MIC=4.7 μM), Escherichia coli (ATCC 25922)(MIC=2.3 μM), Enterobacter cloacae (ATCC 13047)(MIC=18.8 μM);##Fungi : Candida albicans (ATCC 90028)(MIC=9.4 μM), Candida glabrata (ATCC 90030)(MIC=9.4 μM), Candida krusei (ATCC 6258)(MIC=9.4 μM) [Ref.30709056] 1% hemolysis at 1.2 μg/ml , 5% hemolysis at 2.3 μg/ml , 9% hemolysis at 4.7 μg/ml , 19% hemolysis at 9.4 μg/ml , 33% hemolysis at 18.8 μg/ml , 60% hemolysis at 37.5 μg/ml , 78% hemolysis at 75 μg/ml , 93% hemolysis at 150 μg/ml against human red blood cells Linear Free Amidation L [Ref.30709056] No cytotoxicity information found. Not found 30709056 Int J Mol Sci. 2019 Jan 31;20(3). pii: E623. doi: 10.3390/ijms20030623. Bruno Amorim-Carmo , Alessandra Daniele-Silva , Adriana M. S. Parente ,Allanny A. Furtado , Eneas Carvalho , Johny W. F. Oliveira , Elizabeth C. G. Santos , Marcelo S. Silva , Sérgio R. B. Silva , Arnóbio A. Silva-Júnior , Norberto K. Monteiro and Matheus F. Fernandes-Pedrosa Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin DRAMP21026 FFKLIPKLVKKLIKAFK 17 StigA31 (Derived from Stigmurin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida glabrata, Candida krusei [Ref.30709056]Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=2.3 μM), Staphylococcus epidermidis (ATCC 12228)(MIC=2.3 μM), Enterococcus faecalis (ATCC 4028)(MIC=1.2 μM);##Gram-negative bacteria : Pseudomonas aeruginosa (ATCC 27853)(MIC=2.3 μM), Escherichia coli (ATCC 25922)(MIC=1.2 μM), Enterobacter cloacae (ATCC 13047)(MIC=4.7 μM);##Fungi : Candida albicans (ATCC 90028)(MIC=4.7 μM), Candida glabrata (ATCC 90030)(MIC=4.7 μM), Candida krusei (ATCC 6258)(MIC=4.7 μM) [Ref.30709056] 1% hemolysis at 1.2 μg/ml , 6% hemolysis at 2.3 μg/ml , 10% hemolysis at 4.7 μg/ml , 12 % hemolysis at 9.4 μg/ml , 23% hemolysis at 18.8 μg/ml , 45% hemolysis at 37.5 μg/ml , 65% hemolysis at 75 μg/ml , 70% hemolysis at 150 μg/ml against human red blood cells Linear Free Amidation L [Ref.30709056] No cytotoxicity information found. Not found 30709056 Int J Mol Sci. 2019 Jan 31;20(3). pii: E623. doi: 10.3390/ijms20030623. Bruno Amorim-Carmo , Alessandra Daniele-Silva , Adriana M. S. Parente ,Allanny A. Furtado , Eneas Carvalho , Johny W. F. Oliveira , Elizabeth C. G. Santos , Marcelo S. Silva , Sérgio R. B. Silva , Arnóbio A. Silva-Júnior , Norberto K. Monteiro and Matheus F. Fernandes-Pedrosa Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin DRAMP21027 ALWKKILKNAGKAALNKINQIVQ 23 K5, 17-DPS3 (Derived from dermaseptin-PS3 (DPS3)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix These three peptides existed in random coils in aqueous solution, they all adopted Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.30087268]Gram-positive bacteria : Staphylococcuss aureus (NCTC 10788)(MIC=8 μM);##Gram-negative bacteria : Escherichia coli (NCTC 10418)(MIC=8 μM);##Fungi : Candida albicans (NCYC 1467)(MIC=4 μM) [Ref.30087268] 8% hemolysis at 0 μM , 40% hemolysis at 1 μM , 90% hemolysis at 2 μM against horse red blood cells Linear Free Amidation L [Ref.30087268] IC50 = 18.20 μM for H157. ##IC50 = 18.20 μM for PC3. ##IC50 = 132.10 μM for HMEC-1 Not found 30087268 Toxins (Basel). 2018 Aug 7;10(8). pii: E320. doi: 10.3390/toxins10080320. Yining Tan ,Xiaoling Chen , Chengbang Ma , Xinping Xi ,Lei Wang , Mei Zhou ,James F. Burrows ,Hang Fai Kwok 2 ID and Tianbao Chen Biological Activities of Cationicity-Enhanced and Hydrophobicity-Optimized Analogues of an Antimicrobial Peptide, Dermaseptin-PS3, from the Skin Secretion of Phyllomedusa sauvagii DRAMP21028 ALWKDILKNLLKAALNEINQIVQ 23 L10, 11-DPS3 (Derived from dermaseptin-PS3 (DPS3)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix These three peptides existed in random coils in aqueous solution, they all adopted Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.30087268]Gram-positive bacteria : Staphylococcuss aureus (NCTC 10788)(MIC=8 μM);##Gram-negative bacteria : Escherichia coli (NCTC 10418)(MIC=16 μM);##Fungi : Candida albicans (NCYC 1467)(MIC=16 μM) [Ref.30087268] 20% hemolysis at 0 μM , 70% hemolysis at 1 μM , 95% hemolysis at 2 μM against horse red blood cells Linear Free Amidation L [Ref.30087268] IC50 = 0.12 μM for H157. ##IC50 = 1.85 μM for PC3. ##IC50 = 8.76 μM for HMEC-1 Not found 30087268 Toxins (Basel). 2018 Aug 7;10(8). pii: E320. doi: 10.3390/toxins10080320. Yining Tan ,Xiaoling Chen , Chengbang Ma , Xinping Xi ,Lei Wang , Mei Zhou ,James F. Burrows ,Hang Fai Kwok 2 ID and Tianbao Chen Yining Tan ,Xiaoling Chen , Chengbang Ma , Xinping Xi ,Lei Wang , Mei Zhou ,James F. Burrows ,Hang Fai Kwok 2 ID and Tianbao Chen DRAMP21029 ATYRTGRATRESLSGVEISGRLYRLR 26 D5R (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=100 μM), Bacillus subtilis (NCIM 2162)(MIC=20 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=50 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=100 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=20 μM), Saccharomyces cerevisiae (BY4741)(MIC=100 μM) [Ref.26206286] 0% hemolysis at 100μM against human red blood cells Linear Free Free L [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21030 ATYrTGrATrESLSGVEISGrLYrLR 26 D5r (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=100 μM), Bacillus subtilis (NCIM 2162)(MIC=50 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=50 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=200 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=20 μM) [Ref.26206286] 0% hemolysis at 100μM against human red blood cells Linear Free Free Mixed(D-Arg4, D-Arg7, D-Arg10, D-Arg21, D-Arg24) [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21031 ATYRTGRATRESLSGVEISGRLYRLR 26 MyD5R (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=7.5 μM), Bacillus subtilis (NCIM 2162)(MIC=20 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=5 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=10 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=10 μM), Saccharomyces cerevisiae (BY4741)(MIC=20 μM) [Ref.26206286] 23% hemolysis at 10 μM , 50% hemolysis at 20 μM , 75% hemolysis at 50 μM , 87.5% hemolysis at 100 μM against human red blood cells Linear Acylation (Conjugated with myristic acid) Free L [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21032 ATYrTGrATrESLSGVEISGrLYrLR 26 MyD5r (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=7.5 μM), Bacillus subtilis (NCIM 2162)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=5 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=7.5 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=10 μM), Saccharomyces cerevisiae (BY4741)(MIC=20 μM) [Ref.26206286] 17% hemolysis at 10 μM , 25% hemolysis at 20 μM , 50% hemolysis at 50 μM , 70% hemolysis at 100 μM against human red blood cells Linear Acylation (Conjugated with myristic acid) Free Mixed(D-Arg4, D-Arg7, D-Arg10, D-Arg21, D-Arg24) [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21033 ATYRTGRATRESLSGVEISGRLYRLR 26 LaD5R (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=2 μM), Bacillus subtilis (NCIM 2162)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=20 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=10 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=10 μM), Saccharomyces cerevisiae (BY4741)(MIC=10 μM) [Ref.26206286] 0% hemolysis at 100μM against human red blood cells Linear Acylation (Conjugated with lauric acid) Free L [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21034 ATYrTGrATrESLSGVEISGrLYrLR 26 LaD5r (Derived from HD5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Saccharomyces cerevisiae [Ref.26206286]Gram-positive bacteria : Staphylococcus aureus (NCTC 8530)(MIC=20 μM), Bacillus subtilis (NCIM 2162)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (MG 1655)(MIC=10 μM), Pseudomonas aeruginosa (NCTC 6750)(MIC=50 μM);##Fungi : Candida albicans (ATCC 18804)(MIC=10 μM), Saccharomyces cerevisiae (BY4741)(MIC=10 μM) [Ref.26206286] 0% hemolysis at 100μM against human red blood cells Linear Acylation (Conjugated with lauric acid) Free Mixed(D-Arg4, D-Arg7, D-Arg10, D-Arg21, D-Arg24) [Ref.26206286] No cytotoxic information found. Not found 26206286 Peptides. 2015 Sep;71:128-40. doi: 10.1016/j.peptides.2015.07.009. Epub 2015 Jul 20. Basil Mathew Ramakrishnan Nagaraj Antimicrobial activity of human-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs DRAMP21035 KAAKAAKKAAKAAWK 15 AC-UM-14W (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26235946]Gram-positive bacteria : Bacillus subtilis (MIC>200 μg/ml), Staphylococcus aureus (MIC>200 μg/ml), Staphylococcus epidermis (MIC>200 μg/ml);##Gram-negative bacteria : Escherichia coli (MIC>200 μg/ml), Shigella dysentariae (MIC>200 μg/ml), Salmonella typhimurium (MIC>200 μg/ml), Klebsiella pneumonia (MIC>200 μg/ml), Pseudomonas aeruginosa (MIC>200 μg/ml) [Ref.26235946] <1% hemolysis at 12.5 μM , <1% hemolysis at 25 μM against human red blood cells Linear Acylation (Conjugated with acetyl group) Amidation L [Ref.26235946] No cytotoxic information found. Not found 26235946 Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Thuy T. T. Dinh , Do-Hee Kim , Huy X. Luong , Bong-Jin Lee , Young-Woo Kim Antimicrobial activity of doubly-stapled alanine/lysine-based peptides DRAMP21036 RWKIFKKIPKFLHSAKKF 18 PapMA (Derived from Papiliocin and Magainin 2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix PapMA and PapMA-k exhibited α-helical structures in 50 mM DPC micelles and 50% TFE/H2O but displayed unordered structures in aqueous solution. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26053120] Gram-positive bacteria : Bacillus subtilis(MIC=4.0 μM), Enterococcus faecalis(MIC=16 μM), Staphylococcus aureus(MIC=4.0 μM), ;##Gram-negative bacteria : Escherichia coli(MIC=2.0 μM), Pseudomonas aeruginosa(MIC=4.0 μM), Salmonella typhimurium(MIC=4.0 μM) [Ref.26053120] MHC=100 μM against human red blood cells Linear Free Amidation L [Ref.26053120] IC50 = 10 μM against mouse macrophage-derived RAW264.7 cells. ##IC50 = 9 μM for NIH3T3 fibroblasts. Not found 26053120 Biochemistry. 2015 Jun 30;54(25):3921-31. doi: 10.1021/acs.biochem.5b00392. Areum Shin, Eunjung Lee, Dasom Jeon, Young-Guen Park, Jeong Kyu Bang, Yong-Sun Park, Song Yub Shin, and Yangmee Kim Peptoid-Substituted Hybrid Antimicrobial Peptide Derived from Papiliocin and Magainin 2 with Enhanced Bacterial Selectivity and Anti-inflammatory Activity DRAMP21037 RWKIFKKIkKFLHSAKKF 18 PapMA-k (Derived from Papiliocin and Magainin 2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix PapMA and PapMA-k exhibited α-helical structures in 50 mM DPC micelles and 50% TFE/H3O but displayed unordered structures in aqueous solution. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26053120] Gram-positive bacteria : Bacillus subtilis(MIC=4.0 μM), Enterococcus faecalis(MIC=16 μM), Staphylococcus aureus(MIC=4.0 μM), ;##Gram-negative bacteria : Escherichia coli(MIC=2.0 μM), Pseudomonas aeruginosa(MIC=4.0 μM), Salmonella typhimurium(MIC=2.0 μM) [Ref.26053120] MHC=200 μM against human red blood cells Linear Free Amidation The 'k' in sequence is lysine peptoid L [Ref.26053120] IC50 = 42 μM against mouse macrophage-derived RAW264.7 cells. ##IC50 = 39 μM for NIH3T3 fibroblasts. Not found 26053120 Biochemistry. 2015 Jun 30;54(25):3921-31. doi: 10.1021/acs.biochem.5b00392. Areum Shin, Eunjung Lee, Dasom Jeon, Young-Guen Park, Jeong Kyu Bang, Yong-Sun Park, Song Yub Shin, and Yangmee Kim Peptoid-Substituted Hybrid Antimicrobial Peptide Derived from Papiliocin and Magainin 2 with Enhanced Bacterial Selectivity and Anti-inflammatory Activity DRAMP21038 WGRRGWGPGRRYVRN 15 analog 1 (Derived from Ib-AMP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, beta turn In sodium phosphate buffer, the CD spectra of Ib-AMP1 and all linear analogs showed a large absorbance in the region of 190-200 nm, indicating a random coil structure. The spectra of Ib-AMP1 and analogs 1, 2, 3, and 4 became significantly more b-turn in 30 mM SDS micelles Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19778562] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=8 μM), Staphylococcus aureus(KCTC 1621)(MIC=4 μM), Staphylococcus aureus (MRSA)(CCARM 3543)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=16 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=4 μM), Pseudomonas aeruginosa (MDRPA)(CCARM 2095)(MIC=16 μM) [Ref.19778562] MHC>400 μM against human red blood cells Linear Free Amidation L [Ref.19778562] No cytotoxicity information found. Not found 19778562 Peptides. 2009 Dec;30(12):2144-9. doi: 10.1016/j.peptides.2009.09.020. Peng Wang , Jeong-Kyu Bang , Hak Jun Kim , Jin-Kyoung Kim , Yangmee Kim , Song Yub Shin Antimicrobial specificity and mechanism of action of disulfide-removed linear analogs of the plant-derived Cys-rich antimicrobial peptide Ib-AMP1 DRAMP21039 WGRRGWGpGRRYVRN 15 analog 2 (Derived from Ib-AMP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, beta turn In sodium phosphate buffer, the CD spectra of Ib-AMP1 and all linear analogs showed a large absorbance in the region of 190-200 nm, indicating a random coil structure. The spectra of Ib-AMP1 and analogs 1, 2, 3, and 4 became significantly more b-turn in 30 mM SDS micelles Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19778562] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 [Ref.19778562] MHC>400 Linear Free Amidation Mixed(D-Pro8) [Ref.19778562] No cytotoxicity information found. Not found 19778562 Peptides.?2009 Dec;30(12):2144-9. doi: 10.1016/j.peptides.2009.09.020. Peng Wang , Jeong-Kyu Bang , Hak Jun Kim , Jin-Kyoung Kim , Yangmee Kim , Song Yub Shin Antimicrobial specificity and mechanism of action of disulfide-removed linear analogs of the plant-derived Cys-rich antimicrobial peptide Ib-AMP1 DRAMP21040 WGRRGWGaGRRYVRW 15 analog 3 (Derived from Ib-AMP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, beta turn In sodium phosphate buffer, the CD spectra of Ib-AMP1 and all linear analogs showed a large absorbance in the region of 190–200 nm, indicating a random coil structure. The spectra of Ib-AMP1 and analogs 1, 2, 3, and 4 became significantly more b-turn in 30 mM SDS micelles Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19778562] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=8 μM), Staphylococcus aureus(KCTC 1621)(MIC=4 μM), Staphylococcus aureus (MRSA)(CCARM 3543)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=16 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=4 μM), Pseudomonas aeruginosa (MDRPA)(CCARM 2095)(MIC=16 μM) [Ref.19778562] MHC>400 [Ref.19778562] MHC>400 μM against human red blood cells Linear Free Amidation The 'a' in sequence is Ala peptoid residue (Nala) (CH3–NH–CH2–COOH) L [Ref.19778562] No cytotoxicity information found. Not found 19778562 Peptides. 2009 Dec;30(12):2144-9. doi: 10.1016/j.peptides.2009.09.020. Peng Wang , Jeong-Kyu Bang , Hak Jun Kim , Jin-Kyoung Kim , Yangmee Kim , Song Yub Shin Antimicrobial specificity and mechanism of action of disulfide-removed linear analogs of the plant-derived Cys-rich antimicrobial peptide Ib-AMP1 DRAMP21041 WGRRGWGkGRRYVRW 15 analog 4 (Derived from Ib-AMP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, beta turn In sodium phosphate buffer, the CD spectra of Ib-AMP1 and all linear analogs showed a large absorbance in the region of 190–200 nm, indicating a random coil structure. The spectra of Ib-AMP1 and analogs 1, 2, 3, and 4 became significantly more b-turn in 30 mM SDS micelles Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19778562] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=8 μM), Staphylococcus aureus(KCTC 1621)(MIC=4 μM), Staphylococcus aureus (MRSA)(CCARM 3543)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=4 μM), Pseudomonas aeruginosa (MDRPA)(CCARM 2095)(MIC=16 μM) [Ref.19778562] MHC>400 μM against human red blood cells Linear Free Amidation The 'k' in sequence is Lys peptoid residue (Nlys) (NH2–CH2–CH2–CH2–CH2–NH–CH2–COOH). L [Ref.19778562] No cytotoxicity information found. Not found 19778562 Peptides. 2009 Dec;30(12):2144-9. doi: 10.1016/j.peptides.2009.09.020. Peng Wang , Jeong-Kyu Bang , Hak Jun Kim , Jin-Kyoung Kim , Yangmee Kim , Song Yub Shin Antimicrobial specificity and mechanism of action of disulfide-removed linear analogs of the plant-derived Cys-rich antimicrobial peptide Ib-AMP1 DRAMP21042 ILPWKWPWWKWRR 13 A2 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=10 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=20 μg/ml), Pseudomonas aeruginosa(MIC=20 μg/ml), Salmonella typhimurium(MIC=10 μg/ml) [Ref.19428758] HC50=490 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21043 ILKWKWPWWPWRR 13 A3 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=5 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=10 μg/ml), Pseudomonas aeruginosa(MIC=20 μg/ml), Salmonella typhimurium(MIC=10 μg/ml) [Ref.19428758] HC50=400 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21044 ILKWKWKWWPWRR 13 A4 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=10 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=10 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=10 μg/ml), Pseudomonas aeruginosa(MIC=10 μg/ml), Salmonella typhimurium(MIC=10 μg/ml) [Ref.19428758] HC50=560 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21045 ILPWKWKWWKWRR 13 A5 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=5 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=10 μg/ml), Pseudomonas aeruginosa(MIC=10 μg/ml), Salmonella typhimurium(MIC=10 μg/ml) [Ref.19428758] HC50>800 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21046 ILKWKWPWWKWRR 13 A6 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=5 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=10 μg/ml), Pseudomonas aeruginosa(MIC=10 μg/ml), Salmonella typhimurium(MIC=10 μg/ml) [Ref.19428758] HC50>800 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21047 ILKWKWKWWKWRR 13 A7 (Derived from Indolicidin (IN)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.19428758] Gram-positive bacteria : Bacillus subtilis(MIC=5 μg/ml), Staphylococcus epidermidis(MIC=10 μg/ml), Staphylococcus aureus(MIC=5 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=10 μg/ml), Pseudomonas aeruginosa(MIC=10 μg/ml), Salmonella typhimurium(MIC=5 μg/ml) [Ref.19428758] HC50>800 μg/ml against human red blood cells Linear Free Amidation L [Ref.19428758] No cytotoxicity information found. Not found 19428758 Peptides. 2009 May;30(5):832-8. doi: 10.1016/j.peptides.2009.01.015. Yong Hai Nan , Jeong-Kyu Bang , Song Yub Shin Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity DRAMP21048 GLLWKWGWKWKEFLRIVGY 19 peptide 6 (Derived from seq2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28236791] Gram-positive bacteria : Staphylococcus aureus(MIC>1024 μg/ml);##Gram-negative bacteria : Pseudomonas aeruginosa(MIC>1024 μg/ml) [Ref.28236791] 51.36% hemolysis at 128 μg/ml Linear Free Amidation L [Ref.28236791] No cytotoxicity information found. Not found 28236791 Colloids Surf B Biointerfaces. 2017 May 1;153:152-159. doi: 10.1016/j.colsurfb.2017.02.003. P. Maturanaa, M. Martinez , M.E. Noguerac, N.C. Santos , E.A. Disalvoa, L. Semorile , P.C. Maffia , A. Hollmann Lipid selectivity in novel antimicrobial peptides: Implication on antimicrobial and hemolytic activity DRAMP21049 GLLRKWGKKWKEFLRRVWK 19 peptide 6.2 (Derived from seq2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix The spectra obtained confirmed an alpha-helix conversion in the presence of negatively charged micelles. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28236791] Gram-positive bacteria : Staphylococcus aureus(MIC=32 μg/ml);##Gram-negative bacteria : Pseudomonas aeruginosa(MIC=32 μg/ml) [Ref.28236791] 34.46% hemolysis at 128 μg/ml Linear Free Amidation L [Ref.28236791] No cytotoxicity information found. Not found 28236791 Colloids Surf B Biointerfaces. 2017 May 1;153:152-159. doi: 10.1016/j.colsurfb.2017.02.003. P. Maturanaa, M. Martinez , M.E. Noguerac, N.C. Santos , E.A. Disalvoa, L. Semorile , P.C. Maffia , A. Hollmann Lipid selectivity in novel antimicrobial peptides: Implication on antimicrobial and hemolytic activity DRAMP21050 AWCFRVCYRGICYRRCR 17 TP1[K1A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.03 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=0.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.03 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.06 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.125 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.125 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=2 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.125 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.125 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.5 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=2.1 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-1 DRAMP21051 KACFRVCYRGICYRRCR 17 TP1[W2A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=1 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.5 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=8 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-2 DRAMP21052 KWAFRVCYRGICYRRSR 17 TP1[C3A, C16S] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC>16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=4 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC>16 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC>16 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC>16 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC>16 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=4 μg/ml) [Ref.28960954] MHC10=8 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bond between Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-3 DRAMP21053 KWCARVCYRGICYRRCR 17 TP1[F4A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.5 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.5 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=40 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-4 DRAMP21054 KWCFAVCYRGICYRRCR 17 TP1[R5A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.03 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=0.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.5 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.06 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.125 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.5 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=4 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=2 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-5 DRAMP21055 KWCFRACYRGICYRRCR 17 TP1[V6A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=1 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=1.2 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-6 DRAMP21056 KWCFRVAYRGISYRRCR 17 TP1[C7A, C12S] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=2 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=4 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=2 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=2 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=1 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bond between Cys3 and Cys16. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis.2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-7 DRAMP21057 KWCFRVCARGICYRRCR 17 TP1[Y8A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.06 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=8 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=0.125 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=1 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=2 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC= μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=8 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bond between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-8 DRAMP21058 KWCFRVCYAGICYRRCR 17 TP1[R9A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=1 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.03 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.25 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.125 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=2 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.06 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.125 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=1 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=2 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=2 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-9 DRAMP21059 KWCFRVCYRAICYRRCR 17 TP1[G10A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.03 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=0.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.06 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.03 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.25 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.25 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=4 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.6 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.6 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.5 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=2 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.06 μg/ml) [Ref.28960954] MHC10=0.5 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-10 DRAMP21060 KWCFRVCYRGACYRRCR 17 TP1[I11A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=2 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.25 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=1 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=2 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=32 μg/ml against human red blood cells Cyclic Free Amidation (Arg17) Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-11 DRAMP21061 KWCFRVSYRGIAYRRCR 17 TP1[C7S, C12A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=1 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=4 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=8 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=1 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=8 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=2 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=0.6 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bond between Cys3 and Cys16. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-12 DRAMP21062 KWCFRVCYRGICARRCR 17 TP1[Y13A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.06 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.5 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.125 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.5 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=4 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=1 [Ref.28960954] MHC10=1 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bond between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-13 DRAMP21063 KWCFRVCYRGICYARCR 17 TP1[R14A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=0.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.06 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.25 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=1 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.125 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.125 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.125 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.25 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=0.5 [Ref.28960954] MHC10=0.5 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-14 DRAMP21064 KWCFRVCYRGICYRACR 17 TP1[R15A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.03 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=2 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=4 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=2 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=0.45 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-15 DRAMP21065 KWSFRVCYRGICYRRAR 17 TP1[C3S, C16A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=1 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=2 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=4 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=3 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bond between Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-16 DRAMP21066 KWCFRVCYRGICYRRCA 17 TP1[R17A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.015 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=0.5 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.015 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.25 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.25 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=4 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.125 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.125 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.5 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=4 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=0.45 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-17 DRAMP21067 KWAFRVCYRGICYRRAR 17 TP1[C3A, C16A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=1 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=1 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=2 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=8 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=40 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bond between Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-18 DRAMP21068 KWCFRVAYRGIAYRRCR 17 TP1[C7A, C12A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=2 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=2 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=8 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bond between Cys3 and Cys16. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-19 DRAMP21069 KWAFRVAYRGIAYRRAR 17 TP1[C3A, C7A, C12A, C16A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=1 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=8 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=16 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=4 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=4 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC>16 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=0.24 μg/ml against human red blood cells Linear Free Amidation L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-20 DRAMP21070 KWCFRRCYAGICYRRCR 17 TP1[V6R, R9A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC>16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC>16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC>16 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=16 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC>16 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC>16 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=4 μg/ml) [Ref.28960954] MHC10=11 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-21 DRAMP21071 RWCFRVCYRGICYRRCR 17 TP1[K1R] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=1 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.25 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=4 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.125 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.25 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=0.5 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=4 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.25 μg/ml) [Ref.28960954] MHC10=1 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-22 DRAMP21072 KWCGRVCYRGICYRRCR 17 TP1[F4G] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=2 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=1 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=2 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=2 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=2 μg/ml) [Ref.28960954] MHC10=0.47 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-23 DRAMP21073 KWCSRVCYRGICYRRCR 17 TP1[F4S] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=2 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=4 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=4 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=2 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=4 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=4 μg/ml) [Ref.28960954] MHC10=0.23 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-24 DRAMP21074 KWCFRVCGRGICYRRCR 17 TP1[Y8G] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.5 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=2 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=8 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=8 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=2 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=4 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=4 μg/ml) [Ref.28960954] MHC10=0.4 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-25 DRAMP21075 KWCFRVCYRGGCYRRCR 17 TP1[I11G] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.25 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=2 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.5 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=0.2 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12. L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-26 DRAMP21076 KWCARVCARGACYRRCR 17 TP1[F4A, Y8A, I11A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC>16 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC>16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=8 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC>16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC>16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC>16 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC>16 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC>16 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC>16 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC>16 μg/ml) [Ref.28960954] MHC10=0.9 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis.2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-27 DRAMP21077 KWCFVCYRGICYRRCG 16 TP1[-R5, R17G] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=1 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC>16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=8 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC>16 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC>16 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC>16 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=16 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC>16 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC>16 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=4 μg/ml) [Ref.28960954] MHC10=0.3 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis.2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-28 DRAMP21078 AWCARVCYRGICYRRCR 17 TP1[K1A, F4A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=16 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC>16 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=2 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=4 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=4 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=4 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC>16 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=2 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=16 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=8 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC>16 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC>16 μg/ml) [Ref.28960954] MHC10=32 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-29 DRAMP21079 AWCFRVCARGICYRRCR 17 TP1[K1A, Y8A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.5 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=8 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.25 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=1 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=8 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=1 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=4 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=2 μg/ml) [Ref.28960954] MHC10=0.4 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-30 DRAMP21080 AWCFRVCYRGACYRRCR 17 TP1[K1A, I11A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.125 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=4 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.125 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.25 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.5 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=4 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.25 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.5 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC>16 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=1 μg/ml) [Ref.28960954] MHC10=0.2 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-31 DRAMP21081 KWCFRVCYAGICYRRCA 17 TP1[R9A, R17A] (Derived from TP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Cryptococcus neoformans [Ref.28960954] Gram-positive bacteria : Bacillus subtilis ATCC 6051(MIC=0.06 μg/ml), Staphylococcus aureus ATCC 43300 (MRSA)(MIC=2 μg/ml);##Gram-negative bacteria : Escherichia coli ATCC 25922(MIC=0.03 μg/ml), Klebsiella pneumoniae ATCC 13883(MIC=0.06 μg/ml), Klebsiella pneumoniae ATCC 700603 (MDR)(MIC=0.5 μg/ml), Klebsiella pneumoniae BAA 2146 (NDM-1 pos)(MIC=0.5 μg/ml), Klebsiella pneumoniae clinical isolate 100650661 : 1 (XDR;PmxR)(MIC=4 μg/ml), Acinetobacter baumannii ATCC 19606(MIC=0.25 μg/ml), Acinetobacter baumannii clinical isolate 100734512 : 2 (XDR;PmxR)(MIC=0.5 μg/ml), Pseudomonas aeruginosa ATCC 27853(MIC=0.5 μg/ml), Pseudomonas aeruginosa FADDIFA070 (PmxR)(MIC=2 μg/ml);##Fungi : Candida albicans ATCC 90028(MIC=8 μg/ml), Cryptococcus neoformans ATCC 208821(MIC=0.5 μg/ml) [Ref.28960954] MHC10=0.2 μg/ml against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys7 and Cys12 L [Ref.28960954] The peptide did not show cytotoxicity against HEK293 cells at the highest tested concentration, 100 μg/ml. Not found 28960954 ACS Infect Dis. 2017 Dec 8;3(12):917-926. doi: 10.1021/acsinfecdis.7b00123. Ingrid A. Edwards , Alysha G. Elliott , Angela M. Kavanagh , Mark A. T. Blaskovich , and Matthew A. Cooper Structure-Activity and -Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-32 DRAMP21082 KWCFCVCYRGICRCRCRG 18 ccTP 3 (Derived from TP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Beta tile Although there is insufficient information to deconvolute these CD spectra of these two-b-strand cyclic cystine-knot structures due to the various contributions by Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida kefyr, Candida tropicalis [Ref.10673369] Gram-positive bacteria : Staphylococcus aureus(MIC=1.3 μM(low-salt);MIC=0.9 μM(high-salt)), Micrococcus luteus(MIC=0.5 μM(low-salt);MIC=0.5 μM(high-salt)), Enterococcus faecalis(MIC=1.9 μM(low-salt);MIC=1.3 μM(high-salt));##Gram-negative bacteria : Escherichia coli(MIC=10.4 μM(low-salt);MIC=0.9 μM(high-salt)), Pseudomonas aeruginosa(MIC=6.2 μM(low-salt);MIC=10.4 μM(high-salt)), Primula vulgaris(MIC=16.4 μM(low-salt);MIC=28.9 μM(high-salt)), Klebsiella oxytoca(MIC=4.0 μM(low-salt);MIC=7.6 μM(high-salt));##Fungi : Candida albicans(MIC=24.2 μM(low-salt);MIC=30.2 μM(high-salt)), Candida kefyr(MIC=1.1 μM(low-salt);MIC=4.3 μM(high-salt)), Candida tropicalis(MIC=12.4 μM(low-salt);MIC=3.9 μM(high-salt)) [Ref.10673369] EC25=590 μM against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys5 and Cys14, Cys7 and Cys12. L [Ref.10673369] No cytotoxicity information found. Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. James P. Tam, Yi-An Lu, and Jin-Long Yang Marked Increase in Membranolytic Selectivity of Novel Cyclic Tachyplesins Constrained with an Antiparallel Two-b Strand Cystine Knot Framework DRAMP21083 KWCRCVCRRGICRCFCRG 18 ccTP 5 (Derived from TP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Beta tile Although there is insufficient information to deconvolute these CD spectra of these two-b-strand cyclic cystine-knot structures due to the various contributions by Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida kefyr, Candida tropicalis [Ref.10673369] Gram-positive bacteria : Staphylococcus aureus(MIC=1.7 μM(low-salt);MIC=1.3 μM(high-salt)), Micrococcus luteus(MIC=0.5 μM(low-salt);MIC=0.8 μM(high-salt)), Enterococcus faecalis(MIC=0.7 μM(low-salt);MIC=0.5 μM(high-salt));##Gram-negative bacteria : Escherichia coli(MIC=5.5 μM(low-salt);MIC=1.2 μM(high-salt)), Pseudomonas aeruginosa(MIC=3.9 μM(low-salt);MIC=4.7 μM(high-salt)), Primula vulgaris(MIC=16.8 μM(low-salt);MIC=55.6 μM(high-salt)), Klebsiella oxytoca(MIC=2.4 μM(low-salt);MIC=5.4 μM(high-salt));##Fungi : Candida albicans(MIC=7.1 μM(low-salt);MIC=5.1 μM(high-salt)), Candida kefyr(MIC=4.2 μM(low-salt);MIC=0.7 μM(high-salt)), Candida tropicalis(MIC=1.9 μM(low-salt);MIC=4.8 μM(high-salt)) [Ref.10673369] EC25=920 μM against human red blood cells Cyclic Free Amidation Disulfide bonds between Cys3 and Cys16, Cys5 and Cys14, Cys7 and Cys12. L [Ref.10673369] No cytotoxicity information found. Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. James P. Tam, Yi-An Lu, and Jin-Long Yang Marked Increase in Membranolytic Selectivity of Novel Cyclic Tachyplesins Constrained with an Antiparallel Two-b Strand Cystine Knot Framework DRAMP21084 GWCRCVCRRGICRCFCRK 18 ccTP 6 (Derived from TP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Beta tile Although there is insufficient information to deconvolute these CD spectra of these two-b-strand cyclic cystine-knot structures due to the various contributions by Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria, Antifungal activity agaist Candida albicans, Candida kefyr, Candida tropicalis [Ref.10673369] Gram-positive bacteria : Staphylococcus aureus(MIC=1.7 μM(low-salt);MIC=0.7 μM(high-salt)), Micrococcus luteus(MIC=0.3 μM(low-salt);MIC=0.4 μM(high-salt)), Enterococcus faecalis(MIC=1.4 μM(low-salt);MIC=1.2 μM(high-salt));##Gram-negative bacteria : Escherichia coli(MIC=6.1 μM(low-salt);MIC=1.2 μM(high-salt)), Pseudomonas aeruginosa(MIC=2.0 μM(low-salt);MIC=4.7 μM(high-salt)), Primula vulgaris(MIC=17.0 μM(low-salt);MIC=39.8 μM(high-salt)), Klebsiella oxytoca(MIC=4.1 μM(low-salt);MIC=4.1 μM(high-salt));##Fungi : Candida albicans(MIC=10.5 μM(low-salt);MIC=5.2 μM(high-salt)), Candida kefyr(MIC=1.1 μM(low-salt);MIC=0.7 μM(high-salt)), Candida tropicalis(MIC=2.3 μM(low-salt);MIC=1.9 μM(high-salt)) [Ref.10673369] EC25=3900 μM against human red blood cells Cyclic Free Amidation (Gly18) Disulfide bonds between Cys3 and Cys16, Cys5 and Cys14, Cys7 and Cys12. L No cytotoxicity information found Not found 10673369 Biochem Biophys Res Commun. 2000 Jan 27;267(3):783-90. James P. Tam, Yi-An Lu, and Jin-Long Yang Marked Increase in Membranolytic Selectivity of Novel Cyclic Tachyplesins Constrained with an Antiparallel Two-b Strand Cystine Knot Framework DRAMP21085 RFRRLRWKTRWRLKKI 16 PRW4 (PR) (Derived from PMAP-36) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta Sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25818457] Gram-positive bacteria : Staphylococcus aureus 25923(MIC=73.6 mg/L), Staphylococcus aureus 29213(MIC=9.2 mg/L), Staphylococcus epidermidis 12228(MIC=18.4 mg/L), Enterococcus faecalis 29212(MIC=9.2 mg/L), Bacillus subtilis 11060(MIC=18.4 mg/L);##Gram-negative bacteria : Escherichia coli 078(MIC=9.2 mg/L), Escherichia coli K88(MIC=9.2 mg/L), Escherichia coli ER2566(MIC=18.4 mg/L), Escherichia coli 44102(MIC=18.4 mg/L), Escherichia coli 1515(MIC=9.2 mg/L), Escherichia coli 25922(MIC=9.2 mg/L), Escherichia coli UB1005(MIC=9.2 mg/L), Salmonella typhimurium 7731(MIC=18.4 mg/L), Salmonella typhimurium 1402(MIC=18.4 mg/L), Pseudomonas aeruginosa 21625(MIC=73.6 mg/L), Pseudomonas aeruginosa 21630(MIC=36.8 mg/L), Pseudomonas aeruginosa 10419(MIC=36.8 mg/L), Pseudomonas aeruginosa 27853(MIC>294.3 mg/L), Salmonella pullorum 7913(MIC>294.3 mg/L) [Ref.25818457] 0 % hemolysis at 294.3 mg/L against human red blood cells Linear Free Amidation L [Ref.25818457] The cell viability of PRW4 is 100%, 96%, 92%, 86%, 85%, 83%, 82%, 80% and 80% at peptide concentrations of 1.1, 2.3, 4.6, 9.2, 18.4, 36.8, 73.6, 147.1 and 294.3 μg/ml Not found 25818457 Biomaterials. 2015 Jun;52:517-30. doi: 10.1016/j.biomaterials.2015.02.063. Zhi Ma, Dandan Wei, Ping Yan, Xin Zhu, Anshan Shan , Zhongpeng Bi Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of a-helix-based peptide amphiphiles DRAMP21086 RFRRLRWKTRWRLKKIRFGRFLRKIRRFRPK 31 PR-FO (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta Sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25818457] Gram-positive bacteria : Staphylococcus aureus 25923(MIC=8.6 mg/L), Staphylococcus aureus 29213(MIC=4.3 mg/L), Staphylococcus epidermidis 12228(MIC=2.2 mg/L), Enterococcus faecalis 29212(MIC=1.1 mg/L), Bacillus subtilis 11060(MIC=2.2 mg/L);##Gram-negative bacteria : Escherichia coli 078(MIC=2.2 mg/L), Escherichia coli K88(MIC=4.3 mg/L), Escherichia coli ER2566(MIC=2.2 mg/L), Escherichia coli 44102(MIC=8.6 mg/L), Escherichia coli 1515(MIC=2.2 mg/L), Escherichia coli 25922(MIC=2.2 mg/L), Escherichia coli UB1005(MIC=4.3 mg/L), Salmonella typhimurium 7731(MIC=0.5 mg/L), Salmonella typhimurium 1402(MIC=8.6 mg/L), Pseudomonas aeruginosa 21625(MIC=8.6 mg/L), Pseudomonas aeruginosa 21630(MIC=0.5 mg/L), Pseudomonas aeruginosa 10419(MIC=4.3 mg/L), Pseudomonas aeruginosa 27853(MIC=8.6 mg/L), Salmonella pullorum 7913(MIC=8.6 mg/L) [Ref.25818457] 0% hemolysis at 9.2 mg/L , 1% hemolysis at 18.4 mg/L , 4% hemolysis at 36.8mg/L , 5% hemolysis at 73.6 mg/L , 10% hemolysis at 147.1 mg/L , 13% hemolysis at 294.3 mg/L against human red blood cells Linear Free Amidation L [Ref.25818457] The cell viability of PR-FO is 93%, 89%, 84%, 79%, 74%, 69%, 67%, 64% and 62% at peptide concentrations of 1.1, 2.3, 4.6, 9.2, 18.4, 36.8, 73.6, 147.1 and 294.3 μg/ml. Not found 25818457 Biomaterials. 2015 Jun;52:517-30. doi: 10.1016/j.biomaterials.2015.02.063. Zhi Ma, Dandan Wei, Ping Yan, Xin Zhu, Anshan Shan , Zhongpeng Bi Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of a-helix-based peptide amphiphiles DRAMP21087 RFRRLRWKTRWRLKKICYCRRRFCVCV 27 PR-PG (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta Sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25818457] Gram-positive bacteria : Staphylococcus aureus 25923(MIC=29.6 mg/L), Staphylococcus aureus 29213(MIC=7.4 mg/L), Staphylococcus epidermidis 12228(MIC=7.4 mg/L), Enterococcus faecalis 29212(MIC=3.7 mg/L), Bacillus subtilis 11060(MIC=7.4 mg/L);##Gram-negative bacteria : Escherichia coli 078(MIC=14.8 mg/L), Escherichia coli K88(MIC=1.9 mg/L), Escherichia coli ER2566(MIC=3.7 mg/L), Escherichia coli 44102(MIC=1.9 mg/L), Escherichia coli 1515(MIC=14.8 mg/L), Escherichia coli 25922(MIC=3.7 mg/L), Escherichia coli UB1005(MIC=7.4 mg/L), Salmonella typhimurium 7731(MIC=14.8 mg/L), Salmonella typhimurium 1402(MIC=7.4 mg/L), Pseudomonas aeruginosa 21625(MIC=14.8 mg/L), Pseudomonas aeruginosa 21630(MIC=7.4 mg/L), Pseudomonas aeruginosa 10419(MIC=14.8 mg/L), Pseudomonas aeruginosa 27853(MIC=14.8 mg/L), Salmonella pullorum 7913(MIC=14.8 mg/L) [Ref.25818457] 0.5% hemolysis at 1.1 mg/L , 2% hemolysis at 2.3 mg/L , 10% hemolysis at 4.6 mg/L , 23% hemolysis at 9.2 mg/L , 30% hemolysis at 18.4 mg/L , 45% hemolysis at 36.8mg/L , 46% hemolysis at 73.6 mg/L , 47% hemolysis at 147.1 mg/L , 50% hemolysis at 294.3 mg/L against human red blood cells Linear Free Amidation L [Ref.25818457] The cell viability of PR-FG is 92.7%, 76%, 64%, 58%, 53%, 43%, 39%, 37% and 34% at peptide concentrations of 1.1, 2.3, 4.6, 9.2, 18.4, 36.8, 73.6, 147.1 and 294.3 μg/ml. Not found 25818457 Biomaterials. 2015 Jun;52:517-30. doi: 10.1016/j.biomaterials.2015.02.063. Zhi Ma, Dandan Wei, Ping Yan, Xin Zhu, Anshan Shan , Zhongpeng Bi Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of a-helix-based peptide amphiphiles DRAMP21088 RFRRLRWKTRWRLKKIWWPFLRR 23 PR-TR (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta Sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25818457] Gram-positive bacteria : Staphylococcus aureus 25923(MIC=26.7 mg/L), Staphylococcus aureus 29213(MIC=6.7 mg/L), Staphylococcus epidermidis 12228(MIC=13.4 mg/L), Enterococcus faecalis 29212(MIC=3.3 mg/L), Bacillus subtilis 11060(MIC=3.3 mg/L);##Gram-negative bacteria : Escherichia coli 078(MIC=13.4 mg/L), Escherichia coli K88(MIC=1.7 mg/L), Escherichia coli ER2566(MIC=3.3 mg/L), Escherichia coli 44102(MIC=6.7 mg/L), Escherichia coli 1515(MIC=1.7 mg/L), Escherichia coli 25922(MIC=6.7 mg/L), Escherichia coli UB1005(MIC=3.3 mg/L), Salmonella typhimurium 7731(MIC=6.7 mg/L), Salmonella typhimurium 1402(MIC=13.4 mg/L), Pseudomonas aeruginosa 21625(MIC=6.7 mg/L), Pseudomonas aeruginosa 21630(MIC=13.4 mg/L), Pseudomonas aeruginosa 10419(MIC=6.7 mg/L), Pseudomonas aeruginosa 27853(MIC=13.4 mg/L), Salmonella pullorum 7913(MIC=13.4 mg/L) [Ref.25818457] 0% hemolysis at 9.2 mg/L , 1% hemolysis at 18.4 mg/L , 4% hemolysis at 36.8mg/L , 10% hemolysis at 73.6 mg/L , 17% hemolysis at 147.1 mg/L , 22% hemolysis at 294.3 mg/L against human red blood cells Linear Free Amidation L [Ref.25818457] The cell viability of PR-TR is 94%, 89%, 83%, 77%, 74%, 71%, 68%, 66% and 60% at peptide concentrations of 1.1, 2.3, 4.6, 9.2, 18.4, 36.8, 73.6, 147.1 and 294.3 μg/ml Not found 25818457 Biomaterials. 2015 Jun;52:517-30. doi: 10.1016/j.biomaterials.2015.02.063. Zhi Ma, Dandan Wei, Ping Yan, Xin Zhu, Anshan Shan , Zhongpeng Bi Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of a-helix-based peptide amphiphiles DRAMP21089 RFRRLRCKTRCRLKKI 16 C4 (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>128 μM), Staphylococcus epidermidis 12228(MIC>128 μM), Enterococcus faecalis 29212(MIC>128 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC=2 μM), Escherichia coli 1005(MIC>128 μM), Salmonella typhimurium 7731(MIC128 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21090 RFRRLRDKTRDRLKKI 16 D4 (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>128 μM), Staphylococcus epidermidis 12228(MIC>128 μM), Enterococcus faecalis 29212(MIC>128 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC>128 μM), Escherichia coli 1005(MIC>128 μM), Salmonella typhimurium 7731(MIC>128 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21091 RFRRLRIKTRIRLKKI 16 I4 (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=64 μM), Staphylococcus epidermidis 12228(MIC=16 μM), Enterococcus faecalis 29212(MIC=16 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC=8 μM), Escherichia coli 1005(MIC=16 μM), Salmonella typhimurium 7731(MIC=16 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21092 RFRRLRPKTRPRLKKI 16 P4 (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>128 μM), Staphylococcus epidermidis 12228(MIC>128 μM), Enterococcus faecalis 29212(MIC>128 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC=32 μM), Escherichia coli 1005(MIC=32 μM), Salmonella typhimurium 7731(MIC=32 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21093 RFRRLRwKTRwRLKKI 16 PRW4-d (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=8 μM), Staphylococcus epidermidis 12228(MIC=16 μM), Enterococcus faecalis 29212(MIC=4 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC=4 μM), Escherichia coli 1005(MIC=8 μM), Salmonella typhimurium 7731(MIC=4 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation Mixed(D-Trp7, D-Trp11) [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21094 RFRRLRWRTRWRLRRI 16 PRW4-R (Derived from PRW4) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25735802] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=4 μM), Staphylococcus epidermidis 12228(MIC=4 μM), Enterococcus faecalis 29212(MIC=2 μM);##Gram-negative bacteria : Escherichia coli 25922(MIC=4 μM), Escherichia coli 1005(MIC=2 μM), Salmonella typhimurium 7731(MIC=4 μM) [Ref.25735802] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.25735802] The peptide exhibited no cytoxicity against HaCaT cells in the range of 0/25-256 μM. Not found 25735802 Acta Biomater. 2015 May;18:155-67. doi: 10.1016/j.actbio.2015.02.023. Xin Zhu, Licong Zhang, Jue Wang, Zhi Ma, Wei Xu, Jianping Li, Anshan Shan Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity DRAMP21095 IRCRRRFCRI 10 IR1 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=64 μM), Staphylococcus epidermidis(MIC=64 μM), Streptococcus faecalis(MIC=64 μM), Bacillus subtilis(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(MIC=8 μM), Salmonella pullorum(MIC=16 μM), Salmonella typhimurium(MIC=128 μM), Bacteriump yocyaneum(MIC=64 μM) [Ref.24621994] MHC10>128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21096 IRIRCRRRFCRIRI 14 IR2 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Beta sheet, beta hairpin Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=4 μM), Staphylococcus epidermidis(MIC=4 μM), Streptococcus faecalis(MIC=4 μM), Bacillus subtilis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=1 μM), Salmonella pullorum(MIC=1 μM), Salmonella typhimurium(MIC=4 μM), Bacteriump yocyaneum(MIC=4 μM) [Ref.24621994] MHC10=128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21097 FRCRRRFCRF 10 FR1 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=32 μM), Staphylococcus epidermidis(MIC=16 μM), Streptococcus faecalis(MIC=32 μM), Bacillus subtilis(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Salmonella pullorum(MIC=16 μM), Salmonella typhimurium(MIC=32 μM), Bacteriump yocyaneum(MIC>128 μM) [Ref.24621994] MHC10>128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21098 FRFRCRRRFCRFRF 14 FR2 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=2 μM), Staphylococcus epidermidis(MIC=2 μM), Streptococcus faecalis(MIC=4 μM), Bacillus subtilis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=1 μM), Salmonella pullorum(MIC=1 μM), Salmonella typhimurium(MIC=2 μM), Bacteriump yocyaneum(MIC=4 μM) [Ref.24621994] MHC10=64 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21099 WRCRRRFCRW 10 WR1 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=8 μM), Staphylococcus epidermidis(MIC=8 μM), Streptococcus faecalis(MIC=8 μM), Bacillus subtilis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=2 μM), Salmonella pullorum(MIC=4 μM), Salmonella typhimurium(MIC=16 μM), Bacteriump yocyaneum(MIC>128 μM) [Ref.24621994] MHC10>128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21100 WRWRCRRRFCRWRW 14 WR2 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC=4 μM), Staphylococcus epidermidis(MIC=2 μM), Streptococcus faecalis(MIC=2 μM), Bacillus subtilis(MIC=1 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Salmonella pullorum(MIC=2 μM), Salmonella typhimurium(MIC=4 μM), Bacteriump yocyaneum(MIC=8 μM) [Ref.24621994] MHC10=64 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21101 PRCRRRFCRP 10 PR1 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC>128 μM), Staphylococcus epidermidis(MIC>128 μM), Streptococcus faecalis(MIC>128 μM), Bacillus subtilis(MIC=16 μM);##Gram-negative bacteria : Escherichia coli(MIC=16 μM), Salmonella pullorum(MIC>128 μM), Salmonella typhimurium(MIC>128 μM), Bacteriump yocyaneum(MIC>128 μM) [Ref.24621994] MHC10>128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One.2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21102 PRPRCRRRFCRPRP 14 PR2 (Derived from PG-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC>128 [Ref.24621994] Gram-positive bacteria : Staphylococcus aureus(MIC>128 μM), Staphylococcus epidermidis(MIC>128 μM), Streptococcus faecalis(MIC>128 μM), Bacillus subtilis(MIC=8 μM);##Gram-negative bacteria : Escherichia coli(MIC=16 μM), Salmonella pullorum(MIC>128 μM), Salmonella typhimurium(MIC>128 μM), Bacteriump yocyaneum(MIC>128 μM) [Ref.24621994] MHC10>128 μM against human red blood cells Linear Free Amidation L [Ref.24621994] No cytotoxicity information found. Not found 24621994 PLoS One. 2014 Mar 12;9(3):e91007. doi: 10.1371/journal.pone.0091007. Na Dong , Xin Zhu , Shuli Chou , Anshan Shan , Weizhong Li , Junguang Jiang Antimicrobial potency and selectivity of simplified symmetric-end peptides DRAMP21165 GIMSSLMKKLKKIIKK 16 HYL-11 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=54 μM), Staphylococcus epidermidis(MIC=1.7 μM);##Gram-negative bacteria : Escherichia coli(MIC=22 μM), Pseudomonas aeruginosa 5482(MIC=7.1 μM);##Fungi : Candida albicans(MIC=6.3 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21166 GILSSLLKKLKKIIAK 16 HYL-12 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=16 μM), Staphylococcus epidermidis(MIC=1.8 μM);##Gram-negative bacteria : Escherichia coli(MIC=8 μM), Pseudomonas aeruginosa 5482(MIC=5 μM);##Fungi : Candida albicans(MIC=10 μM) [Ref.26998557] LC50=284 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21164 GIMSSLMKKLAKIIKK 16 HYL-10 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=33 μM), Staphylococcus epidermidis(MIC=2.9 μM);##Gram-negative bacteria : Escherichia coli(MIC=15 μM), Pseudomonas aeruginosa 5482(MIC=5.2 μM);##Fungi : Candida albicans(MIC=7.6 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21158 GIMSSLMKKLKKHIAK 16 HYL-4 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC>100 μM), Staphylococcus epidermidis(MIC=10 μM);##Gram-negative bacteria : Escherichia coli(MIC=26 μM), Pseudomonas aeruginosa 5482(MIC=6.4 μM);##Fungi : Candida albicans(MIC=12 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21159 GIMISLMKKLAAHIAK 16 HYL-5 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=43 μM), Staphylococcus epidermidis(MIC=8.8 μM);##Gram-negative bacteria : Escherichia coli(MIC=12 μM), Pseudomonas aeruginosa 5482(MIC=47 μM);##Fungi : Candida albicans(MIC=12 μM) [Ref.26998557] LC50=320 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21160 GIMSSLMKKLAAIIAK 16 HYL-6 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=7.2 μM), Staphylococcus epidermidis(MIC=5 μM);##Gram-negative bacteria : Escherichia coli(MIC=3.6 μM), Pseudomonas aeruginosa 5482(MIC=8 μM);##Fungi : Candida albicans(MIC=8.4 μM) [Ref.26998557] LC50=93 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21161 GIMSSLMKKLAKIIAK 16 HYL-7 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=9 μM), Staphylococcus epidermidis(MIC=5 μM);##Gram-negative bacteria : Escherichia coli(MIC=3.7 μM), Pseudomonas aeruginosa 5482(MIC=4.5 μM);##Fungi : Candida albicans(MIC=11 μM) [Ref.26998557] LC50=88 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21162 GIMSSLMKKLKKIIAK 16 HYL-8 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=32 μM), Staphylococcus epidermidis(MIC=1.9 μM);##Gram-negative bacteria : Escherichia coli(MIC=9 μM), Pseudomonas aeruginosa 5482(MIC=5 μM);##Fungi : Candida albicans(MIC=5.2 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21163 gimsslmkklkkiiak 16 HYL-9 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=13 μM), Staphylococcus epidermidis(MIC=2.2 μM);##Gram-negative bacteria : Escherichia coli(MIC=6.3 μM), Pseudomonas aeruginosa 5482(MIC=3.2 μM);##Fungi : Candida albicans(MIC=8 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation D [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21157 GIMSSLMKKLAAHIKK 16 HYL-3 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=85 μM), Staphylococcus epidermidis(MIC=11 μM);##Gram-negative bacteria : Escherichia coli(MIC=20 μM), Pseudomonas aeruginosa 5482(MIC=23 μM);##Fungi : Candida albicans(MIC=5 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21156 GIMSSLMKKLAKHIAK 16 HYL-2 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=63 μM), Staphylococcus epidermidis(MIC=6.2 μM);##Gram-negative bacteria : Escherichia coli(MIC=15 μM), Pseudomonas aeruginosa 5482(MIC=7.9 μM);##Fungi : Candida albicans(MIC=14 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21155 GIMSSLMKKLKAHIAK 16 HYL-1 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC>100 μM), Staphylococcus epidermidis(MIC=16 μM);##Gram-negative bacteria : Escherichia coli(MIC=30 μM), Pseudomonas aeruginosa 5482(MIC=26 μM);##Fungi : Candida albicans(MIC=23 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21154 GIMSSLMKKLAAHIAK 16 HYL (Bee, Insecta, Animals) No entry found Not found Not found Solitary wild bee Hylaeus signatus Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=63 μM), Staphylococcus epidermidis(MIC=13 μM);##Gram-negative bacteria : Escherichia coli(MIC=15 μM), Pseudomonas aeruginosa 5482(MIC=20 μM);##Fungi : Candida albicans(MIC=18 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21153 KRIRKRIKKWKR 12 KR-12-a8 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm .Among these peptides, KR-12-a8 had shown the least α-helical structure. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=2 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=2 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 91.2%, 112.8%, 104.1%, 114.4%, 104.4%, 109.4%, 107.2% and 82.2% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21151 LRIVKLILKWLR 12 KR-12-a6 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=2 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=16 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=16 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.24105706] HC50=22 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 100%, 99.1%, 100%, 98.8%, 99.9%, 85.3%, 5.9% and 0% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21150 KRIVKLILKWLR 12 KR-12-a5 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.24105706] HC50=96 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 96.6%, 100.1%, 96.6%, 96.8%, 81.2%, 3.1%, 0% and 0% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21152 KRIRKRIKKWLR 12 KR-12-a7 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=4 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 92.5%, 100.9%, 97.2%, 96.6%, 92.5%, 101.2%, 90.6% and 81.9% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21149 KRIVKLIKKWLR 12 KR-12-a4 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=4 μM), Salmonella typhimurium (KCTC 1926)(MIC=1 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 101.9%, 99.9%, 96.6%, 95.6%, 95.3%, 80.9%, 17.8% and 0% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21146 KRIVQRIKDWLR 12 KR-12-a1 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 108.7%, 111.2%, 107.5%, 107.5%, 103.1%, 111.2%, 107.2%, 98.1% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21148 KRIVKRIKKWLR 12 KR-12-a3 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 104.7%, 111.6%, 105.3%, 108.4%, 111.2%, 104.4%, 108.8% and 95.0% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21147 KRIVQRIKKWLR 12 KR-12-a2 (Derived from KR-12) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra for all the peptides in 10 mM sodium phosphate buffer (pH 7.2) displayed a negative band at approximately 200 nm, indicating that the structure is random. In presence of 0.1% LPS, all the peptides showed characteristic α-helical CD spectra with two dichroic minimal values at 208 and 222 nm and a positive band near 192 nm . Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.24105706] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=1 μM) [Ref.24105706] HC50>800 μM against human red blood cells Linear Free Amidation L [Ref.24105706] The cell viability of RAW264.7 macrophage cells is 111.9%, 103.4%, 102.2%, 102.2%, 100%, 101.2%, 112.5% and 95.0% at peptide concentrations of 0.78, 1.56, 3.12, 6.25, 12.5, 25, 50 and 100 μM. Not found 24105706 J Pept Sci. 2013 Nov;19(11):700-7. doi: 10.1002/psc.2552. Jacob B, Park IS, Bang JK, Shin SY Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity. DRAMP21145 RIRWILRYWRWS 12 Myxinidin3 (Derived from Myxinidin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Beta Sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26450121] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=1 μM), Staphylococcus aureus CCARM 3114(MIC=8 μM), Staphylococcus aureus CCARM 3709(MIC=2 μM), Listeria monocytogenes (KCTC 3710)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2 μM), Escherichia coli CCARM 1229(MIC=1 μM), Escherichia coli CCARM 1238(MIC=2 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM), Salmonella typhimurium CCARM 8009(MIC=4 μM), Salmonella typhimurium CCARM 8013(MIC=4 μM), Pseudomonas aeruginosa (ATCC 27853)(MIC=4 μM), Pseudomonas aeruginosa 3592(MIC=8 μM), Pseudomonas aeruginosa 5018(MIC=8 μM) [Ref.26450121] 27% hemolysis at 50 μM , 45% hemolysis at 100 μM , 63% hemolysis at 200 μM , 59% hemolysis at 400 μM against human red blood cells Linear Free Free L [Ref.26450121] The cell survial rates of normal human keratinocytes (NHK) are 100%, 95.8%, 88.3%, 83.4%, 77.4% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50, 100 μM. Melittin, the control, induced 100% toxicity against NHKs at a concentration of Not found 26450121 Amino Acids. 2016 Feb;48(2):505-22. doi: 10.1007/s00726-015-2104-0. Han HM, Gopal R, Park Y Design and membrane-disruption mechanism of charge-enriched AMPs exhibiting cell selectivity, high-salt resistance, and anti-biofilm properties. DRAMP21142 HKCAKIKWRGVHVKYCA 17 AMP2041 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23893489] Gram-positive bacteria : Staphylococcus aureus(MBC=3.71 μg/ml, 1.83 μM), MRSA(MBC=2.25 μg/ml, 1.11 μM), Streptococcus agalactiae(MBC>100 μg/ml, 55 μM);##Gram-negative bacteria : Pseudomonas aeruginosa(MBC=4.35 μg/ml, 2.14 μM), Escherichia coli(MBC=1.79 μg/ml, 0.88 μM), Salmonella enteritidis(MBC=10.41 μg/ml, 5.13 μM), Stenotrophomonas maltophilia(MBC=7.00 μg/ml, 3.45 μM) [Ref.23893489] <1% hemolysis at 1 μg/ml , <1% hemolysis at 12.5 μg/ml , 5.73% hemolysis at 100 μg/ml , 6.4% hemolysis at 250 μg/ml , 9.4% hemolysis at 500 μg/ml against sheep red blood cells Linear Free Free L [Ref.23893489] The cytotoxicity (vs control) of P2041 is 6% against HUVEC (endothelial) cells at a peptide concentration of 100 μg/ml. ##The cytotoxicity (vs control) of P2041 is 3% agaisnt WI-38 (fibroblast) cells at a peptide concentration of 100 μg/m Not found 23893489 J Pept Sci. 2013 Sep;19(9):554-65. doi: 10.1002/psc.2532. Romani AA, Baroni MC, Taddei S, Ghidini F, Sansoni P, Cavirani S, Cabassi CS In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens. DRAMP21141 KWCRKWQWRGVKFIKCV 17 AMP126 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23893489] Gram-positive bacteria : Staphylococcus aureus(MBC=46.5 μg/ml, 20.65 μM), MRSA(MBC>100 μg/ml, 55 μM), Streptococcus agalactiae(MBC=2.81 μg/ml, 1.24 μM);##Gram-negative bacteria : Pseudomonas aeruginosa(MBC=0.40 μg/ml, 0.17 μM), Escherichia coli(MBC=2.22 μg/ml, 0.98 μM), Salmonella enteritidis(MBC=10.8 μg/ml, 4.80 μM), Stenotrophomonas maltophilia(MBC=16.6 μg/ml, 7.37 μM) [Ref.23893489] <1% hemolysis at 1 μg/ml , <1% hemolysis at 12.5 μg/ml , 5.30% hemolysis at 100 μg/ml , 6.9% hemolysis at 250 μg/ml , 12.5% hemolysis at 500 μg/ml against sheep red blood cells Linear Free Free L [Ref.23893489] The cytotoxicity (vs control) of P126 is 5% against HUVEC (endothelial) cells at a peptide concentration of 100 μg/ml. ##The cytotoxicity (vs control) of P126 is 6% agaisnt WI-38 (fibroblast) cells at a peptide concentration of 100 μg/ml. Not found 23893489 J Pept Sci. 2013 Sep;19(9):554-65. doi: 10.1002/psc.2532. Romani AA, Baroni MC, Taddei S, Ghidini F, Sansoni P, Cavirani S, Cabassi CS In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens. DRAMP21144 KIKWILKYWKWS 12 Myxinidin2 (Derived from Myxinidin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26450121] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=0.25 μM), Staphylococcus aureus CCARM 3114(MIC=16 μM), Staphylococcus aureus CCARM 3709(MIC=2 μM), Listeria monocytogenes (KCTC 3710)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=1 μM), Escherichia coli CCARM 1229(MIC=2 μM), Escherichia coli CCARM 1238(MIC=4 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM), Salmonella typhimurium CCARM 8009(MIC=8 μM), Salmonella typhimurium CCARM 8013(MIC=16 μM), Pseudomonas aeruginosa (ATCC 27853)(MIC=4 μM), Pseudomonas aeruginosa 3592(MIC=8 μM), Pseudomonas aeruginosa 5018(MIC=4 μM) [Ref.26450121] 10% hemolysis at 50 μM , 28% hemolysis at 100 μM , 30% hemolysis at 200 μM , 50% hemolysis at 400 μM against human red blood cells Linear Free Free L [Ref.26450121] The cell survial rates of normal human keratinocytes (NHK) are 100%, 95.8%, 88.3%, 83.4%, 77.4% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50, 100 μM. Melittin, the control, induced 100% toxicity against NHKs at a concentration of Not found 26450121 Amino Acids. 2016 Feb;48(2):505-22. doi: 10.1007/s00726-015-2104-0. Han HM, Gopal R, Park Y Design and membrane-disruption mechanism of charge-enriched AMPs exhibiting cell selectivity, high-salt resistance, and anti-biofilm properties. DRAMP21143 GIHHILKYGKPS 12 Myxinidin1 (Derived from Myxinidin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26450121] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC>32 μM), Staphylococcus aureus CCARM 3114(MIC>32 μM), Staphylococcus aureus CCARM 3709(MIC>32 μM), Listeria monocytogenes (KCTC 3710)(MIC>32 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC>32 μM), Escherichia coli CCARM 1229(MIC>32 μM), Escherichia coli CCARM 1238(MIC>32 μM), Salmonella typhimurium (KCTC 1926)(MIC>32 μM), Salmonella typhimurium CCARM 8009(MIC>32 μM), Salmonella typhimurium CCARM 8013(MIC>32 μM), Pseudomonas aeruginosa (ATCC 27853)(MIC>32 μM), Pseudomonas aeruginosa 3592(MIC>32 μM), Pseudomonas aeruginosa 5018(MIC>32 μM) [Ref.26450121] 0% hemolysis at 50 μM , 0% hemolysis at 100 μM , 0% hemolysis at 200 μM , 0% hemolysis at 400 μM against human red blood cells Linear Free Free L [Ref.26450121] The cell survial rates of normal human keratinocytes (NHK) are 100%, 95.8%, 88.3%, 83.4%, 77.4% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50, 100 μM. Melittin, the control, induced 100% toxicity against NHKs at a concentration of Not found 26450121 Amino Acids. 2016 Feb;48(2):505-22. doi: 10.1007/s00726-015-2104-0. Han HM, Gopal R, Park Y Design and membrane-disruption mechanism of charge-enriched AMPs exhibiting cell selectivity, high-salt resistance, and anti-biofilm properties. DRAMP21140 KGCALVKVRGLTLKVCK 17 AMP72 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix, beta sheet, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23893489] Gram-positive bacteria : Staphylococcus aureus(MBC=6.88 μg/ml, 3.78 μM), MRSA(MBC=1.72 μg/ml, 0.94 μM), Streptococcus agalactiae(MBC>55 μg/ml, 100 μM);##Gram-negative bacteria : Pseudomonas aeruginosa(MBC=3.30 μg/ml, 1.81 μM), Escherichia coli(MBC=3.40 μg/ml, 1.87 μM), Salmonella enteritidis(MBC=3.20 μg/ml, 1.76 μM), Stenotrophomonas maltophilia(MBC=18.5 μg/ml, 10.19 μM) [Ref.23893489] <1% hemolysis at 1 μg/ml , <1% hemolysis at 12.5 μg/ml , 1.5% hemolysis at 100 μg/ml , 4.2% hemolysis at 250 μg/ml , 12.0% hemolysis at 500 μg/ml against sheep red blood cells Linear Free Free L [Ref.23893489] The cytotoxicity (vs control) of P72 is 3% against HUVEC (endothelial) cells at a peptide concentration of 100 μg/ml. ##The cytotoxicity (vs control) of P72 is 4% agaisnt WI-38 (fibroblast) cells at a peptide concentration of 100 μg/ml. # Not found 23893489 J Pept Sci. 2013 Sep;19(9):554-65. doi: 10.1002/psc.2532. Romani AA, Baroni MC, Taddei S, Ghidini F, Sansoni P, Cavirani S, Cabassi CS In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens. DRAMP21139 RLLRPLLQLLKQKLR 15 GNU7 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisiae [Ref.23946320] Gram-positive bacteria : Bacillus subtilis(MIC=2 mg/L), Enterococcus faecalis(MIC=2 mg/L), Micrococcus luteus(MIC=2 mg/L), Staphylococcus aureus(MIC=2 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=2 mg/L), Pseudomonas aeruginosa(MIC=2 mg/L), Salmonella typhimurium(MIC=2 mg/L);##Fungi : Candida albicans(MIC=2 mg/L), Cryptococcus neoformans(MIC=2 mg/L), Saccharomyces cerevisiae(MIC=4 mg/L) [Ref.23946320] 0% hemolysis at 140 mg/L against human red blood cells Linear Free Free L [Ref.23946320] The cell viability of hPBMCs is at peptide concentrations of 4, 8, 16, 32, 64 μg/ml Not found 23946320 J Antimicrob Chemother. 2014 Jan;69(1):121-32. doi: 10.1093/jac/dkt322. Hyun Kim, Ju Hye Jang, Sun Chang Kim and Ju Hyun Cho De novo generation of short antimicrobial peptides with enhanced stability and cell specificity DRAMP21138 RIIRPIIQIIKQKIR 15 GNU6 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisiae [Ref.23946320] Gram-positive bacteria : Bacillus subtilis(MIC=2 mg/L), Enterococcus faecalis(MIC=2 mg/L), Micrococcus luteus(MIC=2 mg/L), Staphylococcus aureus(MIC=2 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=4 mg/L), Pseudomonas aeruginosa(MIC=2 mg/L), Salmonella typhimurium(MIC=4 mg/L);##Fungi : Candida albicans(MIC=2 mg/L), Cryptococcus neoformans(MIC=2 mg/L), Saccharomyces cerevisiae(MIC=4 mg/L) [Ref.23946320] 0% hemolysis at 140 mg/L against human red blood cells Linear Free Free L [Ref.23946320] The cell viability of hPBMCs is 102.6%, 102.6%, 107.9%, 96.8% and 97.9% at peptide concentrations of 4, 8, 16, 32, 64 μg/ml Not found 23946320 J Antimicrob Chemother. 2014 Jan;69(1):121-32. doi: 10.1093/jac/dkt322. Hyun Kim, Ju Hye Jang, Sun Chang Kim and Ju Hyun Cho De novo generation of short antimicrobial peptides with enhanced stability and cell specificity DRAMP21137 RVVRPVVQVVKQKVR 15 GNU5 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Cryptococcus neoformans, Saccharomyces cerevisiae [Ref.23946320] Gram-positive bacteria : Bacillus subtilis(MIC=16 mg/L), Enterococcus faecalis(MIC=8 mg/L), Micrococcus luteus(MIC=2 mg/L), Staphylococcus aureus(MIC=4 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=32 mg/L), Pseudomonas aeruginosa(MIC=8 mg/L), Salmonella typhimurium(MIC>64 mg/L);##Fungi : Candida albicans(MIC=2 mg/L), Cryptococcus neoformans(MIC=2 mg/L), Saccharomyces cerevisiae(MIC=2 mg/L) [Ref.23946320] 0% hemolysis at 140 mg/L against human red blood cells Linear Free Free L [Ref.23946320] The cell viability of hPBMCs is at peptide concentrations of 4, 8, 16, 32, 64 μg/ml Not found 23946320 J Antimicrob Chemother. 2014 Jan;69(1):121-32. doi: 10.1093/jac/dkt322. Hyun Kim, Ju Hye Jang, Sun Chang Kim and Ju Hyun Cho De novo generation of short antimicrobial peptides with enhanced stability and cell specificity DRAMP21135 RRWWHWWRR 9 P7 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=4.33 μM, MBC=16 μM), Staphylococcus aureus(MIC=11.3 μM, MBC=128 μM);##Gram-negative bacteria : Escherichia coli(MIC=8.67 μM, MBC=128 μM) [Ref.28372989] MHC5=86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 102.4%, 99.2%, 112.8%, 107.2% and 85.2% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21136 HRWWRWWRH 9 P8 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=1 μM, MBC=1 μM), Staphylococcus aureus(MIC=16 μM, MBC=32 μM);##Gram-negative bacteria : Escherichia coli(MIC=8 μM, MBC=32 μM) [Ref.28372989] MHC5=86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 96%, 98.4%, 86.8%, 84.8% and 88.8% and at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21134 HRWWRWWRR 9 P6 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=1 μM, MBC=1 μM), Staphylococcus aureus(MIC=8 μM, MBC=8 μM);##Gram-negative bacteria : Escherichia coli(MIC=8 μM, MBC=32 μM) [Ref.28372989] MHC5=86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 92.4%, 83.2%, 82.4%, 76% and 68% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21133 RRWWRWWRR 9 P5 (Derived from Octa 2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=1 μM, MBC=1 μM), Staphylococcus aureus(MIC=5.6 μM, MBC=8 μM);##Gram-negative bacteria : Escherichia coli(MIC=3 μM, MBC=16 μM) [Ref.28372989] MHC5=33.33 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 = 86.67 μM for hPBMCs. The cell viability of hPBMCs is 98%, 96%, 89.6%, 78%, 92.8% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21132 RRWHRHWRR 9 P4 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=2 μM, MBC=8 μM), Staphylococcus aureus(MIC=128 μM, MBC=128 μM);##Gram-negative bacteria : Escherichia coli(MIC=40 μM, MBC>128 μM) [Ref.28372989] MHC5>86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 90.8%, 94.1%, 92%, 95.6% and 86.5% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21131 RRHWRWWRR 9 P3 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=7.3 μM, MBC=64 μM), Staphylococcus aureus(MIC=40 μM, MBC>128 μM);##Gram-negative bacteria : Escherichia coli(MIC=26 μM, MBC=128 μM) [Ref.28372989] MHC5>86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 99.6%, 97.6%, 100%, 99.6% and 93.2% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21130 RRWHRWWRR 9 P2 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=5.2 μM, MBC=32 μM), Staphylococcus aureus(MIC=25.6 μM, MBC=128 μM);##Gram-negative bacteria : Escherichia coli(MIC=14.4 μM, MBC>128 μM) [Ref.28372989] MHC5>86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 99.6%, 98%, 95.6%, 98.8% and 90.4% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21129 RRWWRHWRR 9 P1 (Derived from P5) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28372989] Gram-positive bacteria : Bacillus subtilis(MIC=10 μM, MBC=32 μM), Staphylococcus aureus(MIC=48 μM, MBC>128 μM);##Gram-negative bacteria : Escherichia coli(MIC=21.33 μM, MBC=128 μM) [Ref.28372989] MHC5>86.67 μM against human red blood cells Linear Free Amidation L [Ref.28372989] IC50 > 86.67 μM for hPBMCs. The cell viability of hPBMCs is 104.0%, 107.6%, 112.4%, 101.6% and 93.2% at peptide concentrations of 0.33, 0.67, 6.67, 12.33 and 86.67 μM. Not found 28372989 Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1844-1854. doi: 10.1016/j.bbagen.2017.03.024. Bacalum M, Janosi L, Zorila F, Tepes AM, Ionescu C, Bogdan E, Hadade N, Craciun L, Grosu I, Turcu I, Radu M Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. DRAMP21128 RFRRLRKKFRKRLKKI 16 T9F (Derived from RI16) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25494332] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=128 μM), Staphylococcus epidermidis 12228(MIC=32 μM), ;##Gram-negative bacteria : Escherichia coli 25922(MIC=64 μM), Salmonella typhimurium 7731(MIC=128 μM), Pseudomonas aeruginosa 27853(MIC=256 μM), Pseudomonas aeruginosa 10419(MIC=256 μM), Pseudomonas aeruginosa 21625(MIC=256 μM), Pseudomonas aeruginosa 21630(MIC=256 μM), Pseudomonas aeruginosa LC(MIC=64 μM), Pseudomonas aeruginosa LCCI(MIC=256 μM), Pseudomonas aeruginosa LCGE(MIC=256 μM), Pseudomonas aeruginosa LCCE(MIC=256 μM) [Ref.25494332] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.25494332] The LD50 of J774.1 macrophage cells is larger than 256 μM Not found 25494332 PLoS One. 2014 Dec 10;9(12):e114605. doi: 10.1371/journal.pone.0114605. Zhu X, Ma Z, Wang J, Chou S, Shan A Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide. DRAMP21127 RFRRLRKKKRKRLKKI 16 T9K (Derived from RI16) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25494332] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=128 μM), Staphylococcus epidermidis 12228(MIC=128 μM), ;##Gram-negative bacteria : Escherichia coli 25922(MIC=128 μM), Salmonella typhimurium 7731(MIC=256 μM), Pseudomonas aeruginosa 27853(MIC=128 μM), Pseudomonas aeruginosa 10419(MIC=256 μM), Pseudomonas aeruginosa 21625(MIC=256 μM), Pseudomonas aeruginosa 21630(MIC=256 μM), Pseudomonas aeruginosa LC(MIC=256 μM), Pseudomonas aeruginosa LCCI(MIC=256 μM), Pseudomonas aeruginosa LCGE(MIC=256 μM), Pseudomonas aeruginosa LCCE(MIC=256 μM) [Ref.25494332] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.25494332] The LD50 of J774.1 macrophage cells is larger than 256 μM Not found 25494332 PLoS One. 2014 Dec 10;9(12):e114605. doi: 10.1371/journal.pone.0114605. Zhu X, Ma Z, Wang J, Chou S, Shan A Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide. DRAMP21126 RFRRLRKKIRKRLKKI 16 T9I (Derived from RI16) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25494332] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=256 μM), Staphylococcus epidermidis 12228(MIC=32 μM), ;##Gram-negative bacteria : Escherichia coli 25922(MIC=128 μM), Salmonella typhimurium 7731(MIC=256 μM), Pseudomonas aeruginosa 27853(MIC=256 μM), Pseudomonas aeruginosa 10419(MIC=256 μM), Pseudomonas aeruginosa 21625(MIC=256 μM), Pseudomonas aeruginosa 21630(MIC=256 μM), Pseudomonas aeruginosa LC(MIC=64 μM), Pseudomonas aeruginosa LCCI(MIC=256 μM), Pseudomonas aeruginosa LCGE(MIC=256 μM), Pseudomonas aeruginosa LCCE(MIC=256 μM) [Ref.25494332] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.25494332] The LD50 of J774.1 macrophage cells is larger than 256 μM Not found 25494332 PLoS One. 2014 Dec 10;9(12):e114605. doi: 10.1371/journal.pone.0114605. Zhu X, Ma Z, Wang J, Chou S, Shan A Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide. DRAMP21125 RFRRLRKKWRKRLKKI 16 T9W (Derived from RI16) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25494332] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=128 μM), Staphylococcus epidermidis 12228(MIC=64 μM), ;##Gram-negative bacteria : Escherichia coli 25922(MIC=64 μM), Salmonella typhimurium 7731(MIC=128 μM), Pseudomonas aeruginosa 27853(MIC=2 μM), Pseudomonas aeruginosa 10419(MIC=4 μM), Pseudomonas aeruginosa 21625(MIC=4 μM), Pseudomonas aeruginosa 21630(MIC=4 μM), Pseudomonas aeruginosa LC(MIC=1 μM), Pseudomonas aeruginosa LCCI(MIC=2 μM), Pseudomonas aeruginosa LCGE(MIC=4 μM), Pseudomonas aeruginosa LCCE(MIC=4 μM) [Ref.25494332] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.25494332] The LD50 of J774.1 macrophage cells is larger than 256 μM Not found 25494332 PLoS One. 2014 Dec 10;9(12):e114605. doi: 10.1371/journal.pone.0114605. Zhu X, Ma Z, Wang J, Chou S, Shan A Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide. DRAMP21124 RFRRLRKKTRKRLKKI 16 RI16 (Derived from PMAP-36) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25494332] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=128 μM), Staphylococcus epidermidis 12228(MIC=32 μM), ;##Gram-negative bacteria : Escherichia coli 25922(MIC=128 μM), Salmonella typhimurium 7731(MIC=128 μM), Pseudomonas aeruginosa 27853(MIC=256 μM), Pseudomonas aeruginosa 10419(MIC=256 μM), Pseudomonas aeruginosa 21625(MIC=256 μM), Pseudomonas aeruginosa 21630(MIC=256 μM), Pseudomonas aeruginosa LC(MIC=32 μM), Pseudomonas aeruginosa LCCI(MIC=256 μM), Pseudomonas aeruginosa LCGE(MIC=256 μM), Pseudomonas aeruginosa LCCE(MIC=256 μM) [Ref.25494332] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.25494332] The LD50 of J774.1 macrophage cells is larger than 256 μM Not found 25494332 PLoS One. 2014 Dec 10;9(12):e114605. doi: 10.1371/journal.pone.0114605. Zhu X, Ma Z, Wang J, Chou S, Shan A Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide. DRAMP21123 KRIVKLlLKWLR 12 KR-12-a5 (7-(D)L) (Derived from LL-37) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28525841] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28525841] MHC10=111 μM against human red blood cells Linear Free Amidation Mixed(7 is D) [Ref.28525841] The cell viability of mouse macrophage RAW264.7 cells is 100%, 97.4%, 98.1%, 93.6%, 100.8%, 104.5% and 104.5% at peptide concentrations of 0, 4, 8, 16, 32, 64, 128 and 256 μM Not found 28525841 Eur J Med Chem. 2017 Aug 18;136:428-441. doi: 10.1016/j.ejmech.2017.05.028. Kim EY, Rajasekaran G, Shin SY LL-37-derived short antimicrobial peptide KR-12-a5 and its d-amino acid substituted analogs with cell selectivity, anti-biofilm activity, synergistic effect with conventional antibiotics, and anti-inflammatory activity. DRAMP21122 KRIVKlILKWLR 12 KR-12-a5 (6-(D)L) (Derived from LL-37) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28525841] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=4 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28525841] MHC10=202 μM against human red blood cells Linear Free Amidation Mixed(6 is D) [Ref.28525841] The cell viability of mouse macrophage RAW264.7 cells is 100%, 101.9%, 118.9%, 107.5%, 111.3%, 110.6% and 110.6% at peptide concentrations of 0, 4, 8, 16, 32, 64, 128 and 256 μM Not found 28525841 Eur J Med Chem. 2017 Aug 18;136:428-441. doi: 10.1016/j.ejmech.2017.05.028. Kim EY, Rajasekaran G, Shin SY LL-37-derived short antimicrobial peptide KR-12-a5 and its d-amino acid substituted analogs with cell selectivity, anti-biofilm activity, synergistic effect with conventional antibiotics, and anti-inflammatory activity. DRAMP21121 KRIVkLILKWLR 12 KR-12-a5 (5-(D)K) (Derived from LL-37) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28525841] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28525841] MHC10=79 μM against human red blood cells Linear Free Amidation Mixed(5 is D) [Ref.28525841] The cell viability of mouse macrophage RAW264.7 cells is 100%, 103.4%, 116.6%, 118.9%, 115.1%, 107.9% and 105.7% at peptide concentrations of 0, 4, 8, 16, 32, 64, 128 and 256 μM Not found 28525841 Eur J Med Chem. 2017 Aug 18;136:428-441. doi: 10.1016/j.ejmech.2017.05.028. Kim EY, Rajasekaran G, Shin SY LL-37-derived short antimicrobial peptide KR-12-a5 and its d-amino acid substituted analogs with cell selectivity, anti-biofilm activity, synergistic effect with conventional antibiotics, and anti-inflammatory activity. DRAMP21119 KWCFRVCYRGRCYRRCR 17 I11R (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC=1.56 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=1.56 μM), Pseudomonas aeruginosa PAO1(MIC=6.25 μM) [Ref.26549611] MHC2=180 μM against human red blood cells Linear Free Amidation L [Ref.26549611] No cytotoxicity information found. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21120 KRIVKLILKWLR 12 KR-12-a5 (Derived from LL-37) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28525841] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28525841] MHC10=25 μM against human red blood cells Linear Free Amidation L [Ref.28525841] The cell viability of mouse macrophage RAW264.7 cells is 100%, 116.6%, 112.1%, 115.1%, 112.8%, 106.8% and 108.3% at peptide concentrations of 0, 4, 8, 16, 32, 64, 128 and 256 μM Not found 28525841 Eur J Med Chem. 2017 Aug 18;136:428-441. doi: 10.1016/j.ejmech.2017.05.028. Kim EY, Rajasekaran G, Shin SY LL-37-derived short antimicrobial peptide KR-12-a5 and its d-amino acid substituted analogs with cell selectivity, anti-biofilm activity, synergistic effect with conventional antibiotics, and anti-inflammatory activity. DRAMP21118 KWCFRVCYRGSCYRRCR 17 I11S (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=0.8 μM), Pseudomonas aeruginosa PAO1(MIC=3.13 μM) [Ref.26549611] MHC2=190 μM against human red blood cells Linear Free Amidation L [Ref.26549611] The cell viability of human embryonic fibroblasts HEF is 90.6%, 92.9%, 84.1%, 70.6% and 34.1% at peptide concentrations of 6.25, 12.5, 25, 50 and 100 μM. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21117 KWCFRVCRRGICYRRCR 17 Y8R (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=1.56 μM), Pseudomonas aeruginosa PAO1(MIC=6.25 μM) [Ref.26549611] MHC2=195 μM against human red blood cells Linear Free Amidation L [Ref.26549611] No cytotoxicity information found. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21116 KWCFRVCSRGICYRRCR 17 Y8S (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC=3.13 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=0.8 μM), Pseudomonas aeruginosa PAO1(MIC=3.13 μM) [Ref.26549611] MHC2=310 μM against human red blood cells Linear Free Amidation L [Ref.26549611] The cell viability of human embryonic fibroblasts HEF is 100%, 92.9%, 87.1%, 72.9%, 60.0% and 45.0% at peptide concentrations of 0, 6.25, 12.5, 25, 50 and 100 μM. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21115 KWCFRRCYRGICYRRCR 17 V6R (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC>50 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=1.56 μM), Pseudomonas aeruginosa PAO1(MIC>50 μM) [Ref.26549611] MHC2=200 μM against human red blood cells Linear Free Amidation L [Ref.26549611] No cytotoxicity information found. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21114 KWCFRSCYRGICYRRCR 17 V6S (Derived from tachyplesin I) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26549611] Gram-positive bacteria : Staphylococcus aureus 209P(MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli C600(MIC=1.56 μM), Pseudomonas aeruginosa PAO1(MIC=12.5 μM) [Ref.26549611] MHC2=280 μM against human red blood cells Linear Free Amidation L [Ref.26549611] No cytotoxicity information found. Not found 26549611 Biotechnol Appl Biochem. 2017 Jan;64(1):35-42. doi: 10.1002/bab.1456. Panteleev PV, Ovchinnikova TV Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. DRAMP21111 LRRAARWARRLLRR 14 ASA (Derived from SLZP) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Sporothrix schenckii, Trichophyton mentagrophytes, Aspergillus fumigatus, Candida parapsilosis [Ref.25069749] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=3.15 μg/ml), Bacillus cereus(MIC=3.15 μg/ml);##Gram-negative bacteria : E. coli (ATCC 9637)(MIC=25 μg/ml), Pseudomonas aeruginosa (ATCC BAA-427)(MIC=25 μg/ml), Klebsiella pneumoniae (ATCC 27736)(MIC=6.25 μg/ml);##Fungi : Sporothrix schenckii(MIC=12.5 μg/ml), Trichophyton mentagrophytes(MIC=100 μg/ml), Aspergillus fumigatus(MIC=50 μg/ml), Candida parapsilosis (ATCC 22019)(MIC=12.5 μg/ml) [Ref.25069749] 3% hemolysis at 10 μg/ml , 5% hemolysis at 20 μg/ml , 7.5% hemolysis at 30 μg/ml , 10% hemolysis at 40 μg/ml , 12% hemolysis at 50 μg/ml , 13% hemolysis at 60 μg/ml , 15% hemolysis at 70 μg/ml , 19% hemolysis at 80 μg/ml against human red blood cells Linear Free Amidation L [Ref.25069749] The cell viability of murine fibroblast cells (3T3) is 100%, 93.6%, 86.8%, 82.9%, 80% and 77.9% at peptide concentrations of 1.5, 3, 4.5, 6 and 9 μM. Not found 25069749 Amino Acids. 2014 Nov;46(11):2531-43. doi: 10.1007/s00726-014-1802-3. Ahmad A, Azmi S, Srivastava S, Kumar A, Tripathi JK, Mishra NN, Shukla PK, Ghosh JK Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms DRAMP21112 LRRllRWlRRLLRR 14 DLSA (Derived from SLZP) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Sporothrix schenckii, Trichophyton mentagrophytes, Aspergillus fumigatus, Candida parapsilosis [Ref.25069749] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=3.15 μg/ml), Bacillus cereus(MIC=3.15 μg/ml);##Gram-negative bacteria : E. coli (ATCC 9637)(MIC=12.5 μg/ml), Pseudomonas aeruginosa (ATCC BAA-427)(MIC=12.5 μg/ml), Klebsiella pneumoniae (ATCC 27736)(MIC=6.25 μg/ml);##Fungi : Sporothrix schenckii(MIC=6.25 μg/ml), Trichophyton mentagrophytes(MIC=12.5 μg/ml), Aspergillus fumigatus(MIC=6.25 μg/ml), Candida parapsilosis (ATCC 22019)(MIC=12.5 μg/ml) [Ref.25069749] 0% hemolysis at 80 μg/ml against human red blood cells Linear Free Amidation Mixed(4, 5, 8 is D) [Ref.25069749] The cell viability of murine fibroblast cells (3T3) is 84.8%, 83.4%, 76.9%, 72.1% and 62.8% at peptide concentrations of 1.5, 3, 4.5, 6 and 9 μM. Not found 25069749 Amino Acids. 2014 Nov;46(11):2531-43. doi: 10.1007/s00726-014-1802-3. Ahmad A, Azmi S, Srivastava S, Kumar A, Tripathi JK, Mishra NN, Shukla PK, Ghosh JK Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms DRAMP21113 LRRPPRWPRRLLRR 14 PSA (Derived from SLZP) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Sporothrix schenckii, Trichophyton mentagrophytes, Aspergillus fumigatus, Candida parapsilosis [Ref.25069749] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=12.5 μg/ml), Bacillus cereus(MIC>100 μg/ml);##Gram-negative bacteria : E. coli (ATCC 9637)(MIC=25 μg/ml), Pseudomonas aeruginosa (ATCC BAA-427)(MIC=100 μg/ml), Klebsiella pneumoniae (ATCC 27736)(MIC=12.5 μg/ml);##Fungi : Sporothrix schenckii(MIC=100 μg/ml), Trichophyton mentagrophytes(MIC>100 μg/ml), Aspergillus fumigatus(MIC>100 μg/ml), Candida parapsilosis (ATCC 22019)(MIC>100 μg/ml) [Ref.25069749] 0% hemolysis at 80 μg/ml against human red blood cells Linear Free Amidation L [Ref.25069749] The cell viability of murine fibroblast cells (3T3) is 100%, 100%, 100%, 99.9%, 84.8% and 82.1% at peptide concentrations of 1.5, 3, 4.5, 6 and 9 μM. Not found 25069749 Amino Acids. 2014 Nov;46(11):2531-43. doi: 10.1007/s00726-014-1802-3. Ahmad A, Azmi S, Srivastava S, Kumar A, Tripathi JK, Mishra NN, Shukla PK, Ghosh JK Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms DRAMP21103 RWTWRGSGRWTWR 13 L-RW (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.25683050] Gram-positive bacteria : Staphylococcus aureus(MIC=8 μg/ml), Micrococcus luteus(MIC=16 μg/ml), Bacillus subtilis(MIC=16 μg/ml);##Gram-negative bacteria : Escherichia coli(MIC=16 μg/ml), Pseudomonas aeruginosa(MIC=125 μg/ml), Acinetobacter baumannii(MIC=32 μg/ml), Stenotrophomonas maltophilia(MIC>500 μg/ml) [Ref.25683050] 0% hemolysis at 8 mg/L , 3.25% hemolysis at 16 mg/L , 0% hemolysis at 32mg/L , 0% hemolysis at 64 mg/L , 0% hemolysis at 125 mg/L , 0% hemolysis at mg/L , 2.5% hemolysis at 500 mg/L against rabbit red blood cells Linear Acylation (Conjugated with acetyl group) Amidation L [Ref.25683050] The inhibition ratio of I-RW against human bronchial epithelial cell line BEAS-2B cells is 11.3%, 2.1%, 0.5%, 6.2%, 1.5%, 8.2%, 37.4% and 51.8% at peptide concentrations of 2.5, 5, 10, 20, 40, 80, 160 and 320 μg/ml Not found 25683050 J Pept Sci. 2015 Apr;21(4):274-82. doi: 10.1002/psc.2728.  Lanlan Yu, Qiannan Fan, Xiu Yue, Yexuan Maoa and Lingbo Qu Activity of a novel-designed antimicrobial peptide and its interaction with lipids DRAMP21110 LRRLLRWLRRLLRR 14 SLZP (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Sporothrix schenckii, Trichophyton mentagrophytes, Aspergillus fumigatus, Candida parapsilosis [Ref.25069749] Gram-positive bacteria : Staphylococcus aureus (ATCC 25923)(MIC=1.56 μg/ml), Bacillus cereus(MIC=3.15 μg/ml);##Gram-negative bacteria : E. coli (ATCC 9637)(MIC=25 μg/ml), Pseudomonas aeruginosa (ATCC BAA-427)(MIC=25 μg/ml), Klebsiella pneumoniae (ATCC 27736)(MIC=3.15 μg/ml);##Fungi : Sporothrix schenckii(MIC=3.15 μg/ml), Trichophyton mentagrophytes(MIC=6.25 μg/ml), Aspergillus fumigatus(MIC=6.25 μg/ml), Candida parapsilosis (ATCC 22019)(MIC=6.25 μg/ml) [Ref.25069749] 15% hemolysis at 10 μg/ml , 25% hemolysis at 20 μg/ml , 30% hemolysis at 30 μg/ml , 40% hemolysis at 40 μg/ml , 50% hemolysis at 50 μg/ml , 55% hemolysis at 60 μg/ml , 70% hemolysis at 70 μg/ml , 80% hemolysis at 80μg/ml against human red blood cells Linear Free Amidation L [Ref.25069749] The cell viability of murine fibroblast cells (3T3) is 85.9%, 77.5%, 73.7%, 50.0%, 23.7% and 0% at peptide concentrations of 1.5, 3, 4.5, 6 and 9 μM. Not found 25069749 Amino Acids. 2014 Nov;46(11):2531-43. doi: 10.1007/s00726-014-1802-3. Ahmad A, Azmi S, Srivastava S, Kumar A, Tripathi JK, Mishra NN, Shukla PK, Ghosh JK Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms DRAMP21109 GIGGALLSAKAALGLAKGLAEHFAN 25 FPA-Bombinin-BO (toads, amphibians, animals) No entry found Not found Not found Asian bombinid toad species, Bombina orientalis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.25056849] Gram-positive bacteria : Staphylococcus aureus(MIC=7 μM, MBC=14 μM);##Gram-negative bacteria : Escherichia coli(MIC=14 μM, MBC=14 μM);##Fungi : Candida albicans(MIC=7 μM, MBC=14 μM) [Ref.25056849] 100% hemolysis at 125 mg/L against horse red blood cells Linear Free Amidation L [Ref.25056849] No cytotoxicity information found Not found 25056849 Chem Biol Drug Des. 2015 Mar;85(3):259-67. doi: 10.1111/cbdd.12396. Xiaojuan Hou, Qiang Du, Renjie Li, Mei Zhou, Hui Wang, Lei Wang, Can Guo, Tianbao Chen and Chris Shaw Feleucin-BO1: A Novel Antimicrobial Non-Apeptide Amide from the Skin Secretion of the Toad, Bombina orientalis, and Design of a Potent Broad-Spectrum Synthetic Analogue, Feleucin-K3 DRAMP21108 FLKLLKKLL 9 Feleucin-K3 (Derived from Feleucin-BO1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix In F-K3, these latter residues are substituted with Lys (K) residues, whose side-chains occupied the same positions, producing a model cationic amphipathic character in this analogue. Function: Antibacterial activity against Gram-positive bacteria [Ref.25056849] Gram-positive bacteria : Staphylococcus aureus(MIC=34 μM, MBC=128 μM) [Ref.25056849] 100% hemolysis at >250 mg/L against horse red blood cells Linear Free Amidation L [Ref.25056849] No cytotoxicity information found Not found 25056849 Chem Biol Drug Des. 2015 Mar;85(3):259-67. doi: 10.1111/cbdd.12396. Xiaojuan Hou, Qiang Du, Renjie Li, Mei Zhou, Hui Wang2, Lei Wang2, Can Guo, Tianbao Chen and Chris Shaw Feleucin-BO1: A Novel Antimicrobial Non-Apeptide Amide from the Skin Secretion of the Toad, Bombina orientalis, and Design of a Potent Broad-Spectrum Synthetic Analogue, Feleucin-K3 DRAMP21104 GIGGALLNVGKVALKGLAKGLAEHFAN 27 Feleucin-2 (toads, amphibians, animals) X5JB11  Belongs to the bombinin family. feleucin-2 Bombina variegata (Yellow-bellied toad) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.25003126] Gram-positive bacteria : Staphylococcus aureus(MIC=8 mg/L, MBC=32 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=32 mg/L, MBC=32 mg/L);##Fungi : Candida albicans(MIC=32 mg/L, MBC=32 mg/L) [Ref.25003126] 100% hemolysis at 64 mg/L against horse red blood cells Linear Free Amidation L [Ref.25003126] No cytotoxicity information found Not found 25003126 Biomed Res Int. 2014;2014:671362. doi: 10.1155/2014/671362. Bing Bai, Xiaojuan Hou, Lei Wang, Lilin Ge, Yu Luo, Chengbang Ma, Mei Zhou, Jinao Duan, Tianbao Chen, and Chris Shaw Feleucins: Novel Bombinin Precursor-Encoded Nonapeptide Amides from the Skin Secretion of Bombina variegata DRAMP21105 FLGLLGGLL 9 Feleucin-BV1 (toads, amphibians, animals) No entry found Not found Not found Bombina variegata Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria [Ref.25003126] Gram-positive bacteria : Staphylococcus aureus(MIC=256 mg/L, MBC=256 mg/L) [Ref.25003126] 100% hemolysis at >512 mg/L against horse red blood cells Linear Free Amidation L [Ref.25003126] No cytotoxicity information found Not found 25003126 Biomed Res Int. 2014;2014:671362. doi: 10.1155/2014/671362. Bing Bai, Xiaojuan Hou, Lei Wang, Lilin Ge, Yu Luo, Chengbang Ma, Mei Zhou, Jinao Duan, Tianbao Chen, and Chris Shaw Feleucins: Novel Bombinin Precursor-Encoded Nonapeptide Amides from the Skin Secretion of Bombina variegata DRAMP21106 FLGLIGSLL 9 Feleucin-BV2 (toads, amphibians, animals) No entry found Not found Not found Bombina variegata Antimicrobial, Antibacterial, Anti-Gram+ Not found Not found Not found Function: Antibacterial activity against Gram-positive bacteria [Ref.25003126] Gram-positive bacteria : Staphylococcus aureus(MIC=128 mg/L, MBC=256 mg/L) [Ref.25003126] 100% hemolysis at >512 mg/L against horse red blood cells Linear Free Amidation L [Ref.25003126] No cytotoxicity information found Not found 25003126 Biomed Res Int. 2014;2014:671362. doi: 10.1155/2014/671362. Bing Bai, Xiaojuan Hou, Lei Wang, Lilin Ge, Yu Luo, Chengbang Ma, Mei Zhou, Jinao Duan, Tianbao Chen, and Chris Shaw Feleucins: Novel Bombinin Precursor-Encoded Nonapeptide Amides from the Skin Secretion of Bombina variegata DRAMP21107 FLGLLGSLL 9 Feleucin-BO1 (toads, amphibians, animals) No entry found Not found Not found Asian bombinid toad species, Bombina orientalis Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix The Phe (F) and Leu (L) residue side-chains are oriented on one side of the peptide In feleucin-BO1, while the short side-chains of the hydrophilic Gly (G) and Ser (S) residues are oriented on the other. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.25056849] Gram-positive bacteria : Staphylococcus aureus(MIC=3 μM, MBC=6 μM);##Gram-negative bacteria : Escherichia coli(MIC=12 μM, MBC=25 μM);##Fungi : Candida albicans(MIC=6 μM, MBC=12 μM) [Ref.25056849] 100% hemolysis at 80 mg/L against horse red blood cells Linear Free Amidation L [Ref.25056849] No cytotoxicity information found Not found 25056849 Chem Biol Drug Des. 2015 Mar;85(3):259-67. doi: 10.1111/cbdd.12396. Xiaojuan Hou, Qiang Du, Renjie Li, Mei Zhou, Hui Wang, Lei Wang, Can Guo, Tianbao Chen and Chris Shaw Feleucin-BO1: A Novel Antimicrobial Non-Apeptide Amide from the Skin Secretion of the Toad, Bombina orientalis, and Design of a Potent Broad-Spectrum Synthetic Analogue, Feleucin-K3 DRAMP21232 GIMDTVKNAAKNLAGQLLDKLKCKITAC 28 Ranatuerin-2PLx (R2PLx; Frogs, Amphibians, Animals) A0A3P8MS06 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily. Not found Lithobates palustris (Pickerel frog) (Rana palustris) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level Random coil, alpha helix The CD spectra of both peptides shows the pattern of random coil in aqueous solution and a typical α-helix CD spectra in 50% of TFE solution. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.30279210] Gram-positive bacteria : Staphylococcus aureus(NCTC 10788)(MIC=32 μM, MBC=128 μM), MRSA (ATCC 12493)(MIC=256 μM, MBC=512 μM), Enterococcus faecalis(NCTC 12697)(MIC=128 μM, MBC=512 μM);##Gram-negative bacteria : Escherichia coli(NCTC 10418)(MIC=32 μM, MBC=64 μM), Pseudomonas aeruginosa(ATCC 27853)(MIC>512 μM, MBC>512 μM);##Fungi : Candida albicans(NCTC 1467)(MIC=256 μM, MBC=512 μM) [Ref.30279210] 0% hemolysis at 4 μM , 1% hemolysis at 8 μM , 5% hemolysis at 16 μM , 10% hemolysis at 32 μM , 13% hemolysis at 64 μM , 20% hemolysis at 128 μM , 30% hemolysis at 256 μM , 44% hemolysis at 512 μM against human red blood cells Linear Free Free L [Ref.30279210] No cytotoxicity information found Not found 30279210 Biosci Rep. 2018 Nov 9;38(6). pii: BSR20180710. doi: 10.1042/BSR20180710. Chen X, Zhang L, Ma C, Zhang Y, Xi X, Wang L, Zhou M, Burrows JF, Chen T A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells. DRAMP21231 KKKKKKNGFAAWGAFGA 17 S-6K-F17-3GN (Derived from S-6K-F17) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Not found Substitutions with polar, known ‘helix-breaker’ Gly residues led to losses in helical character until finally the peptide containing 3 Gly and 1 Asn (S- 6K-F17-3GN) shows a severe loss in helical structure. Function: Antibacterial activity against Gram-negative bacteria [Ref.29275987] Gram-negative bacteria : Escherichia coli(MIC=4.2 μM) [Ref.29275987] MHC2=587 μM against human red blood cells Cyclic Free Amidation (Ala17) The 'A' at position 10 and 14 are 2-(4'-pentenyl)alanine residues and there is a hydrocarbon staple crosslinking them. L No cytotoxicity information found Not found 29275987 Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Stone TA, Cole GB, Nguyen HQ, Sharpe S, Deber CM Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides. DRAMP21230 KKKKKKAGFAAWGAFGA 17 S-6K-F17-3G (Derived from S-6K-F17) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.29275987] Gram-negative bacteria : Escherichia coli(MIC=4.2 μM) [Ref.29275987] MHC2=128 μM against human red blood cells Cyclic Free Amidation (Ala17) The 'A' at position 10 and 14 are 2-(4'-pentenyl)alanine residues and there is a hydrocarbon staple crosslinking them. L No cytotoxicity information found Not found 29275987 Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Stone TA, Cole GB, Nguyen HQ, Sharpe S, Deber CM Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides. DRAMP21229 KKKKKKAGFAAWAAFGA 17 S-6K-F17-2G (Derived from S-6K-F17) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.29275987] Gram-negative bacteria : Escherichia coli(MIC=1.6 μM) [Ref.29275987] MHC2=15 μM against human red blood cells Cyclic Free Amidation (Ala17) The 'A' at position 10 and 14 are 2-(4'-pentenyl)alanine residues and there is a hydrocarbon staple crosslinking them. L No cytotoxicity information found Not found 29275987 Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Stone TA, Cole GB, Nguyen HQ, Sharpe S, Deber CM Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides. DRAMP21227 ILKKIWKPIKKLF 13 IsCT-P (Derived from IsCT) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.16871429] Gram-positive bacteria : Staphylococcus aureus (KCTC 1621)(MIC=1 μM), Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), MRSA (CCARM 3001)(MIC=2 μM), MRSA (CCARM 3543)(MIC=1 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=1 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM), MDRPA (CCARM 2095)(MIC=1 μM) [Ref.16871429] HC50>400 μM against human red blood cells Linear Free Amidation L [Ref.16871429] No cytotoxicity information found Not found 16871429 Biotechnol Lett. 2006 Sep;28(18):1431-7.  Lim SS, Yoon SP, Park Y, Zhu WL, Park IS, Hahm KS, Shin SY Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT. DRAMP21228 ILKKIWKaIKKLF 13 IsCT-a (Derived from IsCT-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.16871429] Gram-positive bacteria : Staphylococcus aureus (KCTC 1621)(MIC=1 μM), Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=1 μM), MRSA (CCARM 3001)(MIC=2 μM), MRSA (CCARM 3543)(MIC=1 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=2 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM), MDRPA (CCARM 2095)(MIC=2 μM) [Ref.16871429] HC50>400 μM against human red blood cells Linear Free Amidation The 'a' in sequence is Ala peptoid residue (N-methylglycine) L [Ref.16871429] No cytotoxicity information found Not found 16871429 Biotechnol Lett. 2006 Sep;28(18):1431-7.  Lim SS, Yoon SP, Park Y, Zhu WL, Park IS, Hahm KS, Shin SY Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT. DRAMP21225 KKFkWWWkFKK 11 STPk (Derived from STP) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.17604338] Gram-positive bacteria : Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM), Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA1 (CCARM 3001)(MIC=2 μM), MRSA2 (CCARM 3543)(MIC=0.5 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=1 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=2 μM), MDRPA1 (CCARM 2095)(MIC=4 μM), MDRPA2 (CCARM 2109)(MIC=8 μM) [Ref.17604338] MHC10>200 μM against human red blood cells Linear Free Amidation The 'k' in sequence is lysine peptoid residue [NH2-(CH2)4-NH-CH2-COOH] L [Ref.17604338] No cytotoxicity information found Not found 17604338 J Pept Sci. 2007 Aug;13(8):529-35. Zhu WL, Hahm KS, Shin SY Cathelicidin-derived Trp/Pro-rich antimicrobial peptides with lysine peptoid residue (Nlys): therapeutic index and plausible mode of action. DRAMP21226 ILkWKWkWWkWRR 13 Ink (Derived from IN) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.17604338] Gram-positive bacteria : Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM), Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA1 (CCARM 3001)(MIC=2 μM), MRSA2 (CCARM 3543)(MIC=1 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=2 μM), MDRPA1 (CCARM 2095)(MIC=4 μM), MDRPA2 (CCARM 2109)(MIC=8 μM) [Ref.17604338] MHC10>200 μM against human red blood cells Linear Free Amidation The 'k' in sequence is lysine peptoid residue [NH2-(CH2)4-NH-CH2-COOH] L [Ref.17604338] No cytotoxicity information found Not found 17604338 J Pept Sci. 2007 Aug;13(8):529-35. Zhu WL, Hahm KS, Shin SY Cathelicidin-derived Trp/Pro-rich antimicrobial peptides with lysine peptoid residue (Nlys): therapeutic index and plausible mode of action. DRAMP21223 ILKKIWKpIKKLF 13 IsCT-p (Derived from IsCT-P) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil This result indicated that D-Pro in the central position of a short a-helical peptide provides more remarkable structural flexibility than L-Pro. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.16040002] Gram-positive bacteria : Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA (CCARM 3001)(MIC=2 μM), MRSA (CCARM 3543)(MIC=1 μM), Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=2 μM), MDRPA (CCARM 2095)(MIC=2 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.16040002] 0% hemolysis at 200 μM against human red blood cells Linear Free Amidation Mixed(D-Pro8) [Ref.16040002] No cytotoxicity information found Not found 16040002 Biochem Biophys Res Commun. 2005 Sep 9;334(4):1329-35. Lim SS, Kim Y, Park Y, Kim JI, Park IS, Hahm KS, Shin SY The role of the central L- or D-Pro residue on structure and mode of action of a cell-selective alpha-helical IsCT-derived antimicrobial peptide. DRAMP21224 VRRPkWWWkFLRR 13 TPk (Derived from TP) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.17604338] Gram-positive bacteria : Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM), Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA1 (CCARM 3001)(MIC=1 μM), MRSA2 (CCARM 3543)(MIC=0.5 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=4 μM), MDRPA1 (CCARM 2095)(MIC=4 μM), MDRPA2 (CCARM 2109)(MIC=8 μM) [Ref.17604338] MHC10>200 μM against human red blood cells Linear Free Amidation The 'k' in sequence is lysine peptoid residue [NH2-(CH2)4-NH-CH2-COOH] L [Ref.17604338] No cytotoxicity information found Not found 17604338 J Pept Sci. 2007 Aug;13(8):529-35. Zhu WL, Hahm KS, Shin SY Cathelicidin-derived Trp/Pro-rich antimicrobial peptides with lysine peptoid residue (Nlys): therapeutic index and plausible mode of action. DRAMP21222 IirKIirK 8 Control-4D (Derived from IK12-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=125 mg/L), Staphylococcus aureus(MIC>500 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=31.3 mg/L), Pseudomonas aeruginosa(MIC=125 mg/L);##Fungi : Candida albicans(MIC=62.5 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation Mixed(D-Ile2, D-Arg3, D-Ile6, D-Arg7) [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21221 iirkiirk 8 Control-all D (Derived from IK12-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC>500 mg/L), Staphylococcus aureus(MIC>500 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>500 mg/L), Pseudomonas aeruginosa(MIC>500 mg/L);##Fungi : Candida albicans(MIC=250 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation D [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21219 irvkirvkirvk 12 IK12-all D (Derived from IK12-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=1.0 mg/L), Staphylococcus aureus(MIC=7.8 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=7.8 mg/L), Pseudomonas aeruginosa(MIC=15.6 mg/L);##Fungi : Candida albicans(MIC=31.3 mg/L) [Ref.24211081] HC10>125 mg/L against rabbit red blood cells Linear Free Amidation D [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21220 IIRKIIRK 8 Control-all L (Derived from IK12-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC>500 mg/L), Staphylococcus aureus(MIC>500 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>500 mg/L), Pseudomonas aeruginosa(MIC>500 mg/L);##Fungi : Candida albicans(MIC=500 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation L [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21218 IRVKIRVKIRVK 12 IK12-all L (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Beta sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=2.0 mg/L), Staphylococcus aureus(MIC=31.3 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=15.6 mg/L), Pseudomonas aeruginosa(MIC=62.5 mg/L);##Fungi : Candida albicans(MIC=125 mg/L) [Ref.24211081] HC10>125 mg/L against rabbit red blood cells Linear Free Amidation L [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21217 IRIkIrIK 8 IK8-2D (Derived from IK8-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=3.9 mg/L), Staphylococcus aureus(MIC=31.3 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=15.6 mg/L), Pseudomonas aeruginosa(MIC=7.8 mg/L);##Fungi : Candida albicans(MIC=3.9 mg/L) [Ref.24211081] HC10=1600 mg/L against rabbit red blood cells Linear Free Amidation Mixed (D-Lys4, D-Arg6) [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21215 irik 4 IK4-all D (Derived from IK8-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC>500 mg/L), Staphylococcus aureus(MIC>500 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>500 mg/L), Pseudomonas aeruginosa(MIC>500 mg/L);##Fungi : Candida albicans(MIC>500 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation D [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21216 IrIkIrIk 8 IK8-4D (Derived from IK8-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC>500 mg/L), Staphylococcus aureus(MIC>500 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>500 mg/L), Pseudomonas aeruginosa(MIC>500 mg/L);##Fungi : Candida albicans(MIC>500 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation Mixed (D-Arg2, D-Lys4, D-Arg6, D-Lys8) [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21213 irikirik 8 IK8-all D (Derived from IK8-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=2.0 mg/L), Staphylococcus aureus(MIC=3.9 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=3.9 mg/L), Pseudomonas aeruginosa(MIC=7.8 mg/L);##Fungi : Candida albicans(MIC=3.9 mg/L) [Ref.24211081] HC10=1750 mg/L against rabbit red blood cells Linear Free Amidation D [Ref.24211081] The cell viability of mouse alveolar macrophage RAW264.7 cells is 100%, 100%, 95%, 90%, 83.8%, 86.2%, 50%, 8.8% and 5% at peptide concentrations of 1, 2, 4, 8, 16, 31, 62, 100 and 125 mg/L. ##The cell viability of human fetatl lung fibrobl Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21214 irikir 6 IK6-all D (Derived from IK8-all L) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=31.3 mg/L), Staphylococcus aureus(MIC=250 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=125 mg/L), Pseudomonas aeruginosa(MIC=250 mg/L);##Fungi : Candida albicans(MIC=15.6 mg/L) [Ref.24211081] HC10>2000 mg/L against rabbit red blood cells Linear Free Amidation D [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21212 IRIKIRIK 8 IK8-all L (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Beta sheet Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.24211081] Gram-positive bacteria : Staphylococcus epidermidis(MIC=3.9 mg/L), Staphylococcus aureus(MIC=62.5 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=15.6 mg/L), Pseudomonas aeruginosa(MIC=31.3 mg/L);##Fungi : Candida albicans(MIC=3.9 mg/L) [Ref.24211081] HC10=2000 mg/L against rabbit red blood cells Linear Free Amidation L [Ref.24211081] No cytotoxicity information found Not found 24211081 Biomaterials. 2014 Jan;35(4):1315-25. doi: 10.1016/j.biomaterials.2013.10.053. Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. DRAMP21211 HLLKRVQRELIRWLDWLK 18 AmyI-1-18 (N3L, G12R) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=2.9±0.2 μM) [Ref.27478151] 14% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151] No cytotoxicity information found Not found 27478151 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-18 and its amino acid-substituted analogs. DRAMP21208 HLNKRVQRLLIGWLDWLK 18 AmyI-1-18 (E9L) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=3.7±1.5 μM). [Ref.27478151] 5% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151] No cytotoxicity information found Not found 27478151 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-23 and its amino acid-substituted analogs. DRAMP21209 HLNKRVQRLLIRWLDWLK 18 AmyI-1-18 (E9L, G12R) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=4.9±0.5 μM) [Ref.27478151] 9% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151] No cytotoxicity information found Not found 27478151 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-18 and its amino acid-substituted analogs. DRAMP21205 HLNKRVQRELIRWLDWLK 18 AmyI-1-18 (G12R) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=4.6±1.1 μM). ##[Ref.26850838] Fungi: Candida albicans(IC50=61±8 μM) [Ref.27478151] 2% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151##26850840] No cytotoxicity information found Not found 27478151##26850840 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. ##Biopolymers. 2016 Mar;106(2):219-229. doi: 10.1002/bip.22819. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-20 and its amino acid-substituted analogs. ##Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice. DRAMP21210 HLLKRVQRLLIGWLDWLK 18 AmyI-1-18 (N3L, E9L) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=4.2±0.5 μM) [Ref.27478151] 14% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151] No cytotoxicity information found Not found 27478151 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-18 and its amino acid-substituted analogs. DRAMP21207 HLLKRVQRELIGWLDWLK 18 AmyI-1-18 (N3L) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=2.5±0.7 μM). ##[Ref.26850838] Fungi: Candida albicans(IC50=58±22 μM) [Ref.27478151] 3% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151##26850842] No cytotoxicity information found Not found 27478151##26850842 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. ##Biopolymers. 2016 Mar;106(2):219-229. doi: 10.1002/bip.22821. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-22 and its amino acid-substituted analogs. ##Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice. DRAMP21206 HLNKRVQRELIGWLRWLK 18 AmyI-1-18 (D15R) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=11±1 μM). ##[Ref.26850838] Fungi: Candida albicans(IC50=31±4 μM) [Ref.27478151] 2% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151##26850841] No cytotoxicity information found Not found 27478151##26850841 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. ##Biopolymers. 2016 Mar;106(2):219-229. doi: 10.1002/bip.22820. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-21 and its amino acid-substituted analogs. ##Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice. DRAMP21204 HLNKRVQRELRGWLDWLK 18 AmyI-1-18 (I11R) (Derived from AmyI-1-18) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=10±2 μM). ##[Ref.26850838] Fungi: Candida albicans(IC50=62±2 μM) [Ref.27478151] 1% hemolysis at 50 μM against human red blood cells Linear Free Free L [Ref.27478151##26850839] No cytotoxicity information found Not found 27478151##26850839 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. ##Biopolymers. 2016 Mar;106(2):219-229. doi: 10.1002/bip.22818. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-19 and its amino acid-substituted analogs. ##Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice. DRAMP21203 HLNKRVQRELIGWLDWLK 18 AmyI-1-18 (Oryza sativa L., Angiospermae, Plants) P17654 Belongs to the glycosyl hydrolase 13 family. AMY1.1 Oryza sativa subsp. japonica (Rice) Antimicrobial, Antibacterial, Anti-Gram-, Antifungal Protein level Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Antifungal activity gaginst Candida albicans. Important for breakdown of endosperm starch during germination. [Ref.27478151] Gram-negative bacteria : Porphyromonas gingivalis(IC50=13±3 μM). ##[Ref.26850838] Fungi: Candida albicans(IC50=64±2 μM) [Ref.27478151] 0.1% hemolysis at 100 μM against human red blood cells Linear Free Free L [Ref.27478151##26850838] No cytotoxicity information found Not found 27478151##26850838 J Biosci Bioeng. 2016 Dec;122(6):652-659. doi: 10.1016/j.jbiosc.2016.05.008. ##Biopolymers. 2016 Mar;106(2):219-229. doi: 10.1002/bip.22817. Taniguchi M, Ochiai A, Takahashi K, Nakamichi SI, Nomoto T, Saitoh E, Kato T, Tanaka T Antimicrobial activity against Porphyromonas gingivalis and mechanism of action of the cationic octadecapeptide AmyI-1-18 and its amino acid-substituted analogs. ##Effect of alanine, leucine, and arginine substitution on antimicrobial activity against candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice. DRAMP21202 FKKLKKLFKKILKLK 15 HPA3NT3-analog (Derived from HPA3NT3) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Trichosporon beigelli [Ref.19642077] Gram-positive bacteria : Staphylococcus aureus(MIC=8 μM), Bacillus subtilis(MIC=8 μM), Listeria monocytogenes(MIC=4 μM);##Gram-negative bacteria : Escherichia coli(MIC=8 μM), Salmonella typhimurium(MIC=1 μM), Pseudomonas aeruginosa(MIC=2 μM);##Fungi : Candida albicans(MIC=4-8 μM), Trichosporon beigelli(MIC=1 μM) [Ref.19642077] 0% hemolysis at 100 μM , 3% hemolysis at 200 μM against human red blood cells Linear Free Amidation L [Ref.19642077] No cytotoxicity information found. Not found 19642077 J Pept Sci. 2009 Sep;15(9):589-94. doi: 10.1002/psc.1155. Gopal R, Park SC, Ha KJ, Cho SJ, Kim SW, Song PI, Nah JW, Park Y, Hahm KS Effect of Leucine and Lysine substitution on the antimicrobial activity and evaluation of the mechanism of the HPA3NT3 analog peptide. DRAMP21201 GIGKFLHSAKKWGKAFVGEIMNS 23 Magainin 2a (M2a; Frogs, Amphibians, Animals) No entry found Belongs to the gastrin/cholecystokinin family. Magainin subfamily From frog Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=128 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=128 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=128 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=128 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=32 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=64 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=64 μg/ml), Escherichia coli (BCRC 10675)(MIC=64 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=128 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=32 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21200 GYKYINNIIKYINKFFKYIW 20 GW-M4 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=8 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=8 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=8 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=32 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=32 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=16 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=32 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=4 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21199 GANAAKKFANLIKKIFNYIW 20 GW-M3 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=8 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=16 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=16 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=32 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=32 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=32 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=8 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21198 GANAAKKLATFAKKIFTAYW 20 GW-M1 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=64 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=64 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=64 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=128 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=256 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=128 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=64 μg/ml), Escherichia coli (BCRC 10675)(MIC=32 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=32 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=256 μg/ml) [Ref.18586467] MHC=64 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21197 GLTFLKKILNFAKKIYTAIW 20 GW-H3 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=16 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=16 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=16 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=8 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=32 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=32 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=128 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=32 μg/ml), Escherichia coli (BCRC 10675)(MIC=32 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=64 μg/ml) [Ref.18586467] MHC=8 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21196 GYNYAKKLANLAKKFANALW 20 GW-H1 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=16 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=8 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=32 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=16 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=64 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=32 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=16 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=32 μg/ml), Escherichia coli (BCRC 10675)(MIC=8 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=8 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=32 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21195 GATYAKKIIKTITKIATTAW 20 GW-A5 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=128 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=64 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=128 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=128 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=64 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=64 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=64 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=32 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21194 GAKALTKAATAFTKFYKTIW 20 GW-A4 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=128 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=64 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=128 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=64 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=16 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=64 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=64 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21193 GAKYAKIIYNYLKKIANALW 20 GW-A2 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=8 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=16 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=16 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=32 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=32 μg/ml), Streptococcus iniae (laboratory strain)(MIC=64 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=32 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=128 μg/ml), Escherichia coli (BCRC 10675)(MIC=64 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=16 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=8 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21192 GAKYAKYIYNFYKYIAKYIW 20 GW-A1 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=128 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=64 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=128 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=128 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=256 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=128 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=64 μg/ml), Escherichia coli (BCRC 10675)(MIC=64 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=64 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=64 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=256 μg/ml) [Ref.18586467] MHC=8 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21191 GIKIAKKAITIAKKIAKIYW 20 GW-Q6 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=32 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=4 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=32 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=32 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=32 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=16 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=8 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=32 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21190 GANALKKYFTILKKFFKLAW 20 GW-Q5 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=16 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=16 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=16 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=16 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=64 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=64 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=64 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=16 μg/ml), Escherichia coli (BCRC 10675)(MIC=8 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=16 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=8 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=32 μg/ml) [Ref.18586467] MHC=4 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21189 GANAAKKFATIAKKFINYLW 20 GW-Q4 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=16 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=8 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=16 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=8 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=128 μg/ml), Streptococcus iniae (laboratory strain)(MIC=128 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=128 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=32 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=16 μg/ml), Escherichia coli (BCRC 10675)(MIC=16 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=8 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=8 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=64 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21188 GANLAKKFYTYINKFINYAW 20 GW-Q3 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.18586467] Gram-positive bacteria : Staphylococcus aureus (BCRC 10780)(MIC=128 μg/ml), Staphylococcus xylosus (BCRC 12930)(MIC=64 μg/ml), Staphylococcus aureus (BCRC 10781)(MIC=128 μg/ml), Listeria monocytogenes (BCRC 14845)(MIC=128 μg/ml), Streptococcus bovis (BCRC 14729)(MIC=256 μg/ml), Streptococcus iniae (laboratory strain)(MIC=256 μg/ml), Lactococcus garvieae (laboratory strain)(MIC=256 μg/ml);##Gram-negative bacteria : Klebsiella oxytoca (BCRC 13985)(MIC=128 μg/ml), Pseudomonas aeruginosa (BCRC 10944)(MIC=128 μg/ml), Escherichia coli (BCRC 10675)(MIC=64 μg/ml), Enterobacter aerogenes (BCRC 10370)(MIC=32 μg/ml), Enterobacter cloacae (BCRC 10401)(MIC=64 μg/ml), Yersinia enterocolitica (BCRC 13999)(MIC=128 μg/ml) [Ref.18586467] MHC=128 μM against human red blood cells Linear Free Free L [Ref.18586467] No cytotoxicity information found. Not found 18586467 Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. DRAMP21187 WLRAFRRLVRRLARLLRR 18 WRL4 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=6.65 μM), Staphylococcus aureus 1.160(MIC=1.66 μM), Listeria monocytogenes 21662(MIC=3.32 μM), Listeria monocytogenes 21633(MIC=3.32 μM), Bacillus cereus 63301(MIC=53.18 μM), Micrococcus luteus 28001(MIC=13.29 μM), Bacillus pumilus 63202(MIC=26.59 μM), Pseudomonas fluorescens 21620(MIC=53.18 μM), MRSA 43300(MIC=3.32 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=3.32 μM), Escherichia coli 25922(MIC=13.29 μM), Escherichia coli 35150(MIC=26.59 μM), Salmonella paratyphi-A 20501(MIC=6.65 μM), Salmonella paratyphi paratyphi-B 21495(MIC=3.32 μM), Salmonella paratyphi paratyphi-C 21512(MIC=6.65 μM), Shigella flexneri 51571(MIC=1.66 μM), Salmonella choleraesuis 13312(MIC=13.29 μM), Salmonella typhimurium 51005(MIC>53.18 μM), Salmonella enteritidis 21527(MIC>53.28 μM), Vibrio parahemolyticus 21617(MIC=6.65 μM);##Fungi : Candida albicans 10231(MIC=26.59 μM) [Ref.28002968] MHC10=53.18 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WRL4 is 91.27%, 90.42%, 81.13%, 73.24%, 70.14%, 69.30%, 56.62%, 51.27% and 48.25% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21186 WLRAFRRLVRRLARGLRR 18 WRL3 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=0.43 μM), Staphylococcus aureus 1.160(MIC=0.43 μM), Listeria monocytogenes 21662(MIC=0.21 μM), Listeria monocytogenes 21633(MIC=0.21 μM), Bacillus cereus 63301(MIC=0.85 μM), Micrococcus luteus 28001(MIC=0.43 μM), Bacillus pumilus 63202(MIC=0.85 μM), Pseudomonas fluorescens 21620(MIC=0.43 μM), MRSA 43300(MIC=0.85 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=0.85 μM), Escherichia coli 25922(MIC=1.70 μM), Escherichia coli 35150(MIC=1.70 μM), Salmonella paratyphi-A 20501(MIC=0.43 μM), Salmonella paratyphi paratyphi-B 21495(MIC=0.85 μM), Salmonella paratyphi paratyphi-C 21512(MIC=0.43 μM), Shigella flexneri 51571(MIC=0.43 μM), Salmonella choleraesuis 13312(MIC=1.70 μM), Salmonella typhimurium 51005(MIC=6.81 μM), Salmonella enteritidis 21527(MIC=6.81 μM), Vibrio parahemolyticus 21617(MIC=1.70 μM);##Fungi : Candida albicans 10231(MIC=3.40 μM) [Ref.28002968] MHC10=27.22 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WRL3 is 98.31%, 95.21%, 92.96%, 90.70%, 89.30%, 89.01%, 76.90%, 48.45% and 40.73% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21185 WGRAFRRLVRRLARGLRR 18 WRL2 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=3.49 μM), Staphylococcus aureus 1.160(MIC=1.74 μM), Listeria monocytogenes 21662(MIC=1.74 μM), Listeria monocytogenes 21633(MIC=1.74 μM), Bacillus cereus 63301(MIC=55.78 μM), Micrococcus luteus 28001(MIC=27.89 μM), Bacillus pumilus 63202(MIC=55.78 μM), Pseudomonas fluorescens 21620(MIC=55.78 μM), MRSA 43300(MIC=6.97 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=6.97 μM), Escherichia coli 25922(MIC=27.89 μM), Escherichia coli 35150(MIC=13.94 μM), Salmonella paratyphi-A 20501(MIC=3.49 μM), Salmonella paratyphi paratyphi-B 21495(MIC=6.97 μM), Salmonella paratyphi paratyphi-C 21512(MIC=3.49 μM), Shigella flexneri 51571(MIC=3.49 μM), Salmonella choleraesuis 13312(MIC=13.94 μM), Salmonella typhimurium 51005(MIC=13.94 μM), Salmonella enteritidis 21527(MIC>55.78 μM), Vibrio parahemolyticus 21617(MIC=13.94 μM);##Fungi : Candida albicans 10231(MIC=13.94 μM) [Ref.28002968] MHC10>55.78 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WRL2 is 87.32%, 85.35%, 81.13%, 79.15%, 78.87%, 78.03%, 76.34%, 69.86% and 64.79% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21184 WGRAFRRGVRRLARGGRR 18 WR7 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=14.66 μM), Staphylococcus aureus 1.160(MIC=7.33 μM), Listeria monocytogenes 21662(MIC=7.33 μM), Listeria monocytogenes 21633(MIC=7.33 μM), Bacillus cereus 63301(MIC=14.66 μM), Micrococcus luteus 28001(MIC=7.33 μM), Bacillus pumilus 63202(MIC>58.64 μM), Pseudomonas fluorescens 21620(MIC=29.32 μM), MRSA 43300(MIC=14.66 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=3.67 μM), Escherichia coli 25922(MIC=14.66 μM), Escherichia coli 35150(MIC=29.32 μM), Salmonella paratyphi-A 20501(MIC=7.33 μM), Salmonella paratyphi paratyphi-B 21495(MIC=3.67 μM), Salmonella paratyphi paratyphi-C 21512(MIC=7.33 μM), Shigella flexneri 51571(MIC=7.33 μM), Salmonella choleraesuis 13312(MIC=14.66 μM), Salmonella typhimurium 51005(MIC>58.64 μM), Salmonella enteritidis 21527(MIC>58.64 μM), Vibrio parahemolyticus 21617(MIC=29.32 μM);##Fungi : Candida albicans 10231(MIC=29.32 μM) [Ref.28002968] MHC10>58.64 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WR7 is 97.46%, 94.65%, 89.01%, 82.25%, 81.41%, 80.85%, 78.59%, 76.06% and 74.80% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21183 WGRAFSRGVRRLARGGRG 18 WR5 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC=31.77 μM), Staphylococcus aureus 1.160(MIC=15.89 μM), Listeria monocytogenes 21662(MIC=15.89 μM), Listeria monocytogenes 21633(MIC=31.77 μM), Bacillus cereus 63301(MIC>63.54 μM), Micrococcus luteus 28001(MIC>63.54 μM), Bacillus pumilus 63202(MIC>63.54 μM), Pseudomonas fluorescens 21620(MIC>63.54 μM), MRSA 43300(MIC>63.54 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=7.94 μM), Escherichia coli 25922(MIC=31.77 μM), Escherichia coli 35150(MIC=31.77 μM), Salmonella paratyphi-A 20501(MIC=15.89 μM), Salmonella paratyphi paratyphi-B 21495(MIC=15.89 μM), Salmonella paratyphi paratyphi-C 21512(MIC=15.89 μM), Shigella flexneri 51571(MIC=15.89 μM), Salmonella choleraesuis 13312(MIC=15.89 μM), Salmonella typhimurium 51005(MIC>63.54 μM), Salmonella enteritidis 21527(MIC>63.54 μM), Vibrio parahemolyticus 21617(MIC>63.54 μM);##Fungi : Candida albicans 10231(MIC>63.54 μM) [Ref.28002968] MHC10>63.54 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WR5 is 98.59%, 97.46%, 96.06%, 96.09%, 92.96%, 91.83%, 89.58%, 87.32% and 85.48% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21182 WGRAFSAGVHRLARGGRG 18 WR3 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>67.01 μM), Staphylococcus aureus 1.160(MIC>67.01 μM), Listeria monocytogenes 21662(MIC=33.50 μM), Listeria monocytogenes 21633(MIC=67.01 μM), Bacillus cereus 63301(MIC>67.01 μM), Micrococcus luteus 28001(MIC>67.01 μM), Bacillus pumilus 63202(MIC>67.01 μM), Pseudomonas fluorescens 21620(MIC>67.01 μM), MRSA 43300(MIC>67.01 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC=16.75 μM), Escherichia coli 25922(MIC>67.01 μM), Escherichia coli 35150(MIC>67.01 μM), Salmonella paratyphi-A 20501(MIC=33.50 μM), Salmonella paratyphi paratyphi-B 21495(MIC>67.01 μM), Salmonella paratyphi paratyphi-C 21512(MIC>67.01 μM), Shigella flexneri 51571(MIC>67.01 μM), Salmonella choleraesuis 13312(MIC=33.50 μM), Salmonella typhimurium 51005(MIC>67.01 μM), Salmonella enteritidis 21527(MIC>67.01 μM), Vibrio parahemolyticus 21617(MIC>67.01 μM);##Fungi : Candida albicans 10231(MIC>67.01 μM) [Ref.28002968] MHC10>67.01 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WR3 is 100%, 98.87%, 92.11%, 90.42%, 90.42%, 88.45%, 87.61%, 87.89% and 87.22% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21181 WGRAFSAGVHRLANGGNG 18 WR1 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>70.09s μM), Staphylococcus aureus 1.160(MIC=70.09 μM), Listeria monocytogenes 21662(MIC>70.09 μM), Listeria monocytogenes 21633(MIC>70.09 μM), Bacillus cereus 63301(MIC>70.09 μM), Micrococcus luteus 28001(MIC>70.09 μM), Bacillus pumilus 63202(MIC>70.09 μM), Pseudomonas fluorescens 21620(MIC>70.09 μM), MRSA 43300(MIC>70.09 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC>70.09 μM), Escherichia coli 25922(MIC>70.09 μM), Escherichia coli 35150(MIC>70.09 μM), Salmonella paratyphi-A 20501(MIC>70.09 μM), Salmonella paratyphi paratyphi-B 21495(MIC>70.09 μM), Salmonella paratyphi paratyphi-C 21512(MIC>70.09 μM), Shigella flexneri 51571(MIC>70.09 μM), Salmonella choleraesuis 13312(MIC>70.09 μM), Salmonella typhimurium 51005(MIC>70.09 μM), Salmonella enteritidis 21527(MIC>70.09 μM), Vibrio parahemolyticus 21617(MIC>70.09 μM);##Fungi : Candida albicans 10231(MIC>70.09 μM) [Ref.28002968] MHC10>70.09 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WR1 is 99.44%, 96.62%, 95.21%, 94.08%, 92.96%, 92.99%, 92.68%, 87.04% and 77.58% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21180 WGEAFSAGVHRLANGGNG 18 WG18 (Derived from leucocin A) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil, alpha helix, beta sheet, turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.28002968] Gram-positive bacteria : Staphylococcus aureus 29213(MIC>71.15 μM), Staphylococcus aureus 1.160(MIC>71.15 μM), Listeria monocytogenes 21662(MIC>71.15 μM), Listeria monocytogenes 21633(MIC>71.15 μM), Bacillus cereus 63301(MIC>71.15 μM), Micrococcus luteus 28001(MIC>71.15 μM), Bacillus pumilus 63202(MIC>71.15 μM), Pseudomonas fluorescens 21620(MIC>71.15 μM), MRSA 43300(MIC>71.15 μM);##Gram-negative bacteria : Escherichia coli O157 : H7 21530(MIC>71.15 μM), Escherichia coli 25922(MIC>71.15 μM), Escherichia coli 35150(MIC>71.15 μM), Salmonella paratyphi-A 20501(MIC>71.15 μM), Salmonella paratyphi paratyphi-B 21495(MIC>71.15 μM), Salmonella paratyphi paratyphi-C 21512(MIC>71.15 μM), Shigella flexneri 51571(MIC>71.15 μM), Salmonella choleraesuis 13312(MIC>71.15 μM), Salmonella typhimurium 51005(MIC>71.15 μM), Salmonella enteritidis 21527(MIC>71.15 μM), Vibrio parahemolyticus 21617(MIC>71.15 μM);##Fungi : Candida albicans 10231(MIC>71.15 μM) [Ref.28002968] MHC10>71.15 μM against human red blood cells Linear Free Amidation L [Ref.28002968] The cell viability of RAW264.7 cells induced by WG18 is 98.87%, 94.93%, 93.52%, 90.14%, 85.35%, 83.10%, 80.56%, 75.77% and 73.62% at peptide concentrations of 0.25, 0.5, 1, 2, 4, 8, 16, 32 and 64 μM. Not found 28002968 J Med Chem. 2016 Dec 22;59(24):10946-10962. doi: 10.1021/acs.jmedchem.6b00922. Ma Z, Yang J, Han J, Gao L, Liu H, Lu Z, Zhao H, Bie X Insights into the Antimicrobial Activity and Cytotoxicity of Engineered α-Helical PeptideAmphiphiles. DRAMP21179 GILSSLWKKPKKIIAK 16 HYL-26 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC>100 μM), Staphylococcus epidermidis(MIC>100 μM);##Gram-negative bacteria : Escherichia coli(MIC>100μM), Pseudomonas aeruginosa 5482(MIC=98 μM);##Fungi : Candida albicans(MIC>100 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21178 GILSSLWKKLKKWIAK 16 HYL-25 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=2.5 μM), Staphylococcus epidermidis(MIC=1.6 μM);##Gram-negative bacteria : Escherichia coli(MIC=2.5 μM), Pseudomonas aeruginosa 5482(MIC=13 μM);##Fungi : Candida albicans(MIC=13 μM) [Ref.26998557] LC50=57 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21177 GILSSLLKKLKKWIAK 16 HYL-24 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=8 μM), Staphylococcus epidermidis(MIC=1.6 μM);##Gram-negative bacteria : Escherichia coli(MIC=4 μM), Pseudomonas aeruginosa 5482(MIC=8 μM);##Fungi : Candida albicans(MIC=16 μM) [Ref.26998557] LC50=115 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21176 GILSSLLKKWKKIIAK 16 HYL-23 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=20 μM), Staphylococcus epidermidis(MIC=2.7 μM);##Gram-negative bacteria : Escherichia coli(MIC=7.5 μM), Pseudomonas aeruginosa 5482(MIC=5 μM);##Fungi : Candida albicans(MIC=11 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21175 GKLSSLWKKLKKIIAK 16 HYL-22 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=26 μM), Staphylococcus epidermidis(MIC=2.5 μM);##Gram-negative bacteria : Escherichia coli(MIC=20 μM), Pseudomonas aeruginosa 5482(MIC=6.8 μM);##Fungi : Candida albicans(MIC=34 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21174 gilsslwkklkkiiak 16 HYL-21 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=6.3 μM), Staphylococcus epidermidis(MIC=1.7 μM);##Gram-negative bacteria : Escherichia coli(MIC=5 μM), Pseudomonas aeruginosa 5482(MIC=6.7 μM);##Fungi : Candida albicans(MIC=8 μM) [Ref.26998557] LC50=191 μM against human red blood cells Linear Free Amidation D [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21173 GILSSLWKKLKKIIAK 16 HYL-20 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=5.3 μM), Staphylococcus epidermidis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=3.4 μM), Pseudomonas aeruginosa 5482(MIC=5.3 μM);##Fungi : Candida albicans(MIC=11 μM) [Ref.26998557] LC50=197 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21172 GILSSWLKKLKKIIAK 16 HYL-19 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=16 μM), Staphylococcus epidermidis(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(MIC=11 μM), Pseudomonas aeruginosa 5482(MIC=4 μM);##Fungi : Candida albicans(MIC=17 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21168 GILKSLLKKLKKIIAK 16 HYL-15 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=17 μM), Staphylococcus epidermidis(MIC=2.2 μM);##Gram-negative bacteria : Escherichia coli(MIC=10 μM), Pseudomonas aeruginosa 5482(MIC=5 μM);##Fungi : Candida albicans(MIC=24 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21169 GILSKLLKKLKKIIAK 16 HYL-16 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=23 μM), Staphylococcus epidermidis(MIC=1.8 μM);##Gram-negative bacteria : Escherichia coli(MIC=18 μM), Pseudomonas aeruginosa 5482(MIC=4.5 μM);##Fungi : Candida albicans(MIC=45 μM) [Ref.26998557] LC50>400 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21170 kILSSLLKKLKKIIAK 16 HYL-17 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=32 μM), Staphylococcus epidermidis(MIC=1.4 μM);##Gram-negative bacteria : Escherichia coli(MIC=16 μM), Pseudomonas aeruginosa 5482(MIC=5 μM);##Fungi : Candida albicans(MIC=25 μM) [Ref.26998557] LC50=364 μM against human red blood cells Linear Free Amidation Mixed(1 is D) [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21171 GIWSSLLKKLKKIIAK 16 HYL-18 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=20 μM), Staphylococcus epidermidis(MIC=1.5 μM);##Gram-negative bacteria : Escherichia coli(MIC=1.6 μM), Pseudomonas aeruginosa 5482(MIC=6.3 μM);##Fungi : Candida albicans(MIC=16 μM) [Ref.26998557] LC50=165 μM against human red blood cells Linear Free Amidation L [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21243 GFFALIPKIISSPLFKTLLSAVGSALS 27 pardaxin-6 (GE-6) (Derived from pardaxin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found 1XC0 Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23598079] Gram-positive bacteria : Micrococcus luteus(MIC=25 mg/L), Staphylococcus aureus(MIC=50 mg/L), Streptococcus pneumoniae(MIC=50 mg/L), Streptococcus agalactiae(MIC=50 mg/L), Staphylococcus sp.(MIC=6.25 mg/L);##Gram-negative bacteria : Grouper Vibrio alginolyticus(MIC=12.5 mg/L), Vibrio harveyi(MIC=12.5 mg/L), Vibrio vulnificus(MIC=50 mg/L) [Ref.23598079] 8% hemolysis at 12.5 mg/L , 29% hemolysis at 25 mg/L , 38% hemolysis at 50 mg/L , 57.5% hemolysis at 100 mg/L , 99% hemolysis at 200 mg/L , 98% hemolysis at 400 mg/L against sheep red blood cells Linear Free Free L [Ref.23598079] No cytotoxicity information found. Not found 23598079 Peptides. 2013 Jun;44:139-48. doi: 10.1016/j.peptides.2013.04.004. Lin MC, Hui CF, Chen JY, Wu JL Truncated antimicrobial peptides from marine organisms retain anticancer activity and antibacterial activity against multidrug-resistant Staphylococcus aureus. DRAMP21242 FIFHIIKGLFHAGKMI 16 Epinecidin-8 (Derived from Epinecidin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23598079] Gram-positive bacteria : Staphylococcus aureus(MIC=6.25 mg/L), Staphylococcus sp.(MIC=12.5 mg/L);##Gram-negative bacteria : Grouper Vibrio alginolyticus(MIC=12.5 mg/L), Vibrio harveyi(MIC=6.25 mg/L) [Ref.23598079] 0% hemolysis at 50 mg/L , 10% hemolysis at 100 mg/L , 20% hemolysis at 200 mg/L , 50% hemolysis at 400 mg/L against sheep red blood cells Linear Free Free L [Ref.23598079] No cytotoxicity information found. Not found 23598079 Peptides. 2013 Jun;44:139-48. doi: 10.1016/j.peptides.2013.04.004. Lin MC, Hui CF, Chen JY, Wu JL Truncated antimicrobial peptides from marine organisms retain anticancer activity and antibacterial activity against multidrug-resistant Staphylococcus aureus. DRAMP21241 GFIFHIIKGLFHAGKMIHGLV 21 Epinecidin-1 (Derived from Epinecidin) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23598079] Gram-positive bacteria : Micrococcus luteus(MIC=6.25 mg/L), Staphylococcus aureus(MIC=50 mg/L), Streptococcus pneumoniae(MIC=50 mg/L), Streptococcus agalactiae(MIC>=100 mg/L), Staphylococcus sp.(MIC=6.25 mg/L);##Gram-negative bacteria : Grouper Vibrio alginolyticus(MIC=6.25 mg/L), Vibrio harveyi(MIC=6.25 mg/L), Vibrio vulnificus(MIC=50 mg/L) [Ref.23598079] 0% hemolysis at 25 mg/L , 10% hemolysis at 50 mg/L , 15% hemolysis at 100 mg/L , 30% hemolysis at 200 mg/L , 50% hemolysis at 400 mg/L against sheep red blood cells Linear Free Free L [Ref.23598079] No cytotoxicity information found. Not found 23598079 Peptides. 2013 Jun;44:139-48. doi: 10.1016/j.peptides.2013.04.004. Lin MC, Hui CF, Chen JY, Wu JL Truncated antimicrobial peptides from marine organisms retain anticancer activity and antibacterial activity against multidrug-resistant Staphylococcus aureus. DRAMP21240 WKRWVRRWKRWLR 13 FK13-a7 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28161291] HC50=138.0 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a7 is 100.2%, 112.8%, 97.0%, 95.1%, 83.4% and 83.8% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK1 Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21239 WKRWVQRWKRWLR 13 FK13-a6 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=8 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28161291] HC50=167.5 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a6 is 91.3%, 94.6%, 103.0%, 96.6%, 61.9% and 28.7% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK13 Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21238 WKRWVQRWKRFLR 13 FK13-a5 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28161291] HC50=230.0 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a5 is 105.3%, 103.9%, 97.1%, 94.0%, 47.5% and 44.2% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK1 Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21237 FKRWVQRWKRFLR 13 FK13-a4 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28161291] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a4 is 94.0%, 95.7%, 108.7%, 93.2%, 52.8% and 10.6% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK13 Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21236 WKRIVRRIWRWLR 13 FK13-a3 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=8 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=16 μM), Salmonella typhimurium(KCTC 1926)(MIC=4 μM) [Ref.28161291] HC50=12.5 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a3 is 102.3%, 112.1%, 104.5%, 103.8%, 74.3% and 70.2% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by F Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21235 WKRIVRWIKRWLR 13 FK13-a2 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=8 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=4 μM), Salmonella typhimurium(KCTC 1926)(MIC=4 μM) [Ref.28161291] HC50=14.0 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a2 is 104.5%, 101.7%, 100.4%, 77.0%, 58.9% and 15.8% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21167 gilssllkklkkiiak 16 HYL-13 (Derived from HYL) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.26998557] Gram-positive bacteria : Staphylococcus aureus 6271(MIC=5.7 μM), Staphylococcus epidermidis(MIC=3.2 μM);##Gram-negative bacteria : Escherichia coli(MIC=4.5 μM), Pseudomonas aeruginosa 5482(MIC=4.5 μM);##Fungi : Candida albicans(MIC=9 μM) [Ref.26998557] LC50=333 μM against human red blood cells Linear Free Amidation D [Ref.26998557] No cytotoxicity information found. Not found 26998557 J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. Nešuta O, Hexnerová R, Buděšínský M, Slaninová J, Bednárová L, Hadravová R, Straka J, Veverka V, Čeřovský V Antimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. DRAMP21234 WKRIVRRIKRWLR 13 FK13-a1 (Derived from FK13) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.28161291] Gram-positive bacteria : Bacillus subtilis(KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=4 μM), Staphylococcus aureus(KCTC1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=8 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM) [Ref.28161291] HC50>256 μM against human red blood cells Linear Free Amidation L [Ref.28161291] The cell viability of mouse macrophage RAW264.7 induced by FK13-a1 is 95.5%, 107.5%, 100.2%, 96.2%, 44.9% and 37.4% at peptide concentrations of 1.25, 2.5, 5, 10, 20 and 40 μM.## The cell viablity of human keratinocyte HaCaT induced by FK1 Not found 28161291 Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733. doi: 10.1016/j.bbamem.2017.01.037. Rajasekaran G, Kim EY, Shin SY LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity. DRAMP21233 GIMDTVKNAAKNLAGQLLDKLK 22 R2PLx-22 (Derived from R2PLx) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix The CD spectra of both peptides shows the pattern of random coil in aqueous solution and a typical α-helix CD spectra in 50% of TFE solution. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.30279210] Gram-positive bacteria : Staphylococcus aureus(NCTC 10788)(MIC=256 μM, MBC=256 μM), MRSA (ATCC 12493)(MIC>512 μM, MBC>512 μM), Enterococcus faecalis(NCTC 12697)(MIC>512 μM, MBC>512 μM);##Gram-negative bacteria : Escherichia coli(NCTC 10418)(MIC=128 μM, MBC=256 μM), Pseudomonas aeruginosa(ATCC 27853)(MIC= μM, MBC= μM);##Fungi : Candida albicans(NCTC 1467)(MIC=512 μM, MBC>512 μM) [Ref.30279210] 3% hemolysis at 1 μM , 4% hemolysis at 2 μM , 1% hemolysis at 4 μM , 0% hemolysis at 8 μM , 2% hemolysis at 16 μM , 0% hemolysis at 32 μM , 0% hemolysis at 128 μM , 3% hemolysis at 256 μM , 13% hemolysis at 512 μM against human red blood cells Linear Free Free L [Ref.30279210] No cytotoxicity information found Not found 30279210 Biosci Rep. 2018 Nov 9;38(6). pii: BSR20180710. doi: 10.1042/BSR20180710. Chen X, Zhang L, Ma C, Zhang Y, Xi X, Wang L, Zhou M, Burrows JF, Chen T A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells. DRAMP21244 FLSLIPKLVKKIIKAFK 17 TsAP-S1 (Derived from TsAP-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Anticancer against H157, H838, MCF-7, PC3 and U251-MG [Ref.23770440] Gram-positive bacteria : Staphylococcus aureus(MIC=2.5 μM, MBC=20 μM);##Gram-negative bacteria : Escherichia coli(MIC=5 μM, MBC=20 μM);##Fungi : Candida albicans(MIC=2.5 μM, MBC=5 μM) [Ref.23770440] 30% hemolysis at 5 μM , 85% hemolysis at 10 μM , 100% hemolysis at 20 μM against horse red blood cells Linear Free Amidation L [Ref.23770440] No cytotoxicity information found. Not found 23770440 Biochimie. 2013 Sep;95(9):1784-94. doi: 10.1016/j.biochi.2013.06.003. Guo X, Ma C, Du Q, Wei R, Wang L, Zhou M, Chen T, Shaw C Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities. DRAMP21245 FLGMIPKLIKKLIKAFK 17 TsAP-S2 (Derived from TsAP-2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Anticancer against H157, H838, MCF-7, PC3 and U252-MG [Ref.23770440] Gram-positive bacteria : Staphylococcus aureus(MIC=5 μM, MBC=20 μM);##Gram-negative bacteria : Escherichia coli(MIC=5 μM, MBC=40 μM);##Fungi : Candida albicans(MIC=2.5 μM, MBC=10 μM) [Ref.23770440] 30% hemolysis at 5 μM , 85% hemolysis at 10 μM , 100% hemolysis at 20 μM against horse red blood cells Linear Free Amidation L [Ref.23770440] No cytotoxicity information found. Not found 23770440 Biochimie. 2013 Sep;95(9):1784-94. doi: 10.1016/j.biochi.2013.06.003. Guo X, Ma C, Du Q, Wei R, Wang L, Zhou M, Chen T, Shaw C Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow scorpion, Tityus serrulatus: evaluation of their antimicrobial and anticancer activities. DRAMP21246 KKWRWWLKALAKK 13 pEM-2 (Derived from the venom of the snake Bothrops asper) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=5.3 ± 2.3 mg/L, MBC=6.7 ± 2.3 mg/L), Enterococcus faecalis isolates(MIC=6.7 ± 2.3 mg/L, MBC=8.0 ± 0.0 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=4.0 ± 3.5 mg/L, MBC=4.0 ± 3.5 mg/L), Acinetobacter baumannii isolates(MIC=4.0 ± 0.0 mg/L, MBC=5.3 ± 2.3 mg/L) [Ref.27591703] 0% hemolysis at 2 μg/ml , 5% hemolysis at 4 μg/ml , 15% hemolysis at 8 μg/ml , 55% hemolysis at 16 μg/ml , 87% hemolysis at 32 μg/ml , 92% hemolysis at 64 μg/ml against human red blood cells; 0% hemolysis at 16 μg/ml , 2.5% hemolysis at 32 μg/ml , 10% hemolysis at 64 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.27591703] The cell viability of HEK293 cells induced by PV is 99.1%, 99.1%, 98.3%, 94.8%, 93.9%, 87.5% and 84.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μg/mL within 24h. Not found 27591703 Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP21247 KKWRWWLKALAKKLL 15 PV (Derived from pEM-2 and MP-VT1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=0.5 ± 0.0 mg/L, MBC=0.5 ± 0.0 mg/L), Enterococcus faecalis isolates(MIC=0.7 ± 0.3 mg/L, MBC=0.8 ± 0.3 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=1.2 ± 0.8 mg/L, MBC=1.3 ± 0.6 mg/L), Acinetobacter baumannii isolates(MIC=0.4 ± 0.1 mg/L, MBC=0.5 ± 0.0 mg/L) [Ref.27591703] 0% hemolysis at 32 μg/ml , 5% hemolysis at 64 μg/ml against human red blood cells; 0% hemolysis at 32 μg/ml , 8% hemolysis at 64 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.27591703] The cell viability of HEK293 cells induced by PV is 98.8%, 97.4%, 85.8%, 56.2%, 22.8%, 12.2% and 2.3% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μg/mL within 24h. Not found 27591703 Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP21248 LKLKAIAALAKKKW 14 BVP (Derived from pEM-2 and MP-VT1 and MP-B) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=24.0 ± 13.9 mg/L, MBC=37.3 ± 24.4 mg/L), Enterococcus faecalis isolates(MIC=12.0 ± 6.9 mg/L, MBC=18.7 ± 12.2 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=16.0 ± 13.9 mg/L, MBC=18.7 ± 12.2 mg/L), Acinetobacter baumannii isolates(MIC=8.0 ± 0.0 mg/L, MBC=10.7 ± 4.6 mg/L) [Ref.27591703] 0% hemolysis at 64 μg/ml against human red blood cells; 0% hemolysis at 16 μg/ml , 2.5% hemolysis at 32 μg/ml , 10% hemolysis at 64 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.27591703] The cell viability of HEK293 cells induced by PV is 98.9%, 95.4%, 89.7%, 83.4%, 83.1%, 73.7% and 71.5% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μg/mL within 24h. Not found 27591703 Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP21249 KKWRKLLKWLAKK 13 PVP (Derived from MP-B and MP-VT1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=4.3 ± 3.5 mg/L, MBC=6.0 ± 3.5 mg/L), Enterococcus faecalis isolates(MIC=2.7 ± 1.2 mg/L, MBC=3.3 ± 1.2 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=1.3 ± 0.6 mg/L, MBC=1.7 ± 0.6 mg/L), Acinetobacter baumannii isolates(MIC=2.3 ± 1.5 mg/L, MBC=2.7 ± 1.2 mg/L) [Ref.27591703] 0% hemolysis at 64 μg/ml against human red blood cells; 0% hemolysis at 64 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.27591703] The cell viability of HEK293 cells induced by PV is 98.8%, 100%, 97.3%, 94.2%, 92.3%, 89.2% and 84.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μg/mL within 24h. Not found 27591703 Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP21250 KKWRKLLKKLKKLL 14 PV3 (Derived from pEM-2 and MP-VT1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.27591703] Gram-positive bacteria : Staphylococcus aureus isolates(MIC=2.0 ± 1.7 mg/L, MBC=2.3 ± 1.5 mg/L), Enterococcus faecalis isolates(MIC=1.2 ± 0.8 mg/L, MBC=1.3 ± 0.6 mg/L);##Gram-negative bacteria : Pseudomonas aeruginosa isolates(MIC=1.0 ± 0.0 mg/L, MBC=1.3 ± 0.6 mg/L), Acinetobacter baumannii isolates(MIC=1.0 ± 0.0 mg/L, MBC=1.7 ± 0.6 mg/L) [Ref.27591703] 0% hemolysis at 64 μg/ml against human red blood cells; 10% hemolysis at 64 μg/ml against sheep red blood cells Linear Free Amidation L [Ref.27591703] The cell viability of HEK293 cells induced by PV is 98.8%, 99.2%, 95.4%, 93.8%, 91.9%, 77.3% and 55.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μg/mL within 24h. Not found 27591703 Chem Biol Drug Des. 2017 Mar;89(3):327-338. doi: 10.1111/cbdd.12864. Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Pooshang Bagheri K Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. DRAMP21251 FLFSLIPSVIAGLVSAIRN 19 AaeAP1 (Scorpionida, Arachricla, Arthropoda) A0A060QQ43  Not found AP1 Androctonus aeneas Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antibacterial activity against Gram-positive bacteria. Antifungal activity against Candida albicans [Ref.25626077] Gram-positive bacteria : Staphylococcus aureus(MIC=16 mg/L, MBC=32 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>512 mg/L);##Fungi : Candida albicans(MIC=32 mg/L, MBC=64 mg/L) [Ref.25626077] 100% hemolysis at 16 μg/ml against horse red blood cells Linear Free Amidation L [Ref.25626077] No cytotoxicity information found. Not found 25626077 Toxins (Basel). 2015 Jan 23;7(2):219-37. doi: 10.3390/toxins7020219. Du Q, Hou X, Wang L, Zhang Y, Xi X, Wang H, Zhou M, Duan J, Wei M, Chen T, Shaw C AaeAP1 and AaeAP2: novel antimicrobial peptides from the venom of the scorpion, Androctonus aeneas: structural characterisation, molecular cloning of biosynthetic precursor-encoding cDNAs and engineering of analogues with enhanced antimicrobial and anticancer activities. DRAMP21252 FLFSLIPSAIAGLVSAIRN 19 AaeAP2 (Scorpionida, Arachricla, Arthropoda) A0A060QMQ0  Not found AP2 Androctonus aeneas Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Transcript level Not found Not found Function: Antibacterial activity against Gram-positive bacteria. Antifungal activity against Candida albicans [Ref.25626077] Gram-positive bacteria : Staphylococcus aureus(MIC=16 mg/L, MBC=16 mg/L);##Gram-negative bacteria : Escherichia coli(MIC>512 mg/L);##Fungi : Candida albicans(MIC=32 mg/L, MBC=64 mg/L) [Ref.25626077] 100% hemolysis at 64 μg/ml against horse red blood cells Linear Free Amidation L [Ref.25626077] No cytotoxicity information found. Not found 25626077 Toxins (Basel). 2015 Jan 23;7(2):219-37. doi: 10.3390/toxins7020219. Du Q, Hou X, Wang L, Zhang Y, Xi X, Wang H, Zhou M, Duan J, Wei M, Chen T, Shaw C AaeAP1 and AaeAP2: novel antimicrobial peptides from the venom of the scorpion, Androctonus aeneas: structural characterisation, molecular cloning of biosynthetic precursor-encoding cDNAs and engineering of analogues with enhanced antimicrobial and anticancer activities. DRAMP21253 FLFKLIPKAIKGLVKAIRK 19 AaeAP1a (Derived from AaeAP1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.25626077] Gram-positive bacteria : Staphylococcus aureus(MIC=4 mg/L, MBC=32 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=16 mg/L, MBC=32 mg/L);##Fungi : Candida albicans(MIC=4 mg/L, MBC=16 mg/L) [Ref.25626077] 100% hemolysis at 32 μg/ml against horse red blood cells Linear Free Amidation L [Ref.25626077] No cytotoxicity information found. Not found 25626077 Toxins (Basel). 2015 Jan 23;7(2):219-37. doi: 10.3390/toxins7020219. Du Q, Hou X, Wang L, Zhang Y, Xi X, Wang H, Zhou M, Duan J, Wei M, Chen T, Shaw C AaeAP1 and AaeAP2: novel antimicrobial peptides from the venom of the scorpion, Androctonus aeneas: structural characterisation, molecular cloning of biosynthetic precursor-encoding cDNAs and engineering of analogues with enhanced antimicrobial and anticancer activities. DRAMP21254 FLFKLIPKVIKGLVKAIRK 19 AaeAP2a (Derived from AaeAP2) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans [Ref.25626077] Gram-positive bacteria : Staphylococcus aureus(MIC=4 mg/L, MBC=32 mg/L);##Gram-negative bacteria : Escherichia coli(MIC=16 mg/L, MBC=32 mg/L);##Fungi : Candida albicans(MIC=4 mg/L, MBC=16 mg/L) [Ref.25626077] 100% hemolysis at 64 μg/ml against horse red blood cells Linear Free Amidation L [Ref.25626077] No cytotoxicity information found. Not found 25626077 Toxins (Basel). 2015 Jan 23;7(2):219-37. doi: 10.3390/toxins7020219. Du Q, Hou X, Wang L, Zhang Y, Xi X, Wang H, Zhou M, Duan J, Wei M, Chen T, Shaw C AaeAP1 and AaeAP2: novel antimicrobial peptides from the venom of the scorpion, Androctonus aeneas: structural characterisation, molecular cloning of biosynthetic precursor-encoding cDNAs and engineering of analogues with enhanced antimicrobial and anticancer activities. DRAMP21255 WLSKTAKKL 9 WL1 (Derived from CP-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unordered conformation Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29266746] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC>128 μM), Staphylococcus aureus ATCC 43300(MIC>128 μM), Staphylococcus epidermidis ATCC 12228(MIC>128 μM), Bacillus subtilis CMCC 63501(MIC>128 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC>128 μM), Escherichia coli UB1005(MIC>128 μM), Pseudomonas aeruginosa ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 7731(MIC>128 μM), Salmonella pullorum C79-13(MIC>128 μM) [Ref.29266746] MHC5>128 μM against human red blood cells Linear Free Amidation L [Ref.29266746] The cell viability of IPEC-J2 cells induced by WL1 is 99.2%, 89.8%, 86.2%, 90.8%, 87.8%, 94.3% and 76.5% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of IPEC-J2 cells induced by the control Melittin is 7 Not found 29266746 Chem Biol Drug Des. 2018 May;91(5):1017-1029. doi: 10.1111/cbdd.13165. Dong N, Wang Z, Chou S, Zhang L, Shan A, Jiang J Antibacterial activities and molecular mechanism of amino-terminal fragments from pig nematode antimicrobial peptide CP-1. DRAMP21256 WLSKTAKKLWLSKTAKKL 18 WL2 (Derived from CP-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29266746] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC=128 μM), Staphylococcus aureus ATCC 43300(MIC=128 μM), Staphylococcus epidermidis ATCC 12228(MIC=128 μM), Bacillus subtilis CMCC 63501(MIC=64 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC=8 μM), Escherichia coli UB1005(MIC=8 μM), Pseudomonas aeruginosa ATCC 27853(MIC=16 μM), Salmonella typhimurium ATCC 7731(MIC=32 μM), Salmonella pullorum C79-13(MIC=16 μM) [Ref.29266746] MHC5>128 μM against human red blood cells Linear Free Amidation L [Ref.29266746] The cell viability of IPEC-J2 cells induced by WL2 is 99.0%, 95.0%, 89%, 89.8%, 85.2%, 86.8% and 75.1% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of IPEC-J2 cells induced by the control Melittin is 77. Not found 29266746 Chem Biol Drug Des. 2018 May;91(5):1017-1029. doi: 10.1111/cbdd.13165. Dong N, Wang Z, Chou S, Zhang L, Shan A, Jiang J Antibacterial activities and molecular mechanism of amino-terminal fragments from pig nematode antimicrobial peptide CP-1. DRAMP21257 WLSKTAKKLWLSKTAKKLWLSKTAKKL 27 WL3 (Derived from CP-1) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil, alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29266746] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC=32 μM), Staphylococcus aureus ATCC 43300(MIC=32 μM), Staphylococcus epidermidis ATCC 12228(MIC=32 μM), Bacillus subtilis CMCC 63501(MIC=8 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC=2 μM), Escherichia coli UB1005(MIC=2 μM), Pseudomonas aeruginosa ATCC 27853(MIC=2 μM), Salmonella typhimurium ATCC 7731(MIC=8 μM), Salmonella pullorum C79-13(MIC=2 μM) [Ref.29266746] MHC5>128 μM against human red blood cells Linear Free Amidation L [Ref.29266746] The cell viability of IPEC-J2 cells induced by WL3 is 97.0%, 100.4%, 91.4%, 91.5%, 87.2%, 86.7% and 78.7% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of IPEC-J2 cells induced by the control Melittin is Not found 29266746 Chem Biol Drug Des. 2018 May;91(5):1017-1029. doi: 10.1111/cbdd.13165. Dong N, Wang Z, Chou S, Zhang L, Shan A, Jiang J Antibacterial activities and molecular mechanism of amino-terminal fragments from pig nematode antimicrobial peptide CP-1. DRAMP21258 SWLSKTAKKLENSAKKRISEGIAIAIQGGPR 31 Cecropin P1 (CP-1) (nematodes, animals) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found 2N92 resolved by NMR Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.29266746] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC>128 μM), Staphylococcus aureus ATCC 43300(MIC>128 μM), Staphylococcus epidermidis ATCC 12228(MIC>128 μM), Bacillus subtilis CMCC 63501(MIC=1 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC=0.5 μM), Escherichia coli UB1005(MIC=0.5 μM), Pseudomonas aeruginosa ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 7731(MIC=2 μM), Salmonella pullorum C79-13(MIC=0.5 μM) [Ref.29266746] MHC5>128 μM against human red blood cells Linear Free Amidation L [Ref.29266746] The cell viability of IPEC-J2 cells induced by CP-1 is 87.9%, 100.4%, 93.5%, 88.5%, 91.8%, 84.2% and 86.3% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of IPEC-J2 cells induced by the control Melittin is Not found 29266746 Chem Biol Drug Des. 2018 May;91(5):1017-1029. doi: 10.1111/cbdd.13165. Dong N, Wang Z, Chou S, Zhang L, Shan A, Jiang J Antibacterial activities and molecular mechanism of amino-terminal fragments from pig nematode antimicrobial peptide CP-1. DRAMP21259 MDSFQKIEKIGEGTYGVVYKAKDKVSGRLVALKKIRLENESEGVPSTA 48 Scolopendin 1 (Centipedes, Arthropoda, Animals) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans, Candida parapsilosis, Trichosporon beigelii [Ref.25209888] Gram-positive bacteria : Staphylococcus aureus ATCC 25923(MIC=5.0 ± 4.3 μM), Enterococcus faecium ATCC 19434(MIC=10.0 ± 8.7 μM);##Gram-negative bacteria : Escherichia coli O-157 ATCC 43895(MIC=5.0 ± 4.3 μM), Pseudomonas aeruginosa ATCC 27853(MIC= 5.0 ± 4.3 μM);##Fungi : Candida albicans ATCC 90028(MIC=10.0 ± 8.7 μM), Candida parapsilosis ATCC 22019(MIC= 10.0 ± 8.7 μM), Trichosporon beigelii KCTC 7707(MIC=20.0 ± 17.3 μM) [Ref.25209888] 0% hemolysis at 80 μM against human red blood cells Linear Free Amidation L [Ref.25209888] No cytotoxicity information found Not found 25209888 Insect Mol Biol. 2014 Dec;23(6):788-99. doi: 10.1111/imb.12124. Choi H, Hwang JS, Lee DG Identification of a novel antimicrobial peptide, scolopendin 1, derived from centipede Scolopendra subspinipes mutilans and its antifungal mechanism. DRAMP21260 AAKAAAKAAAKAA 13 KL0A10 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Uncertain antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.26385363] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC>128 μM), Staphylococcus epidermidis ATCC 12228(MIC>128 μM), Streptococcus faecalis ATCC 29212(MIC>128 μM), Bacillus subtilis CMCC 63501(MIC>128 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC>128 μM), Escherichia coli K88(MIC>128 μM), Escherichia coli CVCC 1515(MIC>128 μM), Escherichia coli UB1005(MIC>128 μM), Bacterium pyocyaneum ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 14028(MIC>128 μM), Salmonella pullorum C79–13(MIC>128 μM) [Ref.26385363] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.26385363] The cell viability of HEK293 cells induced by KL0A10 is 103.9%, 110%, 110.6%, 107.8%, 110.3%, 110.1%, 107.2% and 106.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of HEK293 cells induced by control M Not found 26385363 Amino Acids. 2016 Feb;48(2):403-17. doi: 10.1007/s00726-015-2094-y. Li W, Tan T, Xu W, Xu L, Dong N, Ma D, Shan A Rational design of mirror-like peptides with alanine regulation. DRAMP21261 LLKAAAKAAAKLL 13 KL4A6 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26385363] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC>128 μM), Staphylococcus epidermidis ATCC 12228(MIC=128 μM), Streptococcus faecalis ATCC 29212(MIC=16 μM), Bacillus subtilis CMCC 63501(MIC=32 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC=2 μM), Escherichia coli K88(MIC=32 μM), Escherichia coli CVCC 1515(MIC=32 μM), Escherichia coli UB1005(MIC=32 μM), Bacterium pyocyaneum ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 14028(MIC=128 μM), Salmonella pullorum C79–13(MIC>128 μM) [Ref.26385363] MHC5>256 μM against human red blood cells Linear Free Amidation L [Ref.26385363] The cell viability of HEK293 cells induced by KL4A6 is 107.8%, 108.3%, 104.4%, 104.7%, 105.6%, 100%, 94.4% and 96.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of HEK293 cells induced by control Meli Not found 26385363 Amino Acids. 2016 Feb;48(2):403-17. doi: 10.1007/s00726-015-2094-y. Li W, Tan T, Xu W, Xu L, Dong N, Ma D, Shan A Rational design of mirror-like peptides with alanine regulation. DRAMP21262 AAKLLLKLLLKAA 13 KL6A4 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26385363] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC=32 μM), Staphylococcus epidermidis ATCC 12228(MIC=16 μM), Streptococcus faecalis ATCC 29212(MIC=16 μM), Bacillus subtilis CMCC 63501(MIC=16 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC=1 μM), Escherichia coli K88(MIC=16 μM), Escherichia coli CVCC 1515(MIC=16 μM), Escherichia coli UB1005(MIC=32 μM), Bacterium pyocyaneum ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 14028(MIC>128 μM), Salmonella pullorum C79–13(MIC>128 μM) [Ref.26385363] MHC5=8 μM against human red blood cells Linear Free Amidation L [Ref.26385363] The cell viability of HEK293 cells induced by KL6A4 is 102.8%, 109.4%, 103.9%, 109.4%, 105.3%, 90.6%, 83.1% and 81.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of HEK293 cells induced by control Me Not found 26385363 Amino Acids. 2016 Feb;48(2):403-17. doi: 10.1007/s00726-015-2094-y. Li W, Tan T, Xu W, Xu L, Dong N, Ma D, Shan A Rational design of mirror-like peptides with alanine regulation. DRAMP21263 LLKLLLKLLLKLL 13 KL10A0 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Uncertain antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.26385363] Gram-positive bacteria : Staphylococcus aureus ATCC 29213(MIC>128 μM), Staphylococcus epidermidis ATCC 12228(MIC>128 μM), Streptococcus faecalis ATCC 29212(MIC>128 μM), Bacillus subtilis CMCC 63501(MIC>128 μM);##Gram-negative bacteria : Escherichia coli ATCC25922(MIC>128 μM), Escherichia coli K88(MIC>128 μM), Escherichia coli CVCC 1515(MIC>128 μM), Escherichia coli UB1005(MIC>128 μM), Bacterium pyocyaneum ATCC 27853(MIC>128 μM), Salmonella typhimurium ATCC 14028(MIC>128 μM), Salmonella pullorum C79–13(MIC>128 μM) [Ref.26385363] MHC5=2 μM against human red blood cells Linear Free Amidation L [Ref.26385363] The cell viability of HEK293 cells induced by KL10A0 is 93.9%, 93.3%, 81.9%, 77.2%, 75.6%, 67.8%, 51.9% and 19.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. The cell viability of HEK293 cells induced by control Melitti Not found 26385363 Amino Acids. 2016 Feb;48(2):403-17. doi: 10.1007/s00726-015-2094-y. Li W, Tan T, Xu W, Xu L, Dong N, Ma D, Shan A Rational design of mirror-like peptides with alanine regulation. DRAMP21264 LKKLLKLLKKLLKLAG 16 LK (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=20 μM) [Ref.23894079] MHC10=0.08 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21265 AKKLLKLLKKLLKLAG 16 LK-L1A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21266 LKKALKLLKKLLKLAG 16 LK-L4A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21267 LKKLAKLLKKLLKLAG 16 LK-L5A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21268 LKKLLKALKKLLKLAG 16 LK-L7A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21269 LKKLLKLAKKLLKLAG 16 LK-L8A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21270 LKKLLKLLKKALKLAG 16 LK-L11A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21271 LKKLLKLLKKLAKLAG 16 LK-L12A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10=0.63 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21272 LKKLLKLLKKLLKAAG 16 LK-L14A (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10=1.25 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21273 LKKLLKLGKKLLKLAG 16 LK-L8G (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=5 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2.5 μM) [Ref.23894079] MHC10=10 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21274 LKKLLKLSKKLLKLAG 16 LK-L8S (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=10 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2.5 μM) [Ref.23894079] MHC10=20 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21275 LKKLLKLPKKLLKLAG 16 LK-L8P (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=160 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21276 LKKLLKLNKKLLKLAG 16 LK-L8N (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2.5 μM) [Ref.23894079] MHC10=640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21277 LKKLLKLQKKLLKLAG 16 LK-L8Q (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2.5 μM) [Ref.23894079] MHC10=320 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21278 LKKLLKLDKKLLKLAG 16 LK-L8D (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10=1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21279 LKKLLKLEKKLLKLAG 16 LK-L8E (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=320 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21280 LKKLLKLKKKLLKLAG 16 LK-L8K (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=160 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21281 LKKLLKLHKKLLKLAG 16 LK-L8H (Derived from LK) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=2.5 μM) [Ref.23894079] MHC10=80 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21282 AKRIVQRIKDFLR 13 Lt-F1A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21283 FKRAVQRIKDFLR 13 Lt-I4A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10>640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21284 FKRIAQRIKDFLR 13 Lt-V5A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=320 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21285 FKRIVQRAKDFLR 13 Lt-I8A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21286 FKRIVQRIKDALR 13 Lt-F11A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10>640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21287 FKRIVQRIKDFAR 13 Lt-F12A (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21288 FKRGVQRIKDFLR 13 Lt-I4G (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21289 FKRSVQRIKDFLR 13 Lt-I4S (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21290 FKRNVQRIKDFLR 13 Lt-I4N (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=20 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21291 FKRQVQRIKDFLR 13 Lt-I4Q (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21292 FKRHVQRIKDFLR 13 Lt-I4H (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21293 FKRIGQRIKDFLR 13 Lt-V5G (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21294 FKRISQRIKDFLR 13 Lt-V5S (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=640 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21295 FKRINQRIKDFLR 13 Lt-V5N (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21296 FKRIQQRIKDFLR 13 Lt-V5Q (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10=1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21297 FKRIHQRIKDFLR 13 Lt-V5H (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21298 FKRIVQRIKDGLR 13 Lt-F11G (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=20 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21299 FKRIVQRIKDSLR 13 Lt-F11S (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21300 FKRIVQRIKDNLR 13 Lt-F11N (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=20 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21301 FKRIVQRIKDQLR 13 Lt-F11Q (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21302 FKRIVQRIKDHLR 13 Lt-F11H (Derived from Lt) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria. [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);##Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=10 μM) [Ref.23894079] MHC10>1280 μM against human red blood cells Linear Free Free L [Ref.23894079] No cytotoxicity information found. Not found 23894079 ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264. Son M, Lee Y, Hwang H, Hyun S, Yu J Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. DRAMP21303 RIIDLLARVRRPQKPKFVTVWVR 23 A7-PMAP-23 (Derived from PMAP-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.10527878] Gram-positive bacteria : Bacillus subtilis (KCTC 1918)(MIC=1.56 μM), Streptococcus pyogenes (KCTC 3096)(MIC=1.56 μM), Staphylococcus aureus (KCTC 1621)(MIC=3.125 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=3.125 μM), Salmonella typhimurium (KCTC 1926)(MIC=1.56 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=1.56 μM) [Ref.10527878] 0% hemolysis at 100 μM against human red blood cells Linear Free Free L [Ref.10527878] No cytotoxicity information found. Not found 10527878 Biochem Biophys Res Commun. 1999 Oct 14;264(1):281-6. Kang JH, Shin SY, Jang SY, Kim KL, Hahm KS. Effects of tryptophan residues of porcine myeloid antibacterial peptide PMAP-23 on antibiotic activity. DRAMP21304 RIIDLLWRVRRPQKPKFVTVAVR 23 A21-PMAP-23 (Derived from PMAP-23) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix, beta turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.10527878] Gram-positive bacteria : Bacillus subtilis (KCTC 1918)(MIC=3.125 μM), Streptococcus pyogenes (KCTC 3096)(MIC=3.125 μM), Staphylococcus aureus (KCTC 1621)(MIC=6.25 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=6.25 μM), Salmonella typhimurium (KCTC 1926)(MIC=3.125 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=3.125 μM) [Ref.10527878] 0% hemolysis at 100 μM against human red blood cells Linear Free Free L [Ref.10527878] No cytotoxicity information found. Not found 10527878 Biochem Biophys Res Commun. 1999 Oct 14;264(1):281-6. Kang JH, Shin SY, Jang SY, Kim KL, Hahm KS. Effects of tryptophan residues of porcine myeloid antibacterial peptide PMAP-23 on antibiotic activity. DRAMP21305 RRRRRRRR 8 R8 (De novo synthesis) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Alpha helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=44 μM);##Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=44 μM) [Ref.23085001] HC50>128 μM against human red blood cells Linear Free Amidation L [Ref.23085001] No cytotoxicity information found. Not found 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-32. doi: 10.1016/j.bbamem.2012.10.010. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM Antimicrobial and cell-penetrating properties of penetratin analogs: effect of sequence and secondary structure. DRAMP21306 FVQWWSKWLGRIL 13 TL-1 (Derived from Temporin-1Tl (TL)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26311041] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=32 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.26311041] HC50=21.4 μM against human red blood cells Linear Free Amidation L [Ref.26311041] The cell viability of RAW264.7 macrophages cells induced by TL-1 is 112.2%, 109.3% and 109.3% at peptide concentrations of 2.5, 5 and 10 μM. Not found 26311041 J Pept Sci. 2015 Oct;21(10):779-85. doi: 10.1002/psc.2807. Rajasekaran G, Kamalakannan R, Shin SY Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions. DRAMP21307 FVRWWSKWLRRIL 13 TL-2 (Derived from Temporin-2Tl (TL)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26311041] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=8 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.26311041] HC50=8.5 μM against human red blood cells Linear Free Amidation L [Ref.26311041] The cell viability of RAW264.7 macrophages cells induced by TL-2 is 111.8%, 112.5% and 81.0% at peptide concentrations of 2.5, 5 and 10 μM. Not found 26311041 J Pept Sci. 2015 Oct;21(10):779-85. doi: 10.1002/psc.2807. Rajasekaran G, Kamalakannan R, Shin SY Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions. DRAMP21308 FVRWWSRWLRRIL 13 TL-3 (Derived from Temporin-3Tl (TL)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26311041] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=8 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=8 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM) [Ref.26311041] HC50=8.0 μM against human red blood cells Linear Free Amidation L [Ref.26311041] The cell viability of RAW264.7 macrophages cells induced by TL-3 is 117.4%, 111.5% and 110.5% at peptide concentrations of 2.5, 5 and 10 μM. Not found 26311041 J Pept Sci. 2015 Oct;21(10):779-85. doi: 10.1002/psc.2807. Rajasekaran G, Kamalakannan R, Shin SY Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions. DRAMP21309 FVKWWSKWLKKIL 13 TL-4 (Derived from Temporin-4Tl (TL)) No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.26311041] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=4 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=8 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);##Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=8 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=16 μM), Salmonella typhimurium (KCTC 1926)(MIC=2 μM) [Ref.26311041] HC50=15.9 μM against human red blood cells Linear Free Amidation L [Ref.26311041] The cell viability of RAW264.7 macrophages cells induced by TL-4 is 116.7%, 118.2% and 87.2% at peptide concentrations of 2.5, 5 and 10 μM. Not found 26311041 J Pept Sci. 2015 Oct;21(10):779-85. doi: 10.1002/psc.2807. Rajasekaran G, Kamalakannan R, Shin SY Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions. DRAMP21311 RWLRKWTRKRLK 12 2W-1 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=64 μM), Staphylococcus aureus 25923 (MIC=32 μM), Staphylococcus epidermidis 12228 (MIC=16 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=16 μM), Escherichia coli 1005 (MIC=16 μM), Staphylococcus typhi (MIC=64 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 2W-1 is 95.9%, 92.4%, 89.0%, 86.4%, 85.7%, 94.1%, 91.9% and 98.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00289. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21312 RRLRWKTRWRLK 12 2W-2 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=16 μM), Staphylococcus aureus 25923 (MIC=16 μM), Staphylococcus epidermidis 12228 (MIC=16 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=16 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=32 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 2W-2 is 94.8%, 92.1%, 95.5%, 98.3%, 94.5%, 95%, 89.5% and 84.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00290. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21313 RRLRKKTWKRLW 12 2W-3 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=64 μM), Staphylococcus aureus 25923 (MIC>128 μM), Staphylococcus epidermidis 12228 (MIC=64 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=16 μM), Escherichia coli 1005 (MIC=32 μM), Staphylococcus typhi (MIC=64 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 2W-3 is 95.2%, 89.7%, 87.2%, 91.6%, 85%, 88.4%, 84.8% AND 89.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00291. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21314 RWLRKWTRKWLK 12 3W-1 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=8 μM), Staphylococcus aureus 25923 (MIC=16 μM), Staphylococcus epidermidis 12228 (MIC=8 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=16 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3W-1 is 99.5%, 96.2%, 95.7%, 90.9%, 69.1%, 6.4%, -1% and 0% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00292. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21315 WRLRWKTRWRLK 12 3W-2 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=4 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=4 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Pseudomonas aeruginosa 25349 (MIC=8 μM), Acinetobacter baumannii AB1901 (MIC=4 μM), Acinetobacter baumannii AB1902 (MIC=4 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3W-2 is 100.9%, 96%, 103.4%, 97.2%, 104.7%, 103.6%, 97.6%, 90.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00293. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21316 RRLWKKTWKRLW 12 3W-3 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=8 μM), Staphylococcus aureus 25923 (MIC=16 μM), Staphylococcus epidermidis 12228 (MIC=8 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=8 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3W-3 is 94.8%, 100.9%, 93.4%, 94.0%, 93.6%, 73.4%, 14.5% and -1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00294. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21317 RWLRWKTRWRLK 12 3W-4 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=4 μM), Staphylococcus aureus 25923 (MIC=16 μM), Staphylococcus epidermidis 12228 (MIC=16 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=2 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=8 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3W-4 is 100.2%, 92.2%, 96.2%, 89.0%, 94.1%, 97.4%, 94.3% and 88.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00295. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21318 RRLRWWTRWRLK 12 3W-5 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=4 μM), Staphylococcus aureus 25923 (MIC=8 μM), Staphylococcus epidermidis 12228 (MIC=8 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=8 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3W-5 is 96.4%, 99.1%, 100.2%, 101.4%, 97.8%, 99%, 102.6% and 82.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00296. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21319 VRLRVKTRVRLK 12 3V (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=16 μM), Staphylococcus aureus 25923 (MIC=64 μM), Staphylococcus epidermidis 12228 (MIC=32 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=16 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3V is 98.6%, 101.4%, 103.4%, 92.4%, 101%, 101.9%, 93.6% and 97.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00297. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21320 LRLRLKTRLRLK 12 3L (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=32 μM), Staphylococcus aureus 25923 (MIC=32 μM), Staphylococcus epidermidis 12228 (MIC=64 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=16 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 3L is 95.9%, 92.4%, 91.6%, 82.1%, 104.3%, 97.1%, 99.5% and 96.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00298. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21321 RWLRWWTRWRLK 12 4W (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=4 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=4 μM) [Ref.31276398] MHC=128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by 4W is 95.3%, 88.3%, 89.7%, 97.9%, 91.2%, 77.6%, 32.8% and 0% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00299. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21322 WRVRWKTRWRVK 12 RTV (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=4 μM), Staphylococcus epidermidis 12228 (MIC=4 μM), Staphylococcus aureus 11011 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=4 μM), Escherichia coli 20411 (MIC=4 μM), Acinetobacter baumannii AB1901 (MIC=8 μM), Acinetobacter baumannii AB1902 (MIC=8 μM), Pseudomonas aeruginosa 25349 (MIC=32 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RTV is 106.6%, 103.1%, 94.0%, 106.4%, 96.4%, 104.8%, 95.5% and 96.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00300. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21323 WRIRWKTRWRIK 12 RTI (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=2 μM), Pseudomonas aeruginosa 25349 (MIC=8 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RTI is 103.1%, 97.4%, 103.8%, 106.4%, 96.4%, 104.8%, 95.7% and 96.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00301. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21324 WRFRWKTRWRFK 12 RTF (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=4 μM), Pseudomonas aeruginosa 25349 (MIC=8 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RTF is 100.7%, 101.6%, 97.8%, 99.0%, 100.9%, 97.4%, 95.3% and 90.3% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00302. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21325 WRLRWRTRWRLR 12 RTL (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=4 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=4 μM), Pseudomonas aeruginosa 25349 (MIC=16 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RTL is 102.2%, 104.5%, 94.8%, 103.1%, 103.6%, 103.6%, 105.5% and 105.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00303. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21326 WRLRWRLRWRLR 12 RLR (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=1 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=1 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=4 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RLR is 100%, 91.4%, 104.8%, 94.5%, 98.6%, 99.8%, 98.8% and 82.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00304. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21327 WRVRWRVRWRVR 12 RVR (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=1 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=1 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=4 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=2 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RVR is 97.9%, 98.6%, 91.7%, 102.9%, 102.2%, 100.3%, 98.1% and 97.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00305. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21328 WRTRWRTRWRTR 12 RTR (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=4 μM), Staphylococcus aureus 25923 (MIC=8 μM), Staphylococcus epidermidis 12228 (MIC=8 μM), Staphylococcus aureus 11011 (MIC=4 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=4 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=32 μM), Acinetobacter baumannii AB1902 (MIC=32 μM), Pseudomonas aeruginosa 25349 (MIC>64 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RTR is 97.2%, 106.9%, 96.7%, 104.0%, 94.5%, 98.6%, 102.2% and 103.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00306. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21329 WRFRWRFRWRFR 12 RFR (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=1 μM), Staphylococcus aureus 25923 (MIC=1 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=8 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=4 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=2 μM), Pseudomonas aeruginosa 25349 (MIC=8 μM). [Ref.31276398] MHC=64μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RFR is 106.2%, 97.6%, 99.8%, 101.7%, 100.9%, 101.6%, 78.1% and 45.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00307. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21330 WKVKWKVKWKVK 12 KVK (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=1 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM) ;##Gram-negative bacteria: Escherichia coli 25922 (MIC=2 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=1 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=1 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by KVK is 101.2%, 98.3%, 98.3%, 99.1%, 95.2%, 101.9%, 96.6% and 100.5% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00308. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21331 WKLKWKLKWKLK 12 KLK (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=4 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=4 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC=128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by KLK is 103.3%, 100.2%, 100.5%, 97.8%, 99.1%, 96.4%, 98.4% and 44.5% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00309. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21332 WKIKWKIKWKIK 12 KIK (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=2 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=2 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=2 μM), Acinetobacter baumannii AB1901 (MIC=1 μM), Acinetobacter baumannii AB1902 (MIC=2 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC=64μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by KIK is 100.7%, 106.9%, 95.5%, 101.6%, 103.1%, 102.8%, 61.9% and 32.2% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00310. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21333 WRVRWKVRWRVK 12 RVK (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC=1 μM), Staphylococcus aureus 25923 (MIC=2 μM), Staphylococcus epidermidis 12228 (MIC=2 μM), Staphylococcus aureus 11011 (MIC=2 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=4 μM), Escherichia coli 1005 (MIC=2 μM), Staphylococcus typhi (MIC=2 μM), Escherichia coli 20411 (MIC=1 μM), Acinetobacter baumannii AB1901 (MIC=2 μM), Acinetobacter baumannii AB1902 (MIC=4 μM), Pseudomonas aeruginosa 25349 (MIC=4 μM). [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RVK is 101.0%, 98.6%, 100.3%, 103.3%, 104.1%, 101.0%, 103.8% and 91.9% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00311. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21334 SFLTTVKKLVTNLAALAGTVIDTIKCKVTGGCRT 34 Ranatuerin-2Pb (Frogs, amphibians, animals) A0A513ZTP5 Not found Not found Lithobates pipiens (Northern leopard frog) (Rana pipiens) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Transcript level 50% Helix, 7.8% antiparallel, 1.2% parallel, 10.9% turn and 29.8% others in 50% TFE/H2O. ##3.5% Helix, 26.6% antiparallel, 0% parallel, 18.3% turn and Ranatuerin-2Pb might also possess two helical segments at respective N-terminus and C-terminus, and the last two residues are probably included in the helix domain. Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31242693] Gram-positive bacteria:Staphylococcus aureus (MIC=8 μM; MBC=8 μM), MRSA (MIC=16 μM; MBC=32 μM), Enterococcus faecalis (MIC>256 μM; MBC>256 μM);##Gram-negative bacteria: Escherichia coli (MIC=8 μM; MBC=8 μM), Pseudomonas aeruginosa (MIC>256 μM; MBC>256 μM);##Fungi: Candida albicans (MIC=8 μM; MBC=16 μM) [Ref.31242693] 7% hemolysis at 2 μM, 23% hemolysis at 8 μM, 50% hemolysis at 16 μM, 71% hemolysis at 32 μM, 100% hemolysis at 64 μM on horse erythrocytes. Linear Free Free L [Ref.31242693] The IC50 values which represents the inhibitory effect of Ranatuerin-2Pb on the proliferation of NCI-H157, MCF-7, U251MG and PC-3 are 1.453 μM, 7.254 μM, 2.172 μM and 2.251 μM. In addtion, Ranatuerin-2Pb showed no inhibitory effect on the proliferation of MDA-MB-435s. DETAILED DATA: ①The cell viabillity of NCI-H157 induced by Ranatuerin-2Pb is 96.2%, 96.9%, 85.6%, 60%, 5% and 4.4% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 100%, 95%, 89.4%, 41.2%, 16.2% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ②The cell viability of MCF-7 induced by Ranatuerin-2Pb is 100.6%, 92.5%, 90%, 99.4%, 36.2% and 11.2% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 100%, 98.1%, 92.5%, 7.5%, 8.7% and 8.7% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ③The cell viability of U251-MG induced by Ranatuerin-2Pb is 100%, 105.6%, 108.1%, 102.5%, 59.4% and 17.5% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 99.4%, 99.4%, 75.6%, 18.7%, 11.9% and 18.1% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ④The cell viability of PC-3 induced by Ranatuerin-2Pb is 108.7%, 112.5%, 84.4%, 80.6%, 28.1% and 16.2% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 110%, 113.1%, 109.4%, 33.1%, 16.9% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ⑤ The cell viability of MDA-MB-435S induced by Ranatuerin-2Pb is 96.9%, 88.8%, 96.9%, 88.1%, 100 and 25.6%, while the cell viability induced by Melittin is 100%, 93.1%, 82.5%, 18.8%, 18.8% and 18.1%. Not found 31242693 Biomolecules. 2019 Jun 25;9(6):249. doi: 10.3390/biom9060249. Zhou, XW; Shi, DN; Zhong, RM; Ye, ZM; Ma, CB; Zhou, M; Xi, XP; Wang, L; Chen, TB; Kwok, HF Bioevaluation of Ranatuerin-2Pb from the Frog Skin Secretion of Rana pipiens and its Truncated Analogues DRAMP21335 SFLTTVKKLVTNLAALAGTVIDTIKCKVTGGC 32 RPa (Frogs, amphibians, animals) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 33.6% Helix, 18.1% antiparallel, 4.3% parallel, 11.4% turn and 32.5% others in 50% TFE/H2O. ##2.4% Helix, 30.6% antiparallel, 0% parallel, 17.3% turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31242693] Gram-positive bacteria:Staphylococcus aureus (MIC=16 μM; MBC=32 μM), MRSA (MIC=>256 μM; MBC>256 μM), Enterococcus faecalis (MIC>256 μM; MBC>256 μM);##Gram-negative bacteria: Escherichia coli (MIC=32 μM; MBC=64 μM), Pseudomonas aeruginosa (MIC>256 μM; MBC>256 μM);##Fungi: Candida albicans (MIC>256 μM; MBC>256 μM) [Ref.31242693] 7% hemolysis at 16 μM, 23% hemolysis at 32 μM, 50% hemolysis at 64 μM, 76% hemolysis at 128 μM, 90% hemolysis at 256 μM, 100% hemolysis at 512 μM on horse erythrocytes. Linear Free Free L [Ref.31242693] RPa only possessed inhibitory effect on the proliferation of H157 with the IC value of 5.841 μM, while showed no inhibitory effect on the proliferation of MCF-7, U251MG, PC-3 and MDA-MB-435s. DETAILED DATA: ①The cell viabillity of NCI-H157 induced by RPa is 97.5%, 94.4%, 92.5%, 71.2%, 40.6% and 4.4% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 100%, 95%, 89.4%, 41.2%, 16.2% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ②The cell viability of MCF-7 induced by RPa is 100.6%, 93.1%, 97.5%, 97.5%, 93.7% and 78.1% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM , while the cell viability induced by Melittin is 100%, 98.1%, 92.5%, 7.5%, 8.7% and 8.7% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ③The cell viability of U251-MG induced by RPa is 100%, 105.6%, 108.1%, 102.5%, 59.4% and 17.5% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 99.4%, 99.4%, 75.6%, 18.7%, 11.9% and 18.1% at 0.001, 0.01, 0.1, 1, 10, 100 μM.④The cell viability of PC-3 induced by RPb is 108.7%, 104.4%, 92.5%, 92.5%, 82.5% and 24.4% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 110%, 113.1%, 109.4%, 33.1%, 16.9% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ⑤The cell viability of MDA-MB-435S induced by RPa is 97.5%, 95%, 97.5%, 73.1%, 68.8% and 36.9%, while the cell viability induced by Melittin is 100%, 93.1%, 82.5%, 18.8%, 18.8% and 18.1%. Not found 31242693 Biomolecules. 2019 Jun 25;9(6):249. doi: 10.3390/biom9060249. Zhou, XW; Shi, DN; Zhong, RM; Ye, ZM; Ma, CB; Zhou, M; Xi, XP; Wang, L; Chen, TB; Kwok, HF Bioevaluation of Ranatuerin-2Pb from the Frog Skin Secretion of Rana pipiens and its Truncated Analogues DRAMP21336 SFLTTVKKLVTNLAAL 16 RPb (Frogs, amphibians, animals) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 49.6% Helix, 7.6% antiparallel, 0% parallel, 9.8% turn and 33% others in 50% TFE/H2O. ##0.3% Helix, 25.4% antiparallel, 0% parallel, 19.4% turn and 55 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31242693] Gram-positive bacteria:Staphylococcus aureus (MIC=8 μM; MBC=8 μM), MRSA (MIC=16 μM; MBC=32 μM), Enterococcus faecalis (MIC=32 μM; MBC=128 μM);##Gram-negative bacteria: Escherichia coli (MIC=16 μM; MBC=16 μM), Pseudomonas aeruginosa (MIC=64 μM; MBC=256 μM);##Fungi: Candida albicans (MIC=16 μM; MBC=16 μM) [Ref.31242693] 7% hemolysis at 16 μM, 18% hemolysis at 32 μM, 20% hemolysis at 64 μM, 40% hemolysis at 128 μM, 70% hemolysis at 256 μM, 100% hemolysis at 512 μM on horse erythrocytes. Linear Free Amidation L [Ref.31242693] RPb only possessed inhibitory effect on the proliferation of H157 with the IC value of 6.856 μM, while showed no inhibitory effect on the proliferation of MCF-7, U251MG, PC-3 and MDA-MB-435s. DETAILED DATA: ①The cell viabillity of NCI-H157 induced by RPb is 98.7%, 102.5%, 96.9%, 98.1%, 38.1%, 9.4% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 100%, 95%, 89.4%, 41.2%, 16.2% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ②The cell viability of MCF-7 induced by RPb is 100.6%, 92.5%, 90%, 99.4%, 36.2% and 11.2% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, , while the cell viability induced by Melittin is 100%, 98.1%, 92.5%, 7.5%, 8.7% and 8.7% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ③The cell viability of U251-MG induced by RPb is 105%, 103.1%, 109.4%, 102.5%, 105.6% and 13.1% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 99.4%, 99.4%, 75.6%, 18.7%, 11.9% and 18.1% at 0.001, 0.01, 0.1, 1, 10, 100 μM.④The cell viability of PC-3 induced by RPa is 108.8%, 103.8%, 118.1%, 125.6%, 116.9% and 68.8% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 110%, 113.1%, 109.4%, 33.1%, 16.9% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ⑤The cell viability of MDA-MB-435S induced by RPa is 98.1%, 95%, 100.6%, 97.5%, 80.6% and 43.1%, while the cell viability induced by Melittin is 100%, 93.1%, 82.5%, 18.8%, 18.8% and 18.1%. Not found 31242693 Biomolecules. 2019 Jun 25;9(6):249. doi: 10.3390/biom9060249. Zhou, XW; Shi, DN; Zhong, RM; Ye, ZM; Ma, CB; Zhou, M; Xi, XP; Wang, L; Chen, TB; Kwok, HF Bioevaluation of Ranatuerin-2Pb from the Frog Skin Secretion of Rana pipiens and its Truncated Analogues DRAMP21337 GRFKRFRKKFKKLFKKLSPVIPLLHL 26 BMAP-27 (Bovine, mammals, animals) P54228 Belongs to the cathelicidin family CATHL6 Bos taurus (Bovine) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level 73% α-helix in 50% TFE/H2O An α-helix occurred from Arg2 to Leu17 in the N-terminal region and a short α-helix is observed from Leu23 to Leu26 in the Cterminal region; the two regions are connected with a flexible region containing two proline residues. 2KET resolved by NMR Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31226350] Gram-positive bacteria:Staphylococcus aureus (MIC=1-2 μM);##Gram-negative bacteria: Escherichia coli (MIC=2-4 μM) [Ref.31226350] 50% hemolysis at 75 μM for human red blood cells Linear Free Amidation L [Ref.31226350] The CC50 values which represent peptide concentration (μM) inducing 50% cytotoxicity to human cancer cell lines of BMAP-27 on MDA361 and A549 are 4.2 μM and 5.3 μM. DETAILED DATA: ①The cell viability of MDA-361 induced by BMAP-27 is 100%, 100%, 98.9%, 97.7%, 87.6%, 59.8%, 34.7%, 12.4%, 10.3%, 8.3% and 9.4% at peptide concentrations of 0.1, 0.2, 0.4, 0.8, 1.6, 3.2, 6.4, 13, 25, 50 and 100 μM. ②The cell viability of A549 induced by BMAP-27 is 100%, 99.1%, 97.7%, 94.7%, 74.5%, 41.4%, 24.4%, 11.3%, 9.7%, 10.3% and 7.4% at peptide concentrations of 0.1, 0.2, 0.4, 0.8, 1.6, 3.2, 6.4, 13, 25, 50 and 100 μM. Not found 31226350 Peptides. 2019 Jun 18;118:170106. doi: 10.1016/j.peptides.2019.170106. Yang S, Lee CW, Kim HJ, Jung HH, Kim JI, Shin SY, Shin SH Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide DRAMP21338 FLRALWNVAKSVF 13 [Arg]3-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 23% α-helix in 60% TFE/Water. ## 0%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4560. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=1.6 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=1.6 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.8 μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.4 μmol/L), Enterobacter cloacae β-12 (MIC=6.3 μmol/L), Pseudomonas aeruginosa ATCC 27853 (MIC=6.3 μmol/L);##Fungi: Candida albicans MDM8 (MIC=0.8 μmol/L), Candida tropicalis IOC 4560 (MIC=0.8 μmol/L) [Ref.31212183] 25% hemolysis at 6.3 μmol/L, 65% hemolysis at 25 μmol/L, 75% hemolysis at 50 μmol/L, 100% hemolysis at 100 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21339 FLGALWRVAKSVF 13 [Arg]7-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 22% α-helix in 60% TFE/Water. ## 0%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4561. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=1.6 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=1.6 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.4 μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L), Enterobacter cloacae β-12 (MIC=6.3 μmol/L), Pseudomonas aeruginosa ATCC 27853 (MIC=6.3 μmol/L);##Fungi: Candida albicans MDM8 (MIC=0.8 μmol/L), Candida tropicalis IOC 4560 (MIC=0.8 μmol/L) [Ref.31212183] 10% hemolysis at 6.3 μmol/L, 50% hemolysis at 12.5 μmol/L, 60% hemolysis at 25 μmol/L, 90% hemolysis at 500 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21340 FLGALWNVAKRVF 13 [Arg]11-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 25% α-helix in 60% TFE/Water. ## 2%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4562. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=1.6 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=1.6 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.8 μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L), Enterobacter cloacae β-12 (MIC=6.3 μmol/L), Pseudomonas aeruginosa ATCC 27853 (MIC=12.5 μmol/L);##Fungi: Candida albicans MDM8 (MIC=0.8 μmol/L), Candida tropicalis IOC 4560 (MIC=0.8 μmol/L) [Ref.31212183] 25% hemolysis at 6.3 μmol/L, 50% hemolysis at 12.5 μmol/L, 70% hemolysis at 25 μmol/L, 90% hemolysis at 500 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21341 GLGALWNVAKSVF 13 [Gly]1-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 37% α-helix in 60% TFE/Water. ## 2%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4563. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.8 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=25 μmol/L), Bacillus megaterium ATCC 10778 (MIC=3.1 μmol/L), Bacillus subtilis ATCC 6633 (MIC=3.1 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=50 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.4 μmol/L);##Fungi: Candida albicans MDM8 (MIC=25 μmol/L), Candida tropicalis IOC 4560 (MIC=6.3 μmol/L) [Ref.31212183] 10% hemolysis at 50 μmol/L, 30% hemolysis at 100 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21342 FLGALWNPAKSVF 13 [Pro]8-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 12% α-helix in 60% TFE/Water. ## 2%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida tropicalis IOC 4564. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=12.5 μmol/L), Bacillus subtilis ATCC 6633 (MIC=50 μmol/L);##Gram-negative bacteria: Serratia marcescens ATCC 4112 (MIC=12.5 μmol/L);##Fungi: Candida tropicalis IOC 4560 (MIC=50 μmol/L) [Ref.31212183] 0% hemolysis at 100 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21343 FLGALWNVLKSVF 13 [Leu]9-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 62% α-helix in 60% TFE/Water. ## 3%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4565. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=3.1 μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=0.8 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.4 μmol/L), Pseudomonas aeruginosa ATCC 27853 (MIC=50 μmol/L);##Fungi: Candida albicans MDM8 (MIC=1.6 μmol/L), Candida tropicalis IOC 4560 (MIC=1.6 μmol/L) [Ref.31212183] 20% hemolysis at 3.1 μmol/L, 70% hemolysis at 25 μmol/L, 100% hemolysis at 100 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21344 FLGALWNVFKSVF 13 [Phe]9-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 32% α-helix in 60% TFE/Water. ## 1%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4566. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.2 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=1.6 μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L);##Fungi: Candida albicans MDM8 (MIC=6.3 μmol/L), Candida tropicalis IOC 4560 (MIC=0.8 μmol/L) [Ref.31212183] 10% hemolysis at 1.6 μmol/L, 40% hemolysis at 3.1 μmol/L, 60% hemolysis at 6.3 μmol/L, 85% hemolysis at 25 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21345 FLGALWNVAKSLF 13 [Leu]12-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 23% α-helix in 60% TFE/Water. ## 2%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4567. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=1.6μmol/L), Bacillus subtilis ATCC 6633 (MIC=0.8 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=0.8 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.4 μmol/L), Enterobacter cloacae β-12 (MIC=6.3 μmol/L), Pseudomonas aeruginosa ATCC 27853 (MIC=50 μmol/L);##Fungi: Candida albicans MDM8 (MIC=3.1 μmol/L), Candida tropicalis IOC 4560 (MIC=1.6 μmol/L) [Ref.31212183] 20% hemolysis at 6.3 μmol/L, 60% hemolysis at 12.5 μmol/L, 75% hemolysis at 25 μmol/L, 90% hemolysis at 50 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21346 FLGALWNVAKSYF 13 [Tyr]12-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 24% α-helix in 60% TFE/Water. ## 2%α-helix in water. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans and Candida tropicalis IOC 4568. [Ref.31212183] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.8 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=1.6 μmol/L), Bacillus megaterium ATCC 10778 (MIC=1.6 μmol/L), Bacillus subtilis ATCC 6633 (MIC=1.6 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=6.3 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L);##Fungi: Candida albicans MDM8 (MIC=12.5 μmol/L), Candida tropicalis IOC 4560 (MIC=6.3 μmol/L) [Ref.31212183] 25% hemolysis at 12.5 μmol/L, 60% hemolysis at 25 μmol/L, 85% hemolysis at 50 μmol/L, 100% hemolysis at 100 μmol/L for human red blood cells Linear Free Amidation L [Ref.31212183] No cytotoxicity information found Not found 31212183 Bioorg Chem. 2019 Jun 8;90:103038. doi: 10.1016/j.bioorg.2019.103038. Pedron CN, Araújo I, da Silva Junior PI, Dias da Silva F, Torres MT, Oliveira Junior VX Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens DRAMP21347 IHHIHHH 7 2IH1 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 18% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC>64μM), Escherichia coli UB1005 (MIC>64μM), Escherichia coli K88 (MIC>64μM), Escherichia coli K99 (MIC>64μM), Escherichia coli 078 (MIC>64μM), Escherichia coli 987P (MIC>64μM), Pseudomonas aeruginosa 27853 (MIC>64μM), Pseudomonas aeruginosa PAO1 (MIC>64μM), Salmonella typhimurium 14028 (MIC>64μM), Salmonella typhimurium 7731 (MIC>64μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 2IH1 is 103.6%, 102.2%, 101.7%, 103.9%, 103.6%, 106.1% and 103.3% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 2IH1 is 107.9%, 104.5%, 103.4%, 102.5%, 101.1%, 105.6% and 102.0% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21348 IHHIHHHIHHIHHH 14 2IH2 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=64μM), Escherichia coli UB1005 (MIC=64μM), Escherichia coli K88 (MIC>64μM), Escherichia coli K99 (MIC=64μM), Escherichia coli 078 (MIC>64μM), Escherichia coli 987P (MIC=64μM), Pseudomonas aeruginosa 27853 (MIC=8μM), Pseudomonas aeruginosa PAO1 (MIC=64μM), Salmonella typhimurium 14028 (MIC>64μM), Salmonella typhimurium 7731 (MIC>64μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 2IH2 is 104.7%, 104.7%, 102.8%, 103.6%, 105.3%, 102.2% and 102.5% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 2IH2 is 105.1%, 104.8%, 103.7%, 104.2%, 104.2%, 105.6%, 104.2% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21349 IHHIHHHIHHIHHHIHHIHHH 21 2IH3 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=2μM), Escherichia coli UB1005 (MIC=2μM), Escherichia coli K88 (MIC=2μM), Escherichia coli K99 (MIC=2μM), Escherichia coli 078 (MIC=4μM), Escherichia coli 987P (MIC=2μM), Pseudomonas aeruginosa 27853 (MIC=0.5μM), Pseudomonas aeruginosa PAO1 (MIC=1μM), Salmonella typhimurium 14028 (MIC=16>64μM), Salmonella typhimurium 7731 (MIC=8μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 2IH3 is 108.3%, 102.8%, 104.4%, 102.2%, 105%, 105.3% and 103.3% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 2IH3 is 102.5%, 104.5%, 105.6%, 103.7%, 102.0%, 103.1% and 103.1% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21350 IHHIHHHIHHIHHHIHHIHHHIHHIHHH 28 2IH4 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=1μM), Escherichia coli UB1005 (MIC=2μM), Escherichia coli K88 (MIC=4>64μM), Escherichia coli K99 (MIC=1μM), Escherichia coli 078 (MIC=4>64μM), Escherichia coli 987P (MIC=1μM), Pseudomonas aeruginosa 27853 (MIC=1μM), Pseudomonas aeruginosa PAO1 (MIC=1μM), Salmonella typhimurium 14028 (MIC=64μM), Salmonella typhimurium 7731 (MIC>64μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 2IH4 is at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 2IH4 is 103.7%, 103.7%, 104.8%, 103.4%, 105.3%, 94.9% and 57.9% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21351 IHHIHHI 7 3IH1 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 53% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC>64μM), Escherichia coli UB1005 (MIC>64μM), Escherichia coli K88 (MIC>64μM), Escherichia coli K99 (MIC>64μM), Escherichia coli 078 (MIC>64μM), Escherichia coli 987P (MIC>64μM), Pseudomonas aeruginosa 27853 (MIC>64μM), Pseudomonas aeruginosa PAO1 (MIC>64μM), Salmonella typhimurium 14028 (MIC>64μM), Salmonella typhimurium 7731 (MIC>64μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 3IH1 is 105.6%, 101.1%, 100.6%, 102.5%, 100.3%, 101.4% and 101.1% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 3IH1 is 102.2%, 103.1%, 102.0%, 103.4%, 103.1%, 102.0% and 101.7% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21352 IHHIHHIIHHIHHI 14 3IH2 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=4μM), Escherichia coli UB1005 (MIC=8μM), Escherichia coli K88 (MIC=4μM), Escherichia coli K99 (MIC=4μM), Escherichia coli 078 (MIC=8μM), Escherichia coli 987P (MIC=2μM), Pseudomonas aeruginosa 27853 (MIC=4μM), Pseudomonas aeruginosa PAO1 (MIC=4μM), Salmonella typhimurium 14028 (MIC=32μM), Salmonella typhimurium 7731 (MIC=16μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 3IH2 is 105.8%, 105.8%, 105.2%, 104.2%, 101.1%, 101.7% and 100.8% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 3IH2 is 106.2%, 105.9%, 105.9%, 105.6%, 104.2%, 104.8% and 101.4% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21353 IHHIHHIIHHIHHIIHHIHHI 21 3IH3 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=1μM), Escherichia coli UB1005 (MIC=1μM), Escherichia coli K88 (MIC=1μM), Escherichia coli K99 (MIC=1μM), Escherichia coli 078 (MIC=0.5μM), Escherichia coli 987P (MIC=0.5μM), Pseudomonas aeruginosa 27853 (MIC=1μM), Pseudomonas aeruginosa PAO1 (MIC=0.5μM), Salmonella typhimurium 14028 (MIC=2μM), Salmonella typhimurium 7731 (MIC=1μM) [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 3IH3 is 103.6%, 102.2%, 102.8%, 105%, 103.1%, 104.2% and 105.8% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 3IH3 is 103.9%, 103.1%, 103.9%, 102.2%, 104.2%, 103.1% and 101.7% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21354 IHHIHHIIHHIHHIIHHIHHIIHHIHHI 28 3IH4 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form 95% α-helix in 50% TFE/H2O The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=2μM), Escherichia coli UB1005 (MIC=4μM), Escherichia coli K88 (MIC=2μM), Escherichia coli K99 (MIC=4μM), Escherichia coli 078 (MIC=4μM), Escherichia coli 987P (MIC=4μM), Pseudomonas aeruginosa 27853 (MIC=8μM), Pseudomonas aeruginosa PAO1 (MIC=4μM), Salmonella typhimurium 14028 (MIC>64μM), Salmonella typhimurium 7731 (MIC>64μM) [Ref.31199117] 8% hemolysis at 63μM, 15% hemolysis at 128μM against human red blood cells Linear Free Amidation L [Ref.31199117] ①The cell viability of HEK293T cells induced by 3IH4 is 106.9%, 101.1%, 101.9%, 103.6%, 102.5%, 101.7% and 80.6% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 3IH4 is 104.2%, 105.3, 104.2%, 104.2%, 101.4%, 100.6%, 56.5% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM. Not found 31199117 ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14. Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L. Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition DRAMP21355 KKKKKAAFAKAWAAFAA 17 5Kamp (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=6.3μM), Pseudomonas aeruginosa PAO1(MIC=25μM), Pseudomonas aeruginosa PA214(MIC=25μM), Pseudomonas aeruginosa PA287(MIC=50μM), Pseudomonas aeruginosa PA330(MIC=50μM), Pseudomonas aeruginosa PA380(MIC=50μM) [Ref.31194548] 0% hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21356 KKKKAAFAKAWAKAFAA 17 4Kamp (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=12.5μM), Pseudomonas aeruginosa PAO1(MIC=50μM), Pseudomonas aeruginosa PA214(MIC=50μM), Pseudomonas aeruginosa PA287(MIC>50μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC=50μM) [Ref.31194548] 0% hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21357 KKKAAFAKAWAKAFKAA 17 3Kamp (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=25μM), Pseudomonas aeruginosa PAO1(MIC=50μM), Pseudomonas aeruginosa PA214(MIC=50μM), Pseudomonas aeruginosa PA287(MIC>50μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 0% hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21358 KKAKAFAKAWAKAFKAA 17 2Kamp (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=12.5μM), Pseudomonas aeruginosa PAO1(MIC=25μM), Pseudomonas aeruginosa PA214(MIC=50μM), Pseudomonas aeruginosa PA287(MIC=50μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 0% hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21359 KAAKKFAKAWAKAFKAA 17 1Kamp (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=12.5μM), Pseudomonas aeruginosa PAO1(MIC=50μM), Pseudomonas aeruginosa PA214(MIC>50μM), Pseudomonas aeruginosa PA287(MIC>50μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 0% hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21360 KKKKKKALFALWLAFLA 17 6K-F17-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=12.5μM), Pseudomonas aeruginosa PAO1(MIC>50μM), Pseudomonas aeruginosa PA214(MIC=50μM), Pseudomonas aeruginosa PA287(MIC=25μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 33% (± 22) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21361 KKKKKALFLKLWAAFLA 17 5Kamp-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=3.1μM), Pseudomonas aeruginosa PAO1(MIC=12.5μM), Pseudomonas aeruginosa PA214(MIC=6.3μM), Pseudomonas aeruginosa PA287(MIC=6.3μM), Pseudomonas aeruginosa PA330(MIC=12.5μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 49% (± 22) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21362 KKKKAAFLKLWLKLFAA 17 4Kamp-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=12.5μM), Pseudomonas aeruginosa PAO1(MIC>50μM), Pseudomonas aeruginosa PA214(MIC>50μM), Pseudomonas aeruginosa PA287(MIC>50μM), Pseudomonas aeruginosa PA330(MIC>50μM), Pseudomonas aeruginosa PA380(MIC>50μM) [Ref.31194548] 8% (± 2.0) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21363 KKKAAFLKLWAKLFKAL 17 3Kamp-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=3.1μM), Pseudomonas aeruginosa PAO1(MIC=3.1μM), Pseudomonas aeruginosa PA214(MIC=3.1μM), Pseudomonas aeruginosa PA287(MIC=3.1μM), Pseudomonas aeruginosa PA330(MIC=6.3μM), Pseudomonas aeruginosa PA380(MIC=3.1μM) [Ref.31194548] 100% (± 4.5) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21364 KKLKAFLKAWAKLFKAL 17 2Kamp-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=1.6μM), Pseudomonas aeruginosa PAO1(MIC=3.1μM), Pseudomonas aeruginosa PA214(MIC=3.1μM), Pseudomonas aeruginosa PA287(MIC=3.1μM), Pseudomonas aeruginosa PA330(MIC=6.3μM), Pseudomonas aeruginosa PA380(MIC=1.5μM) [Ref.31194548] 89% (± 7.3) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21365 KALKKFLKAWAKLFKAL 17 1Kamp-4L (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly in 10 mM Tris buffer 10 Mm NaCl pH 7.4, supplemented with either 2 mg/ml E.coli or POPC lipid extract. Peptides are shown as ideal helices with side chains shown as stick models for Lys, Trp, and Phe and as space-filling models. Function: Antibacterial activity against Gram-negative bacteria. [Ref.31194548] Gram-negative Bacteria: Escherichia coli K12 (MIC=1.6μM), Pseudomonas aeruginosa PAO1(MIC=3.1μM), Pseudomonas aeruginosa PA214(MIC=3.1μM), Pseudomonas aeruginosa PA287(MIC=3.1μM), Pseudomonas aeruginosa PA330(MIC=6.3μM), Pseudomonas aeruginosa PA380(MIC=6.3μM) [Ref.31194548] 81% (± 9.4) hemolysis at 40μM against human blood cells. Linear Free Amidation L [Ref.31194548] No cytotoxicity information found Not found 31194548 J Med Chem. 2019 Jul 1. doi: 10.1021/acs.jmedchem.9b00657. Stone TA, Cole GB, Ravamehr-Lake D, Nguyen HQ, Khan F, Sharpe S, Deber CM Positive Charge Patterning and Hydrophobicity of Membrane-Active Antimicrobial Peptides as Determinants of Activity, Toxicity, and Pharmacokinetic Stability DRAMP21366 KLGALWNVAKSVF 13 [Lys]1-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 3% Helical content in water, 2% helical content in PBS (pH7.4), 30% helical content in SDS (20 mmol/L), 32% helical content in TFE/Water (3:2, v:v), 4 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=25 μmol/L), Bacillus megaterium ATCC 10778 (MIC=3.1 μmol/L);##Gram-negative bacteria: Serratia marcescens ATCC 4112 (MIC=1.6 μmol/L), Enterobacter cloacae β-12 (MIC=25 μmol/L);##Fungi: Candida albicans MDM8 (MIC=3.1 μmol/L), Candida tropicalis IOC 4560 (MIC=0.8 μmol/L) [Ref.31181304] 15% hemolysis at 25 μmol/L, 25% hemolysis at 50 μmol/L, 40% hemolysis at 100 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] The cell viability of MCF-7 cells induced by [Lys1]-VmCT1-NH2 is 120%, 120%, 120%, 110%, 120%, 120%, 115% and 115% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21367 FLGALWNVKKSVF 13 [Lys]9-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Antifungal Synthetic form 2% Helical content in water, 3% helical content in PBS (pH7.4), 21% helical content in SDS (20 mmol/L), 21% helical content in TFE/Water (3:2, v:v), 3 Not found Function: Antibacterial activity against Gram-positive bacteria. Antifungal activity against Candida albicans MDM8. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L);##Fungi: Candida albicans MDM8 (MIC=50 μmol/L) [Ref.31181304] 0% hemolysis at 100 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] The cell viability of MCF-7 cells induced by [Lys9]-VmCT1-NH2 is 120%, 120%, 105%, 110%, 110%, 108%, 120% and 120% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21368 KLGALWNVAKSKF 13 [Lys]1[Lys]12-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 2% Helical content in water, 0% helical content in PBS (pH7.4), 19% helical content in SDS (20 mmol/L), 13% helical content in TFE/Water (3:2, v:v), 0 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=12.5 μmol/L), Bacillus megaterium ATCC 10778 (MIC=6.3 μmol/L);##Gram-negative bacteria: Enterobacter cloacae β-12 (MIC=25μmol/L);##Fungi: Candida albicans MDM8 (MIC=6.3 μmol/L), Candida tropicalis IOC 4560 (MIC=3.1 μmol/L) [Ref.31181304] 0% hemolysis at 100 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] The cell viability of MCF-7 cells induced by [Lys1][Lys12]-VmCT1-NH2 is 105%, 110%, 95%, 100%, 110%, 120%, 120% and 120% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21369 FLKALWKVAKSVF 13 [Lys]3[Lys]7-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 0% Helical content in water, 5% helical content in PBS (pH7.4), 37% helical content in SDS (20 mmol/L), 52% helical content in TFE/Water (3:1, v:v), 0 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.4 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.4 μmol/L), Staphylococcus epidermidis ATCC 12228 (MIC=3.1 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.1 μmol/L), Enterobacter cloacae β-12 (MIC=3.1 μmol/L);##Fungi: Candida albicans MDM8 (MIC=0.8 μmol/L), Candida tropicalis IOC 4560 (MIC=0.4 μmol/L) [Ref.31181304] 15% hemolysis at 3.1 μmol/L, 45% hemolysis at 6.3 μmol/L, 65% hemolysis at 12.5 μmol/L, 85% hemolysis at 25 μmol/L, 90% hemolysis at 100 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] ①The cell viability of MCF-7 cells induced by [Lys3][Lys7]-VmCT1-NH2 is 95%, 95%, 90%, 85%, 80%, 70%, 50%, 40% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. ②The cell viability of MCF-10A cells induced by [Lys3][Lys7]-VmCT1-NH2 is 120%, 120%, 120%,120%, 95% and 90% at peptide concentrations of 0.8, 1.6, 3.1, 6.3, 12.5 and 25 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21370 FLKALWNVAKKVF 13 [Lys]3[Lys]11-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 0% Helical content in water, 4% helical content in PBS (pH7.4), 28% helical content in SDS (20 mmol/L), 33% helical content in TFE/Water (3:2, v:v), 2 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.4 μmol/L), Staphylococcus epidermidis ATCC 12228 (MIC=1.6 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L), Enterobacter cloacae β-12 (MIC=3.1 μmol/L);##Fungi: Candida albicans MDM8 (MIC=1.6 μmol/L), Candida tropicalis IOC 4560 (MIC=0.4 μmol/L) [Ref.31181304] 40% hemolysis at 12.5 μmol/L, 70% hemolysis at 25 μmol/L, 80% hemolysis at 50 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] ①The cell viability of MCF-7 cells induced by [Lys3][Lys11]-VmCT1-NH2 is 95%, 100%, 80%, 80%, 55%, 45%, 20% and 20% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. ②The cell viability of MCF-10A cells induced by [Lys3][Lys11]-VmCT1-NH2 is 120%, 120%, 90%, 100%, 120% and 95% at peptide concentrations of 0.8, 1.6, 3.1, 6.3, 12.5 and 25 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21371 FLGALWKVAKKVF 13 [Lys]7[Lys]11-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 0% Helical content in water, 3% helical content in PBS (pH7.4), 27% helical content in SDS (20 mmol/L), 39% helical content in TFE/Water (3:2, v:v), 1 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.4 μmol/L), Staphylococcus epidermidis ATCC 12228 (MIC=6.3 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=3.1 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.2 μmol/L), Enterobacter cloacae β-12 (MIC=3.1 μmol/L);##Fungi: Candida albicans MDM8 (MIC=1.6 μmol/L), Candida tropicalis IOC 4560 (MIC=0.4μmol/L) [Ref.31181304] 45% hemolysis at 12.5 μmol/L, 100% hemolysis at 50 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] ①The cell viability of MCF-7 cells induced by [Lys7][Lys11]-VmCT1-NH2 is 105%, 105%, 95%, 85%, 65%, 45%, 25% and 25% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. ②The cell viability of MCF-10A cells induced by [Lys7][Lys11]-VmCT1-NH2 is 120%, 120%, 85%, 90%, 120% and 120%at peptide concentrations of 0.8, 1.6, 3.1, 6.3, 12.5 and 25 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21372 FLKALWKVAKKVF 13 [Lys]3[Lys]7[Lys]11-VmCT1-NH2 (Derived from VmCT1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form 0% Helical content in water, 3% helical content in PBS (pH7.4), 25% helical content in SDS (20 mmol/L), 23% helical content in TFE/Water (3:2, v:v), 2 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans MDM8 and Candida tropicalis IOC 4560. [Ref.31181304] Gram-positive bacteria: Micrococcus luteus A270 (MIC=0.4 μmol/L), Staphylococcus aureus ATCC 29213 (MIC=0.8 μmol/L), Bacillus megaterium ATCC 10778 (MIC=0.2 μmol/L), Staphylococcus epidermidis ATCC 12228 (MIC=3.1 μmol/L);##Gram-negative bacteria: Escherichia coli SBS 363 (MIC=1.6 μmol/L)，Serratia marcescens ATCC 4112 (MIC=0.1μmol/L), Enterobacter cloacae β-12 (MIC=3.1 μmol/L);##Fungi: Candida albicans MDM8 (MIC=0.8 μmol/L), Candida tropicalis IOC 4560 (MIC=0.4μmol/L) [Ref.31181304] 40% hemolysis at 12.5 μmol/L, 60% hemolysis at 25 μmol/L, 80% hemolysis at 50 μmol/L, 100% hemolysis at 100 μmol/L against human red blood cells Linear Free Amidation L [Ref.31181304] ①The cell viability of MCF-7 cells induced by [Lys3][Lys7][Lys11]-VmCT1-NH2 is 90%, 90%, 90%, 60%, 50%, 30%, 20% and 20% at peptide concentrations of 0.8, 1.6, 3.1, 12.5, 25, 50 and 100 μM. ②The cell viability of MCF-10A cells induced by [Lys3][Lys7][Lys11]-VmCT1-NH2 is 120%, 120%, 85%, 120%, 115% and 120%at peptide concentrations of 0.8, 1.6, 3.1, 6.3, 12.5 and 25 μM. Not found 31181304 Eur J Pharm Sci. 2019 Jun 7;136:104952. doi: 10.1016/j.ejps.2019.06.006. Pedron CN, de Oliveira CS, da Silva AF, Andrade GP, da Silva Pinhal MA, Cerchiaro G, da Silva Junior PI, da Silva FD, Torres MT, Oliveira VX The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1 DRAMP21373 AIKIRKLFKKLLR 13 SP1 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP1 is 87.8%, 88.5%, 83.1%, 95.3%, 97.3% and 68.9% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21374 GIKIRKLFKKLLR 13 SP2 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=6.25–12.5 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP2 is 108.8%, 110.1%, 116.9%, 104.7%, 108.8% and 83.1% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21375 GWAKLITKAIKKI 13 SP3 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=25–50 µg/mL) [Ref.31163671] 10% hemolysis at 50–100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP3 is 80.4%, 77.0%, 87.8%, 98.0%, 76.4% and 84.5% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21376 GIKFFLKKLKKHI 13 SP4 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=25–50 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP4 is 102.0%, 114.2%, 100.7%, 93.2%, 108.1% and 83.1% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21377 IRPAKLRWFKKIK 13 SP5 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC >100 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP5 is 110.8%, 100.7%, 104.7%, 110.1%, 87.8% and 90.5% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21378 RLFIKKLKFITRR 13 SP6 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=25–50 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP6 is 92.6%, 100%, 102.7%, 106.8%, 93.2% and 99.3% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21379 NAMRGAKRVWRHI 13 SP7 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC >100 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP7 is 91.9%, 95.9%, 103.4%, 94.6%, 93.9% and 91.2% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21380 KFRKFGKQVWVRL 13 SP8 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP8 is 98.0%, 104.7%, 98.0%, 103.4%, 93.2%, 92.6% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21381 aikirklfkkllr 13 SP1D * (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at 25–50 μg/mL against human blood cells. Linear Free Amidation D [Ref.31163671] The cell viability of Hepa 1-6 induced by SP1D is 80.4%, 102.0%, 81.8%, 81.8%, 74.3% and 66.2% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21382 KVWSRLRKIFSTR 13 SP9 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=6.25–12.5 µg/mL) [Ref.31163671] 10% hemolysis at 50–100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP9 is 104.7%, 110.8%, 108.8%, 108.8%, 97.3% and 79.1% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21383 AKVLKISRRAFRK 13 SP10 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC >100 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP10 is 114.2%, 82.4%, 94.6%, 98.6%, 103.4% and 98.6% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21384 IRRWRLHWFRRAI 13 SP11 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP11 is 95.3%, 109.5%, 108.1%, 89.2%, 112.8% and 81.1% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21385 IRRRIRLIVRRQI 13 SP12 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP12 is 98.0%, 99.3%, 95.9%, 92.6%, 100% and 89.2% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21386 HFKIRKRFVKKLV 13 SP13 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC >100 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP13 is 104.1%, 106.8%, 111.5%, 101.4%, 107.4%, 118.2% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21387 RWIRWVWRKKLRI 13 SP14 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=12.5–25 µg/mL) [Ref.31163671] 10% hemolysis at 50–100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP14 is 102.7%, 95.3%, 88.5%, 93.9%, 100% and 98.6% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21388 RWIRWVWRKKLR 12 SP15 * (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC= 3.125–6.25 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation L [Ref.31163671] The cell viability of Hepa 1-6 induced by SP15 is 90.5%, 90.5%, 89.2%, 83.1%, 93.2% and 52.7% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21389 rwirwvwrkklr 12 SP15D * (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix mainly Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.31163671] Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=0.78–1.56 µg/mL) [Ref.31163671] 10% hemolysis at >100 μg/mL against human blood cells. Linear Free Amidation D [Ref.31163671] The cell viability of Hepa 1-6 induced by SP15D is 91.2%, 96.6%, 96.6%, 73.6%, 58.1% and 25% at peptide concentrations of 3.125, 6.25, 12.5, 25, 50 and 100 μg/mL. Not found 31163671 Pharmaceuticals (Basel). 2019 Jun 3;12(2). pii: E82. doi: 10.3390/ph12020082. Boris Vishnepolsky, George Zaalishvili, Margarita Karapetian, Tornike Nasrashvili, Nato Kuljanishvili, Andrei Gabrielian, Alex Rosenthal, Darrell E. Hurt, Michael Tartakovsky, Maya Grigolava and Malak Pirtskhalava De Novo Design and In Vitro Testing of Antimicrobial Peptides against Gram-Negative Bacteria. DRAMP21390 RWKRHISEQLRRRDRLQR 18 K17 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=45.5-91 μM);##Gram-negative bacteria: Escherichia coli (MIC>120μM), Pseudomonas aeruginosa (MIC>120μM);##Fungi: Candida albicans (MIC>120μM) [Ref.31145591] 2% hemolysis at 600 μM, 3% hemolysis at 700 μM, 4% hemolysis at 800 μM, 5% hemolysis at 900 μM, 6% hemolysis at 1000 μM, against mouse blood cells. Linear Free Free L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21391 RWKRHISEQLRRRDRLQRQAF 21 K18 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=28.8-57.6 μM);##Gram-negative bacteria: Escherichia coli (MIC=60-120μM), Pseudomonas aeruginosa (MIC=60-120μM);##Fungi: Candida albicans (MIC>120μM) [Ref.31145591] 3% hemolysis at 500μM, 16% hemolysis at 600 μM, 27% hemolysis at 700 μM, 38% hemolysis at 800 μM, 50% hemolysis at 900 μM, 62% hemolysis at 1000μM against mouse blood cells. Linear Free Free L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21392 RWKRHISEQLRRRDRLQRQAJ 21 K22 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=14.4-28.8 μM);##Gram-negative bacteria: Escherichia coli (MIC=30-60μM), Pseudomonas aeruginosa (MIC=60-120μM);##Fungi: Candida albicans (MIC=60-120μM) [Ref.31145591] 3% hemolysis at 500μM, 10% hemolysis at 600 μM, 13% hemolysis at 700 μM, 17% hemolysis at 800 μM, 20% hemolysis at 900 μM, 25% hemolysis at 1000μM against mouse blood cells. Linear Free Free The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21393 RWKRHISEQLRRRDRLQRQAJ 21 K22.2 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=4-8 μM);##Gram-negative bacteria: Escherichia coli (MIC=17.5-35μM), Pseudomonas aeruginosa (MIC=17.5-35μM);##Fungi: Candida albicans (MIC=60-120μM) [Ref.31145591] 3% hemolysis at 500μM, 5% hemolysis at 600 μM, 10% hemolysis at 700 μM, 15% hemolysis at 800 μM, 17% hemolysis at 900 μM, 20% hemolysis at 1000μM against mouse blood cells. Linear Free Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21394 RWKRHISEQLRRRDRLQRQAJ 21 K30 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Helix–loop–helix in the presence of anionic membrane lipids mimicking bacterial membranes. Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=0.9-1.8 μM);##Gram-negative bacteria: Escherichia coli (MIC=6.4-12.8μM), Pseudomonas aeruginosa (MIC=13.5-27μM);##Fungi: Candida albicans (MIC=30-60μM) [Ref.31145591] 3% hemolysis at 600μM, 4% hemolysis at 700 μM, 5% hemolysis at 800 μM, 6% hemolysis at 900 μM, 9% hemolysis at 1000 μM,against mouse blood cells. Linear Acylation (Arg1 conjugated with 4-methylhexanoyl group) Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21395 RWKRHISEQLRRRDRLQRQAJ 21 K31 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=1.8-3.2 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.2-6.4μM), Pseudomonas aeruginosa (MIC=3.2-6.4μM);##Fungi: Candida albicans (MIC=3.2-6.4μM) [Ref.31145591] 50% hemolysis at 10μM, 70% hemolysis at 61μM, 75% hemolysis at 100 μM, 80% hemolysis at 200 μM, 85% hemolysis at 300 μM, 90% hemolysis at 900 μM, 92% hemolysis at 500μM against mouse blood cells. Linear Acylation (Arg1 conjugated with myristoyl group) Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21396 RWKRHISEQLRRRDRLQRQAJ 21 K33 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=1.8-3.2 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.2-6.4μM), Pseudomonas aeruginosa (MIC=6.4-12.8μM);##Fungi: Candida albicans (MIC=1.8-3.7μM) [Ref.31145591] 75% hemolysis at 10μM, 97% hemolysis at 123μM, 100% hemolysis at 500μM against mouse blood cells. Linear Acylation (Arg1 conjugated with palmitoyl group) Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21397 RWKRHISEQLRRRDRLQRQAJ 21 K36 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=0.9-1.8 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.2-6.4μM), Pseudomonas aeruginosa (MIC=6.4-12.8μM);##Fungi: Candida albicans (MIC=15-30μM) [Ref.31145591] 5% hemolysis at 200μM, 10% hemolysis at 300 μM, 17% hemolysis at 400 μM, 23% hemolysis at 500 μM, 30% hemolysis at 600μM, 32% hemolysis at 700 μM, 35% hemolysis at 800 μM, 40% hemolysis at 900 μM, 42% hemolysis at 1000μM against mouse blood cells. Linear Acylation (Arg1 conjugated with Fmoc group) Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21398 RWKRHISEQLRRRDRLQRQAJ 21 K46 (Derived from ATG16) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans. [Ref.31145591] Gram-positive bacteria: Staphylococcus aureus(MIC=1.8-3.2 μM);##Gram-negative bacteria: Escherichia coli (MIC=3.2-6.4μM), Pseudomonas aeruginosa (MIC=6.4-12.8μM);##Fungi: Candida albicans (MIC=30-60μM) [Ref.31145591] 10% hemolysis at 200μM, 15% hemolysis at 500μM, 17% hemolysis at 600 μM, 20% hemolysis at 700 μM, 25% hemolysis at 800 μM, 30% hemolysis at 900 μM, 42% hemolysis at 1000μM against mouse blood cells. Linear Acylation (Arg1 conjugated with capryl group) Amidation (2-Nal, position 21) The 'J' in the sequence is the 2-naphthyl alanine (2-Nal) residue. L [Ref.31145591] No cytotoxicity information found Not found 31145591 Bioconjug Chem. 2019 Jun 18. doi: 10.1021/acs.bioconjchem.9b00290. Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. DRAMP21399 RRYGTCIYQGRLWAF 15 Pep-H (Human, mammals, animals) No entry found Belongs to the alpha-defensin family. Not found Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram+ Not found β-strand mainly (according to PDB entry 3HJ2) Not found Function: Antibacterial activity against Gram-positive bacteria. [Ref.31133658] Gram-positive bacteria:M.tb H37Rv (MIC=10 μg/ml) [Ref.31133658] 2.7% hemolysis at 1μg/ml, 5% hemolysis at 5μg/ml, 6% hemolysis at 50μg/ml, 8% hemolysis at 100 μg/ml against human blood cells. Linear Free Free L [Ref.31133658] The cell viability of MDMs induced by Pep-H is 94.2%, 91.5%, 90.4%, 88.0% and 84.1% at peptide concentrations of 1, 5, 25, 50, 100 μg/mL Not found 31133658 Sci Rep. 2019; 9: 7866. Published online 2019 May 27. doi: 10.1038/s41598-019-44256-6 Richa Sharma， Ragini Raghav, Kumari Priyanka, Praveen Rishi, Sadhna Sharma, Sudha Srivastava, Indu Verma Exploiting chitosan and gold nanoparticles for antimycobacterial activity of in silico identified antimicrobial motif of human neutrophil peptide-1 DRAMP21400 CGIYRSLKLIKSLVLIK 17 NBC2253 (De Novo Synthesis)  No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31119600] Gram-positive bacteria:MRSA(MIC=6.7 ± 0.02µM);##Gram-negative bacteria:Escherichia coli O157:H7(MIC=25 ± 0.03µM) [Ref.31119600] No hemolytic activity against bovine blood cells Linear The sulfhydryl side chain of the cysteine residue was conjugated to AuNC(previously modified with SPDP) via a disulfide bond. Free L [Ref.31119600] The cell viability of Vero ATCC CCL 1-81 cells induced by NBC2253 is 87.8%, 66.4%, 62.2%, 69.1% and 68.8% at peptide concentrations of 1.2, 3.7, 11.1, 33.3 and 100 μM. Not found 31119600 Protein J. 2019 May 22. doi: 10.1007/s10930-019-09840-9. Prada YA, Guzmán F, Ortíz C, Cabanzo R, Torres R, Mejía-Ospino E New Synthetic Peptides Conjugated to Gold Nanoclusters: Antibiotic Activity Against Escherichia coli O157:H7 and Methicillin-Resistant Staphylococcus aureus (MRSA). DRAMP21401 CALKLTKAKRLVRKIGF 17 NBC2254 (De Novo Synthesis)  No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31119600] Gram-positive bacteria:MRSA(MIC=73 ± 0.02µM);##Gram-negative bacteria:Escherichia coli O157:H7(MIC=3.5 ± 0.05µM) [Ref.31119600] No hemolytic activity against bovine blood cells Linear The sulfhydryl side chain of the cysteine residue was conjugated to AuNC(previously modified with SPDP) via a disulfide bond. Free L [Ref.31119600] The cell viability of Vero ATCC CCL 1-81 cells induced by NBC2254 is 93.7%, 90.1%, 89.5%, 95.9% and 78.6% at peptide concentrations of 1.2, 3.7, 11.1, 33.3 and 100 μM. Not found 31119600 Protein J. 2019 May 22. doi: 10.1007/s10930-019-09840-9. Prada YA, Guzmán F, Ortíz C, Cabanzo R, Torres R, Mejía-Ospino E New Synthetic Peptides Conjugated to Gold Nanoclusters: Antibiotic Activity Against Escherichia coli O157:H7 and Methicillin-Resistant Staphylococcus aureus (MRSA). DRAMP21402 KFKKLFKKLSPVFKRIVQRIKDFLR 25 B1 (Derived from LL-37 and BMAP-27) No entry found Belongs to the cathelicidin family. Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form 88 % of the α-helices and 12% of the random coil was predicted using HNN The helicity percentages of the secondary structure of B1 are predicted using HNN Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31118709] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=20μM), Staphylococcus aureus ATCC 33591(MIC=20μM), Staphylococcus aureus ATCC 43300(MIC=20μM), Staphylococcus aureus ATCC BAA-41(MIC=20μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC=20μM), Escherichia coli 35218 (MIC=20μM), Pseudomonas aeruginosa BAA-2114 (MIC=10μM) [Ref.31118709] 0% hemolysis at 10μM, 8% hemolysis at 25μM, 19% hemolysis at 50μM, 23% hemolysis at 75μM, 30% hemolysis at 100μM, 38% hemolysis at 125μM, 40% hemolysis at 150μM, 43% hemolysis at 175μM, 50% hemolysis at 200μM against human blood cells. Linear Free Free L [Ref.31118709] The cell viability of HEK293 mammalian cell line induced by B1 is 87.0%, 67.1%, 52.3%, 54.3%, 50.6% and 50% at peptide concentrations of 10, 20, 40, 60, 80 and 100 μM. Not found 31118709 Infect Drug Resist. 2019; 12: 1035–1045. Published online 2019 Apr 30. doi: 10.2147/IDR.S199473 Yara Al Tall, Ahmad Abualhaijaa, Mohammad Alsaggar, Ammar Almaaytah, Majed Masadeh, and Karem H Alzoub Design and characterization of a new hybrid peptide from LL-37 and BMAP-27 DRAMP21403 ITEVITILLNRLTDRLEK 18 peptide 1 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix mainly in 10 mM phosphate buffer, pH7.4 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31117348] Gram-positive bacteria:Staphylococcus aureus ATCC 6538(MIC>100μM), Bacillus subtilis ATCC 6633(MIC>100μM);##Gram-negative bacteria:Escherichia coli ATCC 15597(MIC>100μM), Pseudomonas aeruginosa (MIC>100μM), Salmonella Typhimurium 6192(MIC>100μM), Klebsiella pneumoniae NCTC 5055(MIC>100μM) [Ref.31117348] 5% hemolysis at 250 μM against human blood cells. Linear Free Free L [Ref.31117348] No cytotoxicity information found Not found 31117348 ACS Infect Dis. 2019 May 30. doi: 10.1021/acsinfecdis.9b00157. Hammond K, Lewis H, Faruqui N, Russell C, Hoogenboom BW, Ryadnov MG Helminth Defense Molecules as Design Templates for Membrane Active Antibiotics. DRAMP21404 ITKVITKLLNRLTKILSK 18 peptide 2 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix mainly in 10 mM phosphate buffer, pH7.4 Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31117348] Gram-positive bacteria:Staphylococcus aureus ATCC 6538(MIC=15 ± 2.5μM), Bacillus subtilis ATCC 6633(MIC=15 ± 2.5μM);##Gram-negative bacteria:Escherichia coli ATCC 15597(MIC=3.1μM), Pseudomonas aeruginosa (MIC=25μM), Salmonella Typhimurium 6192(MIC=40 ± 5μM), Klebsiella pneumoniae NCTC 5055(MIC=50μM) [Ref.31117348] 5% hemolysis at 250 μM against human blood cells. Linear Free Free L [Ref.31117348] ①The cell viability of MCF7 cells induced by peptide 2 is 94.2%, 88.6%, 82.0%, 55.0%, 44.0%, 32.4%, 15.3%, 15.8%, 12.8% and 1.2% at peptide concentrations of 1, 10, 15, 20, 25, 30, 35, 40, 50 and 100 μM. EC50=22.5±0.7 μM. ②The cell viability of Hela cells induced by peptide 2 is 96.1%, 95.4%, 83.8%, 64.2%, 57.7%, 49.5%, 31.5%, 30.2%, 7.8% and 0.2% at peptide concentrations of 1, 10, 15, 20, 25, 30, 35, 40, 50 and 100 μM. EC50=29.8±1 μM. ③The cell viabiity of HDF cells induced by peptide 2 is 96.3%, 89.7%, 89.9%, 92.7%, 95.0%, 93.4%, 93.1%, 96.1%, 88.6% and 67.4% at peptide concentrations of 1, 10, 15, 20, 25, 30, 35, 40, 50 and 100 μM. Not found 31117348 ACS Infect Dis. 2019 May 30. doi: 10.1021/acsinfecdis.9b00157. Hammond K, Lewis H, Faruqui N, Russell C, Hoogenboom BW, Ryadnov MG Helminth Defense Molecules as Design Templates for Membrane Active Antibiotics. DRAMP21405 GKIIKLKASLKLL 13 LGL13K (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31071184] Gram-positive bacteria:Staphylococcus aureus Xen36(MIC=83.3μg/ml), Staphylococcus aureus USA300(Uknow);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=10.4μg/ml) [Ref.31071184] LD50=560μg/ml against human blood cells Linear Free Amidation L [Ref.31071184] The cytotoxicity of L-GL13K on HEK cells is 2.1%, 3.3%, 2.4%, 1.2%24.3%, 51.7% and 73.6% at peptide concentrations of 1, 3.9, 15.6, 62.5, 250 and 1000 μg/mL, while the cytotoxicity of PMX on HEK cells (Control samples) is 1.2%, 1.2%, 6.6%, 3.6%, 39.6%, 47.1% and 68.5% at peptide concentrations of 1, 3.9, 15.6, 62.5, 250 and 1000 μg/mL. Not found 31071184 PLoS One. 2019 May 9;14(5):e0216669. doi: 10.1371/journal.pone.0216669. eCollection 2019. Gorr SU, Flory CM, Schumacher RJ In vivo activity and low toxicity of the second-generation antimicrobial peptide DGL13K. DRAMP21406 Gkiiklkaslkll 13 DGL13K (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31071184] Gram-positive bacteria:Staphylococcus aureus Xen36(MIC=2.6μg/ml), Staphylococcus aureus USA300(MIC=5.2μg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa (MIC=5.2μg/ml) [Ref.31071184] LD50=950μg/ml against human blood cells Linear Free Amidation Mixed (L-Gly1) [Ref.31071184] The cytotoxicity of D-GL13K on HEK cells is 1.5%, 0.9%, 2.1%, 1.5%, 34.2%, 32.4% and 41.1% at peptide concentrations of 1, 3.9, 15.6, 62.5, 250 and 1000 μg/mL, while the cytotoxicity of PMX on HEK cells (Control samples) is 1.2%, 1.2%, 6.6%, 3.6%, 39.6%, 47.1% and 68.5% at peptide concentrations of 1, 3.9, 15.6, 62.5, 250 and 1000 μg/mL. Not found 31071184 PLoS One. 2019 May 9;14(5):e0216669. doi: 10.1371/journal.pone.0216669. eCollection 2019. Gorr SU, Flory CM, Schumacher RJ In vivo activity and low toxicity of the second-generation antimicrobial peptide DGL13K. DRAMP21407 KLCKIVVIKVCK 12 Bac4K (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC>64μM), Staphylococcus epidermidis (MIC=32μM), Bacillus subtilis (MIC>64μM), Enterococcus faecalis (MIC>64μM);##Gram-negative bacteria: Escherichia coli (MIC=8μM), Salmonella typhimurium (MIC>64μM), Pseudomonas aeruginosa (MIC>64μM), Acinetobacter baumannii (MIC>64μM) [Ref.31056261] 0.6% hemolysis at 100 μM against human red blood cells. Cyclic Free Free Disulfide bond between Cys3 and Cys11. L [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21408 RLCRIWWIRWCR 12 Bac3W (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC=16μM), Staphylococcus epidermidis (MIC=8μM), Bacillus subtilis (MIC=32μM), Enterococcus faecalis (MIC=32μM);##Gram-negative bacteria: Escherichia coli (MIC=2-4 μM), Salmonella typhimurium (MIC=8 μM), Pseudomonas aeruginosa (MIC=4μM), Acinetobacter baumannii (MIC=16-32μM) [Ref.31056261] 0.9% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. L [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21409 ricrivvirvcr 12 dBac (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC=16μM), Staphylococcus epidermidis (MIC=4-8μM), Bacillus subtilis (MIC=16μM), Enterococcus faecalis (MIC>64μM);##Gram-negative bacteria: Escherichia coli (MIC=4-8μM), Salmonella typhimurium (MIC=32-64μM), Pseudomonas aeruginosa (MIC>64μM), Acinetobacter baumannii (MIC>64μM) [Ref.31056261] 0.7% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. D [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21410 klckivvikvck 12 dBac4K (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC>64μM), Staphylococcus epidermidis (MIC=8-16μM), Bacillus subtilis (MIC>64μM), Enterococcus faecalis (MIC>64μM);##Gram-negative bacteria: Escherichia coli (MIC=4-8μM), Salmonella typhimurium (MIC=32-64μM), Pseudomonas aeruginosa (MIC>64μM), Acinetobacter baumannii (MIC>64μM) [Ref.31056261] 0.7% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. D [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21411 ricriwwirwcr 12 dBac3W (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC=16μM), Staphylococcus epidermidis (MIC=16μM), Bacillus subtilis (MIC=32μM), Enterococcus faecalis (MIC=16-32μM);##Gram-negative bacteria: Escherichia coli (MIC=4-8μM), Salmonella typhimurium (MIC=4-8μM), Pseudomonas aeruginosa (MIC=4-8μM), Acinetobacter baumannii (MIC=32μM) [Ref.31056261] 1.0% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. D [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21412 rkcrivvirvcr 12 dBacK (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC=4-8μM), Staphylococcus epidermidis (MIC=1-2μM), Bacillus subtilis (MIC=1-2μM), Enterococcus faecalis (MIC=4μM);##Gram-negative bacteria: Escherichia coli (MIC=1-2μM), Salmonella typhimurium (MIC=1-2μM), Pseudomonas aeruginosa (MIC=2-4μM), Acinetobacter baumannii (MIC=2-4μM) [Ref.31056261] 0.6% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. D [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21413 rkcrivvirvcr 12 dBacK- (cap) (Derived from CAMPs) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form β-turn Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.31056261] Gram-positive bacteria: Staphylococcus aureus (MIC=1-2μM), Staphylococcus epidermidis (MIC=2μM), Bacillus subtilis (MIC=2μM), Enterococcus faecalis (MIC=4-8μM);##Gram-negative bacteria: Escherichia coli (MIC=2-4μM), Salmonella typhimurium (MIC=2-4μM), Pseudomonas aeruginosa (MIC=4-8μM), Acinetobacter baumannii (MIC=1-2μM) [Ref.31056261] 2.1% hemolysis at 100 μM against human red blood cells Cyclic Free Free Disulfide bond between Cys3 and Cys11. The lysine side-chain residue at position 2(Lys2) is conjugated to the capric acid D [Ref.31056261] No cytotoxicity information found Not found 31056261 Biochem Biophys Res Commun. 2019 Jun 25;514(2):497-502. doi: 10.1016/j.bbrc.2019.04.153. Epub 2019 May 2 Sim JY, Kim S, Lee J, Lim H, Kim HH, Park ZY, Kim JI A significantly enhanced antibacterial spectrum of D-enantiomeric lipopeptide bactenecin. DRAMP21414 RWKIFKKIEKMGRNIRDGIVKAGPAIQVLGSAKAI 35 CecB Q53 (Derived from CecB E53) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Random coil in aqueous solution and amphipathic helix upon interaction with cell membranes Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. Antifungal activity against Candida albicans ATCC 1023. [Ref.31045339] Gram-positive bacteria: Staphylococcus aureus ATCC BAA-44(MIC>20μM), Staphylococcus epidermidis ATCC 700565(MIC=8μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.15μM), Pseudomonas aeruginosa ATCC 27853(MIC=2.2μM), Pseudomonas aeruginosa ATCC 25668(MIC=2.2μM);##Fungi:Candida albicans ATCC 1023(MIC>20μM) [Ref.31045339] 0.1% hemolysis at 20μM, 0.5% hemolysis at 30μM, 0.5% hemolysis at 200μM against human red blood cells Linear Free Amidation L [Ref.31045339] ①The cell viability of Hela cells induced by CecB Q53 is 102.6%, 104.0%, 99.1% and 95.6% at peptide concentrations of 10, 20, 30 and 200 μM. ②The cell viability of CCD cells induced by CecB Q53 is 108.4%, 111.5%, 108.8% and 88.5% at peptide concentrations of 10, 20, 30 and 200 μM. Not found 31045339 ACS Infect Dis. 2019 May 10. doi: 10.1021/acsinfecdis.9b00042. Romoli O, Mukherjee S, Mohid SA, Dutta A, Montali A, Franzolin E, Brady D, Zito F, Bergantino E, Rampazzo C, Tettamanti G, Bhunia A, Sandrelli F Enhanced Silkworm Cecropin B Antimicrobial Activity against Pseudomonas aeruginosa from Single Amino Acid Variation. DRAMP21415 LKKWWKTSKGLLGGLLGKVTSVIK 24 α4-short (Derived from α4) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30967458] Gram-positive bacteria: Staphylococcus aureus 467-1 (MIC=2μM), Staphylococcus aureus 0154-17 (MIC=2μM), Staphylococcus aureus 187-10 (MIC=16μM), Staphylococcus aureus 0194-19 (MIC=2μM), Staphylococcus aureus US300 (MIC=8μM), Staphylococcus aureus 122-12 (MIC=2μM), Enterococcus faecium 23614 (MIC=1μM), Enterococcus faecium 14678 (MIC=1μM), Enterococcus faecium 26125 (MIC=1μM);##Gram-negative bacteria:Pseudomonas aeruginosa 16-21 (MIC=2μM), Pseudomonas aeruginosa 16-72 (MIC=2μM), Pseudomonas aeruginosa 16-73 (MIC=2μM), Pseudomonas aeruginosa 0038-13 (MIC=2μM), Pseudomonas aeruginosa 0038-14 (MIC=1μM), Pseudomonas aeruginosa 0040-21 (MIC=2μM), Pseudomonas aeruginosa 0046-106 (MIC=8μM), Pseudomonas aeruginosa 0068-37 (MIC=16μM), Pseudomonas aeruginosa 0071-75 (MIC=2μM), Pseudomonas aeruginosa 97-5 (MIC=2μM), Pseudomonas aeruginosa 109-10 (MIC=2μM), Pseudomonas aeruginosa 16-21 (MIC=2μM)Pseudomonas aeruginosa 132-37 (MIC=2μM), Pseudomonas aeruginosa 129-5 (MIC=2μM), Pseudomonas aeruginosa 152-19 (MIC=2μM), Pseudomonas aeruginosa 159-30 (MIC=2μM), Pseudomonas aeruginosa 474-1 (MIC=2μM), Acinetobacter baumannii C3 (MIC=1μM), Acinetobacter baumannii D4 (MIC=2μM), Acinetobacter baumannii A2 (MIC=4μM), Escherichia coli YDC518 (MIC=1μM), Escherichia coli YDC575 (MIC=2μM), Escherichia coli YDC596 (MIC=1μM), Escherichia coli YDC107 (MIC=1μM), Escherichia coli YDC337 (MIC=1μM), Escherichia coli YDC748 (MIC=1μM), Klebsiella pneumoniae A2 (MIC=4μM), Klebsiella pneumoniae D4 (MIC=2μM), Klebsiella pneumoniae 438-16 (MIC=4μM) [Ref.30967458] 1% hemolysis at 17 μM, 2% hemolysis at 30 μM, 3% hemolysis at 63 μM against human red blood cells Linear Free Free L [Ref.30967458] The white blood cell toxicity of α4-short is ~0%, ~0%, ~0%, ~0%, ~0%, 1.8% and 3.1% at peptide concentrations of 1, 2, 4, 8, 16, 32 and 64 μM. Not found 30967458 mBio. 2019 Mar-Apr; 10(2): e00226-19. Published online 2019 Apr 9. doi: 10.1128/mBio.00226-19 Shasha Jiang, Berthony Deslouches, Chen Chen, Matthew E. Di, Y. Peter Di Antibacterial Properties and Efficacy of a Novel SPLUNC1-Derived Antimicrobial Peptide, α6-Short, in a Murine Model of Respiratory Infection DRAMP21416 WVKAAAKAAAKVW 13 WV (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-TASSER, random coil in PBS, α-helix in SDS Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30897850] Gram-positive bacteria:Staphylococcus aureus ATCC 27853(MIC>128μM), Staphylococcus epidermidis ATCC 12228(MIC>128μM), Staphylococcus faecalis ATCC 29212(MIC=64μM), Bacillus subtilis CMCC 63501(MIC>128μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=32μM), Escherichia coli UB 1005 (MIC>128μM), Pseudomonas aeruginosa ATCC 27853(MIC>128μM), Salmonella typhimurium ATCC 14028(MIC>128μM) [Ref.30897850] 1.5% hemolysis at 256μM against human red blood cells Linear Free Amidaton L [Ref.30897850] ①The cell viability of RAW 264.7 induced by WV is 102.5%, 93.5%, 97.8%, 95.7%, 99.3%, 99.6%, 93.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on RAW 264.7 cells (Control samples) is 93.1%, 67.8%, 37.7%, 17.8%, 0%, 1.4% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM.②The cell viability of HEK293T induced by WV is 115.2%, 104.3%, 114.5%, 107.6%, 105.8%, 108.0% and 93.8% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on HEK293T cells (Control samples) is 101.4%, 80.1%, 31.9%, 1.4%, 1.4%, 1.8% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM. Not found 30897850 Int J Mol Sci. 2019 Mar; 20(6): 1417. Published online 2019 Mar 20. doi: 10.3390/ijms20061417 Changxuan Shao, Weizhong Li, Peng Tan, Anshan Shan, Xiujing Dou, Deying Ma, Chunyu Liu Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency DRAMP21417 WIKAAAKAAAKIW 13 WI (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-TASSER, random coil in PBS, α-helix in SDS Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30897850] Gram-positive bacteria:Staphylococcus aureus ATCC 27853(MIC=32μM), Staphylococcus epidermidis ATCC 12228(MIC=32μM), Staphylococcus faecalis ATCC 29212(MIC=32μM), Bacillus subtilis CMCC 63501(MIC=8μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=8μM), Escherichia coli UB 1005 (MIC=8μM), Pseudomonas aeruginosa ATCC 27853(MIC=32μM), Salmonella typhimurium ATCC 14028(MIC=32μM) [Ref.30897850] 15% hemolysis at 256μM against human red blood cells Linear Free Amidaton L [Ref.30897850] ①The cell viability of RAW 264.7 induced by WI is 104.0%, 98.2%, 98.6%, 106.5%, 103.6%, 101.8% and 100% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on RAW 264.7 cells (Control samples) is 93.1%, 67.8%, 37.7%, 17.8%, 0%, 1.4% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM.②The cell viability of HEK293T induced by WV is 98.9%, 99.3%, 107.2%, 99.6%, 110.5%, 108.3%, 96.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on HEK293T cells (Control samples) is 101.4%, 80.1%, 31.9%, 1.4%, 1.4%, 1.8% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM. Not found 30897850 Int J Mol Sci. 2019 Mar; 20(6): 1417. Published online 2019 Mar 20. doi: 10.3390/ijms20061417 Changxuan Shao, Weizhong Li, Peng Tan, Anshan Shan, Xiujing Dou, Deying Ma, Chunyu Liu Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency DRAMP21418 WFKAAAKAAAKFW 13 WF (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-TASSER, random coil in PBS, α-helix in SDS Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30897850] Gram-positive bacteria:Staphylococcus aureus ATCC 27853(MIC=8μM), Staphylococcus epidermidis ATCC 12228(MIC=16μM), Staphylococcus faecalis ATCC 29212(MIC=32μM), Bacillus subtilis CMCC 63501(MIC=8μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=4μM), Escherichia coli UB 1005 (MIC=4μM), Pseudomonas aeruginosa ATCC 27853(MIC=16μM), Salmonella typhimurium ATCC 14028(MIC=32μM) [Ref.30897850] 12% hemolysis at 256μM against human red blood cells Linear Free Amidaton L [Ref.30897850] ①The cell viability of RAW 264.7 induced by WF is 102.5%, 103.6%, 105.4%, 108.3%, 105.8%, 101.1% and 92.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on RAW 264.7 cells (Control samples) is 93.1%, 67.8%, 37.7%, 17.8%, 0%, 1.4% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM.②The cell viability of HEK293T induced by WV is 101.8%, 101.4%, 93.5%, 97.1%, 93.8%, 107.6% and 92.0% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on HEK293T cells (Control samples) is 101.4%, 80.1%, 31.9%, 1.4%, 1.4%, 1.8% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM. Not found 30897850 Int J Mol Sci. 2019 Mar; 20(6): 1417. Published online 2019 Mar 20. doi: 10.3390/ijms20061417 Changxuan Shao, Weizhong Li, Peng Tan, Anshan Shan, Xiujing Dou, Deying Ma, Chunyu Liu Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency DRAMP21419 WWKAAAKAAAKWW 13 WW (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-TASSER, random coil in PBS, α-helix in SDS Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30897850] Gram-positive bacteria:Staphylococcus aureus ATCC 27853(MIC=4μM), Staphylococcus epidermidis ATCC 12228(MIC=4μM), Staphylococcus faecalis ATCC 29212(MIC=4μM), Bacillus subtilis CMCC 63501(MIC=4μM);##Gram-negative bacteria:Escherichia coli ATCC 25922 (MIC=2μM), Escherichia coli UB 1005 (MIC=4μM), Pseudomonas aeruginosa ATCC 27853(MIC=8μM), Salmonella typhimurium ATCC 14028(MIC=8μM) [Ref.30897850] 24% hemolysis at 256μM against human red blood cells Linear Free Amidaton L [Ref.30897850] ①The cell viability of RAW 264.7 induced by WW is 104.3%, 103.6%, 109.4%, 103.6%, 97.5%, 89.9%, 63.4% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on RAW 264.7 cells (Control samples) is 93.1%, 67.8%, 37.7%, 17.8%, 0%, 1.4% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM.②The cell viability of HEK293T induced by WV is 102.9%, 111.6%, 105.1%, 104.3%, 101.8%, 84.8%, 43.5% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM, while the cytotoxicity of WV on HEK293T cells (Control samples) is 101.4%, 80.1%, 31.9%, 1.4%, 1.4%, 1.8% and 1.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 μM. Not found 30897850 Int J Mol Sci. 2019 Mar; 20(6): 1417. Published online 2019 Mar 20. doi: 10.3390/ijms20061417 Changxuan Shao, Weizhong Li, Peng Tan, Anshan Shan, Xiujing Dou, Deying Ma, Chunyu Liu Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency DRAMP21420 FLPKLFAKITKKNMAHIRC 19 AY1C (Derived from AY1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Helix-loop-helix derived from NMR Not found 5YKL resolved by NMR Function: Antibacterial activity against Gram-negative bacteria. [Ref.30872680] Gram-negative bacteria:Pseudomonas aeruginosa (MIC=15μM), Escherichia coli (MIC=17μM), Salmonella typhi(MIC=15μM), Klebsiella pneumoniae(MIC=12μM) [Ref.30872680] 4% hemolysis at 10 μM, 9% hemolysis at 50 μM, 8% hemolysis at 100μM against human red blood cells Linear Free Free L [Ref.30872680] No cytotoxicity information found. Not found 30872680 Sci Rep. 2019; 9: 4485. Published online 2019 Mar 14. doi: 10.1038/s41598-019-41005-7 Pal I, Bhattacharyya D, Kar RK, Zarena D, Bhunia A, Atreya HS A Peptide-Nanoparticle System with Improved Efficacy against Multidrug Resistant Bacteria DRAMP21421 FLPKLFAKITKKNMAHIRC 19 AY1C-AgNP (Derived from AY1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Helix-loop-helix derived from NMR Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.30872680] Gram-negative bacteria:Pseudomonas aeruginosa (MIC=15μM), Escherichia coli (MIC=12μM), Salmonella typhi(MIC=15μM), Klebsiella pneumoniae(MIC=10μM) [Ref.30872680] 4% hemolysis at 10 μM, 6% hemolysis at 50 μM, 9% hemolysis at 100μM against human red blood cells Linear Free Free Conjugation with silver nanoparticles L [Ref.30872680] No cytotoxicity information found. Not found 30872680 Sci Rep. 2019; 9: 4485. Published online 2019 Mar 14. doi: 10.1038/s41598-019-41005-7 Pal I, Bhattacharyya D, Kar RK, Zarena D, Bhunia A, Atreya HS A Peptide-Nanoparticle System with Improved Efficacy against Multidrug Resistant Bacteria DRAMP21422 CFLPKLFAKITKKNMAHIR 19 CAY1 (Derived from AY1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Helix-loop-helix derived from NMR Not found 5YKQ resolved by NMR Function: Antibacterial activity against Gram-negative bacteria. [Ref.30872680] Gram-negative bacteria:Pseudomonas aeruginosa (MIC=10μM), Escherichia coli (MIC=10μM), Salmonella typhi(MIC=Not know), Klebsiella pneumoniae(MIC=7μM) [Ref.30872680] 4% hemolysis at 10 μM, 9% hemolysis at 50 μM, 10% hemolysis at 100μM against human red blood cells Linear Free Free L [Ref.30872680] No cytotoxicity information found. Not found 30872680 Sci Rep. 2019; 9: 4485. Published online 2019 Mar 14. doi: 10.1038/s41598-019-41005-7 Pal I, Bhattacharyya D, Kar RK, Zarena D, Bhunia A, Atreya HS A Peptide-Nanoparticle System with Improved Efficacy against Multidrug Resistant Bacteria DRAMP21423 CFLPKLFAKITKKNMAHIR 19 CAY1-AgNP (Derived from AY1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Helix-loop-helix derived from NMR Not found Function: Antibacterial activity against Gram-negative bacteria. [Ref.30872680] Gram-negative bacteria:Pseudomonas aeruginosa (MIC=10μM), Escherichia coli (MIC=10μM), Salmonella typhi(MIC=15μM), Klebsiella pneumoniae(MIC=5μM) [Ref.30872680] 3% hemolysis at 10 μM, 9% hemolysis at 50 μM, 9.5% hemolysis at 100μM against human red blood cells Linear Free Free Conjugation with silver nanoparticles L [Ref.30872680] No cytotoxicity information found. Not found 30872680 Sci Rep. 2019; 9: 4485. Published online 2019 Mar 14. doi: 10.1038/s41598-019-41005-7 Pal I, Bhattacharyya D, Kar RK, Zarena D, Bhunia A, Atreya HS A Peptide-Nanoparticle System with Improved Efficacy against Multidrug Resistant Bacteria DRAMP21424 KKGKGGG 7 B1 (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coils most likely Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=2-4µg/ml), MSSA ATCC 29213(MIC=8-16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=8-16µg/ml) [Ref.30842436] EC10=64μM, EC50=230μM, 32% hemolysis at 150 µM against human red blood cells Linear Free Amidation ①Residue 3 is N-butylglycine. ②Residue 5 and residue 7 are N-1-naphthylmethylglycine. ③Residue 6 is N-4-methylbenzylglycine. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21425 KKGKGGG 7 peptide 2 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=4µg/ml), MSSA ATCC 29213(MIC=8-16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation ①Residue 3 is N-butylglycine. ②Residue 5 and residue 7 are N-1-naphthylmethylglycine. ③Residue 6 is N-benzylglycine resembling Phe. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21426 KKKGGGG 7 peptide 3 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=4µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation ①Residue 4 is N-butylglycine. ②Residue 5 and residue 7 are N-1-naphthylmethylglycine. ③Residue 6 is N-benzylglycine resembling Phe. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21427 GGGGKKK 7 peptide 4 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] EC10=54μM, 24% hemolysis at 150 µM against human red blood cells Linear Free Amidation ①Residue 1 and residue 3 are N-1-naphthylmethylglycine.②Residue 2 is N-benzylglycine resembling Phe.③Residue 4 is N-butylglycine. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21428 GGGKGKK 7 peptide 5 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation ①Residue 1 and residue 3 are N-1-naphthylmethylglycine.②Residue 2 is N-benzylglycine resembling Phe.③Residue 5 is N-butylglycine. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21429 KKLKAFA 7 peptide 6 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=8µg/ml) [Ref.30842436] EC10=5μM, EC50=58μM, 96% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 1-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21430 KKKLAFA 7 peptide 7 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=16µg/ml) [Ref.30842436] EC10=8μM, EC50=140μM, 55% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 1-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21431 KKLKAFA 7 peptide 8 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] EC10=56μM, 34% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21432 KKKLAFA 7 peptide 9 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=16µg/ml) [Ref.30842436] EC10=46μM, 39% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21433 AFAKLKK 7 peptide 10 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8-16µg/ml), MSSA ATCC 29213(MIC=16-32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 1-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21434 AFAKLKK 7 peptide 11 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=4-8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21435 AFALKKK 7 peptide 12 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 1-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21436 AFALKKK 7 peptide 13 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] EC10=110μM, 15% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21437 KKlKafa 7 peptide 14 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=4-8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=16-32µg/ml) [Ref.30842436] EC10=28μM, EC50=128μM, 58% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 1-naphthylmethylglycine Mixed (D-Leu3, D-Ala5, D-Phe6 and D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21438 KKKlafa 7 peptide 15 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=2µg/ml), MSSA ATCC 29213(MIC=8µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=8µg/ml) [Ref.30842436] EC10=8μM, EC50=40μM, 88% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 1-naphthylmethylglycine Mixed (D-Leu4, D-Ala5, D-Phe6 and D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21439 KKKlafa 7 peptide 16 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=2-4µg/ml), MSSA ATCC 29213(MIC=8-16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] EC10=18μM, EC50=118μM, 60% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine Mixed (D-Leu4, D-Ala5, D-Phe6 and D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21440 KKlKafa 7 peptide 17 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=8µg/ml), MSSA ATCC 29213(MIC=16µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] EC10=8μM, 40% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine Mixed (D-Leu3, D-Ala5, D-Phe6 and D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21441 afaKlKK 7 peptide 18 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC=32-64µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 2-naphthylmethylglycine Mixed (D-Ala1, D-Phe2, D-Ala3, D-Leu5) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21442 afalKKK 7 peptide 19 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 2-naphthylmethylglycine Mixed (D-Ala1, D-Phe2, D-Ala3, D-Leu4) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21443 afaKlKK 7 peptide 20 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 1-naphthylmethylglycine Mixed (D-Ala1, D-Phe2, D-Ala3, D-Leu5) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21444 afalKKK 7 peptide 21 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] < 8% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 1 and residue 3 are 1-naphthylmethylglycine Mixed (D-Ala1, D-Phe2, D-Ala3, D-Leu4) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21445 KKKLAYA 7 peptide 22 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=16µg/ml), MSSA ATCC 29213(MIC>64µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC>64µg/ml) [Ref.30842436] EC10=117μM, 14% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21446 KKKXAFA 7 peptide 23 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coils most likely Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria [Ref.30842436] Gram-positive bacteria: MRSP C22963(MIC=2-4 µg/ml), MSSA ATCC 29213(MIC=32-64 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa(MIC= 8 µg/ml) [Ref.30842436] EC10=14μM, EC50=104μM, 59% hemolysis at 150 µM against human red blood cells Linear Free Amidation Nle4 is norleucine. Residue 5 and residue 7 are 2-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21447 KKKXAFA 7 peptide 24 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria: MRSP C22963(MIC=16-32 µg/ml), MSSA ATCC 29213(MIC>64 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa(MIC= 16 µg/ml) [Ref.30842436] EC10=3μM, EC50=41μM, 60% hemolysis at 150 µM against human red blood cells Linear Free Amidation Nle4 is norleucine. Residue 5 and residue 7 are 1-naphthylmethylglycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21448 KKKlaya 7 peptide 25 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=2-4µg/ml), MSSA ATCC 29213(MIC=32-64µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=8µg/ml) [Ref.30842436] EC10=38μM, EC50=138μM, 53% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 1-naphthylmethylglycine Mixed (D-Leu4, D-Ala5, D-Tyr6, D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21449 KKKxafa 7 peptide 26 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Random coils most likely Not found Function: Antibacterial activity against Gram-positive bacteria. Antimicrobial activity against Gram-negative bacteria is uncertain. [Ref.30842436] Gram-positive bacteria: MRSP C22963(MIC=4-8 µg/ml), MSSA ATCC 29213(MIC>64 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa(MIC=8 µg/ml) [Ref.30842436] EC50=63μM, 56% hemolysis at 150 µM against human red blood cells Linear Free Amidation Nle4 is norleucine. Residue 5 and residue 7 are 1-naphthylmethylglycine Mixed (D-Nle4, D-Ala5, D-Phe6, D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21450 KKKxAYA 7 peptide 27 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria: MRSP C22963(MIC=2-4 µg/ml), MSSA ATCC 29213(MIC=64 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa(MIC=64 µg/ml) [Ref.30842436] EC10=3μM, EC50=56μM, 54% hemolysis at 150 µM against human red blood cells Linear Free Amidation Nle4 is norleucine. Residue 5 and residue 7 are 2-naphthylmethylglycine. L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21451 KKKlaya 7 peptide 28 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria:MRSP C22963(MIC=2-4µg/ml), MSSA ATCC 29213(MIC=32µg/ml);##Gram-negative bacteria:Pseudomonas aeruginosa(MIC=32µg/ml) [Ref.30842436] EC10=6μM, EC50=50μM, 64% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine Mixed (D-Leu4, D-Ala5, D-Tyr6, D-Ala7) [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21452 KKKLAFA 7 peptide 29 (Derived from B1) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Unknown Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30842436] Gram-positive bacteria: MRSP C22963(MIC=4-8 µg/ml), MSSA ATCC 29213(MIC=16-32 µg/ml);##Gram-negative bacteria: Pseudomonas aeruginosa(MIC=32 µg/ml) [Ref.30842436] EC10=9μM, 46% hemolysis at 150 µM against human red blood cells Linear Free Amidation Residue 5 and residue 7 are 2-naphthylmethylglycine. Residue 1, residue 2 and residue 3 are N-(4-aminobutyl)glycine L [Ref.30842436] No cytotoxicity information found. Not found 30842436 Sci Rep. 2019; 9: 3679. Published online 2019 Mar 6. doi: 10.1038/s41598-019-39042-3 Ines Greco, Agnete Plahn Emborg, Bimal Jana, Natalia Molchanova, Alberto Oddo, Peter Damborg, Luca Guardabassi, Paul R. Hansen Characterization, mechanism of action and optimization of activity of a novel peptide-peptoid hybrid against bacterial pathogens involved in canine skin infections DRAMP21453 GLPLLISWIKRKRQQGSKKPVPIIYCNRRTGKCQRM 36 Hybrid (Derived from Melittin and thanatin) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form A combination of α-helix and β-lamellar Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30701481] Gram-positive bacteria:Staphylococcus aureus(MIC=0.9-1.5μmol/L), Bacillus subtilis(MIC=0.6-1.2μmol/L);##Gram-negative bacteria:Escherichia coli JM 109(MIC=0.6-1.2 μmol/L), Salmonella typhimurium(MIC=0.3-0.6μmol/L) [Ref.30701481] 0% hemolysis at 45 μmol/L and >0% hemolysis at 60 μmol/L against sheep blood cells Linear Free Free L [Ref.30701481] The average inhibitory rate of the hybrid peptide in the SMMC-7721 cells was 19.14%. Not found 30701481 AMB Express. 2019; 9: 14. Published online 2019 Jan 30. doi: 10.1186/s13568-019-0739-z Xiaofeng Jiang, Kun Qian, Guangping Liu, Laiyu Sun, Guoqing Zhou, Jingfen Li, Xinqiang Fang, Haixia Ge, Zhengbing Lv Design and activity study of a melittin–thanatin hybrid peptide DRAMP21454 GILDWGKKVMDWIKDKM 17 PLP1 (Insects, animals) A0A348G6I7 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. Antifungal activity against Saccharomyces cerevisiae. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC<3.1μM);##Gram-negative bacteria:Escherichia coli (MIC<3.1μM);##Fungi:Saccharomyces cerevisiae (MIC<50μM) [Ref.30658410] 0% hemolysis at 50 μM against rat blood cells Linear Free Amidation L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21455 GWGSIFKTVGKMIAKAAVKAAPEAISAMASQNE 33 PLP2 (Insects, animals) A0A348G5V8 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. Antifungal activity against Saccharomyces cerevisiae. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC<6.2μM);##Gram-negative bacteria:Escherichia coli (MIC<6.2μM);##Fungi:Saccharomyces cerevisiae (MIC<50μM) [Ref.30658410] 10.4% hemolysis at 50 μM against rat blood cells Linear Free Free L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21456 KIKWGKIFKKGGKLIGKTALEAAANAAASEAISAMASQNE 40 PLP3 (Insects, animals) A0A348G5V9 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. Antifungal activity against Saccharomyces cerevisiae. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC<25μM);##Gram-negative bacteria:Escherichia coli (MIC<3.1μM);##Fungi:Saccharomyces cerevisiae (MIC<50μM) [Ref.30658410] 0% hemolysis at 50 μM against rat blood cells Linear Free Free L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21457 GVKELFGKAWGLVKKHLPKACGLLGYVKQ 29 PLP4 (Insects, animals) A0A348G5W0 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. Antifungal activity against Saccharomyces cerevisiae. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC<3.1μM);##Gram-negative bacteria:Escherichia coli (MIC<3.1μM);##Fungi:Saccharomyces cerevisiae (MIC<3.1μM) [Ref.30658410] 10.5% hemolysis at 50 μM against rat blood cells Cyclic Free Free Cys21 is S-(carbamoylmethyl)-L-cysteine and there is a interchain disulfide bond between two PLP4 peptide molecules. L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21458 IWGALLGTLIPAITSAIQ 18 PLP5 (Insects, animals) A0A348G5W1 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-nagetive bacteria. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC Negative);##Gram-negative bacteria:Escherichia coli (MIC<50μM);##Fungi:Saccharomyces cerevisiae (MIC Negative) [Ref.30658410] 6.9% hemolysis at 10μM and 94.8% at 50 μM against rat blood cells Linear Free Amidation L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21459 IKGKKIMKNMGKAMKIAGKVAKAMAPIVVPLIVSAA 36 PLP6 (Insects, animals) A0A348G5W2 Belongs to the formicidae venom precursor-01 superfamily. Not found Odontomachus monticola (Trap-jaw ant) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Protein level α-helix predicted by Proteus Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30658410] Gram-positive bacteria:Staphylococcus aureus (MIC<3.1μM);##Gram-negative bacteria:Escherichia coli (MIC<3.1μM);##Fungi:Saccharomyces cerevisiae (MIC Negative) [Ref.30658410] 0% hemolysis at 50 μM against rat blood cells Linear Free Amidation L [Ref.30658410] No cytotoxicity information found. Not found 30658410 Toxins (Basel). 2019 Jan; 11(1): 50. Published online 2019 Jan 17. doi: 10.3390/toxins11010050 Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components DRAMP21460 IHKFWRCRRRFCRWFKHI 18 PQ (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-Tasser In PBS, the α-helix content of PQ is 26.91% and the β-strand content of that is 11.16%. In SDS, the α-helix content of PQ is 32.02% and the β-strand of that is 6.15%. In TFE, the α-helix content of PQ is 36.82% and the β-strand of that is 4.28%. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=8μM), Staphylococcus aureus ATCC 43300(MIC=8μM), Staphylococcus epidermidis ATCC 12228(MIC=8μM), Streptococci faecalis ATCC 29212(MIC=16μM), Bacillus subtilis CMCC 63501(MIC=16μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=16μM), Escherichia coli UB 1005(MIC=8μM), bacteria pyocyaneum ATCC 27853(MIC=8μM), Salmonella typhimurium ATCC 7731(MIC=8μM), Salmonella Pulloru C79-13(MIC=8μM) [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis. Linear Free Amidation L [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by PQ is 68.2%, 68.6%, 66.8%,63.6%, 69.1%, 62.2%, 55.8% and 28.1% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. Not found 30538681 Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832 Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability DRAMP21461 IHKFWRPGRWFKHI 14 PP (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form A combination of α-helical and β-hairpin In PBS, the α-helix content of PQ is 12.35% and the β-strand content of that is 16.30%. In SDS, the α-helix content of PQ is 9.86% and the β-strand of that is 11.56%. In TFE, the α-helix content of PQ is 37.54% and the β-strand of that is 2.54%. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=16μM), Staphylococcus aureus ATCC 43300(MIC=16μM), Staphylococcus epidermidis ATCC 12228(MIC=16μM), Streptococci faecalis ATCC 29212(MIC=8μM), Bacillus subtilis CMCC 63501(MIC=8μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8μM), Escherichia coli UB 1005(MIC=4μM), bacteria pyocyaneum ATCC 27853(MIC=4μM), Salmonella typhimurium ATCC 7731(MIC=8μM), Salmonella Pulloru C79-13(MIC=4μM) [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis. Linear Free Amidation L [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by PP is 67.7%, 69.1%, 70.5%, 65.4%, 61.3%, 65.0%, 70.5% and 68.7% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. Not found 30538681 Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832 Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability DRAMP21462 IHKFWRGGRWFKHI 14 GG (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form A combination of α-helical and β-hairpin In PBS, the α-helix content of PQ is 1.49% and the β-strand content of that is 32.19%. In SDS, the α-helix content of PQ is 11.99% and the β-strand of that is 9.42%. In TFE, the α-helix content of PQ is 18.98% and the β-strand of that is 11.53%. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=16μM), Staphylococcus aureus ATCC 43300(MIC=32μM), Staphylococcus epidermidis ATCC 12228(MIC=32μM), Streptococci faecalis ATCC 29212(MIC=32μM), Bacillus subtilis CMCC 63501(MIC=16μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8μM), Escherichia coli UB 1005(MIC=8μM), bacteria pyocyaneum ATCC 27853(MIC=16μM), Salmonella typhimurium ATCC 7731(MIC=64μM), Salmonella Pulloru C79-13(MIC=8μM) [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis. Linear Free Amidation L [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by GG is 67.7%, 74.2%, 76.5%, 72.4%, 72.8%, 69.1%, 65.9% and 59.9% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. Not found 30538681 Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832 Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability DRAMP21463 IHKFWRRWFKHI 12 Qa (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix predicted by I-Tasser In PBS, the α-helix content of PQ is 2.89% and the β-strand content of that is 19.89%. In SDS, the α-helix content of PQ is 5.54% and the β-strand of that is 14.12%. In TFE, the α-helix content of PQ is 3.08% and the β-strand of that is 18.1%. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=8μM), Staphylococcus aureus ATCC 43300(MIC=16μM), Staphylococcus epidermidis ATCC 12228(MIC=16μM), Streptococci faecalis ATCC 29212(MIC=16μM), Bacillus subtilis CMCC 63501(MIC=32μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=16μM), Escherichia coli UB 1005(MIC=8μM), bacteria pyocyaneum ATCC 27853(MIC=16μM), Salmonella typhimurium ATCC 7731(MIC=16μM), Salmonella Pulloru C79-13(MIC=16μM) [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis. Linear Free Amidation L [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by Qa is 61.3%, 66.8%, 76.5%, 71.4%, 72.4%, 73.3%, 65.9% and 39.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. Not found 30538681 Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832 Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability DRAMP21464 IHFKWRRWKFHI 12 Qna (De Novo Synthesis) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Linear and unordered conformation In PBS, the α-helix content of PQ is 3.46% and the β-strand content of that is 17.46%. In SDS, the α-helix content of PQ is 1.29% and the β-strand of that is 21.49%. In TFE, the α-helix content of PQ is 0.73% and the β-strand of that is 18.82%. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=32μM), Staphylococcus aureus ATCC 43300(MIC=32μM), Staphylococcus epidermidis ATCC 12228(MIC=32μM), Streptococci faecalis ATCC 29212(MIC=64μM), Bacillus subtilis CMCC 63501(MIC=64μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=32μM), Escherichia coli UB 1005(MIC=16μM), bacteria pyocyaneum ATCC 27853(MIC=32μM), Salmonella typhimurium ATCC 7731(MIC=32μM), Salmonella Pulloru C79-13(MIC=32μM) [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis. Linear Free Amidation L [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by Qna is 67.3%, 65.0%, 73.7%, 77.9%, 68.2%, 68.2%, 62.2% and 51.2% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM. Not found 30538681 Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832 Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability DRAMP21465 DEMKLDGFNMHLE 13 P1-Ll-1577 (De Novo Synthesis) No entry found Not found Not found  Leptodactylus latrans (Anura: Leptodactylidae) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil predicted by PSIPRED and GOR V P1-Ll-1577, although presenting contributions of turn structure, is less ordered in the presence of TFE (percentage of an unordered structure higher than 40%). Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30423858] Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=40.5μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=20μM) [Ref.30423858] 100% hemolysis MHC=640μM against human blood cells Linear Free Amidation L [Ref.30423858] No cytotoxicity information found. Not found 30423858 Molecules. 2018 Nov; 23(11): 2943. Published online 2018 Nov 11. doi: 10.3390/molecules23112943 Alvaro Siano, Maria Veronica Humpola, Eliandre de Oliveira, Fernando Albericio, Arturo C Simonetta, Rafael Lajmanovich, Georgina G Tonarelli Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides DRAMP21466 AAGKGLVSNLLEK 13 P2-Ll-1298 (De Novo Synthesis) No entry found Not found Not found  Leptodactylus latrans (Anura: Leptodactylidae) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Helix(K4-E12) predicted by PSIPRED and helix(L6-L10) predicted by GOR V P2-Ll-1298 showed contributions of α-helix. Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30423858] Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=49μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=24.6μM) [Ref.30423858] 100% hemolysis MHC=320μM against human blood cells Linear Free Amidation L [Ref.30423858] No cytotoxicity information found. Not found 30423858 Molecules. 2018 Nov; 23(11): 2943. Published online 2018 Nov 11. doi: 10.3390/molecules23112943 Alvaro Siano, Maria Veronica Humpola, Eliandre de Oliveira, Fernando Albericio, Arturo C Simonetta, Rafael Lajmanovich, Georgina G Tonarelli Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides DRAMP21467 GLLDFLKAAGKGLVSNLLEK 20 P3-Ll-2085 (De Novo Synthesis) No entry found Not found Not found  Leptodactylus latrans (Anura: Leptodactylidae) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Helix(L2-E19) predicted by PSIPRED and Helix(L3-A9, L13-L17) predicted by GOR V Deconvolution spectra by SELCON and CONTILL method indicated more than 70% helical structure for P3-Ll-2085 Function: Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria. [Ref.30423858] Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=15μM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=15μM) [Ref.30423858] 100% hemolysis MHC=40μM against human blood cells Linear Free Amidation L [Ref.30423858] No cytotoxicity information found. Not found 30423858 Molecules. 2018 Nov; 23(11): 2943. Published online 2018 Nov 11. doi: 10.3390/molecules23112943 Alvaro Siano, Maria Veronica Humpola, Eliandre de Oliveira, Fernando Albericio, Arturo C Simonetta, Rafael Lajmanovich, Georgina G Tonarelli Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides DRAMP21310 RRLRKKTRKRLK 12 RK12 (Derived from PMAP-36) No entry found Not found Not found synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form No α-helix content in 50%TFE Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31276398] Gram-positive bacteria:Staphylococcus aureus 29213 (MIC>128 μM), Staphylococcus aureus 25923 (MIC>128 μM), Staphylococcus epidermidis 12228 (MIC>128 μM);##Gram-negative bacteria: Escherichia coli 25922 (MIC>128 μM), Escherichia coli 1005 (MIC=64 μM), Staphylococcus typhi (MIC>128 μM) [Ref.31276398] MHC>128μM. The minimum hemolytic concentration (MHC) is measured as the lowest concentration of the peptides that caused 5% hemolysis of human red blood cells (hRBCs). Linear Free Amidation L [Ref.31276398] The cell viability of the murine macrophage cell line RAW264.7 induced by RK12 is 91.7%, 96.2%, 95.2%, 95.3%, 96.2%, 94.7%, 98.8% and 99.3% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM Not found 31276398 J Med Chem. 2019 Aug 8;62(15):6941-6957. doi: 10.1021/acs.jmedchem.9b00288. Lyu Y, Chen T, Shang L, Yang Y, Li Z, Zhu J, Shan A. Design of Trp-rich dodecapeptides with broad-spectrum antimicrobial potency and membrane-disruptive mechanism DRAMP21577 WWVAARAARR 10 LP1 No entry found Not found Not found Synthetic construct Antimicrobial, Antifungal Synthetic form ①Random-coil conformation. ②1.9% α-helix and 22.1% β-strand in 20 mM potassium phosphate buffer; 0.6% α-helix and 37.2% β-strand in 20 mM potassium ph LP1 appears to adopt a random-coli conformation. Function: Potential antifungal activity against Candida albicans. [Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 237 μM, MIC > 20 μM), Staphylococcus aureus ATCC 6538 (IC50 = 188 μM, MIC > 20 μM), Enterococcus faecalis ATCC 29212 (IC50 = 134 μM, MIC > 20 μM);##Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 805 μM, MIC > 20 μM);## Fungi: Candida albicans 002 ATCC 64385 (IC50 = 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 = 20 μM, MIC > 20 μM). [Ref.28073163] HC50 = 1810 μM against human red blood cells. Note: HC50 is the half-maximal hemolytic concentration. Linear Free Amidation L No cytotoxicity information found in the reference Not found 28073163 Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006. Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity DRAMP21481 KKKKKKAAFAAWAAFAA 17 6K-F17 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form ①Random coils in aqueous buffer. ②α-helix in SDS detergent micelles. As previously reported, 6K-F17 adopts a random coil structure in aqueous buffer and an α helix in the presence of SDS detergent micelles. Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded. [Ref.29275987] Gram-negative bacteria: E. coli (MIC= 1.6 μM) [Ref.29275987] MHC = 320 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis. Linear Free Amidation L No cytotoxicity information found in the reference Not found 29275987 Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21. Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides DRAMP21494 GFLSILKKVLPKVJAHJK 18 MEP-N No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form ①12% α-helical content in water.②43% α-helical content in 50% TFE. ③48% α-helical content in 8mM SDS. No other descriptive information about the structure found in the literature Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans. [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1 μM), Bacillus subtilis (MIC = 0.5 μM), Staphylococcus aureus (MIC = 2.5 μM);##Gram-negative bacteria: E.coli (MIC = 0.9 μM), Pseudomonas aeruginosa (MIC = 17.3 μM);##Fungi: Candida albicans (MIC = 15 μM). [Ref.22526241] LC50 = 50 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay. Linear Free Amidation The J (position: 14 and 17) in sequence are norleucine. L No cytotoxicity information found in the reference Not found 22526241 Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 27. Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera DRAMP21579 WWVXARAXRR 10 Val-nHSLP No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form 0.7% α-helix and 33.4% β-strand in 20 mM potassium phosphate buffer; 0.8% α-helix and 35.8% β-strand in 20 mM potassium phosphate buffer made 30% in T Overall, the peptides showed some β-strand secondary structural characteristics and little α-helical content. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 20 μM. [Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 2.25 μM, MIC = 5.00 μM), Staphylococcus aureus ATCC 6538 (IC50 = 0.63 μM, MIC = 10.0 μM), Enterococcus faecalis ATCC 29212 (IC50 = 0.66 μM, MIC = 5.00 μM);##Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 38.3 μM, MIC > 20 μM);## Fungi: Candida albicans 002 ATCC 64385 (IC50 > 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 > 20 μM, MIC > 20 μM). [Ref.28073163] HC50 = 13.4 μM against human red blood cells. Note: HC50 is the half-maximal hemolytic concentration. Linear Acylation (Valerylamide) Amidation ①The X (position: 4 and 8) in sequence are (S)-2-(4'-pentenyl)-alanine. ②X (4) and X (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple. L No cytotoxicity information found in the reference Not found 28073163 Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006. Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity DRAMP21581 WWVXAFAXRRR 11 Cap-nHSLP No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form 0.5% α-helix and 30.5% β-strand in 20 mM potassium phosphate buffer; 1.9% α-helix and 37.2% β-strand in 20 mM potassium phosphate buffer made 30% in T Overall, the peptides showed some β-strand secondary structural characteristics and little α-helical content. Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria and antifungal activity against Candida albicans are not noteable under 20 μM. [Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 2.03 μM, MIC = 10.0 μM), Staphylococcus aureus ATCC 6538 (IC50 = 0.63 μM, MIC = 5.00 μM), Enterococcus faecalis ATCC 29212 (IC50 = 0.64 μM, MIC = 5.00 μM);##Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 1.34 μM, MIC > 20 μM);## Fungi: Candida albicans 002 ATCC 64385 (IC50 > 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 > 20 μM, MIC > 20 μM). [Ref.28073163] HC50 = 3.59 μM against human red blood cells. Note: HC50 is the half-maximal hemolytic concentration. Linear Acylation (caproylamide) Amidation ①The X (position: 4 and 8) in sequence are (S)-2-(4'-pentenyl)-alanine. ②X (4) and X (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple. L No cytotoxicity information found in the reference Not found 28073163 Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006. Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity DRAMP21596 KAAKAAKKAAKAAWK 15 Ac-UM-14W No entry found Not found Not found Synthetic construct Non-antimicrobial Synthetic form Less α-helix content found in a 25mM potassium phosphate buffer solution at 20℃ Helix formation of unmodified analog Ac-UM-14W would be unfavorable due to the potential electrostatic repulsion among cationic side-chains of lysine residues in its helical conformation. Function: Non-antibacterial activity against Gram-positive or Gram-negative bacteria. Antibacterial activity is not noteable under 200 μM. [Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 200 μM), Staphylococcus aureus ATCC 6538p (MIC > 200 μM), Staphylococcus epidermis ATCC 12228 (MIC > 200 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC > 200 μM), Shigella dysentariae ATCC 9752 (MIC > 200 μM), Salmonella typhimurium ATCC 14028 (MIC > 200 μM), Klebsiella pneumonia ATCC 10031 (MIC > 200 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 200 μM). [Ref.26235946] <1% hemolysis against human red blood cells at 12.5 μM and <1% hemolysis at 25 μM. Linear Acetylation Amidation L No cytotoxicity information found in the reference Not found 26235946 Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19. Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim Antimicrobial activity of doubly-stapled alanine/lysine-based peptides DRAMP21604 KXWKAXK 7 U1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 100 μM. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 100 μM), Staphylococcus aureus ATCC 6538p (MIC > 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 100 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC > 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM). 0.91%, 0.76%, 0.70%, 0.91%, 0.88%, 0.90%, 0.75% and 0.99% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21606 KXAKWXK 7 U2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 100 μM. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 100 μM), Staphylococcus aureus ATCC 6538p (MIC > 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC > 100 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM). 0.76%, 0.86%, 0.84%, 1.05%, 0.97%, 0.93%, 0.96% and 0.88% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21608 KXWKLXK 7 U3 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylococcus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM). 0.88%, 0.72%, 0.90%, 1.25%, 0.75%, 0.98%, 1.03% and 1.12% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21610 KXLKWXK 7 U4 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylococcus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM). 0.80%, 1.98%, 1.28%, 0.81%, 0.97%, 1.19%, 1.19% and 1.22% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21612 KXWAKXA 7 U5 No entry found Not found Not found Synthetic construct Non-antimicrobial Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Non-antibacterial activity against Gram-positive or Gram-negative bacteria. Antibacterial activity is not noteable under 100 μM. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 100 μM), Staphylococcus aureus ATCC 6538p (MIC > 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC > 100 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC > 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM). 0.86%, 0.78%, 0.75%, 0.82%, 0.94%, 0.87%, 1.03% and 1.10% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21614 KXAWKXA 7 U6 No entry found Not found Not found Synthetic construct Non-antimicrobial Synthetic form α-helix in 25 mM potassium phosphate buffer solution (pH 6.5) As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts. Function: Non-antibacterial activity against Gram-positive or Gram-negative bacteria. Antibacterial activity is not noteable under 100 μM. Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 100 μM), Staphylococcus aureus ATCC 6538p (MIC > 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC > 100 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC > 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM). 0.60%, 0.67%, 0.73%, 0.70%, 0.72%, 1.01%, 0.91% and 1.23% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM. Linear Acetylation Amidation ①The X (position: 2 and 6) in sequence are (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. L No cytotoxicity information found. Not found Not found B KOREAN CHEM SOC Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides DRAMP21616 qqrkrkiwsilaplgttlvklvagig 26 DRIM No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form ①Disordered conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②50 Our CD data show that all four linear peptides were generally disordered in aqueous solution, as expected, but prominent effects were seen regarding the impact of the staple. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 32 μg/mL), Enterococcus faecalis (MIC = 32 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 32 μg/mL), Pseudomonas aeruginosa (MIC = 64 μg/mL) [Ref.28921993] 60.5%, 98.0%, 95.1%, 99.0%, 97.9%, 96.3%, 98.8% and 98.2% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml. Linear Free Amidation D [Ref.28921993] The toxicity of DRIM toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM. Not found 28921993 J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26. Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties. DRAMP21618 PLILLRLLRGQF 12 WWSP No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form ①Disordered conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②Mi Our CD data show that all four linear peptides were generally disordered in aqueous solution, as expected, but prominent effects were seen regarding the impact of the staple. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 16 μg/mL), Enterococcus faecalis (MIC = 64 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL) [Ref.28921993] 3.9%, 2.6%, 3.6%, 4.3%, 4.0%, 4.6%, 3.3% and 2.9% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml. Linear Free Amidation L [Ref.28921993] The toxicity of WWSP toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM. Not found 28921993 J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26. Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties. DRAMP21620 AAVLLPVLLAAP 12 KFGF No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form ①Disordered conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②31 Our CD data show that all four linear peptides were generally disordered in aqueous solution, as expected, but prominent effects were seen regarding the impact of the staple. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC > 256 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL) [Ref.28921993] 0.4%, 0.2%, 0.3%, 0.2%, 1.5%, 0.2% and 0.1% hemolysis against human red blood cells at 7.5, 10, 15, 20, 25, 30 and 40 μg/ml. Linear Free Amidation L [Ref.28921993] The toxicity of KFGF toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM. Not found 28921993 J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26. Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties. DRAMP21622 KLALKALKALKAALKLA 17 MAP-1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form ①Disordered conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②Ty Our CD data show that all four linear peptides were generally disordered in aqueous solution, as expected, but prominent effects were seen regarding the impact of the staple. Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 16 μg/mL), Enterococcus faecalis (MIC = 256 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 16 μg/mL), Pseudomonas aeruginosa (MIC = 256 μg/mL) [Ref.28921993] 1.6%, 0.8%, 0.6%, 0.4%, 0.7%, 1.8%, 0.4% and 0.1% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml. Linear Free Amidation L [Ref.28921993] The toxicity of MAP-1 toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM. Not found 28921993 J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26. Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties. DRAMP21626 GILDTLKQFAKGVGKWLVKGAAQ 23 E2EM23W No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Typical random coil conformation with only 14% helical content in a 25 mM potassium phosphate buffer solution at 20 ℃. E2EM23W showed circular dichroism spectra that are typical for a random coil, and its helical content was only 14%. Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not noteable under 200 μg/mL. [Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 50 μg/mL), Staphylococcus aureus (MIC = 100 μg/mL), Staphylococcus epidermis (MIC > 200 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 200 μg/mL), Shigella dysentariae (MIC > 200 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC > 200 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC > 200 μg/mL). [Ref.24211019] No hemolytic activity information found. Linear Acetylation Amidation L No cytotoxicity information found in the reference Not found 24211019 Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26. Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim Truncated and constrained helical analogs of antimicrobial esculentin-2EM DRAMP21627 TLKQFAKGVGKWLVK 15 E2EM15W No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Random coil coformation with 4% helical content in a 25 mM potassium phosphate buffer solution at 20 ℃. Circular dichroism also revealed that E2EM15W is even less structured under the same conditions, displaying a helical content of 4%; it is well established that the shorter a peptide is, the more difficult it is to form an α-helical conformation. Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not noteable under 200 μg/mL. [Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 200 μg/mL), Staphylococcus aureus (MIC = 100 μg/mL), Staphylococcus epidermis (MIC > 200 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 200 μg/mL), Shigella dysentariae (MIC > 200 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC > 200 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC > 200 μg/mL). [Ref.24211019] No hemolytic activity information found. Linear Acetylation Amidation L No cytotoxicity information found in the reference Not found 24211019 Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26. Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim Truncated and constrained helical analogs of antimicrobial esculentin-2EM DRAMP21631 RLVRILVSKRPVAIKPYFRL 20 SLAY-P1 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 2 μM), Acinetobacter baumannii 5075 (MBC ≤ 2 μM), Pseudomonas aeruginosa 14 (MBC ≤ 2 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC ≤ 2 μM). [Ref.29307492] The peptide showed 4.0% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21632 TTSIRRRYQVSLIRRHRGKR 20 SLAY-P2 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 16 μM), Acinetobacter baumannii 5075 (MBC ≤ 2 μM), Pseudomonas aeruginosa 14 (MBC ≤ 2 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 4 μM). [Ref.29307492] The peptide showed 3.1% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21633 TCRTNRPCFYDLDLNVCRCS 20 SLAY-P3 cyclic No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC ≤ 2 μM), Acinetobacter baumannii 5075 (MBC = 4 μM), Pseudomonas aeruginosa 14 (MBC ≤ 2 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 4 μM). [Ref.29307492] The peptide showed 0.9% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Cyclic Free Free Disulfide bonds between Cys2 and Cys19, Cys8 and Cys17. L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21634 SNGDGTLDAGSTCAPFYARA 20 SLAY-P4 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 2 μM), Acinetobacter baumannii 5075 (MBC = 16 μM), Pseudomonas aeruginosa 14 (MBC = 4 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 4 μM). [Ref.29307492] The peptide showed 1.8% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21635 YYNPLPHDCGRDNNTDICSR 20 SLAY-P5 cyclic No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 4 μM), Acinetobacter baumannii 5075 (MBC = 8 μM), Pseudomonas aeruginosa 14 (MBC ≤ 2 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC ≤ 2 μM). [Ref.29307492] The peptide showed 1.1% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Cyclic Free Free Disulfide bonds between Cys9 and Cys18 L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21636 LSVDKRPVLHPEHIYGHNHY 20 SLAY-P6 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 4 μM), Acinetobacter baumannii 5075 (MBC = 32 μM), Pseudomonas aeruginosa 14 (MBC = 8 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC ≤ 128 μM). [Ref.29307492] The peptide showed 3.1% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21637 IHRDQQHESFLDARPEPGLTE 21 SLAY-P7 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 4 μM), Acinetobacter baumannii 5075 (MBC = 16 μM), Pseudomonas aeruginosa 14 (MBC = 4 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 4 μM). [Ref.29307492] The peptide showed 0.7% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21638 TIDFGVRNINQSNLVYDTER 20 SLAY-P8 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 8 μM), Acinetobacter baumannii 5075 (MBC = 16 μM), Pseudomonas aeruginosa 14 (MBC = 8 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] The peptide showed 10.8% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21639 PCNPDHDYRPFGNFRIAFTT 20 SLAY-P9 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 8 μM), Acinetobacter baumannii 5075 (MBC = 16 μM), Pseudomonas aeruginosa 14 (MBC = 8 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 8 μM). [Ref.29307492] The peptide showed 0% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21640 TRDTNDLISSRTAAPSMV 18 SLAY-P10 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 16 μM), Acinetobacter baumannii 5075 (MBC = 64 μM), Pseudomonas aeruginosa 14 (MBC = 8 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 32 μM). [Ref.29307492] The peptide showed 8.4% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21641 LPLPSCSSHGGDADNTSQRN 20 SLAY-P11 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 16 μM), Acinetobacter baumannii 5075 (MBC = 128 μM), Pseudomonas aeruginosa 14 (MBC = 16 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 32 μM). [Ref.29307492] The peptide showed 2.6% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21642 PNDPDSPCVYRMPNARGCSI 20 SLAY-P12 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 16 μM), Acinetobacter baumannii 5075 (MBC = 128 μM), Pseudomonas aeruginosa 14 (MBC = 16 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 16 μM). [Ref.29307492] The peptide showed 0.9% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21643 YDLSDSNCLPANRDKRYYVI 20 SLAY-P13 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 16 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC = 16 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] The peptide showed 3.1% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21644 SMLAYVDKNDHINPPHSPRS 20 SLAY-P14 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 32 μM), Acinetobacter baumannii 5075 (MBC = 128 μM), Pseudomonas aeruginosa 14 (MBC = 32 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 64 μM). [Ref.29307492] The peptide showed 1.5% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21645 DATPHAALFFTVKDHTAGDN 20 SLAY-P15 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 32 μM), Acinetobacter baumannii 5075 (MBC = 64 μM), Pseudomonas aeruginosa 14 (MBC = 32 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 64 μM). [Ref.29307492] The peptide showed 0.6% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21646 SDDAQRCYPHNRTPFTYTYI 20 SLAY-P16 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 32 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC = 16 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC = 32 μM). [Ref.29307492] The peptide showed 3.3% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21647 EPCSPKNNYHDLFYRT 16 SLAY-P17 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Slight antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 128 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC = 128 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] The peptide showed 1.7% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21648 CNPLNGADRRTDSFPRFTVI 20 SLAY-P18 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC = 128 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC = 64 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] The peptide showed 1.7% hemolysis against human red blood cells at 50 μM. PBS was uesd as a negative control and 1% triton was used as a positive control for 100% lysis. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21649 TCRTNRPCFYDLDLNVCRCS 20 SLAY-P3 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Slight antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC > 128 μM), Acinetobacter baumannii 5075 (MBC = 128 μM), Pseudomonas aeruginosa 14 (MBC > 128 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] No hemolytic activity information found. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries DRAMP21650 YYNPLPHDCGRDNNTDICSR 20 SLAY-P5 No entry found Synthetic construct after SLAY screening and prediction Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Unknown Not mentioned Function: Slight antibacterial activity against Gram-negative bacteria. [Ref.29307492] Gram-negative bacteria: E. coli W3110 (MBC > 128 μM), Acinetobacter baumannii 5075 (MBC > 128 μM), Pseudomonas aeruginosa 14 (MBC = 128 μM), E. coli conferring New Delhi metallo-beta-lactamase (MBC > 128 μM). [Ref.29307492] No hemolytic activity information found. Linear Free Free L No cytotoxicity information found Unknown 29307492 Cell. 2018 Jan 25;172(3):618-628.e13. doi: 10.1016/j.cell.2017.12.009. Epub 2018 Jan 4. Ashley T Tucker, Sean P Leonard, Cory D DuBois, Gregory A Knauf, Ashley L Cunningham, Claus O Wilke, M Stephen Trent, Bryan W Davies Discovery of Next-Generation Antimicrobials through Bacterial Self-Screening of Surface-Displayed Peptide Libraries IKLSPETKDNLKKVLKGAIKGAIAVAKMV 29 Hymenochirin-1B Not found Unknown Hymenochirus boettgeri (Congo dwarf clawed frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Experimental evidence at transcript level α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 12.5 μM), S. aureus ATCC 25923 (MIC = 12.5 μM), S.epidermidis RP62A (MIC = 3.1 μM), S.epidermidis RP62A/1 (MIC = 1.6 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 25 μM), A. baumannii (MIC = 6.25 μM), S. maltophilia (MIC = 6.25 μM), K. pneumoniae (MIC = 25 μM), P. aeruginosa (MIC = 50 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 213 ± 18 μM against freshly prepared human erythrocytes. DRAMP28985 GIKKFLKSXKKFVKXFK 17 peptide 1 (Derived from Mag2) No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM No detailed structure description Function: Antibacterial activity against Gram-positive and Gram-negative bacteria "[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 12.5 μM). ##Gram-negative bacteria: Escherichia coli (MIC = 3.125 μM), Pseudomonas aeruginosa (MIC = 3.125 μM), multiple-drug resistant P.aeruginosa (MIC = 3.125 μM)" [Ref.33466998] It has hemolysis against human red blood cells at 50 μM Linear Free Amidation The X (position: 9 and 15) in sequence indicate Aib residues (2-Aminoisobutyric acid) L No cytotoxicity information found in the reference 33466998 Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444. Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence DRAMP28997 RWWWRWW 7 Unstapled heptapeptide 1 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Helicity = 22.7% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides). "Function: Antibacterial activity against Gram-positive bacteria. It is a heptapeptide designed rationally." Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 83 ± 18 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC > 100 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference PubMed ID is not available Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7. Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides DRAMP28999 WWKWWWK 7 Unstapled heptapeptide 3 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Helicity = 24.6% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides). "Function: Antibacterial activity against Gram-positive bacteria. It is a heptapeptide designed rationally." Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 76 ± 14 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 62 ± 10 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference PubMed ID is not available Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7. Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides DRAMP29001 LLLRLLR 7 Unstapled heptapeptide 5 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Helicity = 30.2% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides). "Function: Antibacterial activity against Gram-positive bacteria. It is a heptapeptide designed rationally." Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 45 ± 9 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 32 ± 5 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference PubMed ID is not available Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7. Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides DRAMP29003 WWRRWWR 7 Unstapled heptapeptide 7 No entry found Synthetic construct Non-Antimicrobial Synthetic form Helicity = 14.1% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides). "Function: Antibacterial activity against Gram-positive bacteria is not significant under the concentration of 100 μg/mL. It is a heptapeptide designed rationally." Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC > 100 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC > 100 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference PubMed ID is not available Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7. Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides DRAMP29005 KLLKLLK 7 Unstapled heptapeptide 9 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Helicity = 33.7% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides). "Function: Antibacterial activity against Gram-positive bacteria. It is a heptapeptide designed rationally." Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 49 ± 11 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 41 ± 9 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference PubMed ID is not available Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7. Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides DRAMP29006 GLFAVIKKVASVIKGL 16 A4K14-citropin1.1 No entry found Synthetic construct Anticancer Synthetic form Helicity = 61.5% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL) [Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%. "Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells. A4K14-citropin 1.1 is a structurally optimized derivative of citropin-1.1 derived from amphibians' skin secreta peptide Citropin, which exhibits broad biological activities. Citropin-1.1 is Amphibian defense peptide with antibiotic and antimicrobial activity. Bowie and his team found that replacement of Asp4 and Gly14 with Ala and Lys (termed A4K14-CITROPIN 1.1) resulted in a more stable α-helix than Citropin on the C-terminal section, and it led to better biologicla activities" [Ref.33363118] Cancer cell lines: C4-2B (IC50 = 29.05 μM), A549 (IC50 = 14.97 μM), U87 (IC50 = 14.8 μM), MCF-7 (14.16 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference 33363118 Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020. Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides DRAMP29018 IKLSKKTKKNLKKVLKGAIKGAIAVAKMV 29 H-14 No entry found Synthetic construct Anticancer Synthetic form α-helical (most likely) No detailed structure description found. "Function: Anticancer activity. Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays" [Ref.30789695] Cancer cell lines: A549 (IC50 = 0.98 ± 0.11 μM), HCT116 (IC50 = 1.841 ± 0.34 μM), HepG2 (IC50 = 4.54 ± 0.25 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference Not found 30789695 ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1. Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy DRAMP29028 KLLKKAGKLLKKAGKLLKKAG 21 Stripe No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-Helix content = 42% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate No detailed structure description found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. The 'Stripe' is a rationally-designed amphipathic helical AMP comprising natural amino acids: the AMP has hydrophobic Ala/Leu on one side of the helix and cationic Lys residues on the other. It has great antimicrobial activity and weak hemolysis. However, Stripe was compeletely degraded within an hour after incubation with proteinase K at 37℃, which means a bad stability." [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 12.5 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 3.125 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 3.125 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 3.125 μM) [Ref.33369262] Stripe showed no hemolytic activity up to a concentration of 100 μM. Linear Free Free L No cytotoxicity information found in the reference 33369262 Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749. Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling DRAMP29029 KLLKKGGKLLKKGGKLLKKGG 21 Stripe-based foldamer peptide 1 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram- Synthetic form α-Helix content = 25% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate [Ref.33369262] Conversely, the Gly-substitutde peptide 1 showed weaker spectral intensity than other peptides, which suggests a decrease in helicity. "Function: Antibacterial activity against Gram-negative bacteria. It is a helical foldmer peptide based on ""Stripe"" (an AMP manually designed) by substituting Ala (position: 6, 13 and 20) with Gly. The peptide was less active than Stripe against four bacteria: S.aureus, E.coli, P.aeruginosa, MDRP. " [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC > 50 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 12.5 μM), Pseudomonas aeruginosa NBRC13275 (MIC > 50 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC > 50 μM) [Ref.33369262] Peptide 1 showed no hemolytic activity up to a concentration of 100 μM. Linear Free Free L No cytotoxicity information found in the reference 33369262 Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749. Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling DRAMP29030 KLLKKXGKLLKKXGKLLKKXG 21 Stripe-based foldamer peptide 2 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-Helix content = 31% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate [Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe. "Function: Antibacterial activity against Gram-negative bacteria. It is a helical foldmer peptide based on ""Stripe"" (an AMP manually designed) by introducing hydrophobic α,α-disubstituted amino acids (Aib). The peptide exhibited two to four times higher antimicrobial activity than Stripe. Besides, it is much more stable than Stripe against proteinase K." [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 3.125 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 1.56 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 1.56 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 1.56 μM) [Ref.33369262] Peptide 2 showed no hemolytic activity up to a concentration of 100 μM. Linear Free Free The X (position: 6, 13 and 20) in sequence denote Aib residue. L No cytotoxicity information found in the reference 33369262 Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749. Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling DRAMP29031 KLLKKZGKLLKKZGKLLKKZG 21 Stripe-based foldamer peptide 3 No entry found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-Helix content = 49% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate [Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe. "Function: Antibacterial activity against Gram-negative bacteria. It is a helical foldmer peptide based on ""Stripe"" (an AMP manually designed) by introducing hydrophobic α,α-disubstituted amino acids (1-aminocyclohexanecarboxylic acid Ac₆c). The peptide showed similar or silightly weaker activity than Stripe." [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 6.25 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 3.125 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 6.25 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 12.5 μM) [Ref.33369262] It exhibits hemolysis at 1.56 μM agasint human red blood cells. Linear Free Free The Z (position: 6, 13 and 20) in sequence denote Ac₆c residue (1-Aminocyclohexanecarboxylic acid). L No cytotoxicity information found in the reference 33369262 Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749. Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling DRAMP29034 IKLSKETKDNLKKVLKGAIKGAIAVAKMV 29 [P5K]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anticancer Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria; Anticancer activity. Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays" [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 6.25 μM), S. aureus ATCC 25923 (MIC = 6.25 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 1.6 μM), C.albicans ATCC 90028 (MIC = 50 μM);##Gram-negative bacteria: E.coli (MIC = 12.5 μM), A. baumannii (MIC = 6.25 μM), S. maltophilia (MIC = 3.1 μM), K. pneumoniae (MIC = 12.5 μM), P. aeruginosa (MIC = 25 μM), P.mirabilis (MIC > 100 μM).##[Ref.30789695] Cancer cell lines: A549 (IC50 = 2.35 ± 0.31 μM), HCT116 (IC50 = 8.09 ± 0.40 μM), HepG2 (IC50 = 4.28 ± 0.38 μM) [Ref.24172540] LC₅₀ = 205 ± 15 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540##30789695 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27.##ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon##Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties##Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy DRAMP29035 IKLSPKTKDNLKKVLKGAIKGAIAVAKMV 29 [E6K]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 1.6 μM), S.epidermidis RP62A (MIC = 0.8 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 6.25 μM), A. baumannii (MIC = 6.25 μM), S. maltophilia (MIC = 1.6 μM), K. pneumoniae (MIC = 6.25 μM), P. aeruginosa (MIC = 12.5 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 186 ± 4 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29036 IKLSPETKKNLKKVLKGAIKGAIAVAKMV 29 [D9K]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anticancer Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria; Anticancer activity. Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays" [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 3.1 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 50 μM);##Gram-negative bacteria: E.coli (MIC = 6.25 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 3.1 μM), K. pneumoniae (MIC = 12.5 μM), P. aeruginosa (MIC = 25 μM), P.mirabilis (MIC > 100 μM).##[Ref.30789695] Cancer cell lines: A549 (IC50 = 1.82 ± 0.23 μM), HCT116 (IC50 = 6.50 ± 0.32 μM), HepG2 (IC50 = 4.96 ± 0.43 μM). [Ref.24172540] LC₅₀ = 174 ± 12 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540##30789695 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27.##ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon.##Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao. An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties.##Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy. DRAMP29037 IKLSKKTKDNLKKVLKGAIKGAIAVAKMV 29 [P5K,E6K]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 3.1 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 3.1 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 1.6 μM), K. pneumoniae (MIC = 6.25 μM), P. aeruginosa (MIC = 12.5 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 137 ± 11 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29038 IKLSKETKKNLKKVLKGAIKGAIAVAKMV 29 [P5K,D9K]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Anticancer Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria; Anticancer activity. Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays" [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 6.25 μM), S. aureus ATCC 25923 (MIC = 3.1 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 1.6 μM), C.albicans ATCC 90028 (MIC = 50 μM);##Gram-negative bacteria: E.coli (MIC = 6.25 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 3.1 μM), K. pneumoniae (MIC = 6.25 μM), P. aeruginosa (MIC = 12.5 μM), P.mirabilis (MIC > 100 μM).##[Ref.30789695] Cancer cell lines: A549 (IC50 = 1.17 ± 0.23 μM), HCT116 (IC50 = 4.93 ± 0.51 μM), HepG2 (IC50 = 2.46 ± 0.32 μM). [Ref.24172540] LC₅₀ = 127 ± 9 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540##30789695 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27.##ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon.##Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao. An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties.##Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Nov DRAMP29039 IKLSPKTKKNLKKVLKGAIKGAIAVAKMV 29 [E6K,D9K]Hymenochirin-1B Not found Synthetic construct "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Immunomodulatory, Anti-inflammatory" Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found "Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. The peptide, at a concentration of 2.5 μM, significantly (P<0.05) stimulates the production of the anti-inflammatory IL-4 and IL-10 but is without significant effect on production of the pro-inflammatory cytokines TNF-α and IL-17" [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 1.6 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 50 μM);##Gram-negative bacteria: E.coli (MIC = 3.1 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 1.6 μM), K. pneumoniae (MIC = 3.1 μM), P. aeruginosa (MIC = 6.25 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 85 ± 5 μM against freshly prepared human erythrocytes. Linear Free Amidation L No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29040 IKLSPkTKDNLKKVLKGAIKGAIAVAKMV 29 [E6k]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 3.1 μM), S.epidermidis RP62A (MIC = 1.6 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 3.1 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 3.1 μM), K. pneumoniae (MIC = 6.25 μM), P. aeruginosa (MIC = 12.5 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 188 ± 8 μM against freshly prepared human erythrocytes. Linear Free Amidation ①Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Lys6) No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29041 IKLSPETKkNLKKVLKGAIKGAIAVAKMV 29 [D9k]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 6.25 μM), S. aureus ATCC 25923 (MIC = 6.25 μM), S.epidermidis RP62A (MIC = 0.8 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 6.25 μM), A. baumannii (MIC = 3.1 μM), S. maltophilia (MIC = 3.1 μM), K. pneumoniae (MIC = 6.25 μM), P. aeruginosa (MIC = 25 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ > 400 μM against freshly prepared human erythrocytes. Linear Free Amidation ①Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Lys9) No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29042 IKLSPkTKkNLKKVLKGAIKGAIAVAKMV 29 [E6k,D9k]Hymenochirin-1B Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical (most likely) No structure indentification experiment and detailed structure description found Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. [Ref.24172540] Gram-positive bacteria: S. aureus ATCC 29213 (MIC = 3.1 μM), S. aureus ATCC 25923 (MIC = 1.6 μM), S.epidermidis RP62A (MIC = 0.8 μM), S.epidermidis RP62A/1 (MIC = 0.8 μM), C.albicans ATCC 90028 (MIC = 100 μM);##Gram-negative bacteria: E.coli (MIC = 3.1 μM), A. baumannii (MIC = 1.6 μM), S. maltophilia (MIC = 1.6 μM), K. pneumoniae (MIC = 3.1 μM), P. aeruginosa (MIC = 6.25 μM), P.mirabilis (MIC > 100 μM). [Ref.24172540] LC₅₀ = 302 ± 21 μM against freshly prepared human erythrocytes. Linear Free Amidation ①Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Lys6 and D-Lys9) No cytotoxicity information found in the reference 24172540 Peptides. 2013 Dec;50:153-9. doi: 10.1016/j.peptides.2013.10.015. Epub 2013 Oct 27. Milena Mechkarska, Manju Prajeep, Gordana D Radosavljevic, Ivan P Jovanovic, Amna Al Baloushi, Agnes Sonnevend, Miodrag L Lukic, J Michael Conlon An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties DRAMP29043 VDKPPYLPRPRPPRRIYNR 19 Oncocin (variant of Oncopeltus antibacterial peptide 4) No entry found Not found Synthetic construct (Oncocin is a variant of the 2 kDa Oncopeltus antibacterial peptide 4, which was originally isolated from oncopeltus fasciatus (milkweed bug)) Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Not found Not found Comment: Oncocin inhibits bacterial protein translation by targeting the ribosome. [Ref.20565063] Gram-negative pathogens: P.aeruginosa DSM3227 (MIC = 4 μg/mL), P. aeruginosa Walter (MIC = 8 μg/mL), P. aeruginosa ATCC27853 (MIC = 4 μg/mL), P. aeruginosa PAO1 (MIC = 2 μg/mL), P. aeruginosa 60811001 (MIC = 2 μg/mL), P. aeruginosa 60909001 (MIC = 2 μg/mL), P. aeruginosa 61118003 (MIC = 2 μg/mL), P. aeruginosa 70108001 (MIC = 4 μg/mL), E. coli 70329001 (MIC = 1 μg/mL), E. coli 70430001 (MIC = 1 μg/mL), E. coli 70419002 (MIC = 8 μg/mL), E. coli 70502001 (MIC = 1 μg/mL), E. coli Neumann (MIC = 2 μg/mL), E. coli 205024 (MIC = 4 μg/mL), E. coli 455/7 (MIC = 0.5 μg/mL), E. coli 8474 (MIC = 0.5 μg/mL), K. pneumoniae DSM681 (MIC = 0.25 μg/mL), K. pneumoniae 57 USA (MIC = 0.25 μg/mL), K. pneumoniae 63 (MIC = 8 μg/mL), K. pneumoniae 8085 (MIC = 0.5 μg/mL), K. pneumoniae ATCC12657 (0.5 μg/mL), K. pneumoniae ATCC27799 (MIC = 1 μg/mL), A. baumannii ICB14067 (MIC = 1 μg/mL), A. baumannii ICB14072 (MIC = 1 μg/mL), A. baumannii ICB14073 (MIC = 2 μg/mL), A. baumannii ICB9250 (MIC = 0.5 μg/mL), A. baumannii M17 (MIC = 1 μg/mL), E. cloacae 34654 (MIC = 0.25 μg/mL), E. cloacae Ha088 (MIC = 0.125 μg/mL), E. cloacae Ha089 (0.125 μg/mL), E. cloacae Ha185 (MIC = 0.5 μg/mL), E. cloacae Ha89 (MIC = 0.25 μg/mL), P. vulgaris ICB9081 (MIC = 4 μg/mL), P. vulgaris ICB9095 (MIC = 4 μg/mL), Stenotrophomonas ICB308054 (MIC = 32 μg/mL), Stenotrophomonas ICB7569 (MIC = 8 μg/mL), Stenotrophomonas ICB7789 (MIC = 32 μg/mL) [Ref.20565063]None of the tested peptides showed any hemolytic activity against human erythrocytes in the studied peptide concentration range up to 600 μg/mL. Linear Free Amidation L [Ref.20565063] Oncocin showed no toxic effects on HeLa- or neuronal-cell-like differentiated SH-SY5Y cells at a peptide concentration of 600 μg/mL, which was about 100-fold above their MIC-values against E.coli BL21 AI. Bacterial ribosome 20565063##28575099 J Med Chem. 2010 Jul 22;53(14):5240-7. doi: 10.1021/jm100378b.##PLoS One. 2017 Jun 2;12(6):e0178943. doi: 10.1371/journal.pone.0178943. Daniel Knappe, Stefania Piantavigna, Anne Hansen, Adam Mechler, Annegret Binas, Oliver Nolte, Lisandra L Martin, Ralf Hoffmann##Böttger R, Hoffmann R, Knappe D Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): A Novel Antibacterial Peptide Optimized against Gram-Negative Human Pathogens##Differential stability of therapeutic peptides with different proteolytic cleavage sites in blood, plasma and serum DRAMP29044 KFFRKLKKSVKKRAKKFFKKPRVIGVSIPF 30 Cbf-K-16 (variant of BF-30) No entry found Not found Synthetic construct (Cbf-K16 is a variant of BF-30, which was found in the venom of the snake bungarus fasciatus) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Comment: Cbf-K16 possessed effective antimicrobial and anti-inflammatory activities and downregulated the expression of adhesion- and cytotoxin-associated genes of drug-resistant H. pylori SS1, making it a potential candidate for anti-infective therapy. [Ref.31704464] Gram-negative drug-resistant clinical isolates: H. pylori SS1 (MIC = 16 μg/mL, MBC = 32 μg/mL); Gram -negative bacteria: H. pylori 26695 (MIC = 32 μg/mL, MBC = 64 μg/mL), H. pylori 11637 (MIC = 16 μg/mL, MBC = 64 μg/mL) ##[Ref.27287456] Gram-positive drug-resistant clinical isolates: MRSA strain no.1 (MIC = 32 μg/mL), MRSA strain no.2 (MIC = 16 μg/mL), S.aureus strain no.1 (MIC = 16 μg/mL), S.aureus strain no.2 (MIC = 64 μg/mL), S.aureus strain no.3 (MIC = 8 μg/mL), S.aureus strain no.4 (MIC = 16 μg/mL), S.aureus strain no.5 (MIC = 4 μg/mL), S.aureus strain no.6 (MIC = 8 μg/mL), S.aureus strain no.7 (MIC = 32 μg/mL), S.epidermidis strain no.1 (MIC = 16 μg/mL), S.epidermidis strain no.2 (MIC = 32 μg/mL);## Gram-positive bacteria: S.aureus ATCC 25923 (MIC = 8 μg/mL);## Gram-negative drug-resistant clinical isolates: E.coli strain no.1 (MIC = 4 μg/mL), E.coli strain no.2 (MIC = 8 μg/mL), E.coli strain no.3 (MIC = 8 μg/mL); ##Gram-negative bacteria: E.coli ATCC 25922 (MIC = 4 μg/mL) [Ref.27287456]Cbf-K-16 has low hemolytic activity Linear Free Free L [Ref.27287456] Cbf-K-16 has low cytotoxicity. Genomic DNA 31704464##27287456 Microb Pathog. 2020 Jan;138:103847. doi: 10.1016/j.micpath.2019.103847. Epub 2019 Nov 5.##Arch Pharm Res. 2016 Jul;39(7):978-88. doi: 10.1007/s12272-016-0769-x. Epub 2016 Jun 10. Jiang M, Ma L, Huang Y, Wu H, Dou J, Zhou C##Bo Li, Wei Kang, Hanhan Liu, Yanrong Wang, Changzhong Yu, Xinyi Zhu, Jie Dou, Haibo Cai, Changlin Zhou Antimicrobial activities of peptide Cbf-K 16 against drug-resistant Helicobacter pylori infection in vitro and in vivo. ##The antimicrobial activity of Cbf-K16 against MRSA was enhanced by β-lactamantibiotics through cell wall non-integrity. DRAMP29045 SQRKLAAKLTSKGGGRLLRPLLQLLKQKLR 30 PA2-GNU7 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Helix-loop-helix structure ①Molecular modelling showed that the hybrid peptide was predicted to form a helix-loop-helix structure. ②The hybrid peptide PA2-GNU7 was constructed by joining the PA2 peptide (SQRKLAAKLTSK) to GNU7 (RLLRPLLQLLKQKLR) with a short linker (Gly × 3). Comment: The specific binding activity of PA2-GNU7 against P. aeruginosa was derived from the binding activity of PA2 peptide. [Ref.31704464] Gram-positive bacteria: S. aureus (MIC = 2 μM);##Gram-negative bacteria: P. aeruginosa (MIC = 2 μM), E. coli (MIC = 1 μM), S. typhimurium (MIC = 2 μM); ##Fungi: C.albicans (MIC = 8 μM) [Ref.31678742]PA2-GNU7 was not toxic to human RBCs at the tested concentrations (0 - 65 μM).The haemolysis was less than 2.5 % up to the concentration of 65 μM. Linear Free Free L Not found Outer membrane proteins (OMPs) like OprF, the major outer membrane porin of P.aeruginosa 31678742 Eur J Med Chem. 2020 Jan 1;185:111814. doi: 10.1016/j.ejmech.2019.111814. Epub 2019 Oct 25. Kim H, Jang JH, Kim SC, Cho JH. Development of a novel hybrid antimicrobial peptide for targeted killing of Pseudomonas aeruginosa DRAMP29046 FRKKWNKWALSR 12 PAMP(9-20) ( the C-terminal 12-residues of PAMP) P53366, O62827, P43145, P35318 Belongs to the adrenomedullin family ADM Homo sapiens et.al Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level α-helical (most likely) Not found Function: Kuwasako et al. identified the C-terminal 12-residues of PAMP [PAMP(9–20)] in porcine adrenal medulla as a major endogenous active peptide of the AM precursor and demonstrated that its hypotensive activity is comparable to that of PAMP. PAMP(9-20) can acts as an potent antimicrobial peptide which is more selective than melittin, and antimicrobial action of PAMP(9-20) seems to exert via an intracellular target. [Ref.32439180] Gram-negative bacteria: E. coli (MIC = 4 μM), P. aeruginosa (MIC = 16 μM), S. typhimurium (MIC = 4 μM)##Gram-positive bacteria:B. subtilis (MIC = 8 μM), S. epidermidis (MIC = 8 μM), S. aureus(MIC = 16 μM) [Ref.32439180]HC10 > 256 μM against sheep RBCs.Note: HC10 is the minimum peptide concentration that caused >10% hemolysis of sheep red blood cells. Linear Free Amidation L Not found Bacterial DNA 32439180 Biochem Biophys Res Commun. 2020 Jun 30;527(3):744-750. doi: 10.1016/j.bbrc.2020.04.063. Epub 2020 May 18. Ajish C, Yang S, Kumar SD, Shin SY. Proadrenomedullin N-terminal 20 peptide (PAMP) and its C-terminal 12-residue peptide, PAMP(9-20): Cell selectivity and antimicrobial mechanism DRAMP29047 ARLDVASEFRKKWNKWALSR 20 PAMP (Proadrenomedullin N-terminal 20 peptide) P35318, E9PML4, L5L428 Belongs to the adrenomedullin family ADM Homo sapiens et.al Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Protein level α-helical Not found 2FLY Introduction: Proadrenomedullin N-terminal 20 peptide (PAMP) is a biologically active molecule (20 amino acid residues) produced by post-translational enzymatic processing of the common precursor of adrenomedullin (AM), a 185-amino acid proadrenomedullin molecule. PMAP can bee found in various types. Function: AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels. PAMP can acts as an potent antimicrobial peptide which is more selective than melittin, and antimicrobial action of PAMP seems to exert via an intracellular target. [Ref.32439180] Gram-negative bacteria: E. coli (MIC = 8 μM), P. aeruginosa (MIC = 32 μM), S. typhimurium (MIC = 16 μM)##Gram-positive bacteria:B. subtilis (MIC = 8 μM), S. epidermidis (MIC = 8 μM), S. aureus(MIC = 16 μM) [Ref.32439180]HC10 > 256 μM against sheep RBCs.Note: HC10 is the minimum peptide concentration that caused >10% hemolysis of sheep red blood cells. Linear Free Amidation L Not found Bacterial DNA 32439180 Biochem Biophys Res Commun. 2020 Jun 30;527(3):744-750. doi: 10.1016/j.bbrc.2020.04.063. Epub 2020 May 18. Ajish C, Yang S, Kumar SD, Shin SY. Proadrenomedullin N-terminal 20 peptide (PAMP) and its C-terminal 12-residue peptide, PAMP(9-20): Cell selectivity and antimicrobial mechanism DRAMP29048 KIAKRIWKILRRR 13 PA-13 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical Not found Function: PA-13 exhibited potent antibacterial activity against P. aeruginosa, including multidrug resistant strains, via penetration through the bacteria’s membrane and causing depolarization, permeabilization and rupture of membranes, and subsequent leakage of intracellular contents and cell death. The peptide displayed low hemolytic and cytotoxic activities against mammalian cells suggesting a therapeutic potential. Furthermore, PA-13 showed anti-inflammatory activity via LPS neutralization. Note: It maintained antimicrobial activity in the presence of physiological salts and displayed rapid binding and penetration activity which resulted in membrane depolarization and permeabilization.  "[Ref.32499514] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC = 3.91 µg/ml), Escherichia coli ATCC 25922 (MIC = 31.25 µg/ml), Escherichia coli O157:H7 MT strain (MIC = 31.25 µg/ml), Shigella sonnei ATCC 11060 (MIC = 3.91 µg/ml), Salmonella Typhimurium ATCC 13311 (MIC = 1.95 µg/ml), Vibrio cholera O1 Inaba DMST 16261 (MIC = 31.25 µg/ml), Acinetobacter baumannii MT strain (MIC = 7.81 µg/ml). ##Clinically isolated MDR P. aeruginosa: P. aeruginosa No.1 (3.91 μg/mL), P. aeruginosa No.2 (7.81μg/mL), P. aeruginosa No.3 (7.81 μg/mL), P. aeruginosa No.4 (7.81 μg/mL), P. aeruginosa No.5 (7.81 μg/mL), P. aeruginosa No.6 (7.81 μg/mL), P. aeruginosa No.7 (7.81 μg/mL), P. aeruginosa No.8 (7.81 μg/mL), P. aeruginosa No.9 (7.81 μg/mL), P. aeruginosa No.10 (7.81 μg/mL), P. aeruginosa No.11 (7.81 μg/mL), P. aeruginosa No.12 (3.91 μg/mL), P. aeruginosa No.13 (15.63 μg/mL), P. aeruginosa No.14 (7.81 μg/mL),##Gram-positive bacteria:Staphylococcus aureus ATCC 25923 (MIC = 62.5 µg/ml) Staphylococcus epidermidis ATCC 12228 (MIC = 3.91 µg/ml), Bacillus cereus ATCC 11778 (MIC = 15.63 µg/ml), Enterococcus faecalis ATCC 29212 (MIC = 250 µg/ml), Listeria monocytogenes 10403 s (MIC = 3.91 µg/ml)" [Ref.32499514]MHC = 125 μg/mL. Note:MHC is the minimum concentration that caused 10% hemolysis of human red blood cells (hRBC). When no 10% hemolysis was observed at 250 µg/ml, a value of 500 µg/ml was used to calculate the therapeutic index. Linear Free Amidation L [Ref.32499514]Cytotoxic activity of PA-13 against the L929 mouse fibroblast cell line was determined by a colorimetric MTT viability assay. At the MIC (3.91 µg/ml), the cell survival was up to 90%. Even at the maximum concentration (250 µg/ml), the survival was common (81.29%). Melittin, used as a positive control, showed a strong and dose-dependent cytotoxic effect; no living cells were detected at 62.5 µg/ml. Peptide PA-13 displayed very little cytotoxicity on L929 cells when compared to melittin. Membrane 32499514 Sci Rep. 2020 Jun 4;10(1):9117. doi: 10.1038/s41598-020-65688-5. Klubthawee N, Adisakwattana P, Hanpithakpong W, Somsri S, Aunpad R A novel, rationally designed, hybrid antimicrobial peptide, inspired by cathelicidin and aurein, exhibits membrane-active mechanisms against Pseudomonas aeruginosa DRAMP29049 ALLKRIKTLL 10 Ano-1β (variant of Anoplin) No entry found Not found Synthetic construct (Ano-1β is a variant of Anoplin, which is a linear cationic α-helical AMPs isolated from the venom sac of anoplius samariensis(solitary spider wasps)) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form 75.3% α-helical content in 30 mM SDS As shown in Fig. 1, the new peptides displayed mostly unordered conformations in the aqueous environment as demonstrated by a negative peak at approximately 195 nm. However, in 30 mM SDS, the new peptides folded typical α-helical conformations, as evidenced by a characteristic positive peak at approximately 195 nm and double negative peaks at approximately 208 nm and 222 nm.  Comment: the incorporation of β-Ala had significant influence on the antimicrobial activity of peptides mainly due to the changes of hydrophobicity and net positive charge. Ano-1β exhibited good antimicrobial potency, which was stable under physiological conditions and displayed preferable in vivo antimicrobial activity with less acute toxicity. In particular, Ano-1β showed low tendency to develop bacterial resistance in contrast to conventional antibiotics rifampicin and gentamicin, and they exhibited better anti-biofilm activity and synergistic or additive effects in combination with conventional antibiotics. Ano-1β might stands as a promising antimicrobial candidate to overcome increasing bacterial resistance, and the incorporation of β-Ala was a reasonable strategy for the development of promising antimicrobial agents. [Ref.32654770] Gram-negative multidrug-resistant bacteria: P. aeruginosa 119 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa 124 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa 86 (MIC = 4 μM or 4.47 μg/mL); ##Gram-negative bacteria: P. aeruginosa ATCC 27853 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa ATCC 9027 (MIC = 8 μM or 8.93 μg/mL), E. coli ATCC 25922 (MIC = 32 μM or 35.72 μg/mL), K. pneumonia ATCC 700603 (MIC = 32 μM or 35.72 μg/mL), A. baumannii ATCC 19606 (MIC = 64 μM or 71.44 μg/mL); ##Gram-positive bacteria: S. aureus ATCC 25923 (MIC = 128 μM or 142.88 μg/mL), S. epidermidis ATCC 12228 (MIC = 8 μM or 8.93 μg/mL) [Ref.32654770]Ano-1β induced inappreciable hemolytic activity with less than 5 % hemolysis at all the tested concentrations and HC > 256 μM. Note: Minimum hemolysis concentration (HC, μM) was defined as the minimal peptide concentration induced 10 % hemolysis. Linear Free Amidation [Ref.32654770] The residue A at position 1 indicates the β-Ala L [Ref.32654770]After 1 h of incubation, Ano-1β, similar to their parent peptide anoplin, maintained more than 80 % cell viability of the two cells at all tested concentrations. After incubating for 24 h, Ano-1β still maintained more than 80 % cell viability of HEK 293 T cells at all tested concentrations but displayed cytotoxicity against Hela cells at the highest concentration (256 μM). The cell viability of Hela after 24 h of incubation is around 80%. Membrane 32654770 Int J Med Microbiol. 2020 Jul;310(5):151433. doi: 10.1016/j.ijmm.2020.151433. Epub 2020 May 27. Zhong C, Zhu Y, Zhu N, Liu T, Gou S, Zhang F, Yao J, Xie J, Ni J Synthesis and anti-pseudomonal activity of new ß-Ala modified analogues of the antimicrobial peptide anoplin DRAMP29050 GLLKRIKALL 10 Ano-8β (variant of Anoplin) No entry found Not found Synthetic construct (Ano-1β is a variant of Anoplin, which is a linear cationic α-helical AMPs isolated from the venom sac of anoplius samariensis(solitary spider wasps)) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form 72.82% α-helical content in 30 mM SDS As shown in Fig. 1, the new peptides displayed mostly unordered conformations in the aqueous environment as demonstrated by a negative peak at approximately 195 nm. However, in 30 mM SDS, the new peptides folded typical α-helical conformations, as evidenced by a characteristic positive peak at approximately 195 nm and double negative peaks at approximately 208 nm and 222 nm.  Comment: the incorporation of β-Ala had significant influence on the antimicrobial activity of peptides mainly due to the changes of hydrophobicity and net positive charge. Ano-8β exhibited good antimicrobial potency, which was stable under physiological conditions and displayed preferable in vivo antimicrobial activity with less acute toxicity. In particular, Ano-8β showed low tendency to develop bacterial resistance in contrast to conventional antibiotics rifampicin and gentamicin, and they exhibited better anti-biofilm activity and synergistic or additive effects in combination with conventional antibiotics. Ano-8β might stands as a promising antimicrobial candidate to overcome increasing bacterial resistance, and the incorporation of β-Ala was a reasonable strategy for the development of promising antimicrobial agents. [Ref.32654770] Gram-negative multidrug-resistant bacteria: P. aeruginosa 119 (MIC = 8 μM or 9.00 μg/mL), P. aeruginosa 124 (MIC = 16 μM or 17.98 μg/mL), P. aeruginosa 86 (MIC = 8 μM or 9.00 μg/mL); ##Gram-negative bacteria: P. aeruginosa ATCC 27853 (MIC = 4 μM or 4.50 μg/mL), P. aeruginosa ATCC 9027 (MIC = 8 μM or 9.00 μg/mL), E. coli ATCC 25922 (MIC = 32 μM or 36 μg/mL), K. pneumonia ATCC 700603 (MIC = 128 μM or 144 μg/mL), A. baumannii ATCC 19606 (MIC > 128 μM or 144 μg/mL); ##Gram-positive bacteria: S. aureus ATCC 25923 (MIC = 128 μM or 144 μg/mL), S. epidermidis ATCC 12228 (MIC = 16 μM or 18 μg/mL) [Ref.32654770]Ano-8β induced inappreciable hemolytic activity with less than 5 % hemolysis at all the tested concentrations and HC > 256 μM. Note: Minimum hemolysis concentration (HC, μM) was defined as the minimal peptide concentration induced 10 % hemolysis. Linear Free Amidation [Ref.32654770] The residue A at position 8 indicates the β-Ala L [Ref.32654770]After 1 h of incubation, Ano-8β, similar to their parent peptide anoplin, maintained more than 80 % cell viability of the two cells at all tested concentrations. After incubating for 24 h, Ano-8β still maintained more than 80 % cell viability of HEK 293 T cells at all tested concentrations but displayed cytotoxicity against Hela cells at the highest concentration (256 μM). The cell viability of Hela after 24 h of incubation is around 70% Membrane 32654770 Int J Med Microbiol. 2020 Jul;310(5):151433. doi: 10.1016/j.ijmm.2020.151433. Epub 2020 May 27. Zhong C, Zhu Y, Zhu N, Liu T, Gou S, Zhang F, Yao J, Xie J, Ni J Synthesis and anti-pseudomonal activity of new ß-Ala modified analogues of the antimicrobial peptide anoplin DRAMP29051 KKRLKKIFKKPMVIGVTIPF 20 Ctn[15-34] (C-terminal fragment of crotalicidin) U5KJM4 Belongs to the cathelicidin family. Crotalus durissus terrificus (South American rattlesnake) Antimicrobial, Antifungal Protein level α-helical preserves helicity Comment: Ctn[15-34] showed to be an effective antifungal peptide, displaying antibiofilm activity and, importantly, interacting with and disrupting fungal plasma membrane. Function: Potent antimicrobial peptide against Gram-negative (P.aeruginosa, K.pneumoniae, E.coli, A.baumannii) (PubMed:25100358, PubMed:26465972). Shows moderate activities against Gram-positive bacteria (E.faecalis, S.aureus, S.pyogenes) (PubMed:25100358, PubMed:26465972). Also shows antifungal activity against standard and clinical isolates of yeasts (MIC=10-40 µM) and dermatophytes (MIC=1-5 µM) (PubMed:27876749). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane (PubMed:26465972). Shows high toxicity towards human fibroblasts (micromolar ranges) (PubMed:26465972). Shows low hemolytic activities on human erythrocytes (PubMed:25100358, PubMed:26465972). Also shows toxicity (micromolar ranges) when tested on many leukemia cell lines (PubMed:26465972). In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote) by inducing cell death through necrosis (PubMed:29208061). [Ref.33172206] Fungi: Candida albicans ATCC 90028 (MIC = 10 µM or 23.7 µg/mL), Candida albicans LABMIC 0125 (MIC = 10 µM or 23.7 µg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L Not found Fungal plasma membrane 33172206 Int J Mol Sci. 2020 Nov 6;21(21):8339. doi: 10.3390/ijms21218339. Aguiar FLL, Santos NC, de Paula Cavalcante CS, Andreu D, Baptista GR, Gonçalves S. Antibiofilm Activity on Candida albicans and Mechanism of Action on Biomembrane Models of the Antimicrobial Peptide Ctn[15-34] DRAMP29052 FLGALFKVASKLVPAAICSISKKC 24 Brevinin-1GHd A0A6M4CA40 Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily Sylvirana guentheri (Gunther's frog) (Rana guentheri) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Transcript level α-helical The results of CD spectroscopy revealed that Brevinin-1GHd adopt a random coil structure in an aqueous environment, while forming an alpha-helix structure in a membrane-mimetic environment. "Comment: Brevinin-1GHd with its excellent antimicrobial and anticancer activities is a promising candidate for a novel antibiotic agent, and study of its structure activity relationships also provided a rational template for further research and peptide analog design. In the reference, the example of Brevinin-1GHd is used to challenge the importance of ""Rana-Box"", which appears in many AMPs originating from frogs and contains an intermolecular disulfide bridge at the C-terminus of the peptide and seven to nine amino acid residues." [Ref.32347293] Gram-positive bacteria: S. aureus (MIC = 2 μM/MBC= 4 µM), MRSA(MIC = 4 μM/MBC = 4µM); ##Gram-negative: E. coli(MIC = 8 μM/MBC = 8 µM), P. aeruginosa(MIC = 32 μM/MBC = 32µM); ##Fungi: C. albicans(MIC = 4 μM/MBC = 8µM） [Ref.32347293] Brevinin-1GHd displayed 13% hemolysis on horse red blood cells at its highest MIC/MBC value of the tested bacteria P. aeruginosa (32 µM). However, when the concentration increased above 64 μM, the hemolytic activity of Brevinin-1GHd also gradually increased. At the concentration of 64, 128, 256 and 512 μM, it displayed about 36%, 64%, 83% and 108% hemolysis. Cyclic Free Free Free L [Ref.32347293]Brevinin-1GHd showed significant cytotoxicity toward human HMEC-1 and HaCaT cells at concentrations of 0.00001 and 0.0001 M, respectively. Brevinin-1GHd induced one cell viability of 56% on HMEC-1 and the other cell viability of 75% on HaCat. Cell membrane 32347293 Biosci Rep. 2020 May 29;40(5):BSR20200019. doi: 10.1042/BSR20200019. Jiang Y, Wu Y, Wang T, Chen X, Zhou M, Ma C, Xi X, Zhang Y, Chen T, Shaw C, Wang L. Brevinin-1GHd: a novel Hylarana guentheri skin secretion-derived Brevinin-1 type peptide with antimicrobial and anticancer therapeutic potential DRAMP29053 AKLIPTIAL 9 RcAlb-PepI (designed in silico using as template the amino acid sequence of Rc-2S-Alb) No entry found Not found Synthetic construct (Rc-2S-Alb comes from Ricinus communis (Castor bean)) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Partially ordered (non-regular) and α-helical RcAlb-PepI and RcAlb-PepII in aqueous solution showed SRCD spectra typical of peptides that present major unordered content of secondary structure. The small (albeit significant) shift of the minimum for the RcAlb-PepII spectrum showed a more partially ordered peptide (although non-canonical) compared with RcAlb-PepI. The SRCD spectra of RcAlb-PepI and RcAlb-PepII in the film were characteristics of partially ordered (non-regular) and α-helix secondary structures. Comment: RcAlb-PepI is safe and apparently effective for its intended use and has great potential for the future development of an antimicrobial agent with the ability to kill or inhibit K. pneumoniae and C. parapsilosis cells. [Ref.31678367] Gram-negative bacteria: E. coli (MIC50 = 102 μM, MIC90 > 250 μM, MBC > 250 μM), K. pneumoniae(MIC50 = 121 μM, MIC90 > 250 μM, MBC > 250 μM)##Gram-positive bacteria: S. aureus (MIC50 = 123 μM, MIC90 > 250 μM, MBC > 250 μM)##Yeast: C. albicans (MIC50 = 62 μM, MIC90 > 250 μM, MFC > 250 μM), C. parapsilosis (MIC50 = 14 μM, MIC90 = 32 μM, MFC = 103 μM), C. tropicalis (MIC50 = 21 μM, MIC90 = 38 μM, MFC = 127 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L Not found Not found 31678367 Biochim Biophys Acta Biomembr. 2020 Feb 1;1862(2):183092. doi: 10.1016/j.bbamem.2019.183092. Epub 2019 Oct 31. Dias LP, Souza PFN, Oliveira JTA, Vasconcelos IM, Araújo NMS, Tilburg MFV, Guedes MIF, Carneiro RF, Lopes JLS, Sousa DOB RcAlb-PepII, a synthetic small peptide bioinspired in the 2S albumin from the seed cake of Ricinus communis, is a potent antimicrobial agent against Klebsiella pneumoniae and Candida parapsilosis DRAMP29054 SLRGCC 6 RcAlb-PepII (designed in silico using as template the amino acid sequence of Rc-2S-Alb) No entry found Not found Synthetic construct (Rc-2S-Alb comes from Ricinus communis (Castor bean)) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Partially ordered (non-regular) and α-helical RcAlb-PepI and RcAlb-PepII in aqueous solution showed SRCD spectra typical of peptides that present major unordered content of secondary structure. The small (albeit significant) shift of the minimum for the RcAlb-PepII spectrum showed a more partially ordered peptide (although non-canonical) compared with RcAlb-PepI. The SRCD spectra of RcAlb-PepI and RcAlb-PepII in the film were characteristics of partially ordered (non-regular) and α-helix secondary structures. Comment: RcAlb-PepII is safe and apparently effective for its intended use and has great potential for the future development of an antimicrobial agent with the ability to kill or inhibit K. pneumoniae and C. parapsilosis cells. [Ref.31678367] Gram-negative bacteria: E. coli (MIC50 = 31 μM, MIC90 = 29 μM, MBC > 250 μM), K. pneumoniae(MIC50 = 11 μM, MIC90 = 21 μM, MBC = 42 μM)##Gram-positive bacteria: S. aureus (MIC50 = 79 μM, MIC90 > 250 μM, MBC > 250 μM)##Yeast: C. albicans (MIC50 = 129 μM, MIC90 > 250 μM, MFC > 250 μM), C. parapsilosis (MIC50 = 9 μM, MIC90 = 17 μM, MFC = 25 μM), C. tropicalis (MIC50 = 29 μM, MIC90 = 28 μM, MFC = 67 μM) [Ref.31678367] RcAlb-PepII was not harmful to human erythrocytes, even at a concentration 10 times higher than the MBC and MFC for K. pneumoniae and C. parapsilosis, respectively. Linear Free Free L [Ref.31678367] At 420 μM concentration (10 and 16.8 times higher than the MBC and MFC for K. pneumoniae and C. parapsilosis, respectively) RcAlb-PepII reduced only in 21.5% the Vero cell viability Intracellular targets 31678367 Biochim Biophys Acta Biomembr. 2020 Feb 1;1862(2):183092. doi: 10.1016/j.bbamem.2019.183092. Epub 2019 Oct 31. Dias LP, Souza PFN, Oliveira JTA, Vasconcelos IM, Araújo NMS, Tilburg MFV, Guedes MIF, Carneiro RF, Lopes JLS, Sousa DOB RcAlb-PepII, a synthetic small peptide bioinspired in the 2S albumin from the seed cake of Ricinus communis, is a potent antimicrobial agent against Klebsiella pneumoniae and Candida parapsilosis DRAMP29055 FFPVIGRILNGIL 13 temporin G P79875 Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily. Rana temporaria (European common frog) Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antibiofilm Protein level Amphipathic alpha-helical (Uniprot:P79875) Not found Function: Amphipathic alpha-helical antimicrobial peptide with activity against Gram-positive bacteria (M.luteus), Gram-negative bacteria (E.coli), and fungi (S.cerevisiae) (PubMed:22439858). Stimulates insulin release from pancreatic beta-cells in a dose-dependent manner, without increasing intracellular calcium (PubMed:29349894). Does not protects BRIN-BD11 beta-cells against cytokine-induced apoptosis (PubMed:29349894). In vivo, intraperitoneal injection together with a glucose load into mice improves glucose tolerance with a concomitant increase in insulin secretion (PubMed:29349894). [Ref.33321906] S. aureus ATCC 25923 biofilm: TG was capable of killing at least 39%, 78% and 87% at 3.12, 6.25, 12.5 and 25 µM. ##[Ref.22439858] Summary: TG had specific bactericidal activities against E. coli ATCC2592, M. luteus or S. cerevisiae. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.33321906]TG was shown to be harmless against human keratinocytes at all concentrations tested with a slight cytotoxicity (~20% reduction of metabolically-active cells) at the highest active concentration Not found 33321906##22439858 Int J Mol Sci. 2020 Dec 10;21(24):9410. doi: 10.3390/ijms21249410.##BMC Biotechnol. 2012 Mar 23;12:10. doi: 10.1186/1472-6750-12-10. Casciaro B, Loffredo MR, Cappiello F, Fabiano G, Torrini L, Mangoni ML##Tao Ke, Su Liang, Jin Huang, Han Mao, Jibao Chen, Caihua Dong, Junyan Huang, Shengyi Liu, Jianxiong Kang, Dongqi Liu, Xiangdong Ma The Antimicrobial Peptide Temporin G: Anti-Biofilm, Anti-Persister Activities, and Potentiator Effect of Tobramycin Efficacy Against Staphylococcus aureus.##A novel PCR-based method for high throughput prokaryotic expression of antimicrobial peptide genes DRAMP29056 LRCMCIKWWSGKHPK 15 TC19 (derived from the human thrombocidin-1-derived peptide L3) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form Not found Not found Comment: TC19 combined low cytotoxicity towards human fibroblasts with efficient and rapid killing in human plasma of MDR strains of several bacterial species of the ESKAPE panel. However, the hemolytic activity data and secondary structure is missing. [Ref.32376222] Gram-positive bacteria: E. coli ESBL (LC99.9 = 3.75 μM in PT buffer, LC99.9 = 15 μM in PBS buffer); ##Gram-negative bacteria: S. aureus JAR060131 (LC99.9 = 3.75 μM in PT buffer, LC99.9 = 7.5-15 μM in PBS buffer, LC99.9 = 15-30 μM in 50% plasma).##Multi-drug resistant (MDR) gram-positive bacteria: E.faecium LUH10330 (LC99.9 = 1.6(1.6-3.2) μM in PBS buffer, LC99.9 =6.4 (3.2-6.4) μM in 50% plasma), S.aureus LUH14616 (LC99.9 = 3.2(3.2-6.4) μM in PBS buffer, LC99.9 = 12.8 (3.2-12.8) μM in 50% plasma).##Multi-drug resistant (MDR) and pan-drug resistant (PDR) gram-negative bacteria: K.pneumoniae LUH8995 (LC99.9 = 1.6(0.8-1.6) μM in PBS buffer, LC99.9 = 3.2 μM in 50% plasma), A.baumannii RUH875 (LC99.9 = 1.6(1.6-3.2) μM in PBS buffer, LC99.9 =6.4 (6.4-12.8) μM in 50% plasma), P.aeruginosa LUH15100 (LC99.9 = 4.8(3.2-6.4) μM in PBS buffer, LC99.9 > 204.8 μM in 50% plasma), E.cloacae LUH15114 (LC99.9 = 25.6 μM in PBS buffer, LC99.9 = 204.8 μM in 50% plasma)##Note: Results are expressed as the lethal concentration (LC) 99.9%, i.e. the lowest peptide concentration that resulted in >= 99.9% killing of bacteria after 2 h of incubation in PT buffer (10 mM phosphate buffer, pH 7.0, with 1% (v/v) TSB), phosphate buffered saline (PBS, pH 7.4) and in PBS with 50% (v/v) human plasma (one experiment, performed in duplicate). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.32891601]Up to 40 μM TC19 did not permeabilize human fibroblasts, whereas at 80 μM an increase in PI-positivity was recorded after 4 h of exposure. After 4h of incubation with TC19 at indicated concentration (80 μM), PI-uptake by normal human dermal fibroblasts (NHDF) had increased from 5% to 20% comparing to the result after 1h of incubation. Bacterial membrane 32376222 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183282. doi: 10.1016/j.bbamem.2020.183282. Epub 2020 May 3. Riool M, de Breij A, Kwakman PHS, Schonkeren-Ravensbergen E, de Boer L, Cordfunke RA, Malanovic N, Drijfhout JW, Nibbering PH, Zaat SAJ. Thrombocidin-1-derived antimicrobial peptide TC19 combats superficial multi-drug resistant bacterial wound infections DRAMP29057 RIVQRIKKWLLKWKKLGY 18 P5 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical Not found Comment: This new peptide could be good candidates for future drug development for anti-biofilm and anti-infective therapy. [Ref.31778756] Gram-negative bacteria: P. aeruginosa (MIC = 64 μg/mL, MBC = 128 μg/mL); ##Gram-positive bacteria: S. aureus (MIC = 16 µg/mL, MBC = 64 μg/mL) [Ref.31778756]P5 displayed less than 10% hemolysis in all the range tested (0-1024 μg/mL) Linear Free Free L Not found Bacterial cytoplasmic membranes 31778756 Microb Pathog. 2020 Feb;139:103886. doi: 10.1016/j.micpath.2019.103886. Epub 2019 Nov 25. Martínez M, Polizzotto A, Flores N, Semorile L, Maffía PC Antibacterial, anti-biofilm and in vivo activities of the antimicrobial peptides P5 and P6.2 DRAMP29058 KGLLRKWGKKWKEFLRRVW 19 P6.2 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram- Synthetic form α-helical Not found Comment: This new peptide could be good candidates for future drug development for anti-biofilm and anti-infective therapy. [Ref.31778756] Gram-negative bacteria: P. aeruginosa (MIC = 16 μg/mL, MBC = 32 μg/mL); ##Gram-positive bacteria: S. aureus (MIC = 32 µg/mL, MBC = 128 μg/mL) [Ref.31778756]P6.2 exhibited a concentration dependent hemolytic activity, reaching values of 30% at the highest concentration(1024 μg/mL), but remaining below 5% until 128 μg/ml, which is fourfold or eightfold the MIC obtained for S.aureus or P.aeruginosa, respectively. Linear Free Free L Not found Bacterial cytoplasmic membranes 31778756 Microb Pathog. 2020 Feb;139:103886. doi: 10.1016/j.micpath.2019.103886. Epub 2019 Nov 25. Martínez M, Polizzotto A, Flores N, Semorile L, Maffía PC Antibacterial, anti-biofilm and in vivo activities of the antimicrobial peptides P5 and P6.2 DRAMP29059 FLQRIIGALGRLF 13 temporin-GHaR No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form α-helical Not found Comment: It showed potent antimicrobial activity with strong hemolytic toxicity [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 1.6μM / 1.6μM), B. subtilis(MIC / MBC = 12.5μM / 25μM), S. mutans(MIC / MBC = 3.1μM / 6.2μM), MRSA(MIC / MBC = 3.1μM / 3.1μM), MRSA-1(MIC /MBC = 3.1μM / 25μM), MRSA-2(MIC / MBC = 6.2μM / 12.5μM), MRSA-3(MIC / MBC = 3.1μM /6.2μM)##Gram-negative bacteria: E. coli(MIC / MBC = 6.2μM / 6.2μM), D31(MIC /MBC = 12.5μM / 25μM), P. aeruginosa(MIC / MBC = 6.2μM / 6.2μM), PAO1(MIC / MBC = 25μM / 50μM)##Fungi: C. albicans(MIC / MBC = 12.5μM / 50μM) [Ref.33291521]HL50 = 48μM against human red blood cells (hRBCs) Linear Free Free L Not found Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29060 FLQRIRGALGRLF 13 GHaR6R (variant of temporin-GHaR) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form α-helical Not found Comment: GHaR6R not only exerted antimicrobial activity by destroying cell membranes of planktonic bacteria, but also exhibited anti-biofilm activity. The low-toxicity peptides of GHaR6R is expected to become promising antimicrobial candidate to develop anti-caries agents. [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 3.1μM / 12.5μM), B. subtilis(MIC / MBC = 25μM / 50μM), S. mutans(MIC / MBC = 12.5μM / 12.5μM), MRSA(MIC / MBC = 6.2μM / 12.5μM), MRSA-1(MIC /MBC = 12.5μM / 25μM), MRSA-2(MIC / MBC = 12.5μM / 25μM), MRSA-3(MIC / MBC = 6.2μM / 25μM)##Gram-negative bacteria: E. coli(MIC / MBC = 12.5μM / 12.5μM), D31(MIC /MBC = 25μM / 50μM), P. aeruginosa(MIC / MBC > 50μM / 50μM), PAO1(MIC / MBC = 3.1μM / 25μM)##Fungi: C. albicans(MIC / MBC = 50μM / 50μM) [Ref.33291521]HL10 = 150μM against human red blood cells (hRBCs) Linear Free Free L [Ref.33291521]GHaR6R induced a cell viability of 98%, 95% and 83% to human oral epithelial cells at 3.1μM, 6.2μM and 12.5μM. Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29061 FLQRIIRALGRLF 13 GHaR7R (variant of temporin-GHaR) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form α-helical Not found Comment: GHaR6R not only exerted antimicrobial activity by destroying cell membranes of planktonic bacteria, but also exhibited anti-biofilm activity. However, the hemolysis and cytotoxicity to HOECs of GHaR7R is too strong to make it not suitable be a good antimicrobial candidate [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 3.1μM / 3.1μM), B. subtilis(MIC / MBC > 50μM / 50μM), S. mutans(MIC / MBC = 6.2μM / 12.5μM), MRSA(MIC / MBC = 3.1μM / 6.2μM), MRSA-1(MIC /MBC = 6.2μM / 25μM), MRSA-2(MIC / MBC = 6.2μM / 50μM), MRSA-3(MIC / MBC = 6.2μM / 25μM)##Gram-negative bacteria: E. coli(MIC / MBC = 3.1μM / 12.5μM), D31(MIC /MBC = 12.5μM / 50μM), P. aeruginosa(MIC / MBC > 50μM / 50μM), PAO1(MIC / MBC > 50μM / 50μM)##Fungi: C. albicans(MIC / MBC = 25μM / 25μM) [Ref.33291521]HL50 = 10μM against human red blood cells (hRBCs) Linear Free Free L [Ref.33291521]GHaR6R induced a cell viability of 62%, 50% and 39% to human oral epithelial cells at 3.1μM, 6.2μM and 12.5μM. Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29062 FLQRIIGRLGRLF 13 GHaR8R (variant of temporin-GHaR) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form α-helical Not found Comment: GHaR6R not only exerted antimicrobial activity by destroying cell membranes of planktonic bacteria, but also exhibited anti-biofilm activity. The low-toxicity peptides of GHaR6R is expected to become promising antimicrobial candidate to develop anti-caries agents. [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 1.6-3.1μM / 3.1μM), B. subtilis(MIC / MBC = 12.5μM / 12.5μM), S. mutans(MIC / MBC = 6.2μM / 6.2μM), MRSA(MIC / MBC = 3.1μM / 3.1μM), MRSA-1(MIC /MBC = 6.2μM / 6.2μM), MRSA-2(MIC / MBC = 3.1μM / 12.5μM), MRSA-3(MIC / MBC = 6.2μM / 12.5μM)##Gram-negative bacteria: E. coli(MIC / MBC = 3.1μM / 3.1μM), D31(MIC /MBC = 12.5μM / 25μM), P. aeruginosa(MIC / MBC > 50μM / 50μM), PAO1(MIC / MBC = 6.2μM / 12.5μM)##Fungi: C. albicans(MIC / MBC = 12.5μM / 12.5μM) [Ref.33291521]HL50 = 160μM against human red blood cells (hRBCs) Linear Free Free L [Ref.33291521]GHaR6R induced a cell viability of 83%, 64% and 50% to human oral epithelial cells at 3.1μM, 6.2μM and 12.5μM. Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29063 FLQRIIGARGRLF 13 GHaR9R (variant of temporin-GHaR) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form Not found the α-helical structure of GHaR9R was destroyed Comment: The antimicorbial activity of GHaR9R is bad comparing to other temporin-GHaR modified peptides. [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 6.2μM / 12.5μM), B. subtilis(MIC / MBC > 50μM / 50μM), S. mutans(MIC / MBC > 50μM / 50μM), MRSA(MIC / MBC > 50μM / 50μM), MRSA-1(MIC / MBC > 50μM / 50μM), MRSA-2(MIC / MBC > 50μM / 50μM), MRSA-3(MIC / MBC > 50μM / 50μM)##Gram-negative bacteria: E. coli(MIC / MBC > 50μM / 50μM), D31(MIC / MBC > 50μM / 50μM), P. aeruginosa(MIC / MBC > 50μM / 50μM), PAO1(MIC / MBC > 50μM / 50μM)##Fungi: C. albicans(MIC / MBC > 50μM / 50μM) [Ref.33291521]GHaR9R didn t show hemolytic toxicity even when the concentration was raised up to 200 μM. Linear Free Free L Not found Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29064 FLQRIIGAWGRLL 13 GHaR9W (variant of temporin-GHaR) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form α-helical Not found Comment: GHaR6R not only exerted antimicrobial activity by destroying cell membranes of planktonic bacteria, but also exhibited anti-biofilm activity. The low-toxicity peptides of GHaR6R is expected to become promising antimicrobial candidate to develop anti-caries agents. [Ref.33291521] Gram-positive bacteria: S. aureus(MIC / MBC = 3.1μM / 6.2μM), B. subtilis(MIC / MBC = 12.5μM / 50μM), S. mutans(MIC / MBC = 6.2μM / 6.2μM), MRSA(MIC / MBC = 6.2μM / 12.5μM), MRSA-1(MIC / MBC = 6.2μM / 12.5μM), MRSA-2(MIC / MBC = 6.2μM / 12.5μM), MRSA-3(MIC / MBC = 6.2μM / 12.5μM)##Gram-negative bacteria: E. coli(MIC / MBC = 12.5μM / 12.5μM), D31(MIC /MBC = 12.5μM / 50μM), P. aeruginosa(MIC / MBC > 50μM / 50μM), PAO1(MIC / MBC = 25μM / 50μM)##Fungi: C. albicans(MIC / MBC = 25μM / 25μM) [Ref.33291521]HL50 = 90μM against human red blood cells (hRBCs) Linear Free Free L [Ref.33291521]GHaR6R induced a cell viability of 74%, 63% and 60% to human oral epithelial cells at 3.1μM, 6.2μM and 12.5μM. Cell membrane 33291521 Molecules. 2020 Dec 4;25(23):5724. doi: 10.3390/molecules25235724. Wei H, Xie Z, Tan X, Guo R, Song Y, Xie X, Wang R, Li L, Wang M, Zhang Y Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis DRAMP29065 KTMMQSGGTFGTFMAIGMGIR 21 AMPR-11(derived from Romo1) P60602 Belongs to the MGR2 family. ROMO1 Homo sapiens (Human) Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Protein level α-helical AMPR-11 formed a random coil structure in distilled water but formed an ordered conformation in 50% hexafluoro-2-propanol (HFIP), which has been used for implementing a membrane-mimic environment Comment: AMP derived from Romo1 (AMPR-11) is a promising agent for treatment of sepsis caused by MDR bacteria, and AMPR-11 could be combined with other potential antibiotics for clinical treatment. [Ref.33291307] Gram-positive bacteria: S. aureus(MBC=100 μg/mL), B. subtilis(MBC=90 μg/mL), E. faecium(MBC=85 μg/mL), S. sindenensis(MBC=95 μg/mL), E. faecalis(MBC=85 μg/mL), S. pneumoniae(MBC=100 μg/mL)##Gram-negative bacteria: E. coli(MBC=85 μg/mL), P. aeruginosa(MBC=100 μg/mL), K. pneumoniae(MBC=100 μg/mL), A. baumannii(MBC=100 μg/mL), E. aerogenes(MBC=90 μg/mL)##Multi-drug resistant bacteria: Methicillin-resistant S. aureus(MBC=100 μg/mL), Carbapenem-resistant P. aeruginosa(MBC=110 μg/mL), Carbapenem-resistant A. baumannii(MBC=110 μg/mL), Carbapenem-resistant K. pneumoniae(MBC=100 μg/mL), Vancomycin-resistant S. aureus(MBC=120 μg/mL), Vancomycin-resistant E. faecium(MBC=100 μg/mL ) [Ref.33291307]At the concentration of 32 μg/mL, AMPR-11 induced a hemolysis of 20% on mouse red blood cells; At the concentration of 256 μg/mL, AMPR-11 induced a hemolysis of 23%. Linear Free Free L [Ref.33291307] ①The cell viability of HeLa cells was 90%, 87%, 83% and 79% at the concentration of 32, 64, 128 and 256 μg/mL. ②The cell viability of HEK293 cells was 86%, 83%, 80% and 78% at the concentration of 32, 64, 128 and 256 μg/mL. ③The cell viability of HeLa cells was 89%, 86%, 83% and 80% at the concentration of 32, 64, 128 and 256 μg/mL. Bacterial membrane 32291307 mBio. 2020 Apr 14;11(2):e03258-19. doi: 10.1128/mBio.03258-19. Lee HR, You DG, Kim HK, Sohn JW, Kim MJ, Park JK, Lee GY, Yoo YD Romo1-Derived Antimicrobial Peptide Is a New Antimicrobial Agent against Multidrug-Resistant Bacteria in a Murine Model of Sepsis DRAMP29066 GFAWNVCVYRNGVRVCHRRAN 21 Marine peptide-N6 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form β-turn, coil and antiparallel sheet ①The structure analysis showed that N6 have one rigid disulfide bridge Cys7-Cys16, which links the two β-strands (Cys3-Asn10 and Arg13-Cys20) and forms an anti-parallel β-sheet. ②The secondary structures of N6NH2 and N6 in ddH2O were characterized by a coil and antiparallel strand or β-turn with a negative minimum at 200 nm. N6NH2 showed a more significant increase in α-helix and antiparallel strand in SDS solution than N6. Similarly, the CD spectrum of N6 and N6NH2 in 50% TFE showed one negative dichroic band at approximately 205 nm, and the positive maximum at 180 nm (strong) and at 230 nm 5Y0H Comment: N6NH2 and N6 are different from common antimicrobial peptides in the secondary structure. N6 has good antimicrobial activity. [Ref.33348729] Gram-negative bacteria: Edwardsiella tarda(MIC = 6.4 μg/mL), Aeromonas veronii(MIC = 6.4 μg/mL), Escherichia coli CVCC195(MIC = 0.5 μg/mL), E. coli CVCC1515(MIC = 1 μg/mL), E. coli CVCC25922(MIC = 0.25 μg/mL), E. coli CVCCO157(MIC = 0.5 μg/mL), Salmonella typhimurium CVCC533(MIC = 1 μg/mL), S. typhimurium ATCC14028(MIC = 2 μg/mL), S. enteritidis CVCC3377(MIC = 0.25 μg/mL), S. pullorum CVCC1802(MIC = 0.5 μg/mL), S. pullorum CVCC1789(MIC = 0.5 μg/mL), Pseudomonas aeruginosa CICC21630(MIC = 4 μg/mL). ##Gram-positive bacteria: Staphylococcus aureus ATCC43300(MIC = 16 μg/mL), S. aureus ATCC546(MIC = 4 μg/mL), S. aureus ATCC25923(MIC = 0.25 μg/mL), S. hyicus 437-2(MIC = 64 μg/mL), S. hyicus 15095(MIC = 16 μg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There is a disulfide bond between Cys7 and Cys16 L [Ref.33348729]Had very low cytotoxicity to mouse peritoneal RAW 264.7 macrophages (cell survival rate >93.35%) Lipopolysaccharide (LPS) and genomic DNA 33348729 Mar Drugs. 2020 Dec 17;18(12):650. doi: 10.3390/md18120650. Han H, Li T, Wang Z, Teng D, Mao R, Hao Y, Yang N, Wang X, Wang J. Improved Stability and Activity of a Marine Peptide-N6NH2 against Edwardsiella tarda and Its Preliminary Application in Fish DRAMP29067 GFAWNVCVYRNGVRVCHRRAN 21 N6NH2 (N6 amidated at its C-terminus) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form β-turn, coil and antiparallel sheet ①The structure analysis showed that N6 have one rigid disulfide bridge Cys7-Cys16, which links the two β-strands (Cys3-Asn10 and Arg13-Cys20) and forms an anti-parallel β-sheet. ②The secondary structures of N6NH2 and N6 in ddH2O were characterized by a coil and antiparallel strand or β-turn with a negative minimum at 200 nm. N6NH2 showed a more significant increase in α-helix and antiparallel strand in SDS solution than N6. Similarly, the CD spectrum of N6 and N6NH2 in 50% TFE showed one negative dichroic band at approximately 205 nm, and the positive maximum at 180 nm (strong) and at 230 nm 5Y0H Comment: In the model of fish peritonitis caused by E. tarda, superior to norfloxacin, N6NH2 improved the survival rate of fish, reduced the bacterial load on the organs, alleviated the organ injury and regulated the immunity of the liver and kidney. Amidation of the C-termini seems to be important in improving the lytic activity of the peptides against pathogenic bacteria. N6NH2 and N6 are different from common antimicrobial peptides in the secondary structure. [Ref.33348729] Gram-negative bacteria: Edwardsiella tarda(MIC = 0.5 μg/mL), Aeromonas veronii(MIC = 2 μg/mL), Escherichia coli CVCC195(MIC = 0.06 μg/mL), E. coli CVCC1515(MIC = 0.06 μg/mL), E. coli CVCC25922(MIC = 0.06 μg/mL), E. coli CVCCO157(MIC = 0.06 μg/mL), Salmonella typhimurium CVCC533(MIC = 0.25 μg/mL), S. typhimurium ATCC14028(MIC = 0.06 μg/mL), S. enteritidis CVCC3377(MIC = 0.06 μg/mL), S. pullorum CVCC1802(MIC = 0.25 μg/mL), S. pullorum CVCC1789(MIC = 0.06 μg/mL), Pseudomonas aeruginosa CICC21630(MIC = 0.06 μg/mL). ##Gram-positive bacteria: Staphylococcus aureus ATCC43300(MIC = 1 μg/mL), S. aureus ATCC546(MIC = 1 μg/mL), S. aureus ATCC25923(MIC = 1 μg/mL), S. hyicus 437-2(MIC = 16 μg/mL), S. hyicus 15095 (MIC = 4 μg/mL). [Ref.33348729]The hemolysis of N6NH2 towards mouse erythrocytes was 0.19% at a concentration of 256 μg/mL, lower than that of N6 (1.9%), indicating their low hemolytic activity Cyclic Free Amidation There is a disulfide bond between Cys7 and Cys16 L [Ref.33348729]Had very low cytotoxicity to mouse peritoneal RAW 264.7 macrophages (cell survival rate >93.35%) Lipopolysaccharide (LPS) and genomic DNA 33348729 Mar Drugs. 2020 Dec 17;18(12):650. doi: 10.3390/md18120650. Han H, Li T, Wang Z, Teng D, Mao R, Hao Y, Yang N, Wang X, Wang J. Improved Stability and Activity of a Marine Peptide-N6NH2 against Edwardsiella tarda and Its Preliminary Application in Fish DRAMP29068 kFwSLLkKAlrLwKkVL 17 CPF-2-1 (Variant of CPF-C1) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form α-helical (most likely) Not found Comment: CPF-2 has potential as a lead compound to treat infections caused by S. aureus and MRSA, including the associated biofilms. [Ref.32590058] Gram-positive: S. aureus ATCC 25923 (MIC = 16 μg/mL, MIC = 16 μg/mL in 10% serum, MIC = 32 μg/mL in 150 mM) [Ref.32590058]It showed almost no hemolytic activity, even at concentrations up to 128 μg/ml. Linear Free Amidation Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Lys1, D-Trp3, D-Lys7, D-Leu10, D-Arg11, D-Trp13 and D-Lys15) Not found Bacterial membrane 32590058 Biochimie. 2020 Sep;176:1-11. doi: 10.1016/j.biochi.2020.06.003. Epub 2020 Jun 23. Xie J, Li Y, Guo X, Rao J, Yan T, Mou L, Wu X, Xie X, Yang W, Zhang B. CPF-C1 analog with effective antimicrobial and antibiofilm activities against Staphylococcus aureus including MRSA DRAMP29069 kFwSLLkKAlrLwAkVL 17 CPF-2-2 (Variant of CPF-C1) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form α-helical (most likely) Not found Comment: CPF-2 has potential as a lead compound to treat infections caused by S. aureus and MRSA, including the associated biofilms. [Ref.32590058] Gram-positive: S. aureus ATCC 25923 (MIC = 8 μg/mL, MIC = 128 μg/mL in 10% serum, MIC = 8 μg/mL in 150 mM, MBIC50 = 16 μg/mL, MBIC90 = 16 μg/mL, MBEC = 16 μg/mL), MRSA ATCC 33591 (MIC = 8 μg/mL), MRSA 054 isolated from clinics (MIC = 8 μg/mL), MRSA 023 isolated from clinics (MIC = 8 μg/mL), MRSA 113 isolated from clinics (MIC = 8 μg/mL), MRSA 048 isolated from clinics (MIC = 8 μg/mL), MRSA 002 isolated from clinics (MIC = 8 μg/mL), MRSA 074 isolated from clinics (MIC = 8 μg/mL), MRSA 051 isolated from clinics (MIC = 16 μg/mL), MRSA 052 isolated from clinics (MIC = 8 μg/mL), MRSA 075 isolated from clinics (MIC = 8 μg/mL), MRSA 071 isolated from clinics (MIC = 8 μg/mL), MRSA 936 isolated from clinics (MIC = 8 μg/mL), S. aureus 725 (MIC = 16 μg/mL), S. aureus 794 (MIC = 8 μg/mL) [Ref.32590058]It showed almost no hemolytic activity, even at concentrations up to 128 μg/ml Linear Free Amidation Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Lys1, D-Trp3, D-Lys7, D-Leu10, D-Arg11, D-Trp13 and D-Lys15) Not found Bacterial membrane 32590058 Biochimie. 2020 Sep;176:1-11. doi: 10.1016/j.biochi.2020.06.003. Epub 2020 Jun 23. Xie J, Li Y, Guo X, Rao J, Yan T, Mou L, Wu X, Xie X, Yang W, Zhang B. CPF-C1 analog with effective antimicrobial and antibiofilm activities against Staphylococcus aureus including MRSA DRAMP29070 GFGSLLGKALRLWKKVL 17 CPF-13 (Variant of CPF-C1) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form α-helical Not found Comment: CPF-13 showed improved antimicrobial activities against S. aureus and stabilities in serum and salt solution. [Ref.32590058] Gram-positive: S. aureus ATCC 25923 (MIC = 4 μg/mL, MIC = 8 μg/mL in 10% serum, MIC = 4 μg/mL in 150 mM, MBIC50 = 4 μg/mL, MBIC90 = 8 μg/mL, MBEC = 8 μg/mL), MRSA ATCC 33591 (MIC = 8 μg/mL), MRSA 054 isolated from clinics (MIC = 8 μg/mL), MRSA 023 isolated from clinics (MIC = 8 μg/mL), MRSA 113 isolated from clinics (MIC = 8 μg/mL), MRSA 048 isolated from clinics (MIC = 8 μg/mL), MRSA 002 isolated from clinics (MIC = 8 μg/mL), MRSA 074 isolated from clinics (MIC = 8 μg/mL), MRSA 051 isolated from clinics (MIC = 8 μg/mL), MRSA 052 isolated from clinics (MIC = 8 μg/mL), MRSA 075 isolated from clinics (MIC = 8 μg/mL), MRSA 071 isolated from clinics (MIC = 8 μg/mL), MRSA 936 isolated from clinics (MIC = 8 μg/mL), S. aureus 725 (MIC = 8 μg/mL), S. aureus 794 (MIC = 8 μg/mL) [Ref.32590058]It showed significant toxicity at high concentrations. At the concentration of 16, 32, 64 and 128 μg/mL, CPF-13 displayed 2%, 10%, 72% and 72% hemolysis, respectively. Linear Free Amidation L Not found Bacterial membrane 32590058 Biochimie. 2020 Sep;176:1-11. doi: 10.1016/j.biochi.2020.06.003. Epub 2020 Jun 23. Xie J, Li Y, Guo X, Rao J, Yan T, Mou L, Wu X, Xie X, Yang W, Zhang B. CPF-C1 analog with effective antimicrobial and antibiofilm activities against Staphylococcus aureus including MRSA DRAMP29071 GFGSLLGKALRLwKkVL 17 CPF-14 (Variant of CPF-C1) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form α-helical Not found Comment: CPF-14 showed improved antimicrobial activities against S. aureus and stabilities in serum and salt solution. [Ref.32590058] Gram-positive: S. aureus ATCC 25923 (MIC = 8 μg/mL, MIC = 4 μg/mL in 10% serum, MIC = 8 μg/mL in 150 mM, MBIC50 = 16 μg/mL, MBIC90 = 16 μg/mL, MBEC = 32 μg/mL), MRSA ATCC 33591 (MIC = 8 μg/mL), MRSA 054 isolated from clinics (MIC = 8 μg/mL), MRSA 023 isolated from clinics (MIC = 8 μg/mL), MRSA 113 isolated from clinics (MIC = 8 μg/mL), MRSA 048 isolated from clinics (MIC = 8 μg/mL), MRSA 002 isolated from clinics (MIC = 8 μg/mL), MRSA 074 isolated from clinics (MIC = 8 μg/mL), MRSA 051 isolated from clinics (MIC = 8 μg/mL), MRSA 052 isolated from clinics (MIC = 8 μg/mL), MRSA 075 isolated from clinics (MIC = 8 μg/mL), MRSA 071 isolated from clinics (MIC = 8 μg/mL), MRSA 936 isolated from clinics (MIC = 8 μg/mL), S. aureus 725 (MIC = 8 μg/mL), S. aureus 794 (MIC = 8 μg/mL) [Ref.32590058]It exhibited low hemolytic activity against mouse RBCs. CPF-14 displayed 4% and 13% hemolysis at the concentration of 64 and 128 μg/mL Linear Free Amidation Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Trp13 and D-Lys15) Not found Bacterial membrane 32590058 Biochimie. 2020 Sep;176:1-11. doi: 10.1016/j.biochi.2020.06.003. Epub 2020 Jun 23. Xie J, Li Y, Guo X, Rao J, Yan T, Mou L, Wu X, Xie X, Yang W, Zhang B. CPF-C1 analog with effective antimicrobial and antibiofilm activities against Staphylococcus aureus including MRSA DRAMP29072 GFGSLLGKAlrLwKkVL 17 CPF-15 (Variant of CPF-C1) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+ Synthetic form α-helical (most likely) Not found Comment: CPF-15 had low antimicrobial activity. [Ref.32590058] Gram-positive: S. aureus ATCC 25923 (MIC = 64 μg/mL) [Ref.32590058]It showed significant toxicity at high concentrations. CPF-15 displayed 5%, 12%, 23%, 50% and 67% at the concentrations of 8, 16, 32, 64, 128 μg/mL Linear Free Amidation Introduction of D-amino acid(s). (Look at 'Stereochemistry') Mixed (D-Leu10, D-Arg11,D-Trp13 and D-Lys15) Not found Bacterial membrane 32590058 Biochimie. 2020 Sep;176:1-11. doi: 10.1016/j.biochi.2020.06.003. Epub 2020 Jun 23. Xie J, Li Y, Guo X, Rao J, Yan T, Mou L, Wu X, Xie X, Yang W, Zhang B. CPF-C1 analog with effective antimicrobial and antibiofilm activities against Staphylococcus aureus including MRSA DRAMP29073 RIVELTLPRVSVRL 14 CF-14 No entry found Not found Catfish skin mucus Antimicrobial, Antibacterial, Anti-Gram- Protein level It formed α-helix in PBS with 2.5% SDS but exhibited low α-content in PBS only. The CD spectra exhibited low α-helical content in PBS only. However, in PBS with 2.5% SDS, the CD spectra for CF-14 showed double-negative bands at 208 nm and 222 nm, indicating that CF-14 formed an α-helical structure under membrane-mimetic conditions. Comment: These results strongly indicated that CF-14 could be a potential novel antibiotic agent against E.coli. Hence, understanding the antibacterial mechanism and analyzing the amino acid sequence of CF-14 can aid in designing effective antimicrobial agents. [Ref.32205189] Gram-negative bacteria: E.coli (MIC = 31.3 μg/mL); ##[Ref.31291603]Gram-positive bacteria: S. putrefaciens (MIC = 62.5 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L Not found Bacterial DNA 32205189##31291603 Fish Shellfish Immunol. 2020 May;100:489-495. doi: 10.1016/j.fsi.2020.03.038. Epub 2020 Mar 20.##Fish Shellfish Immunol. 2019 Sep;92:881-888. doi: 10.1016/j.fsi.2019.07.015. Epub 2019 Jul 7. Li T, Liu Q, Chen H, Li J##Tingting Li, Quanwei Liu, Dangfeng Wang, Jianrong Li Antibacterial activity and mechanism of the cell-penetrating peptide CF-14 on the gram-negative bacteria, Escherichia coli.##Characterization and antimicrobial mechanism of CF-14, a new antimicrobial peptide from the epidermal mucus of catfish DRAMP29074 KRFWQLVPLAIKIYRAWKRR 20 dCATH (duck cathelicidin) A0A493U1S6 Not found Anas platyrhynchos platyrhynchos (Northern mallard) Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Unknown Initially, four analog peptides were designed by truncating two, four, six, and eight amino acids at the N-terminal ends of dCATH peptide. dCATH and its truncated analogs could not adopt the amphipathic α-helical structure since the hydrophobic and charged residues were dispersed all around the molecule. Comment: The peptide induces potent antimicrobial activity. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 8 μM), B. subtilis KCTC 3068 (MIC = 8 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 16 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 8 μM), VREF ATCC 51559(MIC = 16 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 8 μM), P. aeruginosa KCTC 1637(MIC = 16 μM), S. typhimurium KCTC 1926 (MIC = 4 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 16 μM), MDRPA CCARM 2109 (MIC = 16 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 16 μM). [Ref.32698035] HC10 = 5.1 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Free L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40 and 80 μM, the cell survival of dCATH against human bone marrow SH-SY5Y cells is 103%, 103%, 100%, 68%, 36%, 13% and 8%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29075 FWQLVPLAIKIYRAWKRR 18 dCATH 18 (modified from dCATH) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Unknown Initially, four analog peptides were designed by truncating two, four, six, and eight amino acids at the N-terminal ends of dCATH peptide. dCATH and its truncated analogs could not adopt the amphipathic α-helical structure since the hydrophobic and charged residues were dispersed all around the molecule. Comment: The peptide induces potent antimicrobial activity. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 16 μM), B. subtilis KCTC 3068 (MIC = 8 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 32 μM), VREF ATCC 51559(MIC = 32 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 16 μM), P. aeruginosa KCTC 1637(MIC = 16 μM), S. typhimurium KCTC 1926 (MIC = 8 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 32 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 16 μM), C. albicans KCTC 7121 (MIC = 16 μM). [Ref.32698035] HC10 = 1.3 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 18 against human bone marrow SH-SY5Y cells is 102%, 83%, 75%, 52%, 23%, 9%, 7%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29076 QLVPLAIKIYRAWKRR 16 dCATH 16 (modified from dCATH) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Unknown Initially, four analog peptides were designed by truncating two, four, six, and eight amino acids at the N-terminal ends of dCATH peptide. dCATH and its truncated analogs could not adopt the amphipathic α-helical structure since the hydrophobic and charged residues were dispersed all around the molecule. Comment: The peptide induces potent antimicrobial activity. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 16 μM), B. subtilis KCTC 3068 (MIC = 16 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 32 μM), VREF ATCC 51559(MIC = 32 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 32 μM), P. aeruginosa KCTC 1637(MIC = 16 μM), S. typhimurium KCTC 1926 (MIC = 16 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 32 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 16 μM). [Ref.32698035] HC10 = 180 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 16 against human bone marrow SH-SY5Y cells is 98%, 95%, 91%, 86%, 54%, 36%, 32%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29077 VPLAIKIYRAWKRR 14 dCATH 14 (modified from dCATH) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Unknown Initially, four analog peptides were designed by truncating two, four, six, and eight amino acids at the N-terminal ends of dCATH peptide. dCATH and its truncated analogs could not adopt the amphipathic α-helical structure since the hydrophobic and charged residues were dispersed all around the molecule. Comment: The peptide induces potent antimicrobial activity. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 16 μM), B. subtilis KCTC 3068 (MIC = 4 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 32 μM), MRSA CCARM 3095 (MIC = 32 μM), VREF ATCC 51559(MIC = 16 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 16 μM), P. aeruginosa KCTC 1637(MIC = 8 μM), S. typhimurium KCTC 1926 (MIC = 8 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 32 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 16 μM), C. albicans KCTC 7121 (MIC = 16 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 14 against human bone marrow SH-SY5Y cells is 103%, 101%, 100%, 100%, 91%, 74%, 70% Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29078 LAIKIYRAWKRR 12 dCATH 12 (modified from dCATH) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 26.56% α-helix content in 50% TFE; 7.93% α-helix content in 30 mM SDS; 26.91% α-helix content in 0.1% LPS Not found Comment: Contribute to the design of short AMPs with bactericidal and immunomodulatory properties for combating bacterial infection and sepsis. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 4 μM), B. subtilis KCTC 3068 (MIC = 8 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 32 μM), MRSA CCARM 3095 (MIC = 32 μM), VREF ATCC 51559(MIC = 32 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 16 μM), P. aeruginosa KCTC 1637(MIC = 4 μM), S. typhimurium KCTC 1926 (MIC = 8 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 16 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 16 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12 against human bone marrow SH-SY5Y cells is 103%, 103%, 102%, 99%, 97%, 79%, 67% Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29079 LAKKIYRAWKRR 12 dCATH 12-1 (modified from dCATH 12) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 6.24% α-helix content in 50% TFE; 7.52% α-helix content in 30 mM SDS; 8.73% α-helix content in 0.1% LPS Not found Comment: dCATH12-1 displayed high antimicrobial activity with minimal cytotoxicity [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 4 μM), S. epidermidis KCTC 1917 (MIC = 8 μM), B. subtilis KCTC 3068 (MIC = 8 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 16 μM), VREF ATCC 51559(MIC = 16 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 8 μM), P. aeruginosa KCTC 1637(MIC = 4 μM), S. typhimurium KCTC 1926 (MIC = 4 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 32 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 8 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-1 against human bone marrow SH-SY5Y cells is 102%, 102%, 100%, 96%, 96%, 78%, 69%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29080 LAKKIYRAWKRW 12 dCATH 12-2 (modified from dCATH 12) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 22.78% α-helix content in 50% TFE; 8.04% α-helix content in 30 mM SDS; 29.50% α-helix content in 0.1% LPS Not found Comment: dCATH12-2 displayed high antimicrobial activity with minimal cytotoxicity [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 4 μM), S. epidermidis KCTC 1917 (MIC = 8 μM), B. subtilis KCTC 3068 (MIC = 4 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 16 μM), VREF ATCC 51559(MIC = 16 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 16 μM), P. aeruginosa KCTC 1637(MIC = 4 μM), S. typhimurium KCTC 1926 (MIC = 2 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 16 μM), MDRPA CCARM 2109 (MIC = 32 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 8 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-2 against human bone marrow SH-SY5Y cells is 102%, 101%, 100%, 100%, 97%, 92%, 85%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29081 LAKKIYRKWKRW 12 dCATH 12-3 (modified from dCATH 12) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 27.42% α-helix content in 50% TFE; 23.60% α-helix content in 30 mM SDS; 23.51% α-helix content in 0.1% LPS Not found Comment: dCATH12-3 displayed high antimicrobial activity with minimal cytotoxicity [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 4 μM), S. epidermidis KCTC 1917 (MIC = 4 μM), B. subtilis KCTC 3068 (MIC = 4 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 16 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 8 μM), VREF ATCC 51559(MIC = 8 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 8 μM), P. aeruginosa KCTC 1637(MIC = 4 μM), S. typhimurium KCTC 1926 (MIC = 2 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 16 μM), MDRPA CCARM 2109 (MIC = 8 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 8 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-3 against human bone marrow SH-SY5Y cells is 102%, 100%, 100%, 97%, 95%, 95%, 84%. Not found 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29082 LIKKIYRKWKRW 12 dCATH 12-4 (modified from dCATH 12) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 41.28% α-helix content in 50% TFE; 36.63% α-helix content in 30 mM SDS; 42.87% α-helix content in 0.1% LPS Among the 12-meric analog AMPs, Trp rich dCATH 12–4 and dCATH 12-5 displayed high helicity in all membrane-mimetic environment with highest α-helical conformation observed (42.8% and 40.4% respectively) in 0.1% LPS Comment: dCATH 12-4 demonstrated synergistic actions with various conventional antibiotics against antibiotic resistant pathogens, thus indicating their ability as promising adjuncts to combination therapy. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 4 μM), S. epidermidis KCTC 1917 (MIC = 4 μM), B. subtilis KCTC 3068 (MIC = 2 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 16 μM), MRSA CCARM 3090 (MIC = 8 μM), MRSA CCARM 3095 (MIC = 8 μM), VREF ATCC 51559(MIC = 8 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 8 μM), P. aeruginosa KCTC 1637(MIC = 2 μM), S. typhimurium KCTC 1926 (MIC = 2 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 8 μM), MDRPA CCARM 2109 (MIC = 8 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 4 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-4 against human bone marrow SH-SY5Y cells is 102%, 102%, 100%, 100%, 100%, 91%, 83%. Bacterial DNA 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29083 LWKKIYRKWKRW 12 dCATH 12-5 (modified from dCATH 12) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form Random coil in buffer; 38.39% α-helix content in 50% TFE; 29.75% α-helix content in 30 mM SDS; 40.40% α-helix content in 0.1% LPS Among the 12-meric analog AMPs, Trp rich dCATH 12–4 and dCATH 12-5 displayed high helicity in all membrane-mimetic environment with highest α-helical conformation observed (42.8% and 40.4% respectively) in 0.1% LPS Comment: dCATH 12-5 demonstrated synergistic actions with various conventional antibiotics against antibiotic resistant pathogens, thus indicating their ability as promising adjuncts to combination therapy. [Ref.32698035] Gram-positive bacteria: S. aureus KCTC 1621 (MIC = 2 μM), S. epidermidis KCTC 1917 (MIC = 4 μM), B. subtilis KCTC 3068 (MIC = 2 μM);##Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 16 μM), MRSA CCARM 3090 (MIC = 8 μM), MRSA CCARM 3095 (MIC = 8 μM), VREF ATCC 51559(MIC = 8 μM);##Gram-negative bacteria: E. coli KCTC 1682 (MIC = 4 μM), P. aeruginosa KCTC 1637(MIC = 2 μM), S. typhimurium KCTC 1926 (MIC = 2 μM);##Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 8 μM), MDRPA CCARM 2109 (MIC = 4 μM); ##Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 4 μM). [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs). Linear Free Amidation L [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-5 against human bone marrow SH-SY5Y cells is 102%, 101%, 100%, 100%, 100%, 95%, 87%. Bacterial DNA 32698035 Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16. Kumar SD, Shin SY Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization DRAMP29084 GVTFNALKGVAKTVAAQLLKTAR 23 Brevinin-GR23 No entry found Not found Hylarana guentheri Antimicrobial, Antibacterial, Anti-Gram-, Anti-Gram+ Synthetic form α-helical Not found Comment: Although B-GR23 did not show a potent antimicrobial and antibiofilm activity, the outstanding characteristic is the low toxicity on human blood red cells, which makes it an ideal template peptide to derive more powerful antimicrobial peptides [Ref.31549575] Gram-positive bacteria: Staphylococcus aureus (MIC = 16 μM), Streptococcus mutans(MIC > 100 μM);##Gram-negative bacteria: Escherichia coli (MIC = 64 μM), Pseudomonas aeruginosa(MIC > 100 μM);##Yeast: Canidia albican (MIC > 100 μM) [Ref.31549575]B-GR23 induced a hemolysis of 0.13%, 0.23%, 0.38%, 0.75%, 0.83% and 1.60% on human blood red cells at the concentrations of 25, 50, 75, 100, 150 and 200 μM. Linear Free Amidation L Not found Cell membrane 31549575 Biosci Biotechnol Biochem. 2020 Jan;84(1):143-153. doi: 10.1080/09168451.2019.1670045. Epub 2019 Sep 24. Hengren Zhong, Zhipeng Xie, Shuxia Zhang, Hanqi Wei, Yanting Song, Yingxia Zhang, Manchuriga Wang Brevinin-GR23 from frog Hylarana guentheri with antimicrobial and antibiofilm activities against Staphylococcus aureus DRAMP29085 GLVTDTLKGAAKTVAAELLRKAH 23 B-GH23-1 No entry found Not found Hylarana guentheri Antimicrobial, Antibacterial, Anti-Gram- Synthetic form Not found Not found Comment: B-GH23-1 had slight antibacterial activity on S.aureus [Ref.31549575] Gram-positive bacteria: Staphylococcus aureus (MIC = 32-64 μM), Streptococcus mutans(MIC > 100 μM);##Gram-negative bacteria: Escherichia coli (MIC > 100 μM), Pseudomonas aeruginosa(MIC > 100 μM);##Yeast: Canidia albican (MIC > 100 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L Not found Cell membrane 31549575 Biosci Biotechnol Biochem. 2020 Jan;84(1):143-153. doi: 10.1080/09168451.2019.1670045. Epub 2019 Sep 24. Hengren Zhong, Zhipeng Xie, Shuxia Zhang, Hanqi Wei, Yanting Song, Yingxia Zhang, Manchuriga Wang Brevinin-GR23 from frog Hylarana guentheri with antimicrobial and antibiofilm activities against Staphylococcus aureus DRAMP29086 GVITDALKGAAKTVAAELPRKAH 23 B-GH23-2 No entry found Not found Hylarana guentheri Non-antimicrobial Synthetic form Not found Not found Comment: B-GH23-2 did not have any antimicrobial activity. [Ref.31549575] Gram-positive bacteria: Staphylococcus aureus (MIC > 100 μM), Streptococcus mutans(MIC > 100 μM);##Gram-negative bacteria: Escherichia coli (MIC > 100 μM), Pseudomonas aeruginosa(MIC > 100 μM);##Yeast: Canidia albican (MIC > 100 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L Not found Cell membrane 31549575 Biosci Biotechnol Biochem. 2020 Jan;84(1):143-153. doi: 10.1080/09168451.2019.1670045. Epub 2019 Sep 24. Hengren Zhong, Zhipeng Xie, Shuxia Zhang, Hanqi Wei, Yanting Song, Yingxia Zhang, Manchuriga Wang Brevinin-GR23 from frog Hylarana guentheri with antimicrobial and antibiofilm activities against Staphylococcus aureus DRAMP29087 VRLIVKVRIWRR 12 RiLK1 No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal Synthetic form Disordered structure in aqueous solution; β-sheet in the presence of SDS (3 mM) Without SDS: 1.2% α-helix, 47.3% β-sheet, 51.5% random; t = 0 h with SDS: 7.4% α-helix, 51.4% β-sheet, 41.3% random; t = 5 min with SDS: 4.4% α-helix, 53.4% β-sheet, 42.2% random; t = 30 min with SDS: 11% α-helix, 48.7% β-sheet, 40.3% random; t = 1 h with SDS: 9.8% α-helix, 51.1% β-sheet, 39.1% random; t = 5 h with SDS: 6.7% α-helix, 54% β-sheet, 39.3% random; t = 6 h with SDS: 8% α-helix, 52% β-sheet, 40.1% random; t = 24 h with SDS: 8.4% α-helix, 53.6% β-sheet, 38% random Comment: RiLK1 exerted potent killing effects against the clinical isolate (MBC = 1.25 M), two-fold lower than those observed against the strain isolated from food products and those determined with the parental peptide 1018-K6 against ACSSuT strain, thus, suggesting that RiLK1 might have a high potential also in the medical field. "[Ref.32971824] Gram-negative bacteria: E.coli (IC50 = 1.20 ± 0.10 μM, MBC = 2.0 μM), S. Typhimurium (IC50 = 1.30 ± 0.14 μM, MBC = 2.5 μM);##Gram-positive bacteria: S. aureus (IC50 = 1.98 ± 0.25 μM, MBC = 16.0 μM), L. monocytogenes (IC50 = 0.46 ± 0.01 μM, MBC = 2.0 μM);##Fungi: C. albicans ATCC 14053, A. brasiliensis ATCC 9341. Susceptibility testing clearly showed that RiLK1 was very effective, being able to inhibit 100% growth of both fungi at 25 μM concentration (MFC)." No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.32971824] It was observed that the cell viability was recorded as 98%, 98.7%, and 98.9% at the concentrations of RiLK1 (10, 25, 50 μM) Not found 32971824 Int J Mol Sci. 2020 Sep 22;21(18):6952. doi: 10.3390/ijms21186952. Agrillo B, Proroga YTR, Gogliettino M, Balestrieri M, Tatè R, Nicolais L, Palmieri G A Safe and Multitasking Antimicrobial Decapeptide: The Road from De Novo Design to Structural and Functional Characterization DRAMP29088 INWLKIAKKVKGML 14 MK58911 (a peptide analog from the mastoparan class of wasps) No entry found Not found Galleria mellonella Antimicrobial, Antifungal, Antitumor Synthetic form Not found Not found Comment: MK58911 is not toxic in two mammalian cells (lung fibroblasts and glioblastoma cells) and in the G. mellonella model and demonstrates both in vitro and in vivo antifungal efficacy. Moreover, the peptide acted on the membrane of fungal cells and induced necrosis. [Ref.31867293] Fungi: C. neoformans (MIC = 31.2 μg/mL), C. gattii (MIC = 15.6 μg/mL), P. brasiliensis (MIC = 7.8 μg/mL), P. lutzii (MIC = 15.6 μg/mL) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.31867293]MK58911 was not toxic in lung fibroblasts (MRC5) and glioblastoma cells (U87) at tested concentrations, and a high IC50 of >500 μg/mL was observed in both mammalian cells. Fungal cell membrane 31867293 Front Cell Infect Microbiol. 2019 Dec 6;9:419. doi: 10.3389/fcimb.2019.00419. eCollection 2019. Singulani JL, Galeane MC, Ramos MD, Gomes PC, Dos Santos CT, de Souza BM, Palma MS, Fusco Almeida AM, Mendes Giannini MJS. Antifungal Activity, Toxicity, and Membranolytic Action of a Mastoparan Analog Peptide DRAMP29089 AFIQLSKPCISDKECSIVKNYRARCRKGYCVRRRIR 36 NCR044 (Putative Late nodulin) A0A396GSL0 Not found MtrunA17_Chr7g021623 Medicago truncatula (Barrel medic) (Medicago tribuloides) Antimicrobial, Antifungal Protein level α-helix and β-sheet NCR044 contains one short (A23 to R25, G28 to C30) antiparallel β-sheet and a whiff (S11 to E14) of an α-helix. 6U6G Comment: The oxidized form of the NCR044 peptide exhibits potent broad-spectrum antifungal activity in vitro against four economically important fungal pathogens tested in this study. Many factors can strongly affect the efficacy of antifungal peptides. For example, disulfide bonds can help to increase potency of the oxidized form of NCR044. For deployment of NCR044 in crop protection, one could envisage further manipulating the cationicity/hydrophobicity of the oxidized or reduced NCR044 through site-directed mutagenesis and increase its antifungal potency on the surface of plant tissues without causing phytotoxicity. [Ref.32571919] Fungi: Botrytis cinerea (IC50 = 1.55 ± 0.21 μM, IC90 = 2.72 ± 0.05 μM), Fusarium graminearum (IC50 = 1.93 ± 0.23 μM, IC90 = 2.80 ± 0.04 μM), F.virguliforme (IC50 = 1.68 ± 0.20 μM, IC90 = 2.70 ± 0.08 μM), F.oxysporum (IC50 = 0.52 ± 0.01 μM, IC90 = 0.71 ± 0.01 μM) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two disulfide bond between Cys15 and Cys25, Cys9 and Cys30 L Not found Multiple membrane phospholipids 32571919 Proc Natl Acad Sci U S A. 2020 Jul 7;117(27):16043-16054. doi: 10.1073/pnas.2003526117. Epub 2020 Jun 22. Velivelli SLS, Czymmek KJ, Li H, Shaw JB, Buchko GW, Shah DM Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection DRAMP29090 GIWKFLKKAKKFWK 14 MSI-1 No entry found Not found Synthetic construct Antimicrobial, Antifungal, Anti-cryptococcal Synthetic form α-helical in hydrophobic environment Furthermore, the amphipathic structure of this peptide makes it adopt an alpha helical in hydrophobic environment which may lead to the insertion of MSI-1 into the lipid bilayer of the fungal membrane to exert antifungal activity. Comment: The study had demonstrated the potent antifungal activity of MSI-1 against clinical isolated C. neoformans in vitro and in a murine model of cryptococcal meningoencephalitis. [Ref.32504765] Fungal strains: C. neoformans ATCC4906 (MIC = 8 μg/mL), C. neoformans 1201 (MIC = 8 μg/mL), C. neoformans 1768 (MIC = 16 μg/mL), C. neoformans 2011 (MIC = 8 μg/mL), C. neoformans 1386 (MIC = 16 μg/mL), C. neoformans 1965 (MIC = 16 μg/mL), C. gattii ATCC34877 (MIC = 4 μg/mL), C. albicans ATCC10231 (MIC = 32 μg/mL), C. albicans 2713 (MIC = 32 μg/mL), C. albicans 2144 (MIC = 64 μg/mL), C. albicans 1902 (MIC = 64 μg/mL), C. albicans 1869 (MIC = 32 μg/mL), C. albicans 2105 (MIC = 128 μg/mL ) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L Not found Fungal cell membrane 32504765 Peptides. 2020 Aug;130:170334. doi: 10.1016/j.peptides.2020.170334. Epub 2020 Jun 3. Ma L, Wei S, Ye X, Xu P, Chen H, Liu Z, Zhou C Antifungal activity of peptide MSI-1 against Cryptococcus neoformans infection in vitro and in murine cryptococcal meningoencephalitis DRAMP29091 GRTSKQELCTWERGSVRQADKTIAG 25 Skh-AMP1 No entry found Belongs to the Lamiaceae family, subfamily Nepetoideae. Satureja khuzistanica Antimicrobial, Antifungal Natural peptide α-helical Evaluation of the peptide three-dimensional structure showed that, despite the unusual distribution of amino acids in the Wheel projection, Skh-AMP1 maybe forms a α-helix structure with more hydrophobic C-terminal than that of the N-terminal. Comment: The antifungal activity of Skh-AMP1 may be related to its ability to disrupt fungal cell membrane permeabilization and induce enhanced ROS production. Therefore, Skh-AMP1 can be introduced as a novel antifungal candidate for developing new therapeutic agents. [Ref.31128493] Fungi: Candida albicans ATCC 10231 (MIC = 21.6 μM, MFC = 43.2 μM), Candida krusei DSM 70079 (MIC = 20.7 μM, MFC = 41.4 μM), Candida glabrata ATCC 90030 (MIC = 19.8 μM, MFC = 39.6 μM), Aspergillus niger ATCC 9029 (MIC = 22.5 μM, MFC = 45 μM), Aspergillus flavus PFCC 100 (MIC = 23.4 μM, MFC = 58.5 μM), Aspergillus fumigatus Af 293 (MIC = 20.7 μM, MFC = 41.4 μM) [Ref.31128493] Using human erythrocytes, the hemolytic activity of Skh-AMP1 at concentrations from 3.6 μM to 72 μM was reported in the range of 0.19%–2.1%. At the MIC concentration of 25.2 μM, a very low hemolytic activity of 0.67% (SD = 0.02) was observed. Also, this peptide at MFC concentrations (36, 54 and 72 μM) showed 0.98%, 1.45% and 2.1% hemolytic activity for human erythrocytes. Linear Free Free L [Ref.31128493] Skh-AMP1 has about 3.6% cytotoxicity at the concentration of 25.2 μM in 48 h. Therefore, this peptide had no significant cytotoxic effect at the concentrations of 12.6 and 25.2 μM at 6, 24, and 48 h. However, Skh-AMP1 has about 12% and 27% cytotoxicity at the concentration of 50.4 μM and 63 μM, respectively Fungal membrane 31704210##31128493 Peptides. 2020 Jan;123:170195. doi: 10.1016/j.peptides.2019.170195. Epub 2019 Nov 6.##Phytochemistry. 2019 Aug;164:136-143. doi: 10.1016/j.phytochem.2019.05.011. Epub 2019 May 23. Khani S, Seyedjavadi SS, Hosseini HM, Goudarzi M, Valadbeigi S, Khatami S, Ajdary S, Eslamifar A, Amani J, Imani Fooladi AA, Razzaghi-Abyaneh M##Soghra Khani, Sima Sadat Seyedjavadi, Hadi Zare-Zardini, Hamideh Mahmoodzadeh Hosseini, Mehdi Goudarzi, Shohreh Khatami, Jafar Amani, Abbas Ali Imani Fooladi, Mehdi Razzaghi-Abyaneh Effects of the antifungal peptide Skh-AMP1 derived from Satureja khuzistanica on cell membrane permeability, ROS production, and cell morphology of conidia and hyphae of Aspergillus fumigatus. ##Isolation and functional characterization of an antifungal hydrophilic peptide, Skh-AMP1, derived from Satureja khuzistanica leaves DRAMP29093 XTXXXfLXXT 10 polymyxin B (a mixture of polymyxin B1 to B4) No entry found Belongs to the Polymyxins family Paenibacillus polymyxa Antimicrobial, Antibacterial, Anti-Gram-, Anti-inflammatory Natural peptide(s) Ordered (the structure can not be described as α-helix, β-sheet or random coil simply) [Ref2] According to the NMR data, there are eight structures fall into several groups, represented by the three structures. The overall structure is quite flat, with the aromatic ring oriented over the leucine methyl groups, and with a kink between residues 1−3 in the linear part of the peptide. However, differences in the ring pucker are evident, and changes in the ring pucker also affect other parts of the molecule. The peptide is interconverting among three possibilities. Changes in the ring pucker among the structures involves flipping residues 4, 8, and 9 while holding residues 6, 7, and Polymyxin B is an old antibiotic used to treat meningitis, pneumonia, sepsis, and urinary tract infections. While it is useful for many Gram-negative infections, it is not useful Gram-positive infections. It can be give by injection into a vein, muscle, or cerebrospinal fluid or inhaled. Polymyxin antibiotics are relatively neurotoxic and nephrotoxic, so are usually used only as a last resort if modern antibiotics are ineffective or are contraindicated. [Ref.16524407] Gram-negative bacteria: Acinetobacter spp. (MIC50 ≤ 1 μg/mL, MIC90 = 2 μg/mL), Aeromonas spp. (MIC50 ≤ 1 μg/mL, MIC90 ＞ 8 μg/mL), Alcaligenes spp. (MIC50 = 2 μg/mL, MIC90 > 8 μg/mL), Burkholderia cepacia (MIC50 > 8 μg/mL, MIC90 > 8 μg/mL), Pseudomonas aeruginosa (MIC50 ≤ 1 μg/mL, MIC90 = 2 μg/mL), Pseudomonas spp. (non-aeruginosa) (MIC50 ≤ 1μg/mL, MIC90 = 4 μg/mL), Stenotrophomonas maltophilia (MIC50 = 1 μg/mL, MIC90 = 8 μg/mL), other non-enteric bacilli (MIC50 = 4 μg/mL, MIC90 > 4 μg/mL); ##Enterobacteriaceae: Citrobacter spp. (MIC50 ≤ 1 μg/mL, MIC90 ≤ 1 μg/mL), Enterobacter spp. (MIC50 ≤ 1 μg/mL, MIC90 > 8 μg/mL), Escherichia coli (MIC50 ≤ 1 μg/mL, MIC90 ≤ 1 μg/mL), Klebsiella spp. (MIC50 ≤ 1μg/mL, MIC90 ≤ 1μg/mL), indole-positive Proteus spp. etc. (MIC50 > 8 μg/mL, MIC90 > 8 μg/mL), Proteus mirabilis (MIC50 > 8 μg/mL, MIC90 > 8 μg/mL), Salmonella spp. (MIC50 ≤ 1 μg/mL, MIC90 = 4 μg/mL), Shigella spp. (MIC50 ≤ 1 μg/mL, MIC90 ≤ 1 μg/mL), Serratia spp. (MIC50 > 8 μg/mL, MIC90 > 8 μg/mL), other enteric bacilli (MIC50 ≤ 1 μg/mL, MIC90 = 8 μg/mL). ##NOTE: indole-positive Proteus spp. etc. includes Morganella morganii, Proteus spp., Proteus vulgaris, Providencia alcalifaciens, Providencia rettgeri, Providencia spp. and Providencia stuartii. No hemolysis information or data found in the reference(s) presented in this entry Cyclic [Ref.17878146] Acylation of fatty acid (6-methyloctanoic acid for polymyxin B1, 6-methylheptanoic acid for B2, octanoic acid for B3 and heptanoic acid for B4) [Ref.17878146] Thr10 linking to Dab5 forming a cycle. [Ref.17878146] ①The X in position 1, 3, 4, 5, 8 and 9 is α,γ-diaminobutyric acid (Dab). ②Dab4 links to Thr10 by amidation. [Ref.17878146] L (mixed with D-Phe7) Not found Cell membrane 17878146##16524407 J Antimicrob Chemother. 2007 Dec;60(6):1206-15. doi: 10.1093/jac/dkm357. Epub 2007 Sep 17. ##Clin Microbiol Infect. 2006 Apr;12(4):315-21. doi: 10.1111/j.1469-0691.2005.01351.x. Alexandre Prehn Zavascki, Luciano Zubaran Goldani, Jian Li, Roger L Nation ##A C Gales, R N Jones, H S Sader Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review.##Global assessment of the antimicrobial activity of polymyxin B against 54 731 clinical isolates of Gram-negative bacilli: report from the SENTRY antimicrobial surveillance programme (2001-2004). DRAMP29092 FKRLKKLISWIKRKRQQ 17 Hn-Mc (a chimeric peptide comprised of the N-terminus of HPA3NT3 and the C-terminus of melittin) No entry found Not found Synthetic construct Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Anti-inflammatory Synthetic construct Random coil or α-helical structure Hn-Mc adopted a random coil structure in the SUVs containing a mammalian membrane and in the buffer; however, it adopted an α-helical structure in SUVs containing a fungal membrane, indicating that it was not bound to the mammalian membrane but rather adhered to or inserted in the fungal membrane.  Comment: Hn-Mc has a high affinity for the fungal plasma membrane and induces apoptosis in fungal cells, and provide guidance for the development of new antifungal agents. Hn-Mc is an excellent model peptide with potent antibacterial activity and non-cytotoxicity. [Ref.32731574]Yeast: C. albicans (MIC = 16 μM), C. krusei (MIC = 8 μM), C. parapsilosis (MIC = 16 μM), C. tropicalis (MIC = 4 μM), T. beigellii (MIC = 1 μM);##Mold: T. rubrum (MIC = 1-2 μM), F. moniliforme(MIC = 1-2 μM), F. solani(MIC = 1 μM), F. oxysporum(MIC = 1-2 μM), A. flavus(MIC = 2-4 μM), A. fumigatus(MIC = 2-4 μM). ##[Ref.26028561] Drug-susceptible gram-negative bacteria: E. coli (MIC = 1 μM), P. aeruginosa (MIC = 2 μM); ##Drug-susceptible gram-positive bacteria: S. aureus (MIC = 2 μM), B. subtilis(MIC = 2 μM);##Drug-resistant bacteria: P. aeruginosa DRPA-001 (MIC = 1 μM), P. aeruginosa DRPA-002 (MIC = 1 μM), P. aeruginosa DRPA-003 (MIC = 1 μM), P. aeruginosa DRPA-004 (MIC = 1 μM), P. aeruginosa DRPA-005 (MIC = 2 μM), S. aureus DRSA-001 (MIC = 2 μM), S. aureus DRSA-002 (MIC = 2 μM), S. aureus DRSA-003 (MIC = 1 μM), S. aureus DRSA-004 (MIC = 2 μM), S. aureus DRSA-005 (MIC = 2 μM). [Ref.26028561] HPA3NT3 and melittin revealed the hemolysis of 68.2% and 100% at 250 μM, respectively, but Hn-Mc was 1.1% at the same concentration Linear Free Amidation L [Ref.26028561] The IC50 of HPA3NT3, melittin and Hn-Mc against HaCaT cells were 49.5, 2.8 and 357.5 μM, respectively Mitochondria (possibily) 32731574##26028561 Antibiotics (Basel). 2020 Jul 28;9(8):454. doi: 10.3390/antibiotics9080454.##Biochem Biophys Res Commun. 2015 Jul 31;463(3):322-8. doi: 10.1016/j.bbrc.2015.05.063. Epub 2015 May 29. Kim JY, Park SC, Noh G, Kim H, Yoo SH, Kim IR, Lee JR, Jang MK.##Young-Min Kim, Nam-Hong Kim, Jong-Wan Lee, Jin-Sun Jang, Yung-Hoon Park, Seong-Cheol Park, Mi-Kyeong Jang Antifungal Effect of A Chimeric Peptide Hn-Mc against Pathogenic Fungal Strains. ##Novel chimeric peptide with enhanced cell specificity and anti-inflammatory activity. DRAMP29094 GPKTKAACKMACKLATCGKKPGGWKCKLCELGCDAV 36 Turgencin A C0HLN5 Not found Synoicum turgens Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-,Anti-cancer Protein level Random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.32751755]Gram-positive bacteria:Bacillus megaterium(MIC=0.5 µg/mL); Bacillus subtilis(MIC=1.5 µg/mL); Corynebacterium glutamicum(MIC=1.5 µg/mL); Micrococcus luteus(MIC=8.0 µg/mL); Staphylococcus aureus(MIC=23.3 µg/mL);##Gram-negative bacteria:Escherichia coli(MIC=3.0 µg/mL); Pseudomonas aeruginosa(MIC=5.9 µg/mL);##Fungi: Rhodotorula sp(MIC=23.2 µg/mL);Aurobasidium pollulans(MIC=92.6 µg/mL); Candida albicans(MIC=46.3 µg/mL).##[Ref.31940927]Cancer:Human melanoma A2058(IC50=1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys8 and Cys33, Cys12 and Cys29, Cys17 and Cys26; the 'Met' at position 10 is Methionine sulfoxide. L [Ref.31940927]Cytotoxicity: Human fibroblasts MRC-5(IC50=4.8 μM). liposomes 32751755##31940927 Int J Mol Sci.2020 Jul 30;21(15):5460.##Mar Drugs. 2020 Jan 12;18(1):51. Hansen IKØ, Lövdahl T, Simonovic D, Hansen KØ, Andersen AJC, Devold H, Richard CSM, Andersen JH, Strøm MB, Haug T.##Hansen IKØ, Isaksson J, Poth AG, Hansen KØ, Andersen AJC, Richard CSM, Blencke HM, Stensvåg K, Craik DJ, Haug T. Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency.##Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens. DRAMP29095 GIKEMLCNMACAQTVCKKSGGPLCDTCQAACKALG 35 Turgencin B C0HLN6 Not found Synoicum turgens Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-,Anti-cancer Protein level Alpha helix,random coil Not found Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.31940927]Gram-positive bacteria:Corynebacterium glutamicum ATCC 13032(MIC=1.6 µM);Bacillus subtilis ATCC 23857(MIC=1.6 µM);Staphylococcus aureus ATCC 9144(MIC>100µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=12.5 µM);Pseudomonas aeruginosa ATCC 27853(MIC=25.0 µM);##Cancer:Human melanoma A2058(IC50=4.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Amidation Disulfide bond between Cys7 and Cys31, Cys11 and Cys27, Cys16 and Cys24; the 'Met' at position 5 and 9 is Methionine sulfoxide. L [Ref.31940927]Cytotoxicity: Human fibroblasts MRC-5(IC50=7.5 μM). liposomes 31940927 Mar Drugs. 2020 Jan 12;18(1):51. Hansen IKØ, Isaksson J, Poth AG, Hansen KØ, Andersen AJC, Richard CSM, Blencke HM, Stensvåg K, Craik DJ, Haug T. DRAMP29096 GLPGPLGPAGPK 12 Collagencin "S4R4C8, S4R4C7, S4R4C5" Not found Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Predicted Alpha helix,beta sheet,beta turn,random coil The deconvolution of CD spectra in PBS buffer revealed that collagencin structure was organized as follow: 5.5% of α-helix, 19.3% of β-sheet, 36.3% of β-turn and 38.9% unordered. In methanol(organic buffers), a shift between β-sheet (36.4%) and β-turn (22.1%) was observed in collagencin structure while helix (4.9%) and unordered structure (36.6%) contents remained stables.In presence of DPPG phospholipids, a shift between β-sheet and β-turn was observed in collagencin structure. A maximal β-sheet content (49.7%) was observed at highest lipid: peptide ratio (100:1). In presence of POPG, α-helix Function: Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Collagencin highly interacts with both anionic and zwitterionic phospholipids but remains at membrane–water interface, which suggests a carpet mechanism of action of the peptide. Collagencin is probably antihypertensive according to its high similarity to peptide PGPLGLTGP, an ACE inhibitor that was previously isolated from skate skin hydrolysate. [Ref.27038545]32.2% growth inhibition on Listeria innocua HPB29 at 235 µM; 31% growth inhibition on Lactococcus lactis ATCC 11454 at 235 µM ; 32.2% growth inhibition on Carnobacterium divergens M35 at 235 µM; 67% growth inhibition on Staphylococcus aureus ATCC 6538 at 235 µM; 62% growth inhibition on Streptococcus pyogenes ATCC19615 at 235 µM; 64% growth inhibition on Escherichia coli MC4100 at 235 µM; Escherichia coli O157:H7(NA); Aeromonas hydrophila ATCC 7966(NA); Pseudomonas aeruginosa ATCC 27853(NA). [Ref.27038545]non-toxic to horse erythrocytes up to 470 μM; 25% hemolysis against horse erythrocytes at 940 µM. Linear Free Free L [Ref.27038545]No cytotoxicity information found. liposomes 27038545 Biochem Biophys Res Commun. 2016 Apr 29;473(2):642-7. Ennaas N, Hammami R, Gomaa A, Bédard F, Biron É, Subirade M, Beaulieu L, Fliss I. Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane. DRAMP29097 TQQAFQKFLAAVTSALGKQYH 21 SHβAP No entry found Not found Not found Katsuwonus pelamis Antimicrobial, Antibacterial,Anti-Gram+,Anti-Gram-,Antifungal Not found Alpha helix Not found Function:SHβAP showed broad spectrum antimicrobial activity without hemolytic activity.Antimicrobial activity of the peptide was heatstable and pH resistant but is sensitive to proteases and salt.The action mode of SHβAP is bacteriostatic process rather than bactericidal one. [Ref.24495783]Gram-positive bacteria:B.subtilis KCTC1021(MEC=16.0 μg/mL); B.subtilis RM125(MEC=6.5 μg/mL); S.aureus KCTC1621(MEC=57.0 μg/mL);S.iniae FP5229(MEC=23.0 μg/mL);##Gram-negative bacteria:E.coli D31(MEC=15.0 μg/mL); E.coli KCTC1116(MEC=2.6 μg/mL); E.coli ML35p(MEC=6.2 μg/mL); P.aeruginosa KCTC2004(MEC=19.0 μg/mL); S.enterica KCTC2514(MEC=2.0 μg/mL); S.sonnei KCTC2009(MEC=6.0 μg/mL);A.hydrophila KCTC2358(MEC>125.0 μg/mL); V.parahaemolyticus HUFP91(MEC=1.9 μg/mL); V.parahaemolyticus KCCM41664(MEC=1.5 μg/mL);##Yeast:C.albicans KCTC7965(MEC=12.0 μg/mL). [Ref.24495783]not cause hemolysis against RBCs up to 100 μg/mL concentration. Linear Free Free L [Ref.24495783]No cytotoxicity information found. liposomes 24495783 Fish Shellfish Immunol. 2014 Mar;37(1):173-83. Seo JK, Lee MJ, Jung HG, Go HJ, Kim YJ, Park NG. Antimicrobial function of SHβAP, a novel hemoglobin β chain-related antimicrobial peptide, isolated from the liver of skipjack tuna, Katsuwonus pelamis. DRAMP29098 GLSRLFTALK 10 ACWWP1 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Not found Not found Function:The change in cell surface hydrophobicity and membrane-permeable action of the purified ACWWP1 may have contributed to the antibacterial effect. [Ref.25172690]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µg/ml); Bacillus subtilis ATCC 9372(MIC=16 µg/ml); Streptococcus pneumoniae ATCC 49619(MIC=64 µg/ml);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=32 µg/ml); Shigella dysenteriae ATCC 51302(MIC=256 µg/ml); Pseudomonas aeruginosa ATCC 27853 (MIC=64 µg/ml); Salmonella typhimurium ATCC 50013(MIC=32 µg/ml). [Ref.25172690]non-toxic to mouse erythrocytes up to 512 µg/ml. Linear Free Free L [Ref.25172690]No cytotoxicity information found. liposomes 25172690 Food Chem. 2015 Feb 1;168:115-23. Tang W, Zhang H, Wang L, Qian H, Qi X. Targeted separation of antibacterial peptide from protein hydrolysate of anchovy cooking wastewater by equilibrium dialysis. DRAMP29099 GLRKRLRKFRNKIKEKLKKIGQKIQGLLPKLAPRTDY 37 CAP18 G1T9L4 Not found camp Oryctolagus cuniculus Antimicrobial, Antibacterial,Anti-Gram+,Anti-Gram- Homology Alpha helix The peptide adopted an appreciable α-helical content in the presence of the organic cosolvent 40% trifluoroethanol and in the presence of 0.1% lipopolysaccharide. 1LYP Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.CAP18 were active against P. aeruginosa, E. coli, S. aureus, and MRSA. [Ref.11557478]Gram-negative bacteria:Pseudomonas aeruginosa(MIC=1-32 µg/ml); Pseudomonas aeruginosa(MIC50=4 µg/ml); Pseudomonas aeruginosa(MIC90=16 µg/ml); Stenotrophomonas maltophilia(MIC=2-16 µg/ml); Achromobacter xylosoxidans(MIC=2-32 µg/ml).##[Ref.10768969]Gram-positive bacteria:Staphylococcus aureus ATCC 33591(MIC=1.24 µM ); Staphylococcus aureus ATCC 33591(100 mM NaCl,MIC=1.36 µM); Staphylococcus aureus 930918-3(MIC=0.41 µM); Staphylococcus aureus 930918-3(100 mM NaCl,MIC=0.63 µM);##Gram-negative bacteria:Pseudomonas aeruginosa PAO1(25 mM NaCl,EC50=0.22±0.05 µM); Pseudomonas aeruginosa PAO1(175 mM NaCl, EC50=0.11±0.02 µM); Escherichia coli DH5α(MIC=0.19 µM); Escherichia coli DH5α(100 mM NaCl, MIC=0.21 µM); Escherichia coli ML-35p(MIC=0.05 µM); Escherichia coli ML-35p(100 mM NaCl, MIC=0.09 µM); Pseudomonas aeruginosa PAO1(MIC=0.20 µM); Pseudomonas aeruginosa PAO1(100 mM NaCl, MIC=0.62 µM); Pseudomonas aeruginosa MR3007(MIC=0.05 µM); Pseudomonas aeruginosa MR3007(100 mM NaCl, MIC=0.36 µM).##[Ref.26656394]Gram-negative bacteria:Yersinia ruckeri 392/2003(MIC=2-4 µg/ml); Aeromonas salmonicida ATCC 49385(MIC=2 µg/ml); Salmonella enterica serovar Typhimurium LT2(MIC=4-8 µg/ml); Campylobacter jejuni NCTC 11168(MIC=1 µg/ml); Escherichia coli ATCC 25922(MIC=4-8 µg/ml ); Pseudomonas aeruginosa ATCC 27853(MIC=4-8 µg/ml); Escherichia coli BW25113(MIC=4-8 µg/ml); Escherichia coli BW25113 del-rfaC(MIC=4 µg/ml); Escherichia coli ATCC 25922 del-rfaC(MIC=2 µg/ml);##Gram-positive bacterial:Flavobacterium psychrophilum 1947(MIC>>256 µg/ml); Staphylococcus aureus ATCC 29213(MIC>=32 µg/ml); Enterococcus faecalis ATCC 29212(MIC=8 µg/ml); Listeria monocytogenes N22-2(MIC=2-4 µg/ml).##[Ref.30245684]Gram-negative bacterial:Escherichia coli ATCC 25922 del-waaC(MIC=2-4 µg/ml); Escherichia coli ATCC 25922 del-waaE(MIC=4 µg/ml); Escherichia coli ATCC 25922 del-waaF(MIC=2-4 µg/ml); Escherichia coli ATCC 25922 del-waaG(MIC=4 µg/ml); Escherichia coli JW3596(MIC=4 µg/ml); Escherichia coli JW1667(MIC=2-4 µg/ml ).##[Ref.29852015]Gram-negative bacterial:Aeromonas salmonicida ATCC 33658(MIC=4 µg/ml);##Gram-positive bacterial:Lactococcus lactis IL1403(MIC=1-2 µg/ml). [Ref.10768969]non-hemolysis against Human erythrocytes up to 500 µg/ml.##[Ref.26656394]1% hemolysis against Horse erythrocytes at 64 µg/ml. Linear Free Free L Not found liposomes 11557478##10768969##26656394##30245684##29852015 Antimicrob Agents Chemother. 2001 Oct;45(10):2838-2844.##Infect Immun. 2000 May;68(5):2748-2755.##PLoS One. 2015 Dec 11;10(12):e0144611.##Front Microbiol. 2018 Sep 7;9:2153.##PLoS One. 2018 May 31;13(5):e0197742. Saiman L, Tabibi S, Starner TD, San Gabriel P, Winokur PL, Jia HP, McCray PB Jr, Tack BF.##Travis SM, Anderson NN, Forsyth WR, Espiritu C, Conway BD, Greenberg EP, McCray PB Jr, Lehrer RI, Welsh MJ, Tack BF.##Ebbensgaard A, Mordhorst H, Overgaard MT, Nielsen CG, Aarestrup FM, Hansen EB.##Ebbensgaard A, Mordhorst H, Aarestrup FM, Hansen EB.##Ebbensgaard A, Mordhorst H, Overgaard MT, Aarestrup FM, Hansen EB. Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis.##Bactericidal activity of mammalian cathelicidin-derived peptides.##Comparative Evaluation of the Antimicrobial Activity of Different Antimicrobial Peptides against a Range of Pathogenic Bacteria.##The Role of Outer Membrane Proteins and Lipopolysaccharides for the Sensitivity of Escherichia coli to Antimicrobial Peptides. ##Dissection of the antimicrobial and hemolytic activity of Cap18: Generation of Cap18 derivatives with enhanced specificity. DRAMP29100 GIRDVLKGAAKAFVKTVAGHIAN 23 Ascaphin-1 [F2I] P0CJ25 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram- Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria [Ref.19947578]Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=4 µM). [Ref.19947578]25% hemolysis against human erythrocytes at 100 µM. Linear Free Amidation L [Ref.19947578]No cytotoxicity information found. liposomes 19947578 J Chem Inf Model. 2009 Dec;49(12):2873-82. Juretić D, Vukicević D, Ilić N, Antcheva N, Tossi A. Computational design of highly selective antimicrobial peptides. DRAMP29101 GFKDLLKGAAKALVKAVLF 19 Ascaphin-8 [T16A] P0CJ32 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Anti-cancer, Antifungal Protein level Alpha helix 45% α-helix was determined from the circular dichroism spectra recorded in 50% trifluoroethanol-water. Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=6 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=3 µM);##Fungi:Candida albicans ATCC 900280(MIC=6 µM).##Cancer:human hepatoma‐derived cells HepG2 (LC50=9 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=22 µM). Linear Free Amidation L [Ref.18554256]Cytotoxicity:Mouse fibroblasts L929 (LC50=5 µM). liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29102 KFFKRLLKSVRRAVKKFRKKPRLIGLSTLL 30 Hc-CATH No entry found Not found Not found Hydrophis cyanocinctus Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Anti-cancer, Antifungal Not found Alpha helix,β-sheet,random coil The CD spectra in H2O adopts a random-coil conformation. In the membrane-mimetic environments of SDS/H2O solutions (30–120 mm), the secondary structure components of Hc-CATH dissolved in 60 mm SDS/H2O were calculated as 59.9% α-helix, 16% β-sheet, 0% β-turn, and 24% random coil.When dissolved in SDS/H2O solutions with serial concentrations of NaCl (at 0, 100, 200, and 400 mm), the α-helix contents decreased slightly from 59.9 to 33.8% as the NaCl concentration increased. Simultaneously, the contents of the β-turn (0 to 14.9%) and random coil (24 to 30.5%) increased slightly. Function:The microbial killing activity of Hc-CATH is executed through the disruption of cell membrane and lysis of bacterial cells. Antimicrobial activity of Hc-CATH in the presence of a high concentration of sodium chlorideIn addition is strong. Hc-CATH exhibited potent anti-inflammatory activity by inhibiting the LPS-induced production of nitric oxide (NO) and pro-inflammatory cytokines such as TNF-α, IL-1β, and IL-6. [Ref.26013823]Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=2.34 µg/ml); Escherichia coli ATCC 25922(400 Mm NaCl,MIC=4.69 µg/ml); Escherichia coli 1(MIC=2.34 µg/ml);Escherichia coli 2(MIC=2.34 µg/ml); Escherichia coli 3(MIC=2.34 µg/ml); Escherichia coli 4(MIC=9.38 µg/ml); Shigella dysenteriae(MIC=0.59 µg/ml); Klebsiella pneumoniae 1(MIC=37.50 µg/ml); Klebsiella pneumoniae 2(MIC=4.69 µg/ml); Klebsiella pneumoniae 3(MIC=9.38 µg/ml); Klebsiella pneumoniae 4(MIC=9.38 µg/ml); Klebsiella pneumoniae 5(MIC=18.75 µg/ml); Klebsiella pneumoniae 6(MIC=37.50 µg/ml); Klebsiella pneumoniae 7(MIC=37.50 µg/ml); Klebsiella pneumoniae 8(MIC=75.00 µg/ml); Serratia marcescens(MIC>200 µg/ml); Klebsiella oxytoca(MIC=4.69 µg/ml); Proteus vulgaris(MIC>200 µg/ml); Proteus mirabilis(MIC=4.69 µg/ml); Acinetobacter baumannii 1(MIC>200 µg/ml); Acinetobacter baumannii 2(MIC>200 µg/ml); Stenotrophomonas maltophilia(MIC>200 µg/ml); Stenotrophomonas maltophilia 2(MIC=9.38 µg/ml); Pseudomonas aeruginosa ATCC 27853(MIC=18.75 µg/ml); Pseudomonas aeruginosa 1 (MIC=37.50 µg/ml ); Pseudomonas aeruginosa(MIC>200 µg/ml); Salmonella paratyphi A(MIC=4.69 µg/ml);##Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4.69 µg/ml); Staphylococcus aureus 1(MIC>200 µg/ml ); Staphylococcus aureus 2(MIC>200 µg/ml ); Staphylococcus aureus 3(MIC>200 µg/ml ); Staphylococcus aureus 4(MIC=4.69 µg/ml); Staphylococcus aureus 5(MIC=4.69 µg/ml); Bacillus cereus(MIC=9.38 µg/ml); Bacillus subtilis(MIC=75.00 µg/ml); Enterococcus faecium(MIC=37.50 µg/ml); Nocardia asteroides(MIC=9.38 µg/ml); Enterococcus faecalis(MIC>200 µg/ml); Staphylococcus epidermidis(MIC>200 µg/ml);##Fungi:Candida albicans 1(MIC=4.69 µg/ml); Candida albicans 2(MIC=4.69 µg/ml); Candida albicans 3(MIC=4.69 µg/ml); Candida albicans 4(MIC=4.69 µg/ml); Candida albicans 5(MIC=2.34 µg/ml); Candida albicans 6(MIC=2.34 µg/ml); Candida glabrata 1(MIC=2.34 µg/ml); Candida glabrata(MIC>200 µg/ml); Cryptococcus neoformans(MIC>200 µg/ml); Arcyria cinerea(MIC=9.38 µg/ml);##Pathogenic bacteria:Aeromonas sobria(MIC=2.34 µg/ml); Aeromonas hydrophila(MIC=2.34 µg/ml); Aeromonas veronii(MIC=2.34 µg/ml); Vibrio vulnificus(MIC=4.69 µg/ml ); Vibrio harveyi(MIC=9.38 µg/ml); Vibrio fluvialis(MIC=4.69 µg/ml); Vibrio alginolyticus(MIC=4.69 µg/ml); Vibrio parahaemolyticus(MIC=9.38 µg/ml); Vibrio splendidus(MIC=2.34 µg/ml); Vibrio anguillarum(MIC=18.75 µg/ml); Edwardsiella tarda(MIC=2.34 µg/ml). [Ref.26013823]5.25% Hemolysis against Human erythrocytes at 200 µg/ml(55.12 μM). Linear Free Free L [Ref.26013823]4.70% cell death at 200 µg/ml against Human hepatocellular carcinoma HepG2; 3.63% cell death at 200 µg/ml against Human prostate adenocarcinoma PC-3; 1.30% cell death at 200 µg/ml against Mouse fibroblasts L929. liposomes 26013823 J Biol Chem. 2015 Jul 3;290(27):16633-52. Wei L, Gao J, Zhang S, Wu S, Xie Z, Ling G, Kuang YQ, Yang Y, Yu H, Wang Y. Identification and Characterization of the First Cathelicidin from Sea Snakes with Potent Antimicrobial and Anti-inflammatory Activity and Special Mechanism. DRAMP29103 KWKLFKKIHKVGQNIRKGIIKAGPAVAVVGQAAQIAK 37 PEW300 P01507 Not found Synthetic construct(Mutation of cecropin-A) Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix(Predicted) Not found Function:Purified PEW300 exhibited strong antibacterial activity against various Gram-positive and Gram-negative bacteria.PEW300 had no hemolytic activity toward mammalian cells even at high concentration (224 ng/μl).It showed good stability in neutral and alkaline solutions. PEW300 was thermally stable even at up to 100 °C and resistant to proteinase K, pepsin, snailase, and trypsin.The incubation with human serum had no effect on the antibacterial activity of PEW300. [Ref.30607494]Gram-positive bacteria:Staphylococcus aureus ATCC 6538(MIC=14.18 µg/ml); Staphylococcus aureus ATCC 6538(MBC=28.36 µg/ml); Bacillus megaterium ATCC 14945(MIC=7.09 µg/ml); Bacillus megaterium ATCC 14945(MBC=14.18 µg/ml); Bacillus licheniformis ATCC 14580(MIC=14.18 µg/ml); Bacillus licheniformis ATCC 14580(MBC=14.18 µg/ml); Staphylococcus epidermidis ATCC 12228(MIC=7.09 µg/ml); Staphylococcus epidermidis ATCC 12228(MBC=7.09 µg/ml);Bacillus cereus ATCC 10876(MIC=14.18 µg/ml);Bacillus cereus ATCC 10876(MBC=28.36 µg/ml);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=7.09 µg/ml); Escherichia coli ATCC 25922(MBC=7.09 µg/ml); Pseudomonas aeruginosa ATCC 9027(MIC=14.18 µg/ml); Pseudomonas aeruginosa ATCC 9027(MBC=14.18 µg/ml); Stenotrophomonas maltophilia ATCC 51331(MIC=28.35 µg/ml); Stenotrophomonas maltophilia ATCC 51331(MBC=56.70 µg/ml); Pseudomonas otitidis MCC 10330(MIC=14.18 µg/ml); Pseudomonas otitidis MCC 10330(MBC=14.18 µg/ml); Klebsiella pneumoniae ATCC 35657(MIC=9.88 µg/ml); Klebsiella pneumoniae ATCC 35657(MBC=9.88 µg/ml); Salmonella enteritidis ATCC 9120(MIC=4.93 µg/ml); Salmonella enteritidis ATCC 9120(MBC=4.93 µg/ml). [Ref.30607494]non-hemolysis to Sheep erythrocytes up to 224 µg/ml. Linear Free Free L [Ref.30607494]No cytotoxicity information found. liposomes 30607494 Appl Microbiol Biotechnol. 2019 Feb;103(4):1765-1775. Wang M, Lin J, Sun Q, Zheng K, Ma Y, Wang J. Design, expression, and characterization of a novel cecropin A-derived peptide with high antibacterial activity. DRAMP29104 LNLKALLAVAKKIL 14 Mastoparan-C(MP-C) P01516 Not found Vespa crabro Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Anti-cancer,Antifungal Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,24.85% α-helix was determined in 50% TFE. Function:The peptide was tolerant in the presence of physiological salts.MP-C lost antimicrobial activities after incubation with 20 μg/mL trypsin or chymotrypsin,indicating moderate protease resistance. [Ref.29904274]Gram-positive bacteria:Staphylococcus aureus NCTC 10788(MIC=2 µM); Staphylococcus aureus NCTC 10788(MBC=2 µM); Staphylococcus aureus ATCC 12493(MRSA,MIC=4 µM); Staphylococcus aureus ATCC 12493(MRSA,MBC=4 µM); Enterococcus faecalis NCTC 12697(MIC=8 µM); Enterococcus faecalis NCTC 12697(MBC=8 µM);##Gram-negative bacteria:Escherichia coli NCTC 10418(MIC=4 µM); Escherichia coli NCTC 10418(MBC=8 µM); Pseudomonas aeruginosa ATCC 27853(MIC=8 µM); Pseudomonas aeruginosa ATCC 27853(MBC=16 µM); Fungi:Candida albicans NCTC 1467(MIC=4 µM); Candida albicans NCTC 1467(MBC=4 µM);##Cancer:Human squamous lung carcinoma NCI-H157(IC50=13.57 µM);Human breast adenocarcinoma MDA-MB-435S(IC50=27.70 µM);Human prostate adenocarcinoma PC-3(IC50=6.29 µM);Human glioblastoma U251-MG(IC50=36.65 µM); Human breast adenocarcinoma MCF-7(IC50=25.27 µM).##[Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacterial:Escherichia coli ATCC 25922(4.5 mM KCl and 0.004 mM FeCl3,MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(4.5 mM KCl,MIC=8 µM); Klebsiella pneumoniae ATCC 700603(MIC=8 µM); Escherichia coli ATCC 25922(NaCl/MgCl2=150mM/1mM,MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(NaCl/MgCl2=150mM/1mM,MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(0.004mM FeCl3,MIC=4 µM);Escherichia coli(Rifampin-resistant strain,MIC=4 µM). [Ref.29904274]50% hemolysis against horse erythrocytes at 40.11 µM.##[Ref.33285267]10% hemolysis against mouse erythrocytes at 64 µM; 60% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.29904274]Cytotoxicity:Human microvascular endothelial cells HMEC-1(IC50=57.15 µM).##[Ref.33285267]90% Killing against Human embryonic kidney HEK293T cells at 128 µM; Human embryonic kidney HEK293T cells(IC50=16 µM). liposomes 33285267##29904274 Eur J Pharm Sci. 2021 Mar 1;158:105665.##Int J Biol Sci. 2018 Apr 25;14(6):599-607. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. ##Chen X, Zhang L, Wu Y, Wang L, Ma C, Xi X, Bininda-Emonds ORP, Shaw C, Chen T, Zhou M. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria.##Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering. DRAMP29105 CLNLKALLAVAKKILC 16 c Mastoparan-C(cMP-C) P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Anti-cancer,Antifungal Protein level Alpha helix,random coil 76% α-helix was determined from the circular dichroism spectra recorded in 50% TFE/10mM NH4AC solution,28% of the secondary structure retained an α-helical domain in an aqueous environment. Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.29904274]Gram-positive bacteria:Staphylococcus aureus NCTC 10788(MIC=32 µM); Staphylococcus aureus NCTC 10788(MBC=64 µM); Staphylococcus aureus ATCC 12493(MRSA,MIC=128 µM); Staphylococcus aureus ATCC 12493(MRSA,MBC=128 µM); Enterococcus faecalis NCTC 12697(MIC=128 µM); Enterococcus faecalis NCTC 12697(MBC=128 µM);##Gram-negative bacteria:Escherichia coli NCTC 10418(MIC=32 µM); Escherichia coli NCTC 10418(MBC=128 µM); Pseudomonas aeruginosa ATCC 27853(MIC=32 µM); Pseudomonas aeruginosa ATCC 27853(MBC>512 µM);##Fungi:Candida albicans NCTC 1467(MIC=32 µM); Candida albicans NCTC 1467(MBC=128 µM);##Cancer:Human squamous lung carcinoma NCI-H157(IC50=7.02 µM);Human breast adenocarcinoma MDA-MB-435S(IC50=13.87 µM);Human prostate adenocarcinoma PC-3(IC50=13.87 µM);Human glioblastoma U251-MG(IC50=8.56 µM); Human breast adenocarcinoma MCF-7(IC50=13.66 µM). [Ref.29904274]50% hemolysis against horse erythrocytes at 9.19 µM. Cyclic Free Amidation Disulfide bond (Cys1-Cys16) L [Ref.29904274]Cytotoxicity:Human microvascular endothelial cells HMEC-1(IC50=39.53 µM). liposomes 29904274 Int J Biol Sci. 2018 Apr 25;14(6):599-607. Chen X, Zhang L, Wu Y, Wang L, Ma C, Xi X, Bininda-Emonds ORP, Shaw C, Chen T, Zhou M. Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering. DRAMP29106 RKKRRQRRRLNLKALLAVAKKIL 23 t Mastoparan-C(tMP-C, Tat (49-57)-Mastoparan-C) P01516,Q76PP9 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Anti-cancer,Antifungal Protein level Alpha helix,random coil 28% α-helix was determined from the circular dichroism spectra recorded in 50% TFE/10mM NH4AC solution,and it adopted a random coil structure in an aqueous environment. Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.29904274]Gram-positive bacteria:Staphylococcus aureus NCTC 10788(MIC=4 µM); Staphylococcus aureus NCTC 10788(MBC=4 µM); Staphylococcus aureus ATCC 12493(MRSA,MIC=4 µM); Staphylococcus aureus ATCC 12493(MRSA,MBC=8 µM); Enterococcus faecalis NCTC 12697(MIC=8 µM); Enterococcus faecalis NCTC 12697(MBC=16 µM);##Gram-negative bacteria:Escherichia coli NCTC 10418(MIC=2 µM); Escherichia coli NCTC 10418(MBC=2 µM); Pseudomonas aeruginosa ATCC 27853(MIC=4 µM); Pseudomonas aeruginosa ATCC 27853(MBC=4 µM);##Fungi:Candida albicans NCTC 1467(MIC=2 µM); Candida albicans NCTC 1467(MBC=2 µM);##Cancer:Human squamous lung carcinoma NCI-H157(IC50=2.79 µM);Human breast adenocarcinoma MDA-MB-435S(IC50=3.86 µM);Human prostate adenocarcinoma PC-3(IC50=3.86 µM);Human glioblastoma U251-MG(IC50=3.36 µM); Human breast adenocarcinoma MCF-7(IC50=3.70 µM). [Ref.29904274]50% hemolysis against horse erythrocytes at 77.94 µM. Linear Free Amidation L [Ref.29904274]Cytotoxicity:Human microvascular endothelial cells HMEC-1(IC50=9.18 µM). liposomes 29904274 Int J Biol Sci. 2018 Apr 25;14(6):599-607. Chen X, Zhang L, Wu Y, Wang L, Ma C, Xi X, Bininda-Emonds ORP, Shaw C, Chen T, Zhou M. Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering. DRAMP29107 ANLKALLAVAKKIL 14 Mastoparan-C [L1A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,43.88% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]2% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29108 LALKALLAVAKKIL 14 Mastoparan-C [N2A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,19.52% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(MIC=8 µM); Klebsiella pneumoniae ATCC 700603(MIC=8 µM). [Ref.33285267]10% hemolysis against mouse erythrocytes at 128 µM,50% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29109 LNAKALLAVAKKIL 14 Mastoparan-C [L3A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,4.24% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29110 LNLAALLAVAKKIL 14 Mastoparan-C [K4A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,27.41% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=16 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]10% hemolysis against mouse erythrocytes at 128 µM,52% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29111 LNLKAALAVAKKIL 14 Mastoparan-C [L6A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,44.72% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29112 LNLKALAAVAKKIL 14 Mastoparan-C [L7A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,34.08% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µM); Bacillus subtilis ATCC 23857(MIC=8 µM); ##Gram-negative bacteria:Escherichia coli ATCC 25922(4.5 mM KCl and 0.004 mM FeCl3,MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(4.5 mM KCl,MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM); Escherichia coli ATCC 25922(150mM NaCl,MIC=32 µM); Escherichia coli ATCC 25922(1mM MgCl2,MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(150mM NaCl,MIC=32 µM); Pseudomonas aeruginosa ATCC 9027(1mM MgCl2,MIC=64 µM); Pseudomonas aeruginosa ATCC 9027(0.004mM FeCl3,MIC=8 µM);Escherichia coli(Rifampin-resistant strain,MIC=8 µM). [Ref.33285267]8% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]45% Killing against Human embryonic kidney HEK293T cells at 128 µM; Human embryonic kidney HEK293T cells(IC50>128 µM). liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29113 LNLKALLAAAKKIL 14 Mastoparan-C [V9A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,7.45% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]20% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29114 LNLKALLAVAAKIL 14 Mastoparan-C [K11A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,16.69% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=16 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]18% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29115 LNLKALLAVAKAIL 14 Mastoparan-C [K12A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,37.54% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]10% hemolysis against mouse erythrocytes at 32 µM,90% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29116 LNLKALLAVAKKAL 14 Mastoparan-C [I13A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,8.91% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]5% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29117 LNLKALLAVAKKIA 14 Mastoparan-C [L14A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,15.36% α-helix was determined in 60% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]5% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29118 GNLKALLAVAKKIL 14 Mastoparan-C [L1G] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,16.12% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(4.5 mM KCl and 0.004 mM FeCl3,MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(0.004 mM FeCl3,MIC=8 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM); Escherichia coli ATCC 25922(150mM NaCl,MIC=8 µM); Escherichia coli ATCC 25922(1mM MgCl2,MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(150mM NaCl,MIC=32 µM); Pseudomonas aeruginosa ATCC 9027(4.5mM KCl,MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(1mM MgCl2,MIC=64 µM);Escherichia coli(Rifampin-resistant strain,MIC=8 µM). [Ref.33285267]8% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]80% Killing against Human embryonic kidney HEK293T cells at 128 µM; Human embryonic kidney HEK293T cells(IC50=128 µM). liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29119 LNLKALGAVAKKIL 14 Mastoparan-C [L7G] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,7.26% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=128 µM); Bacillus subtilis ATCC 23857(MIC=32 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=32 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=64 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29120 KNLKALLAVAKKIL 14 Mastoparan-C [L1K] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,18.62% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=64 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=8 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29121 GNLKALAAVAKKIL 14 Mastoparan-C [L1G, L7A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,1.61% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC>128 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=64 µM); Pseudomonas aeruginosa ATCC 9027(MIC=64 µM); Klebsiella pneumoniae ATCC 700603(MIC=128 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29122 LNLRALLAVARRIL 14 Mastoparan-C [K4,11,12R] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,24.8% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=4 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(MIC=8 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM). [Ref.33285267]10% hemolysis against mouse erythrocytes at 32 µM,87% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29123 LNLKKLLAVAKKIL 14 Mastoparan-C [A5K] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,25.08% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=8 µM); Bacillus subtilis ATCC 23857(MIC=2 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(MIC=4 µM); Klebsiella pneumoniae ATCC 700603(MIC=4 µM). [Ref.33285267]10% hemolysis against mouse erythrocytes at 128 µM,30% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29124 LNLKKLLKVAKKIL 14 Mastoparan-C [A5,8K] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,3.56% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=4 µM); Klebsiella pneumoniae ATCC 700603(MIC=8 µM). [Ref.33285267]15% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29125 LNLKALLAVAKKI 13 Mastoparan-C (1-13) P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,16.87% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=64 µM); Bacillus subtilis ATCC 23857(MIC=16 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(MIC=32 µM); Klebsiella pneumoniae ATCC 700603(MIC=64 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29126 LNLKALLAVAKK 12 Mastoparan-C (1-12) P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,8.04% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC>128 µM); Bacillus subtilis ATCC 23857(MIC>128 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC>128 µM); Pseudomonas aeruginosa ATCC 9027(MIC>128 µM); Klebsiella pneumoniae ATCC 700603(MIC>128 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29127 LNLKALLAVAK 11 Mastoparan-C (1-11) P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,24.68% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC>128 µM); Bacillus subtilis ATCC 23857(MIC>128 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC>128 µM); Pseudomonas aeruginosa ATCC 9027(MIC>128 µM); Klebsiella pneumoniae ATCC 700603(MIC>128 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29128 GNLKKLLAVAKKIL 14 Mastoparan-C [L1G, A5K] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,22.26% α-helix was determined in50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(4.5 mM KCl and 0.004 mM FeCl3,MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(0.004 mM FeCl3,MIC=4 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM); Escherichia coli ATCC 25922(150mM NaCl,MIC=16 µM); Escherichia coli ATCC 25922(1mM MgCl2,MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(NaCl/MgCl2=150mM/1mM,MIC=32 µM); Pseudomonas aeruginosa ATCC 9027(4.5mM KCl,MIC=16 µM); Escherichia coli(Rifampin-resistant strain,MIC=4 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]65% Killing against Human embryonic kidney HEK293T cells at 128 µM; Human embryonic kidney HEK293T cells(IC50=128 µM). liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29129 LNLKKLAAVAKKIL 14 Mastoparan-C [A5K, L7A] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,8.55% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(MIC=4 µM); Klebsiella pneumoniae ATCC 700603(MIC=32 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29130 LNLKKLLAVAKKI 13 Mastoparan-C (1-13) [A5K] P01516 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Protein level Alpha helix,random coil The CD spectra in water adopts a random-coil conformation,4.42% α-helix was determined in 50% TFE. Function:when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027. [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=128 µM); Bacillus subtilis ATCC 23857(MIC=8 µM);##Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=16 µM); Pseudomonas aeruginosa ATCC 9027(MIC=16 µM); Klebsiella pneumoniae ATCC 700603(MIC=64 µM). [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM. Linear Free Amidation L [Ref.33285267]No cytotoxicity information found. liposomes 33285267 Eur J Pharm Sci. 2021 Mar 1;158:105665. Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J. Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria. DRAMP29131 KLLGPLLKIAAKVGSNLL 18 XT-7 [G1K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=25 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=12.5 µM);##Fungi:Candida albicans ATCC 900280(MIC=50 µM);##Cancer:human hepatoma‐derived cells HepG2 (LC50=230 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=400 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29132 GLLGKLLKIAAKVGSNLL 18 XT-7 [P5K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Alpha helix 53% α-helix was determined from the circular dichroism spectra recorded in 50% trifluoroethanol-water. Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=12.5 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=3 µM);##Fungi:Candida albicans ATCC 900280(MIC=6 µM);##Cancer:human hepatoma‐derived cells HepG2 (LC50=14 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=15 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29133 GLLGPLLKIAKKVGSNLL 18 XT-7 [A11K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=50 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=25 µM);##Fungi:Candida albicans ATCC 900280(MIC=25 µM);##Cancer:human hepatoma‐derived cells HepG2 (LC50=65 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=350 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29134 GLLGPLLKIAAKVGKNLL 18 XT-7 [S15K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=12.5 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=3 µM);##Fungi:Candida albicans ATCC 900280(MIC=25 µM);##Cancer:human hepatoma‐derived cells HepG2 (LC50=24 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=110 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29135 GLLGPLLKIAAKVGKKLL 18 XT-7 [S15K,N16K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=50 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=6 µM);##Fungi:Candida albicans ATCC 900280(MIC=6 µM);##Cancer:hepatoma‐derived cells HepG2 (LC50=10 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=60 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29136 GLLGPLLKIAAKVGSKLL 18 XT-7 [N16K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.23094651]Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=6.3 µM).##[Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=12.5 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=3 µM);##Fungi:Candida albicans ATCC 900280(MIC=12.5 µM);##Cancer: human hepatoma‐derived cells HepG2 (LC50=22 µM). [Ref.23094651]50% hemolysis against rat erythrocytes at 142 µM.##[Ref.18554256]Hemolysis against human erythrocytes (LC50=80 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 23094651##18554256 J Chem Inf Model. 2012 Dec 21;52(12):3341-51.##Chem Biol Drug Des. 2008 Jul;72(1):58-64. Kamech N, Vukičević D, Ladram A, Piesse C, Vasseur J, Bojović V, Simunić J, Juretić D.##Conlon JM, Galadari S, Raza H, Condamine E. Improving the selectivity of antimicrobial peptides from anuran skin.##Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29137 GLLGKLLKIAAKVGKKLL 18 XT-7 [P5K,S15K,N16K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=25 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=3 µM);##Fungi:Candida albicans ATCC 900280(MIC=3 µM);##Cancer:human hepatoma‐derived cells HepG2 (LC50=5 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=25 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29138 GLLKKLLKIAAKVGKKLL 18 XT-7 [G4K,P5K,S15K,N16K] P84381 Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Protein level Not found Not found Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Antifungal activity against Candida albicans. [Ref.18554256]Gram-negative bacteria:Escherichia coli ATCC 25726(MIC=12.5 µM);##Gram-positive bactria:Staphylococcus aureus ATCC 25923(MIC=6 µM);##Fungi:Candida albicans ATCC 900280(MIC=3 µM);##Cancer: human hepatoma‐derived cells HepG2 (LC50=6 µM). [Ref.18554256]Hemolysis against human erythrocytes (LC50=25 µM). Linear Free Amidation L [Ref.18554256]No cytotoxicity information found. liposomes 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. DRAMP29139 IRPIPFIPRGGKT 13 Pxt‐1 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 10.9%,12.2%,12.7% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]0.1% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Amidation L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29140 FIGALLRPALKLLA 14 Pxt‐2 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix,random coil 3.8%,4.0%,4.9% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:showed growth inhibitory effects on both Escherichia coli (Gram-negative) and Staphylococcus aureus (Gram-positive). [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(MIC=50 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(MIC=9.7 µg/ml).##[Ref.26802742]Gram-negative bacteria:Escherichia coli NBRC 14237(MIC<12.5 µM);Pseudomonas aeruginosa NBRC 12582(MIC<50 µM);##Gram-positive bacteria:Staphylococcus aureus NBRC 12732(MIC<12.5 µM);Micrococcus luteus NBRC 12708(MIC<25 µM);##Fungi:Saccharomyces cerevisiae NBRC 10217(ND);Candida albicans NBRC 1594(ND). [Ref.25312021]0.4% Hemolysis against Rat erythrocytes at 20 µM.##[Ref.26802742]2% Hemolysis against Rat erythrocytes at 50 µM. Linear Free Amidation L [Ref.25312021]No cytotoxicity information found. Not found 25312021##26802742 FEBS J. 2015 Jan;282(1):102-13.##J Biochem. 2016 Jun;159(6):619-29. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M.##Shigeri Y, Horie M, Yoshida T, Hagihara Y, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis.##Physicochemical and biological characterizations of Pxt peptides from amphibian (Xenopus tropicalis) skin. DRAMP29141 GLKEVAHSAKKFAKGFISGLTGS 23 Pxt‐3 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix,random coil 0.5%,1.2%,2.0% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml).##[Ref.23935531]Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=64 µm);Pseudomonas aeruginosa ATCC 15692(MIC >256 µM);##Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC >256 µM);Micrococcus luteus(MIC=32 µM);##Fungi:Saccharomyces cerevisiae(MIC=128 µM);##Parasite:Trypanosoma brucei(LC95=8->256 µM). [Ref.25312021]0.2% Hemolysis against Rat erythrocytes at 20 µM.##[Ref.23935531] Hemolysis against Mouse erythrocytes (HC50>256 µm). Linear Free Free L [Ref.23935531]Cytotoxicity against T-lymphocytes(IC50>256 µM). Not found 25312021##23935531 FEBS J. 2015 Jan;282(1):102-13.##PLoS Genet. 2013;9(8):e1003662. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M.##Roelants K, Fry BG, Ye L, Stijlemans B, Brys L, Kok P, Clynen E, Schoofs L, Cornelis P, Bossuyt F. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis.##Origin and functional diversification of an amphibian defense peptide arsenal. DRAMP29142 LKGASKLIPHLLPSRQQ 17 Pxt‐4 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 1.8%,2.8%,3.9% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]0.1% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Free L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29143 FIGALLGPLLNLLK 14 Pxt‐5 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 37.4%,36.5%,34.6% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:showed growth inhibitory effects on both Escherichia coli (Gram-negative) and Staphylococcus aureus (Gram-positive). [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]10.5% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Amidation L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29144 IRPVPFFPPVHAKKVFPLH 19 Pxt‐6 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 2.3%,5.1%,7.4% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]0.3% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Free L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29145 GGLIGTLTAKQIKK 14 Pxt-7 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 2.6%,2.8%,6.6% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]0.4% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Amidation The 'G' at position 1 is pyroglutamic acid L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29146 GLMGTLISKQMKK 13 Pxt‐11 No entry found Not found Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram- Not found Alpha helix,random coil 2.3%,4.2%,6.6% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2). Function:Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. [Ref.25312021]Gram-negative bacteria:Escherichia coli DH5α(Not active up to 150 µg/ml);##Gram-positive bacteria:Staphylococcus aureus JCM 2151(Not active up to 150 µg/ml). [Ref.25312021]0.3% Hemolysis against Rat erythrocytes at 20 µM. Linear Free Amidation The 'G' at position 1 is pyroglutamic acid L [Ref.25312021]No cytotoxicity information found. Not found 25312021 FEBS J. 2015 Jan;282(1):102-13. Shigeri Y, Yasuda A, Hagihara Y, Nishi K, Watanabe K, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Identification of novel peptides from amphibian (Xenopus tropicalis) skin by direct tissue MALDI-MS analysis. DRAMP29147 NLLGSLLKTGLKVGSNLL 18 Pxt‐12(CPF-St7) P84386 Not found Xenopus tropicalis Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-,Antifungal Protein level Alpha helix,random coil 0%,2.5%,6.6% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2);68.2%,57.4%,50.5% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 50% TFE. Induced a significant and dose-dependent histamine release. [Ref.26802742]Gram-negative bacteria:Escherichia coli NBRC 14237(MIC<12.5 µM);Pseudomonas aeruginosa NBRC 12582(MIC<50 µM);##Gram-positive bacteria:Staphylococcus aureus NBRC 12732(MIC<12.5 µM);Micrococcus luteus NBRC 12708(MIC<50 µM);##Fungi:Candida albicans NBRC 1594(ND). ##[Ref.23935531]Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=128 µM);Pseudomonas aeruginosa ATCC 15692(MIC >256 µM);##Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=32 µM);Micrococcus luteus(MIC=2 µM);##Fungi:Saccharomyces cerevisiae(MIC=64 µM);##Parasite:Trypanosoma brucei(LC95=2-64 µM). [Ref.26802742]0% Hemolysis against Rat erythrocytes at 50 µM.##[Ref.23935531]Hemolysis against Mouse erythrocytes(IC50=256 µM). Linear Free Amidation L [Ref.23935531]Cytotoxicity against T-lymphocytes(IC50=128 µM). liposomes 26802742##23935531 J Biochem. 2016 Jun;159(6):619-29.##PLoS Genet. 2013;9(8):e1003662. Shigeri Y, Horie M, Yoshida T, Hagihara Y, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M.##Roelants K, Fry BG, Ye L, Stijlemans B, Brys L, Kok P, Clynen E, Schoofs L, Cornelis P, Bossuyt F. Physicochemical and biological characterizations of Pxt peptides from amphibian (Xenopus tropicalis) skin.##Origin and functional diversification of an amphibian defense peptide arsenal. DRAMP29148 KLLNLLPGLLAGIF 14 Reverse Pxt‐5 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix,random coil 10.9%,17.4%,19.8% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2);87.1%,77.0%,70.7% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 50% TFE. Induced a significant and dose-dependent histamine release. [Ref.26802742]Gram-negative bacteria:Escherichia coli NBRC 14237(MIC<12.5 µM);Pseudomonas aeruginosa NBRC 12582(MIC<50 µM);##Gram-positive bacteria:Staphylococcus aureus NBRC 12732(MIC<12.5 µM);Micrococcus luteus NBRC 12708(MIC<25 µM);##Fungi:Candida albicans NBRC 1594(ND). [Ref.26802742]5.2% Hemolysis against Rat erythrocytes at 50 µM. Linear Free Amidation L [Ref.26802742]No cytotoxicity information found. liposomes 26802742 J Biochem. 2016 Jun;159(6):619-29. Shigeri Y, Horie M, Yoshida T, Hagihara Y, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Physicochemical and biological characterizations of Pxt peptides from amphibian (Xenopus tropicalis) skin. DRAMP29149 ALLKLAPRLLAGIF 14 Reverse Pxt-2 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix,random coil 3.6%,4.7%,7.3% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2);28.6%,26.8%,22.8% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 50% TFE. Induced a significant and dose-dependent histamine release. [Ref.26802742]Gram-negative bacteria:Escherichia coli NBRC 14237(MIC<12.5 µM);Pseudomonas aeruginosa NBRC 12582(MIC<50 µM);##Gram-positive bacteria:Staphylococcus aureus NBRC 12732(MIC<12.5 µM);Micrococcus luteus NBRC 12708(MIC<50 µM);##Fungi:Candida albicans NBRC 1594(ND). [Ref.26802742]1.5% Hemolysis against Rat erythrocytes at 50 µM. Linear Free Amidation L [Ref.26802742]No cytotoxicity information found. liposomes 26802742 J Biochem. 2016 Jun;159(6):619-29. Shigeri Y, Horie M, Yoshida T, Hagihara Y, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Physicochemical and biological characterizations of Pxt peptides from amphibian (Xenopus tropicalis) skin. DRAMP29150 LLNSGVKLGTKLLSGLLN 18 Reverse Pxt-12 No entry found Not found Not found Synthetic construct Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-, Antifungal Not found Alpha helix,random coil 0%,0%,2.0% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 10 mm Tris-HCl (pH 7.2);23.7%,21.0%,17.9% α-helix were mearsured by CD spectra at 10 °C, 25 °C and 37 °C in 50% TFE. Induced a significant and dose-dependent histamine release. [Ref.26802742]Gram-negative bacteria:Escherichia coli NBRC 14237(ND);Pseudomonas aeruginosa NBRC 12582(ND);##Gram-positive bacteria:Staphylococcus aureus NBRC 12732(ND);Micrococcus luteus NBRC 12708(ND);##Fungi:Candida albicans NBRC 1594(ND). [Ref.26802742]0% Hemolysis against Rat erythrocytes at 50 µM. Linear Free Amidation L [Ref.26802742]No cytotoxicity information found. liposomes 26802742 J Biochem. 2016 Jun;159(6):619-29. Shigeri Y, Horie M, Yoshida T, Hagihara Y, Imura T, Inagaki H, Haramoto Y, Ito Y, Asashima M. Physicochemical and biological characterizations of Pxt peptides from amphibian (Xenopus tropicalis) skin. DRAMP29151 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1 Q8BB25 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Hemology Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.35087243]Virus:##SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=119.68 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=74.99 nM);inhibition of infection(Pseudovirus)(IC50=309.4 nM);inhibition of infection(Authentic)(IC50=1138 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=131.8 nM);inhibition of infection(Pseudovirus)(IC50=427.55 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=314.6 nM);inhibition of infection(Pseudovirus)(IC50=414.85 nM).##[Ref.32231345]Virus:##SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=409.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=3237 nM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=239.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=631.8 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=802.1 nM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50=787.6 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=1398 nM),inhibit the replication of HCoV-OC43 in RD cells(IC50=1554 nM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50=207.4 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=3963 nM),inhibit the replication of HCoV-229E in Huh-7 cells(IC50=4375 nM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50=751.0 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=7666 nM),inhibit the replication of HCoV-NL63 in LLC-MK2 cells(IC50=3693 nM);##CoV-WIV1:ihibition of cell-cell fusion in Huh-7 cells(IC50=265.7 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=5425 nM);##CoV-Rs3367:ihibition of cell-cell fusion in Huh-7 cells(IC50=237.0 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=6014 nM);##CoV-SHC014:ihibition of cell-cell fusion in Huh-7 cells(IC50=279.6 nM);##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=286.7-315.0 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=2375.0 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=2468 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 35087243##32231345##30989115##32047258 Cell Res. 2022 Apr;32(4):404-406.##Cell Res. 2020 Apr;30(4):343-355.##Sci Adv. 2019 Apr 10;5(4):eaav4580.##Cell Mol Immunol. 2020 Jul;17(7):765-767. Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L.##Xia S, Yan L, Xu W, Agrawal AS, Algaissi A, Tseng CK, Wang Q, Du L, Tan W, Wilson IA, Jiang S, Yang B, Lu L.##Xia S, Zhu Y, Liu M, Lan Q, Xu W, Wu Y, Ying T, Liu S, Shi Z, Jiang S, Lu L. Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion.##A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike.##Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. DRAMP29152 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1P Q8BB25 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Hemology Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=69.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-C(Palm) L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29153 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1C Q8BB25 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Hemology Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=37.3-48.1 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=139.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-C(Chol) L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29154 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1C1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=56.8 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=480.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29155 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSG 39 EK1C2 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=48.2 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=418.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29156 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSG 39 EK1C3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=10.6 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=86.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29157 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C4 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.35087243]Virus:##SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=3.32 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=0.88 nM);inhibition of infection(Pseudovirus)(IC50=8.63 nM);inhibition of infection(Authentic)(IC50=85.38 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=4.04 nM);inhibition of infection(Pseudovirus)(IC50=9.83 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=2.57 nM);inhibition of infection(Pseudovirus)(IC50=5.58 nM).##[Ref.32231345]Virus:##SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=11.7 nM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=2.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=11.1 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=4.2 nM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50=7.7 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=37.7 nM),inhibit the replication of HCoV-OC43 in RD cells(IC50=24.8 nM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50=5.2 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=12.4 nM),inhibit the replication of HCoV-229E in Huh-7 cells(IC50=101.5 nM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50=21.4 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=76.6 nM),inhibit the replication of HCoV-NL63 in LLC-MK2 cells(IC50=187.6 nM);##CoV-WIV1:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.5 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=30.8 nM);##CoV-Rs3367:ihibition of cell-cell fusion in Huh-7 cells(IC50=8.1 nM),inhibition of Pseudovirus (PsV) infection in Huh-7 cells(IC50=66.9 nM);##CoV-SHC014:ihibition of cell-cell fusion in Huh-7 cells(IC50=4.3 nM);##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=1.3 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=15.8 nM),inhibit the replication of MERS-CoV in VERO-E6 cells(IC50=2468 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-Chol L [Ref.32231345]<10% cytotoxicity against VERO-E6 cells, RD cells, LLC-MK2 cells, Huh-7 cells up to 10000 nM. liposomes 35087243##32231345 Cell Res. 2022 Apr;32(4):404-406.##Cell Res. 2020 Apr;30(4):343-355. Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29158 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C5 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.1 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=31.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29159 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C6 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.9 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=77.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG12-Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29160 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1C7 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.9 nM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=84.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG24-Chol L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29161 LKVLLYEEFKLLESLIMEILEYQKDSDIKENAEDTK 36 EK1-scrambled No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32231345]Virus:SARS-CoV-2,SARS-CoV,MERS-CoV,HCoV-OC43,HCoV-229E,HCoV-NL63,CoV-WIV1,CoV-Rs3367,CoV-SHC014(No inhibition on the concentration up to 10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 32231345 Cell Res. 2020 Apr;30(4):343-355. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. DRAMP29162 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYGSGC 40 EKL1C No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found EKL1C is a Peptide-based pan-CoV fusion inhibitor,targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.35087243]Virus:##SARS-CoV-2 Omicron:inhibition of cell-cell fusion in Calu-3 cells(IC50=12.18 nM);inhibition of cell-cell infusion in Caco2 cells(IC50=5.52 nM);inhibition of infection(Pseudovirus)(IC50=26.14 nM);inhibition of infection(Authentic)(IC50=182.2 nM);##SARS-CoV-2 Delta:inhibition of cell-cell fusion(IC50=14.42 nM);inhibition of infection(Pseudovirus)(IC50=31.99 nM);##SARS-CoV-2 D614G:inhibition of cell-cell fusion(IC50=11.77 nM);inhibition of infection(Pseudovirus)(IC50=23.6 nM).##[Ref.34367893]Virus:##SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.045±0.006 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.037±0.009 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.040±0.005 μmol/L),inhibition of cell-cell fusion(IC50=0.008±0.001 μmol/L);inhibited authentic SARS-CoV-2 infection in Vero E6 cells(IC50=0.003±0.001 μmol/L);##SARS-CoV-2 variants(inhibition of Pseudovirus(PsV) infection):V341L(IC50=0.047±0.013 μmol/L);F342L(IC50=0.026±0.007 μmol/L);V367F(IC50=0.066±0.012 μmol/L);R408I(IC50=0.148±0.012 μmol/L);N435D(IC50=0.135±0.013 μmol/L);G476S(IC50=0.065±0.008 μmol/L);V483A(IC50=0.078±0.011 μmol/L);N501Y(IC50=0.069±0.006 μmol/L);D614G(IC50=0.104±0.010 μmol/L);12 mutations(P.1)(IC50=0.046±0.006 μmol/L);K417N-E484K-N501Y(IC50=0.113±0.013 μmol/L);8 mutations(B.1.1.7)(IC50=0.120±0.009 μmol/L);wide type(IC50=0.049±0.007 μmol/L);##inhibition of multiple HCoV Pseudovirus:SARS-CoV (IC50=0.076±0.014 μmol/L), MERS-CoV(IC50=0.048±0.006 μmol/L), HCoV-OC43(IC50=0.668±0.081 μmol/L), HCoV-NL63(IC50=0.035±0.003 μmol/L), SARSr-CoV-WIV1(IC50=0.218±0.013 μmol/L), and HCoV-Rs3367 (IC50=0.046±0.003 μmol/L),inhibition of authentic HCoV-OC43 infection in RD cells (IC50=0.281±0.018 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L [Ref.34367893]Huh-7 cells:CC50=10 μmol/L;Caco-2 cells:CC50=13.81 μmol/L;293T/ACE2 cells:CC50=8.49 μmol/L. liposomes 35087243##34367893 Cell Res. 2022 Apr;32(4):404-406.##Acta Pharm Sin B. 2021 Aug 2. Xia S, Chan JF, Wang L, Jiao F, Chik KK, Chu H, Lan Q, Xu W, Wang Q, Wang C, Yuen KY, Lu L, Jiang S.##Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. Peptide-based pan-CoV fusion inhibitors maintain high potency against SARS-CoV-2 Omicron variant.##A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29163 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1-C16 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found EK1-C16 at 0.31 μM could effectively inhibit authentic SARS-CoV-2 WT infection. [Ref.35336956]Virus:##SARS-CoV-2 WT:inhibition of pseudovirus (PsV) infection in Caco2 cells(IC50=0.48 μM);##SARS-CoV-2 Alpha:inhibition of pseudovirus (PsV) infection(IC50=0.19 μM);##SARS-CoV-2 Beta:inhibition of pseudovirus (PsV) infection(IC50=0.43 μM);##SARS-CoV-2 Gamma:inhibition of pseudovirus (PsV) infection(IC50=0.26 μM);##SARS-CoV-2 Delta:inhibition of pseudovirus (PsV) infection(IC50=0.11 μM);##SARS-CoV-2 Omicron:inhibition of pseudovirus (PsV) infection(IC50=0.23 μM);inhibition of authentic infection in Vero-E6-TMPRSS-2 cells(IC50=0.75 μM);##SARS-CoV:inhibition of pseudovirus (PsV) infection(IC50=0.17 μM);##SARSr-CoV WIV1:inhibition of pseudovirus (PsV) infection(IC50=0.15 μM);##SARSr-CoV Rs3367:inhibition of pseudovirus (PsV) infection(IC50=0.3 μM);##MERS-CoV:inhibition of pseudovirus (PsV) infection in Caco2 cells(IC50=0.10 μM);inhibition of cell-cell fusion(IC50=0.012 μM);##HCoV-OC43:inhibition of authentic infection in RD cells(IC50=0.07 μM);inhibition of cell-cell fusion(IC50=0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-C16(palmitic acid) L [Ref.35336956]showed no significant cytotoxicity against RD cells at the concentration of 5 μM. Not found 35336956 Viruses. 2022 Mar 6;14(3):549. Lan Q, Chan JF, Xu W, Wang L, Jiao F, Zhang G, Pu J, Zhou J, Xia S, Lu L, Yuen KY, Jiang S, Wang Q. A Palmitic Acid-Conjugated, Peptide-Based pan-CoV Fusion Inhibitor Potently Inhibits Infection of SARS-CoV-2 Omicron and Other Variants of Concern. DRAMP29164 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKW 45 EKL0 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.583±0.073 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.442±0.037 μmol/L),inhibition of cell-cell fusion(IC50=0.277±0.029 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29165 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEY 36 EKL1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:##SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.622±0.089 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.746±0.152 μmol/L),inhibition of cell-cell fusion(IC50=0.220±0.034 μmol/L);inhibited authentic SARS-CoV-2 infection in Vero E6 cells(IC50=1.407±0.189 μmol/L);##inhibition of multiple HCoV Pseudovirus:SARS-CoV (IC50=6.716±5.937 μmol/L), MERS-CoV(IC50=4.086±0.345 μmol/L), HCoV-OC43(IC50=10.530±3.778 μmol/L), HCoV-NL63(IC50=3.700±0.222 μmol/L), SARSr-CoV-WIV1(IC50=30.270±4.713 μmol/L), and HCoV-Rs3367 (IC50=88.300±24.600 μmol/L),inhibition of authentic HCoV-OC43 infection in RD cells (IC50=20.290±1.092 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29166 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYV 36 EKL2 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.526±0.049 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=4.714±1.173 μmol/L),inhibition of cell-cell fusion(IC50=1.240±0.246 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29167 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKW 36 EKL3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50>10 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50>5 μmol/L),inhibition of cell-cell fusion(IC50=2.167±0.270 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29168 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGC 49 EKL0C No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.122±0.012 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.147±0.055 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.162±0.022 μmol/L),inhibition of cell-cell fusion(IC50=0.021±0.003 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29169 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVGSGC 40 EKL2C No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.115±0.019 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.054±0.014 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.200±0.020 μmol/L),inhibition of cell-cell fusion(IC50=0.022±0.001 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29170 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGC 40 EKL3C No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.127±0.293 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=1.176±1.230 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.892±0.069 μmol/L),inhibition of cell-cell fusion(IC50=0.045±0.004 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29171 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGK 49 EKL0P No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.093±0.012 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.619±0.341 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.176±0.019 μmol/L),inhibition of cell-cell fusion(IC50=0.083±0.009 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Palm L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29172 NVTFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYGSGK 40 EKL1P No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=0.182±0.034 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.812±0.182 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.231±0.022 μmol/L),inhibition of cell-cell fusion(IC50=0.064±0.004 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Palm L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29173 TFLDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVGSGK 40 EKL2P No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=1.129±0.166 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50=0.973±0.254 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=0.304±0.051 μmol/L),inhibition of cell-cell fusion(IC50=0.183±0.028 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Palm L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29174 LDLEYEMKKLEEAIKKLEESYIDLKELGTYEYYVKWGSGK 40 EKL3P No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets a highly conserved target site in HR1 domains in S protein of HCoVs. [Ref.34367893]Virus:SARS-CoV-2:Inhibition of Pseudovirus(PsV) infection in Huh-7 cells(IC50=3.987±0.682 μmol/L),Inhibition of Pseudovirus(PsV) infection in 293T/ACE2 cells(IC50>5 μmol/L),Inhibition of Pseudovirus(PsV) infection in Caco-2 cells(IC50=2.214±0.371 μmol/L),inhibition of cell-cell fusion(IC50=0.193±0.021 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Palm L No cytotoxicity information found in the reference(s) presented liposomes 34367893 Acta Pharm Sin B. 2021 Aug 2. Zhou J, Xu W, Liu Z, Wang C, Xia S, Lan Q, Cai Y, Su S, Pu J, Xing L, Xie Y, Lu L, Jiang S, Wang Q. A highly potent and stable pan-coronavirus fusion inhibitor as a candidate prophylactic and therapeutic for COVID-19 and other coronavirus diseases. DRAMP29175 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 2019-nCoV-HR2P(SARS-CoV-2-S(1168-1203),SARS-HR2P) Q5DIC5 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Hemology Alpha helix Not found Mechanism of action:2019-nCoV HR1 and HR2 regions are able to interact with each other to form 6-HB and suggest that 2019-nCoV-HR2P may inhibit 2019-nCoV fusion with and entry into the target cell. "[Ref.32047258]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in Huh-7 cells(IC50=0.18 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.98 µM).##[Ref.30989115]SARS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50=0.52±0.11 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=2.81 µM);##MERS-CoV:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-OC43:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-229E:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##HCoV-NL63:ihibition of cell-cell fusion in Huh-7 cells(IC50>5 µM);##CoV-WIV1:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=2.73 µM);##CoV-Rs3367:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=3.05 µM)." No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 30989115##32047258 Sci Adv. 2019 Apr 10;5(4):eaav4580.##Cell Mol Immunol. 2020 Jul;17(7):765-767. Xia S, Yan L, Xu W, Agrawal AS, Algaissi A, Tseng CK, Wang Q, Du L, Tan W, Wilson IA, Jiang S, Yang B, Lu L.##Xia S, Zhu Y, Liu M, Lan Q, Xu W, Wu Y, Ying T, Liu S, Shi Z, Jiang S, Lu L. A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike.##Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. DRAMP29176 NGAICWGPCPTAFRQIGNCGHFKVRCCKIR 30 MBD-4 (11-40)(P9) P82019 Belongs to the beta-defensin family. Defb4 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found 6M56 Mechanism of action:Mechanistic studies show that positively charged P9 broadly inhibits viral replication by binding to different viruses and then inhibits virus–host endosomal acidification to prevent the endosomal release of pH-dependent viruses. [Ref.32843628]Virus:##SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=2.4 µg/ml);##SARS-CoV:Inhibition of infection in Vero E6 cells(IC50=6.2 µg/ml);##MERS-CoV:Inhibition of infection in Vero E6 cells(IC50=8.8 µg/ml);##Human rhinovirus (HRV):inhibition of infection in RD cells(IC50=34 µg/ml);##Human parainfluenza virus 3:Inhibition of infection in LLC-MK2 cells(IC50>25 µg/ml);##Human Influenza A Virus H1N1:Inhibition of infection In MDCK cells(IC50=1.6 µg/ml);##Human Influenza A Virus H7N9:Inhibition of infection In MDCK cells(IC50=3.3 µg/ml).##[Ref.26911565]Virus:Human Influenza A Virus H1N1(IC50=1.2 µg/ml);Human Influenza A Virus H3N2(IC50=1.2 µg/ml);Human Influenza A Virus H5N1(IC50=2.4 µg/ml);Human Influenza A Virus H7N7(IC50=0.8 µg/ml);Human Influenza A Virus H7N9(IC50=4.6 µg/ml);MERS-CoV(IC50=4.8 µg/ml);SARS-CoV(IC50=4.8 µg/ml) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.26911565]Xytotoxicity against Madin-Darby canine kidney cells(TC50=380 μg/ml). Not found 26911565##32843628 Sci Rep. 2016 Feb 25;6:22008. ##Nat Commun. 2020 Aug 25;11(1):4252. Zhao H, Zhou J, Zhang K, Chu H, Liu D, Poon VK, Chan CC, Leung HC, Fai N, Lin YP, Zhang AJ, Jin DY, Yuen KY, Zheng BJ.##Zhao H, To KKW, Sze KH, Yung TT, Bian M, Lam H, Yeung ML, Li C, Chu H, Yuen KY. A novel peptide with potent and broad-spectrum antiviral activities against multiple respiratory viruses. ##A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2. DRAMP29177 NGAICWGPCPTAFRQIGNCGRFRVRCCRIR 30 MBD-4 (11-40) (P9 [H21R,K23R,K28R], P9R) P82019 Belongs to the beta-defensin family. Defb5 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found 6M56 Mechanism of action:Mechanistic studies show that positively charged P9R broadly inhibits viral replication by binding to different viruses and then inhibits virus–host endosomal acidification to prevent the endosomal release of pH-dependent viruses. [Ref.32843628]Virus:##SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=0.9 µg/ml);##SARS-CoV:Inhibition of infection in Vero E6 cells(IC50=4.2 µg/ml);##MERS-CoV:Inhibition of infection in Vero E6 cells(IC50=22 µg/ml);##Human rhinovirus (HRV):inhibition of infection in RD cells(IC50=5.7 µg/ml);##Human parainfluenza virus 3:Inhibition of infection in LLC-MK2 cells(IC50>25 µg/ml);##Human Influenza A Virus H1N1:Inhibition of infection In MDCK cells(IC50=0.6 µg/ml);##Human Influenza A Virus H7N9:Inhibition of infection In MDCK cells(IC50=0.9 µg/ml). [Ref.32843628]P9R did not cause the hemolysis of Chicken red blood cells. Linear Free Free L [Ref.32843628]the CC50 of P9R was >300 μg/ml for MDCK, VeroE6 and A549 cells. Not found 32843628 Nat Commun. 2020 Aug 25;11(1):4252. Zhao H, To KKW, Sze KH, Yung TT, Bian M, Lam H, Yeung ML, Li C, Chu H, Yuen KY. A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2. DRAMP29178 NGAICWGPCPTAFRQIGNCGRFRVRCCRIR 30 8P9R(branched P9R) No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found 6M56 Mechanism of action:Have dual-antiviral mechanisms of cross-linking viruses to stop viral entry (mediated by TMPRSS2 for SARS-CoV-2) and of reducing endosomal acidification to inhibit viral entry through endocytic pathway. [Ref.33750821]Virus:SARS-CoV-2:inhibition of replication in high salt condition(IC50 = 0.3 μg/ml) [Ref.33750821]no obvious hemolysis was observed when turkey red blood cells were treated at 200 μg/ml. Branched Free Free L [Ref.33750821]Vero-E6 cells:the cytotoxicity indicated that TC50 of 8P9R was higher than 200 μg/ml. Not found 33750821 Nat Commun. 2021 Mar 9;12(1):1517. Zhao H, To KKW, Lam H, Zhou X, Chan JF, Peng Z, Lee ACY, Cai J, Chan WM, Ip JD, Chan CC, Yeung ML, Zhang AJ, Chu AWH, Jiang S, Yuen KY. Cross-linking peptide and repurposed drugs inhibit both entry pathways of SARS-CoV-2. DRAMP29179 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 IPB01(SARS-CoV-S (1151-1185),SR9, SARS-CoV-2-S (1169-1203)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Alpha helix Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.022±0.005 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=33.74±11.827 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM).##[Ref.17942557]Virus:SARS-CoV:Inhibition of virus entry in VERO-E6 cells(EC50=0.005 µM).##[Ref.18442051]Virus:SARS-CoV: inhibition of PsV entry in Vero-E6 cells(EC50=0.34 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented liposomes 17942557##18442051##32376627 J Virol. 2008 Jan;82(1):588-92.##J Cell Biochem. 2008 Aug 15;104(6):2335-47.##J Virol. 2020 Jul 1;94(14):e00635-20. Ujike M, Nishikawa H, Otaka A, Yamamoto N, Yamamoto N, Matsuoka M, Kodama E, Fujii N, Taguchi F. ##Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. ##Zhu Y, Yu D, Yan H, Chong H, He Y. Heptad repeat-derived peptides block protease-mediated direct entry from the cell surface of severe acute respiratory syndrome coronavirus but not entry via the endosomal pathway.##Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.##Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29180 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELK 36 IPB02(SARS-CoV-2-S (1169-1203)-K) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Alpha helix Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.025 ± 0.002 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.08±0.017 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=0.251 ± 0.118 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29181 INASVVNIQKEIDRLNEVAKNLNESLIDLQELGK 34 IPB03(SARS-CoV-2-S (1172-1205)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Alpha helix Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.015 ± 0.002 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.947 ± 0.179 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.315 ± 0.463 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29182 SVVNIQKEIDRLNEVAKNLNESLIDLQELGK 31 IPB04(SARS-CoV-2-S (1175-1205)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Alpha helix Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.033 ± 0.013 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.218 ± 0.063 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.053 ± 0.444 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29183 IQKEIDRLNEVAKNLNESLIDLQELGK 27 IPB05(SARS-CoV-2-S (1179-1205)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29184 IDRLNEVAKNLNESLIDLQELGK 23 IPB06(SARS-CoV-2-S (1183-1205)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29185 IQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 33 IPB07(SARS-CoV-2-S (1179-1211)) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Alpha helix Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=0.017 ± 0.001 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=0.993 ± 0.08 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.037 ± 0.836 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29186 ISGINASVVNIQKEIDRLNEVAKNLNESLIK 31 IPB08(SARS-CoV-2-S (1169-1198)-K) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50=4.66 ± 1.565 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50=1.738 ± 0.898 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC=1.13 ± 0.472 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29187 SVVNIQKEIDRLNEVAKNLNESLIK 25 IPB09(SARS-CoV-2-S (1175-1198)-K) P59594,P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The peptide was designed based on HR2 sequence lipopeptide fusion inhibitor,which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. It can also inhibit the SARS-CoV pseudovirus efficiently. [Ref.32376627]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T/ACE2 cells(IC50>5 µM),inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>25 µM);##SARS-CoV:inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC>25 µM);##Vesicular Stomatitis Virus (VSV):inhibition of Pseudovirus (PsV) infection in 293T/ACE2 cells(IC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 32376627 J Virol. 2020 Jul 1;94(14):e00635-20. Zhu Y, Yu D, Yan H, Chong H, He Y. Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. DRAMP29188 DEDLEELERLYRKAEEVAKEAKDASRRGDDERAKEQMERAMRLFDQVFELAQELQEKQTDGNRQKATHLDKAVKEAADELYQRVR 85 AHB1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. [Ref.32907861]Virus:SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=35 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32907861 Science. 2020 Oct 23;370(6515):426-431. Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. DRAMP29189 ELEEQVMHVLDQVSELAHELLHKLTGEELERAAYFNWWATEMMLELIKSDDEREIREIEEEARRILEHLEELARK 75 AHB2 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. [Ref.32907861]Virus:SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=15.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32907861 Science. 2020 Oct 23;370(6515):426-431. Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. DRAMP29190 DKEWILQKIYEIMRLLDELGHAEASMRVSDLIYEFMKKGDERLLEEAERLLEEVER 56 LCB1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. [Ref.32907861]Virus:SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=23.54 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32907861 Science. 2020 Oct 23;370(6515):426-431. Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. DRAMP29191 NDDELHMLMTDLVYEALHFAKDEEIKKRVFQLFELADKAYKNNDRQKLEKVVEELKELLERLLS 64 LCB3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide is a high-affinity protein minibinder to the SARS-CoV-2 spike receptor binding domain (RBD) that compete with ACE2 binding. [Ref.32907861]Virus:SARS-CoV-2:Inhibition of infection in Vero E6 cells(IC50=48.1 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32907861 Science. 2020 Oct 23;370(6515):426-431. Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. DRAMP29192 TFLDKFNHEAEDLFYQ 16 ACE2 (27-42)(SAP1) Q9BYF1 Belongs to the peptidase M2 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=2.39±0.20 mM);Inhibition of infection in 293T/ACE2/GFP cells(IC50=3 mM);##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(80% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM;##HCoV-NL63:Inhibition of cytopathic effect in LLC-MK2 cells(30% Inhibition at 3 mM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29193 EDLFYQSSL 9 ACE2 (37-45)(SAP2) Q9BYF1 Belongs to the peptidase M3 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=3.72±0.37 mM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29194 LAQMYPL 7 ACE2 (79-85)(SAP3) Q9BYF1 Belongs to the peptidase M4 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29195 GKGDFRIL 8 ACE2 (352-359)(SAP4) Q9BYF1 Belongs to the peptidase M5 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29196 QAKTFLDKFNHEA 13 ACE2 (24-36)(SAP5) Q9BYF1 Belongs to the peptidase M6 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50>7.5 mM);No nhibition of infection in 293T/ACE2/GFP cells up to 3 mM;##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(30% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29197 EDLFYQ 6 ACE2 (37-42)(SAP6) Q9BYF1 Belongs to the peptidase M4 family. ACE2 Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:Inhibiting SARS-CoV-2 infection by disrupting the Spike-ACE2 interaction interface with peptide-based inhibitors. [Ref.33356169]Virus:##SARS-CoV-2:Inhibition of infection in 293T/ACE2 cells(IC50=1.9±0.14 mM);Inhibition of infection in 293T/ACE2/GFP cells(IC50=3 mM);##SARS-CoV:Inhibition of infection in 293T/ACE2 cells(85% inhibition at 3 mM);##Vesicular Stomatitis Virus (VSV):No nhibition of infection in 293T/ACE2 cells up to 3 mM;##HCoV-NL63:Inhibition of cytopathic effect in LLC-MK2 cells(30% Inhibition at 3 mM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 33356169 Bioconjug Chem. 2021 Jan 20;32(1):215-223. Larue RC, Xing E, Kenney AD, Zhang Y, Tuazon JA, Li J, Yount JS, Li PK, Sharma A. Rationally Designed ACE2-Derived Peptides Inhibit SARS-CoV-2. DRAMP29198 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSGSGC 42 SARS-CoV-2-S(1168–1203)-GSGSGC P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. [Ref.33082259]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50=10±8 nM,IC90=98±57 nM),inhibition of infection in Vero E6 cells(IC50~ 6 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=8±4 nM,IC90=96±50 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50=6±4 nM,IC90=75±42 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50=9±7 nM,IC90=78±59 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50=35±10 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 3 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=7±5 nM,IC90=43±6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33082259]Human embryonic kidney HEK293T cells:18% Cytotoxicity at 10 µM;Vero E6 cells:12% Cytotoxicity at 1 µM,30% Cytotoxicity at 10 µM;Human airway epithelial cells:25% Cytotoxicity at 1 µM. liposomes 33082259##33597220 mBio. 2020 Oct 20;11(5):e01935-20.##Science. 2021 Mar 26;371(6536):1379-1382. Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M.##de Vries RD, Schmitz KS, Bovier FT, Predella C, Khao J, Noack D, Haagmans BL, Herfst S, Stearns KN, Drew-Bear J, Biswas S, Rockx B, McGill G, Dorrello NV, Gellman SH, Alabi CA, de Swart RL, Moscona A, Porotto M. Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain.##Intranasal fusion inhibitory lipopeptide prevents direct-contact SARS-CoV-2 transmission in ferrets. DRAMP29199 SLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGSGSGC 42 MERS-CoV-HR2P-GSGSGC R9UQ53,K9N5Q8 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. [Ref.33082259]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50>650 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 36 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=1000 nM,IC90>1000 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50>1000,IC90>1000 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50>700 nM,IC90>1000 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50=417±180 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 4 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=40±34 nM,IC90>700 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33082259]Human embryonic kidney HEK293T cells:<10% Cytotoxicity at 10 µM;Vero E6 cells:12% Cytotoxicity at 10 µM. liposomes 33082259 mBio. 2020 Oct 20;11(5):e01935-20. Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M. Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain. DRAMP29200 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSGC 42 EK1-GSGSGC Q8BB25 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Hemology Not found Not found Mechanism of action:The lipopeptide is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. [Ref.33082259]Virus:##SARS-CoV-2:ihibition of cell-cell fusion in 293T cells(IC50=293±60 nM,IC90>900 nM),inhibition of infection in Vero E6 cells(IC50~ 41 nM);##SARS-CoV-2_D614G:ihibition of cell-cell fusion in 293T cells(IC50=261±136 nM,IC90=892±100 nM);##SARS-CoV-2_S943P:ihibition of cell-cell fusion in 293T cells(IC50=286±104 nM,IC90>1000 nM);##SARS-CoV-2_S247R:ihibition of cell-cell fusion in 293T cells(IC50=194±107 nM,IC90=893±77 nM);##MERS-CoV:ihibition of cell-cell fusion in 293T cells(IC50>1000 nM,IC90>1000 nM),inhibition of infection in Vero E6 cells(IC50~ 2 nM);##SARS-CoV-1:ihibition of cell-cell fusion in 293T cells(IC50=36±5 nM,IC90>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33082259]Human embryonic kidney HEK293T cells:<5% Cytotoxicity at 10 µM;Vero E6 cells:18% Cytotoxicity at 10 µM. liposomes 33082259 mBio. 2020 Oct 20;11(5):e01935-20. Outlaw VK, Bovier FT, Mears MC, Cajimat MN, Zhu Y, Lin MJ, Addetia A, Lieberman NAP, Peddu V, Xie X, Shi PY, Greninger AL, Gellman SH, Bente DA, Moscona A, Porotto M. Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain. DRAMP29201 ANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQ 42 SARS-CoV-2 HR1P P0DTC2 Belongs to the betacoronaviruses spike protein family. S Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Protein level Not found Not found Mechanism of action:The peptide acted as a fusion inhibitor which against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. [Ref.32047258]Virus:SARS-CoV-2(No inhibition of cell-cell fusion up to 40 µM in Huh-7 cells,No inhibition of infection up to 40 µM in 293T/ACE2 cells) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32047258 Cell Mol Immunol. 2020 Jul;17(7):765-767. Xia S, Zhu Y, Liu M, Lan Q, Xu W, Wu Y, Ying T, Liu S, Shi Z, Jiang S, Lu L. Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. DRAMP29202 PHSCN 5 ATN-161 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide inhibits the spike protein interaction with α5β1 integrin and the interaction between α5β1 integrin and ACE2. [Ref.33102950]Virus:SARS-CoV-2:inhibition of replication In VeroE6 cells(IC50=3.16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation L No cytotoxicity information found in the reference(s) presented Not found 33102950 JACC Basic Transl Sci. 2021 Jan;6(1):1-8. Beddingfield BJ, Iwanaga N, Chapagain PP, Zheng W, Roy CJ, Hu TY, Kolls JK, Bix GJ. The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2 Infection. DRAMP29203 RVKR 4 CMK No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:CMK blocks virus entry, but it further suppresses cleavage of spikes and the syncytium. "[Ref.33007239]Virus:SARS-CoV-2:inhibition of virus production in Vero E6 cells(IC50=0.057 µM).##[Ref.31683742]Virus:Zika virus (ZIKV):inhibition of virus release in Vero cells(IC50=18.59 µM);Japanese encephalitis virus (JEV):inhibition of virus release in BHK-21 cells(IC50=19.91 µM).##[Ref.23617302]Virus:Hepatitis B virus (HBV):Inhibition of HBeAg secretion in HepG2.2.15 cells(26±11% inhibition at 20 µM,21±13% Inhibition at 100 µM)." No hemolysis information or data found in the reference(s) presented in this entry Linear Decanoyl(C10) chloromethylketone(CMK) L [Ref.31683742]Vero cells:CC50=712.9 µM.[Ref.33007239]Vero E6 cells:IC50=318.2 µM. Not found 23617302##31683742##33007239 Liver Int. 2013 Sep;33(8):1230-8. ##Viruses. 2019 Oct 31;11(11):1011.##Cell Rep. 2020 Oct 13;33(2):108254. Pang YJ, Tan XJ, Li DM, Zheng ZH, Lei RX, Peng XM.##Imran M, Saleemi MK, Chen Z, Wang X, Zhou D, Li Y, Zhao Z, Zheng B, Li Q, Cao S, Ye J.##Cheng YW, Chao TL, Li CL, Chiu MF, Kao HC, Wang SH, Pang YH, Lin CH, Tsai YM, Lee WH, Tao MH, Ho TC, Wu PY, Jang LT, Chen PJ, Chang SY, Yeh SH. Therapeutic potential of furin inhibitors for the chronic infection of hepatitis B virus.##Decanoyl-Arg-Val-Lys-Arg-Chloromethylketone: An Antiviral Compound That Acts against Flaviviruses through the Inhibition of Furin-Mediated prM Cleavage.##Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects. DRAMP29204 LQTALYALMEEIHIAALEKTWTALRHQYT 29 Covid3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acts as an inhibitor of the RBD–ACE2 interaction [Ref.34624194]Virus:##SARS-CoV-2:inhibition of infection in Vero cells(IC50=6.56 ± 2.14 μM);##SARS-CoV-2 variants B.1.1.7:inhibition of infection in Vero cells(IC50=33.40 ± 10.75 μM);##SARS-CoV-2 variants B.1.351:inhibition of infection in Vero cells(IC50=11.13 ± 3.82 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation D No cytotoxicity information found in the reference(s) presented Not found 34624194 J Med Chem. 2021 Oct 28;64(20):14955-14967. Valiente PA, Wen H, Nim S, Lee J, Kim HJ, Kim J, Perez-Riba A, Paudel YP, Hwang I, Kim KD, Kim S, Kim PM. Computational Design of Potent D-Peptide Inhibitors of SARS-CoV-2. DRAMP29205 RFDGKGLGIYQYMEEIEHAASRFAYFFYQHLA 32 Covid_extented_1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide acts as an inhibitor of the RBD–ACE2 interaction [Ref.34624194]Virus:##SARS-CoV-2:inhibition of infection in Vero cells(IC50=5.76 ± 1.65 μM);##SARS-CoV-2 variants B.1.1.7:inhibition of infection in Vero cells(IC50=5.57 ± 4.04 μM);##SARS-CoV-2 variants B.1.351:inhibition of infection in Vero cells(IC50=7.37 ± 1.80 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation D No cytotoxicity information found in the reference(s) presented Not found 34624194 J Med Chem. 2021 Oct 28;64(20):14955-14967. Valiente PA, Wen H, Nim S, Lee J, Kim HJ, Kim J, Perez-Riba A, Paudel YP, Hwang I, Kim KD, Kim S, Kim PM. Computational Design of Potent D-Peptide Inhibitors of SARS-CoV-2. DRAMP29206 SALEEQYKTFLDKFLHELEDLLYQLALAL 29 P7 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein. [Ref.33580154]Virus:SARS-CoV-2:54% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50>1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Not found 33580154 Commun Biol. 2021 Feb 12;4(1):197. Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O. Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. DRAMP29207 SALEEQLKTFLDKFMHELEDLLYQLAL 27 P8 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Alpha helix Not found Mechanism of action:The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein. [Ref.33580154]Virus:SARS-CoV-2:91% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=46 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. Not found 33580154 Commun Biol. 2021 Feb 12;4(1):197. Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O. Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. DRAMP29208 SALEEQYKTFLDKFMHELEDLLYQLSL 27 P9 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein. [Ref.33580154]Virus:SARS-CoV-2:93% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=53 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. Not found 33580154 Commun Biol. 2021 Feb 12;4(1):197. Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O. Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. DRAMP29209 SALEEQYKTFLDKFMHELEDLLYQLAL 27 P10 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The peptide was designed mimicking the N-terminal helix of hACE2 protein,which could prevent the SARS-CoV-2 from infecting human cells, blocking the interaction between hACE2 and the virus spike protein. [Ref.33580154]Virus:SARS-CoV-2:95% inhibition of replication in Vero-E6 cells at 10 μM;inhibition of replication in Calu-3 cells(IC50=42 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.33580154]The peptide proved to be devoid of cell toxicity on Vero-E6 and Calu-3 cells. Not found 33580154 Commun Biol. 2021 Feb 12;4(1):197. Karoyan P, Vieillard V, Gómez-Morales L, Odile E, Guihot A, Luyt CE, Denis A, Grondin P, Lequin O. Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection. DRAMP29210 RGAHIKGRWKSRCHRF 16 FBP No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The fusion-inhibition peptide FBP could broadly inhibit influenza virus and SARS-CoV-2 by interfering the viral fusion by the endocytic pathway and showed potently antiviral activity against the influenza virus in mice and SARS-CoV-2 variants in hamsters. [Ref.35259078]Virus:A(H1N1)(IC50 = 3.9 μg/ml);A(H3N2)(IC50 = 1.6 μg/ml);FluB (IC50 = 7.1 μg/ml);SARS-CoV-2 (HKU001a):inhibition of infection in Vero-E6 cells(IC50=2.9 μg/ml);SARS-CoV-2 (B.1.1.63, D614G):inhibition of infection in Vero-E6 cells(IC50=3.0 μg/ml);SARS-CoV-2(Delta):inhibition of infection in Vera-E6 cells(IC50=3.9 μg/ml). [Ref.35259078]No significant hemolysis against Turkey red blood cells (RBC). Linear Free Free L [Ref.35259078]No significant cytotoxicity was detected in MDCK(Madin Darby canine kidney) cells at 1 mg/ml(TC50 > 1 mg/ml). liposomes 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY. Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. DRAMP29211 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P4HC No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level. [Ref.34769299]Virus:##SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.8 μM);##SARS-CoV-2 B.1.1.7 (Alpha):inhibition of Pseudoviruse infection in Caco2 cells(IC50=2.28 μM);##SARS-CoV-2 B.1.351 (Beta):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.62 μM);##SARS-CoV-2 P.1 (Gamma):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.48 μM);##SARS-CoV-2 B.1.617.2 (Delta):inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.11 μM);##HCoV-229E(Authentic):inhibition of infection in Caco2 cells(IC50=0.48 μM);##HCoV-OC43(Authentic):inhibition of infection in Caco2 cells(IC50=0.41 μM);##SARS-CoV:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.35 μM);##MERS-CoV:inhibition of Pseudoviruse infection in Caco2 cells(IC50=0.10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-25-HC L [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. liposomes 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. 25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses. DRAMP29212 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P8HC No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level. [Ref.34769299]Virus:SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=3.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-25-HC L [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. liposomes 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. 25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses. DRAMP29213 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P12HC No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level. [Ref.34769299]Virus:SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=5.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG12-25-HC L [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. liposomes 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. 25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses. DRAMP29214 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELGSGSG 41 EK1P24HC No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found The peptide targets two different sites when mediating virus–cell fusion,which are blocking viral 6-HB formation and reducing the membrane cholesterol level. [Ref.34769299]Virus:SARS-CoV-2:inhibition of Pseudoviruse infection in Caco2 cells(IC50=10.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG24-25-HC L [Ref.34769299]no apparent cytotoxicity against Caco-2 cells at concentrations of up to 20 μM. liposomes 34769299 Int J Mol Sci. 2021 Nov 1;22(21):11869. Lan Q, Wang C, Zhou J, Wang L, Jiao F, Zhang Y, Cai Y, Lu L, Xia S, Jiang S. 25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses. DRAMP29215 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP20 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 48% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=1.36 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=50.52 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=33.85 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=103.17 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=128.87 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=111.41 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=79.09 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=88.49 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=92.16 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=73.86 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=228.4 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=817.21 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=471.54 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol(cholesterol) L No cytotoxicity information found in the reference(s) presented Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29216 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP21 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=7.5 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=191.4 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=126.65 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free C16(palmitic acid) L No cytotoxicity information found in the reference(s) presented Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29217 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP22 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=6.23 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=179.95 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=86.33 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free C18(stearic acid) L No cytotoxicity information found in the reference(s) presented Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29218 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP23 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=39.07 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=1236.38 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=507.32 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Toc(tocophenol) L No cytotoxicity information found in the reference(s) presented Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29219 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP24 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 16% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.33 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=3.77 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=2.89 nM);inhibition of live SARS-CoV-2 infection in Vero cells(IC50=8.97 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.29 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.5 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.42 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.97 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.22 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.06 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=21.64 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=69.9 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=375.56 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=421.48 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-K(Chol) L [Ref.34057039]Huh-7 cells:CC50=6.6 μM;Vero-E6 cells:CC50=13.67 μM. Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29220 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP25 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 18% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.29 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=2.13 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.43 nM),inhibition of live SARS-CoV-2 infection in Vero cells(IC50=25.71 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.8 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.52 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.56 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.71 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=5.87 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.76 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=17.69 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=48.5 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=353.22 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=336.14 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG5-K(Chol) L [Ref.34057039]Huh-7 cells:CC50=3.54 μM;Vero-E6 cells:CC50=6.95 μM. Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29221 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP26 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.26 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=3.05 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.82 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG6-K(Chol) L No cytotoxicity information found in the reference(s) presented Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29222 SVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 37 IBP27 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 12% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found Mechanism of action:Peptides derived from HR2 sequences of viral fusion proteins, including the S protein of emerging CoVs, can competitively bind to the HR1 domain and block the formation of the viral 6-HB core, thereby inhibiting infection of the virus from which they were derived. [Ref.34057039]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.32 nM);inhibition of pseudovirus infections in 293T/ACE2 cells(IC50=2.77 nM);inhibition of pseudovirus infections in Huh-7 cells(IC50=1.54 nM),inhibition of live SARS-CoV-2 infection in Vero cells(IC50=29.85 nM);##SARS-CoV-2 D614G:inhibition of pseudovirus infections in Huh-7 cells(IC50=6.75 nM);##SARS-CoV-2 N501Y:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.87 nM);##SARS-CoV-2 ΔH69-V70:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.56 nM);##SARS-CoV-2 E484K:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.55 nM);##SARS-CoV-2 B.1.1.7:inhibition of pseudovirus infections in Huh-7 cells(IC50=7.18 nM);##SARS-CoV-2 B.1.351:inhibition of pseudovirus infections in Huh-7 cells(IC50=8.25 nM);##SARS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=24.95 nM);##MERS-CoV:inhibition of pseudovirus infections in Huh-7 cells(IC50=60.08 nM);##HCoV-NL63:inhibition of pseudovirus infections in Huh-7 cells(IC50=179.53 nM);##HCoV-229E:inhibition of pseudovirus infections in Huh-7 cells(IC50=231.18 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34057039]Huh-7 cells:CC50=4.04 μM;Vero-E6 cells:CC50=5.05 μM. Not found 34057039 Emerg Microbes Infect. 2021 Dec;10(1):1227-1240. Yu D, Zhu Y, Jiao T, Wu T, Xiao X, Qin B, Chong H, Lei X, Ren L, Cui S, Wang J, He Y. Structure-based design and characterization of novel fusion-inhibitory lipopeptides against SARS-CoV-2 and emerging variants. DRAMP29223 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 IBP02V1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 0% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=1.1±0.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=17.8 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=14.3 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.6±0.1 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=50 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=21.5 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=33.6±3.5 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=66.9±7.6 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=62.5±17.2 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=203.9±8.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29224 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V2 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 22% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.6±0.03 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=20.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=18.1 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.4±0.04 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=19.3 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=20.8 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=56.5±9.4nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=55.3±2.8 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=67.5±8 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=535.7±44.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29225 EISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 48% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.4±0.02 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=14.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=17.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.2±0.02 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=40.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=14.4 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=48±5.8 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=38.5±6.2 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=75.8±9.9 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=545.7±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29226 ELSGINASVVNLQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V4 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 59% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.3±0.02 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=18.6 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=15.2 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.1±0.02 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=29.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=26.3 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=63±1.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=22.4±2.2 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=66.3±3.1 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=502±24.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29227 SLTQINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 36 IBP02V5 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 16% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=2.1±0.5 nM);inhibition of SARS-CoV-2 pseudovirus infection in 293T/ACE2 cells(IC50=21 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=23.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=1.3±0.1 nM);inhibition of pseudovirus infection in 293T/ACE2 cells(IC50=98.8 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=27.5 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=65.9±13.2 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=68.4±9.7 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=70.8±8.7 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=1128.4±148.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L [Ref.34344868]No significant cytotoxicity in both 293T/ACE2 and Huh-7 cells at a concentration of 10 μM. liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29228 SLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 36 MERS-LP No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 8% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=102.9±7.2 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=5046±905.2 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=79.1±9.8 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=82.9±8.6 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50>25000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L No cytotoxicity information found in the reference(s) presented liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29229 SLDYINVTFLDLQDEMNRLQEAIKVLNQSYINLKDI 36 OC43-LP No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 22% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=4.1±1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=82.8±22.1 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=2.4±0.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=97.5±5.9 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=250.4±39.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=5.2±0.5 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=416.5±227.5 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=2008.8±697.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L No cytotoxicity information found in the reference(s) presented liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29230 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKELK 37 EK1V1 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 39% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37 °C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=273.5±4.1 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=2672.1±384.5 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=214.5±20.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=1790.8±363.2 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=4370.3±719.7 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=499.8±163.3 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=487.2±41.3 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=1255.6±453.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Chol L No cytotoxicity information found in the reference(s) presented liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29231 SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL 36 EK1V2 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found 68% α-helicity in phosphate-buffered saline (PBS; pH 7.2) with a final concentration of 10 μM and incubated at 37°C Not found The peptide is a fusion inhibitor against SARS-CoV-2. [Ref.34344868]Virus:##SARS-CoV-2:inhibition of SARS-CoV-2 S protein-mediated cell-cell fusion(IC50=0.9±0.2 nM);inhibition of SARS-CoV-2 pseudovirus infection in Huh-7 cells(IC50=87.2±8.3 nM);##SARS-CoV-2 D614G:inhibition of S protein-mediated cell-cell fusion(IC50=0.5±0.2 nM);inhibition of pseudovirus infection in Huh-7 cells(IC50=106.5±5.4 nM);##SARS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=252±5.6 nM);##MERS-CoV:inhibition of pseudovirus infection in Huh-7 cells(IC50=1.1±0.3 nM);##HCoV-NL63:inhibition of pseudovirus infection in Huh-7 cells(IC50=59.4±13.1 nM);##HCoV-229E:inhibition of pseudovirus infection in Huh-7 cells(IC50=503.3±20.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG8-K(Chol) L No cytotoxicity information found in the reference(s) presented liposomes 34344868 Signal Transduct Target Ther. 2021 Aug 3;6(1):294. Zhu Y, Yu D, Hu Y, Wu T, Chong H, He Y. SARS-CoV-2-derived fusion inhibitor lipopeptides exhibit highly potent and broad-spectrum activity against divergent human coronaviruses. DRAMP29232 ISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 35 P3 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Comment: No comments found on DRAMP database [Ref.32482145]Virus:HCoV-19:inhibition of HCoV-19 S mediated cell–cell fusion(EC50=0.72 μM);neutralizing activities against pseudotype HCoV-19 virus(EC50=0.32 μM);inhibition of authentic HCoV-19 virus infection in Vero E6 cells(EC50=0.58 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 32482145 Emerg Microbes Infect. 2020 Dec;9(1):1238-1241. Sun H, Li Y, Liu P, Qiao C, Wang X, Wu L, Liu K, Hu Y, Su C, Tan S, Zou S, Wu G, Yan J, Gao GF, Qi J, Wang Q. Structural basis of HCoV-19 fusion core and an effective inhibition peptide against virus entry. DRAMP29233 XxXVXAaXXXX 11 Alisporivir, Debio-025 No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Comment: No comments found on DRAMP database [Ref.32376613]Virus:SARS-CoV-2:Inhibition of infection in Vero E6 cells(EC50=0.46±0.04 µM,E90=3.10±1.40 μM).##[Ref.32568027]Virus:##SARS-CoV-2:Inhibition of infection in Vero E6 cells(EC50=4.9±1.3 µM);##SARS-CoV:Inhibition of infection in Vero E6 cells(EC50=4.3±1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 1 is alpha-aminobutyric acid,position 2 is N-methylalanine,the 'V' at position 3 is N-methylalanine,the 'X' at position 5,8,9 are N-methylleucine,the 'X' at position 10 is N-methylvaline and position 11 is N-methyl-(4R)-4-[(E)-but-2-enyl]-4-methyl-L-threonyl Mixed(D-Ala7,D-meth-Ala2) [Ref.32376613]Vero E6 cells:CC50>20µM. Not found 32376613##32568027 Antimicrob Agents Chemother. 2020 Jun 23;64(7):e00876-20. ##J Gen Virol. 2020 Sep;101(9):925-940. Softic L, Brillet R, Berry F, Ahnou N, Nevers Q, Morin-Dewaele M, Hamadat S, Bruscella P, Fourati S, Pawlotsky JM, Ahmed-Belkacem A.##Ogando NS, Dalebout TJ, Zevenhoven-Dobbe JC, Limpens RWAL, van der Meer Y, Caly L, Druce J, de Vries JJC, Kikkert M, Bárcena M, Sidorov I, Snijder EJ. Inhibition of SARS-CoV-2 Infection by the Cyclophilin Inhibitor Alisporivir (Debio 025).##SARS-coronavirus-2 replication in Vero E6 cells: replication kinetics, rapid adaptation and cytopathology. DRAMP29234 PxTXXLPX 8 Plitidepsin, Aplidine No entry found Not found Not found Synthetic construct Antimicrobial, Antiviral(SARS-CoV-2) Not found Not found Not found Mechanism of action:The antiviral activity of plitidepsin against SARS-CoV-2 is mediated through inhibition of the known target eEF1A (eukaryotic translation elongation factor 1A). [Ref.33495306]Virus:SARS-CoV-2:inhibition of replication In Vero E6 cells(IC50=0.70 nM,IC90=1.76 nM);inhibition of replication In hACE2-HEK293T cells(IC50=0.73 nM,IC90=0.88 nM);inhibition of replication In pneumocyte-like cells(IC50=1.62 nM,IC90=3.14 nM).##[Ref.35231500]Virus:##SARS-CoV-2 D614G:inhibition of replication in Vero E6 cells(IC50=5.2 nM);##SARS-CoV-2 Delta:inhibition of replication in Vero E6 cells(IC50=3.9 nM);##SARS-CoV-2 Omicron:inhibition of replication in Vero E6 cells(IC50=4.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Pyruvoyl Free The 'X' at position 2 is N-methylleucine,position 4 is 4-amino-3-hydroxy-5-methyl-Heptanoic acid, position 5 is Hydroxyisovalerylpropionyl, and position 8 is N-methyl-4-methyl-tyrosine.There is a Sidechain-Mainchain Bond between position 3 and 8. Mixed(D-meth-Leu2) [Ref.33495306]Vero E6 cells:CC10=0.36 nM,CC50=1.99 nM;hACE2-293T cells:CC10=2.00 nM,CC50>200 nM;pneumocyte-like cells:CC10=20.88 nM,CC50=65.43 nM. Not found 35231500##33495306 Antiviral Res. 2022 Apr;200:105270.##Science. 2021 Feb 26;371(6532):926-931. Sachse M, Tenorio R, Fernández de Castro I, Muñoz-Basagoiti J, Perez-Zsolt D, Raïch-Regué D, Rodon J, Losada A, Avilés P, Cuevas C, Paredes R, Segalés J, Clotet B, Vergara-Alert J, Izquierdo-Useros N, Risco C.##White KM, Rosales R, Yildiz S, Kehrer T, Miorin L, Moreno E, Jangra S, Uccellini MB, Rathnasinghe R, Coughlan L, Martinez-Romero C, Batra J, Rojc A, Bouhaddou M, Fabius JM, Obernier K, Dejosez M, Guillén MJ, Losada A, Avilés P, Schotsaert M, Zwaka T, Vignuzzi M, Shokat KM, Krogan NJ, García-Sastre A. Unraveling the antiviral activity of plitidepsin against SARS-CoV-2 by subcellular and morphological analysis.##Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by targeting the host protein eEF1A. DRAMP00828 GLPTCGETCFGGTCNTPGCTCDPWPVCTHN 30 Cycloviolacin-O24 (Plant defensin) P84637 Belongs to the cyclotide family. Bracelet subfamily. Not found Viola odorata (Sweet violet) Antiviral,Insecticidal Protein level Bridge Not found "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=308 nM). [Ref:16872274] It has 75% hemolytic activity at 25.0 μM against human type A red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=6170 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents. DRAMP29242 SKHSSLDCVLRP 12 Peptide 1(lactoferrin 418–429) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=4 ± 0.37 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=3.1 ± 0.12 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.8 ± 0.7 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29243 KANEGLTWNSLKDK 14 Peptide 4(lactoferrin 441–454) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=1± 0.15 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=50.000 ± 250 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=1.000 ± 360 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29244 TNGESTADWAKN 12 Peptide 6(lactoferrin 552-563) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=400 ±0.02 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=50.000 ± 230 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=10.000± 120 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29245 KSETKN 6 Peptide 8(lactoferrin 633-638) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.5 ± 0.01 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=500 ± 0.46 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=400.000 ± 210 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29246 SLDCVLRP 8 Peptide 13(lactoferrin 422–429) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.3 ± 0.5 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=2.5± 0.37 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=300± 0.2 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29247 VLRP 4 Peptide 14(lactoferrin 426–429) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.45 ± 0.1 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=1 ± 0.05 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=250 ± 0.42 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29248 SKHSSLDC 8 Peptide 16(lactoferrin 418-425) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=80 ± 0.19 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=0.1 ± 0.001 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.0 ± 0.45 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220 Sci Rep. 2017 Sep 6;7(1):10593. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors. DRAMP29249 SLDC 4 Peptide 15(lactoferrin 422-425) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=0.5 ± 0.001 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=4.6 ± 0.05 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=4.3 ± 0.03 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220##34681184 Sci Rep. 2017 Sep 6;7(1):10593.##Pharmaceuticals (Basel). 2021 Sep 23;14(10):959. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P.##Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors.##Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies. DRAMP29250 SKHS 4 Peptide 17(lactoferrin 418–421) P24627 Belongs to the transferrin family LTF Synthetic construct Antimicrobial,Antiviral Protein level Not found Not found 3IB0 Function:Antiviral activity against Influenza virus. [Ref.28878220]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=3 ± 0.61 pM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=0.048 ± 0.0012 pM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=5.0 ± 0.02 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 28878220##34681184 Sci Rep. 2017 Sep 6;7(1):10593.##Pharmaceuticals (Basel). 2021 Sep 23;14(10):959. Scala MC, Sala M, Pietrantoni A, Spensiero A, Di Micco S, Agamennone M, Bertamino A, Novellino E, Bifulco G, Gomez-Monterrey IM, Superti F, Campiglia P.##Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M. Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors.##Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies. DRAMP29251 SAHS 4 Ac-SAHS-NH2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34681184]Virus:A/Roma-ISS/02/08 H1N1:inhibition of virus replication in MDCK cells(EC50=5.77 ± 0.01 × 10−7 μM);##A/Parma/24/09 H1N1:inhibition of virus replication in MDCK cells(EC50=4.3 ± 0.3 × 10−10 μM);##A/Parma0/5/06 H3N2:inhibition of virus replication in MDCK cells(EC50=9.36 ± 0.1 × 10−7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation L No cytotoxicity information found in the reference(s) presented hemagglutinin (HA) 34681184 Pharmaceuticals (Basel). 2021 Sep 23;14(10):959.  Scala MC, Agamennone M, Pietrantoni A, Di Sarno V, Bertamino A, Superti F, Campiglia P, Sala M. Discovery of a Novel Tetrapeptide against Influenza A Virus: Rational Design, Synthesis, Bioactivity Evaluation and Computational Studies. DRAMP29252 GGVLVQPG 8 Peptide 2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral(SARS-CoV-2) Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34502335]Virus:SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥17.6 ± 2.4 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=50.05 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=48.42 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Amidation L [Ref.34502335]Vero cell:CC50=83.0 ± 17.0 µM. Main protease 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A. Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation. DRAMP29253 GGVLVQPG 8 Peptide 3 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral(SARS-CoV-2) Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34502335]Virus:SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50>20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=58.09 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=81.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Methyl amidation L [Ref.34502335]Vero cell:CC50=81.8 ± 2.1 µM. Main protease 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A. Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation. DRAMP29254 GGVLVQPG 8 Peptide 4 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral(SARS-CoV-2) Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34502335]Virus:SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=78.20 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Pivaloylation Methyl amidation L [Ref.34502335]Vero cell:CC50=74.9 ± 4.9 µM. Main protease 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A. Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation. DRAMP29255 GVLVQ 5 Peptide 5 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral(SARS-CoV-2) Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34502335]Virus:SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50=59.80 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Methyl amidation L [Ref.34502335]Vero cell:CC50=75.0 ±2.2 µM. Main protease 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A. Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation. DRAMP29256 GVLV 4 Peptide 6 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral(SARS-CoV-2) Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.34502335]Virus:SARS-CoV-2 UC-1074:inhibition of virus activity in Vero cells(EC50≥20 μM);##SARS-CoV-2 UC-1075:inhibition of virus activity in Vero cells(EC50>20 μM);##cytomegalovirus (HCMV) AD-169 Strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>4 µM);##cytomegalovirus (HCMV) Davis strain:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK+ VZV Strain OKA:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM);##varicella-zoster virus (VZV) TK-VZV Strain 07–1:inhibition of virus activity in human embryonic lung (HEL) cells(EC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acylation Methyl amidation L [Ref.34502335]Vero cell:CC50=77.4 ±0.7 µM. Main protease 34502335 Int J Mol Sci. 2021 Aug 30;22(17):9427. Di Micco S, Musella S, Sala M, Scala MC, Andrei G, Snoeck R, Bifulco G, Campiglia P, Fasano A. Peptide Derivatives of the Zonulin Inhibitor Larazotide (AT1001) as Potential Anti SARS-CoV-2: Molecular Modelling, Synthesis and Bioactivity Evaluation. DRAMP29257 YWKIXNTLVNIC 12 compound 1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=1.5 ± 0.1 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 4 indicates MeYMe(N-methyl-4-O-methyl-tyrosine). L No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29258 YXKXKXXKXXKC 12 compound 2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=0.25 ± 0.01 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=1.7 ± 0.1 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=3.9 ± 0.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 2,7,9 and 10 indicates MeYMe(N-methyl-4-O-methyl-tyrosine), position 4 indicates MeF(N-methyl-phenylalanine), position 6 indicates MeS(N-methyl-serine). L No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29259 YTNFYLYPYXFC 12 compound 3 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=2.2 ± 0.1 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 10 indicates MeYMe(N-methyl-4-O-methyl-tyrosine). L No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29260 YXIAKYNXXIPC 12 compound 4 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=4.6 ± 0.3 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 2 indicates N-methyl-glycine, position 8 and 9 indicates N-methyl-4-O-methyl-tyrosine. L No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29261 YTLPFHNXTFFC 12 compound 5 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50≥50 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 8 indicates N-methyl-glycine. L No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29262 yAIIXYNKYXNC 12 compound 6 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.30783498]Virus:Zika Virus(ZIKV):inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50=3.2 ± 0.4 μM);##Dengue virus serotype 2:inhibition of flaviviral Protease(Zika virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM);##West Nile virus:inhibition of flaviviral Protease(West Nile virus NS2B-NS3 protease) activity in Huh-7 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Thioether-acyl moiety (−S-Ac−)(forms a macrocycle through the side chain of the underlined cysteine residue) Amidation The 'X' at position 5 indicates N-methyl-4-O-methyl-tyrosine, position 10 indicates N-methyl-leucine. Mixed(D-Tyr1) No cytotoxicity information found in the reference(s) presented NS2B-NS3 protease 30783498 ACS Med Chem Lett. 2019 Jan 4;10(2):168-174. Nitsche C, Passioura T, Varava P, Mahawaththa MC, Leuthold MM, Klein CD, Suga H, Otting G. De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease. DRAMP29263 PVPNLTCAVACELKWESE 18 E1P37 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=41.0 ± 8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29264 VPNLTCAVACELKWESEF 18 E1P37-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=80.0 ± 62.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29265 PNLTCAVACELKWESEFR 18 E1P37-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=99.0 ± 22.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29266 NLTCAVACELKWESEFWR 18 E1P38 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29267 LTCAVACELKWESEFWRW 18 E1P38-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29268 TCAVACELKWESEFWRWT 18 E1P38-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29269 CAVACELKWESEFWRWTE 18 E1P39 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=11.3 ± 1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29270 AVACELKWESEFWRWTEQ 18 E1P39-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=44.0 ± 13.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29271 VACELKWESEFWRWTEQL 18 E1P39-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=37.7 ± 7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29272 ACELKWESEFWRWTEQLA 18 E1P40 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29273 CELKWESEFWRWTEQLAS 18 E1P40-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=34.0 ± 15.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29274 ELKWESEFWRWTEQLASN 18 E1P40-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29275 LKWESEFWRWTEQLASNY 18 E1P41 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29276 KWESEFWRWTEQLASNYW 18 E1P41-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=66.7 ± 20.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29277 WESEFWRWTEQLASNYWI 18 E1P41-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=22.0 ± 0.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29278 ESEFWRWTEQLASNYWIL 18 E1P42 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=50.0 ± 8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29279 SEFWRWTEQLASNYWILE 18 E1P42-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=31.0 ± 3.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29280 EFWRWTEQLASNYWILEY 18 E1P42-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29281 FWRWTEQLASNYWILEYL 18 E1P43 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=43.0 ± 10.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29282 WRWTEQLASNYWILEYLW 18 E1P43-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=6.8 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29283 RWTEQLASNYWILEYLWK 18 E1P43-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=19.7 ± 9.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29284 WTEQLASNYWILEYLWKV 18 E1P44 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29285 TEQLASNYWILEYLWKVP 18 E1P44-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29286 EQLASNYWILEYLWKVPF 18 E1P44-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=90.3 ± 15.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29287 QLASNYWILEYLWKVPFD 18 E1P45 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=27.7 ±5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29288 LASNYWILEYLWKVPFDF 18 E1P45-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=12.7 ±1.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29289 ASNYWILEYLWKVPFDFW 18 E1P45-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=11.3 ± 3.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29290 SNYWILEYLWKVPFDFWR 18 E1P46 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=19.7 ± 8.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29291 NYWILEYLWKVPFDFWRG 18 E1P46-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=12.3 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29292 YWILEYLWKVPFDFWRGV 18 E1P46-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=32.3 ± 11.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29293 WILEYLWKVPFDFWRGVI 18 E1P47 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=2.7 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29294 ILEYLWKVPFDFWRGVIS 18 E1P47-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=5.4 ± 0.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29295 LEYLWKVPFDFWRGVISL 18 E1P47-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=6.6± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29296 EYLWKVPFDFWRGVISLT 18 E1P48 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=44.7 ± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29297 YLWKVPFDFWRGVISLTP 18 E1P48-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=70.7 ±9.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29298 LWKVPFDFWRGVISLTPL 18 E1P48-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=14.7 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29299 WKVPFDFWRGVISLTPLL 18 E1P49 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=17.3 ± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29300 KVPFDFWRGVISLTPLLV 18 E1P49-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=63.3 ± 5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29301 VPFDFWRGVISLTPLLVC 18 E1P49-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29302 PFDFWRGVISLTPLLVCV 18 E1P50 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29303 FDFWRGVISLTPLLVCVA 18 E1P50-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29304 DFWRGVISLTPLLVCVAA 18 E1P50-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29305 FWRGVISLTPLLVCVAAL 18 E1P51 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29306 WRGVISLTPLLVCVAALL 18 E1P51-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29307 RGVISLTPLLVCVAALLL 18 E1P51-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29308 GVISLTPLLVCVAALLLL 18 E1P52 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=55.7± 5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29309 VISLTPLLVCVAALLLLE 18 E1P52-1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29310 ISLTPLLVCVAALLLLEQ 18 E1P52-2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found Not found Not found Function:Antiviral activity against Influenza virus. [Ref.26905802]Virus:HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50>125 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented gp41 26905802 Biochim Biophys Acta. 2016 Jun;1860(6):1139-48. Gómara MJ, Sánchez-Merino V, Paús A, Merino-Mansilla A, Gatell JM, Yuste E, Haro I. Definition of an 18-mer Synthetic Peptide Derived from the GB virus C E1 Protein as a New HIV-1 Entry Inhibitor. DRAMP29311 GPNFAEISKINTTLLDLSDEMAMLLQEVVKQLNDSYI 37 HKU4-HR2P1 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found α-helix 10.5%-13.5% α-helix determined by circular dichroism (CD). Mechanism:The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. [Ref.30646495]Virus:MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.09 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=2.15 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=2.72 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. membrane 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L. Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. DRAMP29312 EISKINTTLLDLSDEMAMLLQEVVKQLNDSYIDLKEL 37 HKU4-HR2P2 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found α-helix 10.5%-13.5% α-helix determined by circular dichroism (CD). Mechanism:The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. [Ref.30646495]Virus:MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=0.38 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.34 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.44 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. membrane 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L. Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. DRAMP29313 LDLSDEMAMLLQEVVKQLNDSYIDLKELGNYTYYNKW 37 HKU4-HR2P3 No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found α-helix 10.5%-13.5% α-helix determined by circular dichroism (CD). Mechanism:The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. [Ref.30646495]Virus:MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=0.55 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.48 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=0.52 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. membrane 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L. Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. DRAMP29314 GGGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 39 MERS-HR2P No entry found Not found Not found Synthetic construct Antimicrobial,Antiviral Not found α-helix 10.5%-13.5% α-helix determined by circular dichroism (CD). Mechanism:The peptide bind with HR1 of MERS-CoV and thus disrupting the process of MERS-6HB formation can inhibit virus–cell membrane fusion and abolish viral infection. [Ref.30646495]Virus:MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.07 μM);##MERS-CoV Q1020:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=1.14 μM);##MERS-CoV Q1020H:inhibition of Pseudovirus Infection in Huh-7 cells(IC50=1.71 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30646495]No cytotoxicity against Huh-7 cells up to 100 μM. membrane 30646495 Viruses. 2019 Jan 14;11(1):56. doi: 10.3390/v11010056 Xia S, Lan Q, Pu J, Wang C, Liu Z, Xu W, Wang Q, Liu H, Jiang S, Lu L. Potent MERS-CoV Fusion Inhibitory Peptides Identified from HR2 Domain in Spike Protein of Bat Coronavirus HKU4. DRAMP29949 GFGCPFNQGKCHRHCRSIRRRGGYCDGFLKQRCVCYRK 38 BmKDfsin3 A0A384E0Y8 Flaviviridae Not found Mesobuthus martensii Karsch Antimicrobial, Antiviral Not found Not found Not found Mechanism: BmKDfsin3 is revealed to enter into cells. Using an upstream MyD88 dimerization inhibitor ST2345 or kinase IRAK-1/4 inhibitor I, the inhibition of p38 activation represses HCV replication in vitro. [Ref.31963532]Hepatitis C virus (HCV): inhibition of viral replication in Huh7.5.1 cells(IC50=3.35±1.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys4 and Cys25, Cys11 and Cys33, Cys15 and Cys35. L "[Ref.31963532]Human hepatocellular carcinoma Huh-7.5.1 cells: CC50=60.63±1.36 µM." Not found 31963532 Antibiotics (Basel). 2020 Jan 17;9(1):33. Cheng Y, Sun F, Li S, Gao M, Wang L, Sarhan M, Abdel-Rahman MA, Li W, Kwok HF, Wu Y, Cao Z. Inhibitory Activity of a Scorpion Defensin BmKDfsin3 against Hepatitis C Virus. DRAMP29950 MITHGCYTRTRHKHKLKKTL 20 SA-35 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: It is likely that these peptides exert anti-RSV activity through a combination of two mechanisms: destabilization of the viral envelope and competitive inhibition of attachment/fusion of the virus with the target cell. [Ref.32124885]Respiratory syncytial virus (RSV):SA-35 caused a significant decrease of the RSV infectivity by 33 times at concentrations 1 mg/ml. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32124885]MA-104 cells:CC50= 2.1 ± 0.1 mg/ml. Not found 32124885 J Mater Chem B. 2020 Apr 1;8(13):2607-2617 Kozhikhova KV, Shilovskiy IP, Shatilov AA, Timofeeva AV, Turetskiy EA, Vishniakova LI, Nikolskii AA, Barvinskaya ED, Karthikeyan S, Smirnov VV, Kudlay DA, Andreev SM, Khaitov MR Linear and dendrimeric antiviral peptides: design, chemical synthesis and activity against human respiratory syncytial virus. DRAMP29951 KRRGGGKLLKLLLKLLLKLLKC 22 NC-783 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: It is likely that these peptides exert anti-RSV activity through a combination of two mechanisms: destabilization of the viral envelope and competitive inhibition of attachment/fusion of the virus with the target cell. [Ref.32124885]Respiratory syncytial virus (RSV):inhibition of viral infection in the MA-104 cell(IC50=0.04mg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32124885]MA-104 cells:CC50= 0.04 ± 0.01 mg/ml. Not found 32124885 J Mater Chem B. 2020 Apr 1;8(13):2607-2617 Kozhikhova KV, Shilovskiy IP, Shatilov AA, Timofeeva AV, Turetskiy EA, Vishniakova LI, Nikolskii AA, Barvinskaya ED, Karthikeyan S, Smirnov VV, Kudlay DA, Andreev SM, Khaitov MR Linear and dendrimeric antiviral peptides: design, chemical synthesis and activity against human respiratory syncytial virus. DRAMP29952 gikefkrivqrikdflrnlv 20 GI-20D No entry found Filoviridae Not found Synthetic construct(derived from LL-37) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry. [Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=0.99 µM);inhibition of viral infection in primary macrophages(IC50=2.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation D No cytotoxicity information or data found in the reference(s) presented in this entry Not found 32252021 iScience. 2020 Apr 24;23(4):100999. Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K. Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. DRAMP29953 GXKRlVQRlKDXlRNLV 17 17BIPHE2 No entry found Filoviridae Not found Synthetic construct(derived from LL-37) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Act as CatB inhibitors to block the endosomal processing of EBOV GP, thus preventing virus entry. [Ref.32252021]Ebola Virus(EBOV):inhibition of viral infection in Hela cells(IC50=0.71 µM);inhibition of viral infection in primary macrophages(IC50=5.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation The 'X' at position 2 and 12 indicates biphenylalanine. Mixed(D-Leu5, 9, 13) No cytotoxicity information or data found in the reference(s) presented in this entry Not found 32252021 iScience. 2020 Apr 24;23(4):100999. Yu Y, Cooper CL, Wang G, Morwitzer MJ, Kota K, Tran JP, Bradfute SB, Liu Y, Shao J, Zhang AK, Luo LG, Reid SP, Hinrichs SH, Su K. Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection. DRAMP29954 RGAHINGRWDSRCHRF 16 FBP1 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: FBP could have dual functions: blocked HA-mediated fusion by binding and inhibited endosomal acidification from interfering viral entry by the endocytic pathway. [Ref.35259078]influenza A virus(H1N1): inhibition of viral multicycle growth in MDCK cells(>50% inhibition at 100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY. Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. DRAMP29955 RGAHIKGRWDSRCHRF 16 FBP2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: FBP could have dual functions: blocked HA-mediated fusion by binding and inhibited endosomal acidification from interfering viral entry by the endocytic pathway. [Ref.35259078]influenza A virus(H1N1): inhibition of viral multicycle growth in MDCK cells(>50% inhibition at 50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY. Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. DRAMP29956 IPLRGAFINGRWDSQCHRFS 20 U5 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Bind to the HA stem of group 1 influenza A virus. [Ref.35259078]influenza A virus(H1N1): inhibition of viral replication in MDCK cells(IC50=12.9 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY. Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. DRAMP29957 FINGRWDSQCHRFSNGAIACA 21 U4 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Bind to the HA stem of group 1 influenza A virus. [Ref.35259078]influenza A virus(H1N1): inhibition of viral replication in MDCK cells(IC50=6.6 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 35259078 Emerg Microbes Infect. 2022 Dec;11(1):926-937. Zhao H, Meng X, Peng Z, Lam H, Zhang C, Zhou X, Chan JF, Kao RYT, To KK, Yuen KY. Fusion-inhibition peptide broadly inhibits influenza virus and SARS-CoV-2, including Delta and Omicron variants. DRAMP29958 WEDWVR 6 C6b No entry found Retroviridae Not found Synthetic construct(derived from gp36 membrane proximal external region of FIV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM. Structural basis of antiviral activity of peptides from MPER of FIV gp36 DRAMP29959 DWVRWI 6 C6a No entry found Retroviridae Not found Synthetic construct(derived from gp36 membrane proximal external region of FIV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50=0.06-0.15 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM. Structural basis of antiviral activity of peptides from MPER of FIV gp36 DRAMP29960 WEDWVRWI 8 C8 No entry found Retroviridae Not found Synthetic construct(derived from gp36 membrane proximal external region of FIV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Elicit antiviral activity by inhibiting the fusion of the FIV and host cell membrane. [Ref.30240422]Feline immunodeficiency virus (FIV): inhibition of virus replication in lymphoid cells(IC50=0.05-0.06 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30240422 PLoS One. 2018 Sep 21;13(9):e0204042 Grimaldi M, Stillitano I, Amodio G, Santoro A, Buonocore M, Moltedo O, Remondelli P, D'Ursi AM. Structural basis of antiviral activity of peptides from MPER of FIV gp36 DRAMP29961 XGSGSGVALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSI 42 Chol-PEG4-VG No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.1 ± 0.0001 nM,IC50<0.0007 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 1 indicates cholesterol-PEG4 conjugated cysteine. L [Ref.28344321]Vero cells: CC50>10000 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29962 XGSGSGVALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSI 42 Chol-VG No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=1.7 ± 0.42 nM,IC50=0.06 ± 0.035 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 1 indicates cholesterol-conjugated cysteine. L [Ref.28344321]Vero cells: CC50=9000 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29963 VALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-PEG24-Chol No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.1 ± 0.0003 nM,IC50=0.007 ± 0.007 nM);##Nipah virus(NiV):inhibition of virus infection in Vero cells(IC90~2 nM. No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-PEG24 conjugated cysteine. L [Ref.28344321]Vero cells: CC50=1300 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29964 VALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-Chol No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.7 ± 0.26 nM,IC50=0.015 ± 0.07 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-conjugated cysteine. L [Ref.28344321]Vero cells: CC50+10000 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29965 VALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX 42 VG-PEG4-Chol No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=0.7 ± 0.007 nM,IC50=0.03 ± 0.04 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 42 indicates cholesterol-PEG4 conjugated cysteine. L [Ref.28344321]Vero cells: CC50=4500 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29966 VALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGC 42 VG No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion. [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=280 ± 247 nM,IC50=1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.28344321]Vero cells: CC50>10000 nM. membrane 28344321 Sci Rep. 2017 Mar 8;7:43610. Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides DRAMP29967 SKVNGQSGRMEFFWTIAK 18 m15 /Leu17 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29968 SKVNGQSGRMEFFWTALK 18 m14 /lle16 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>10% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29969 SKVNGQSGRMAFFWTILK 18 m9 /Glu11 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>50% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29970 SKVNGQSGRMEFAWTILK 18 m11 /Phe13 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>80% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29971 SKVNGQSGRAEFFWTILK 18 m8 /Met10 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>80% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29972 SKVNGQAGRMEFFWTILK 18 m6 /Ser7 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(~60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29973 SKVNGASGRMEFFWTILK 18 m5 /GIn6 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>60% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29974 SKVAGQSGRMEFFWTILK 18 m4 /Asn4 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>70% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29975 SKANGQSGRMEFFWTILK 18 m3 /Val3 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>50% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29976 SAVNGQSGRMEFFWTILK 18 m2 /Arg2 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(~20% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29977 AKVNGQSGRMEFFWTILK 18 m1 /Ser1 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Pseudovirus influenza A virus(HA(VN/04)/HIV): inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(>20% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP29978 AWDFGSLGGVFTSIGKALHQVFGAIYGAA 29 DENV2 Ep (419-447) Q9WDA6 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: an initial, nonspecific interaction of the hydrophobicC terminus of the peptide inhibitor with the viral membranecarries it with the virion into the endosome, allowing aspecific interaction of the peptide with domain II as theprotein reconfigures, inhibiting the final zipping of thestem [Ref.20881042]DENV2(dengue virus type 2): Inhibition of DENV-2 infection in BHK-21 cells (IC90~250µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented low-pH endosome 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP29979 GDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG 38 SARS-CoV-S (1149–1186) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: as GST-fusion polypeptide [Ref.15158473]SARS-CoV: inhibition of SARS-CoV cytopathic effect in Vero E6 cells ( synthetic HR2-38 IC50=0.5-5nM, GST-HR2-38 IC50=66.2nM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented GST 15158473 Biochem Biophys Res Commun. 2004 Jun 18;319(1):283-8. Zhu J, Xiao G, Xu Y, Yuan F, Zheng C, Liu Y, Yan H, Cole DK, Bell JI, Rao Z, Tien P, Gao GF. Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. DRAMP29980 AWDFGSLGGVFTSIGKALHQVFGGAFGAA 29 DENV2 Ep (419-447)[A24G,I25A,Y26F] Q9WDA6 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: an initial, nonspecific interaction of the hydrophobicC terminus of the peptide inhibitor with the viral membranecarries it with the virion into the endosome, allowing aspecific interaction of the peptide with domain II as theprotein reconfigures, inhibiting the final zipping of thestem [Ref.20881042]DENV2(dengue virus type 2): Inhibition of DENV-2 infection in BHK-21 cells (IC90~2µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented low-pH endosome 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP29981 ALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFEL 33 SARS-CoV Sgp (471-503) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: block the binding between the RBD and angiotensin-convertingenzyme 2, resulting in the inhibition of SARS-CoV entrance into host cells in vitro [Ref.16153058]SARS-CoV(Severe acute respiratory syndrome): inhibition of SARS-CoV infction in Vero cells (EC50=41.6µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented not found 16153058 J Comb Chem. 2005 Sep-Oct;7(5):648-56. Hu H, Li L, Kao RY, Kou B, Wang Z, Zhang L, Zhang H, Hao Z, Tsui WH, Ni A, Cui L, Fan B, Guo F, Rao S, Jiang C, Li Q, Sun M, He W, Liu G. Screening and identification of linear B-cell epitopes and entry-blocking peptide of severe acute respiratory syndrome (SARS)-associated coronavirus using synthetic overlapping peptide library. DRAMP29982 SLTQINTTLLDLEYEMRSLQQVVKALNESYIDLKEL 36 MERS-CoV-HR2P [T1263E,L1267R] K9N5Q8 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: interact with the viral HR1 domain to form heterologous 6-HB and block viral fusion coreformation, resulting in inhibition of MERS-CoV S protein-mediated membrane fusion. [Ref.24473083]MERS-COV(Middle East respiratory syndrome coronavirus): inhibition of cell–cell fusion infection in Huh-7 and 293T/MERS/EGFP cells (IC50=0.93±0.15µM); inhibition of MERS-CoV infection in Vero cells (IC50=0.6µM); inhibition of MERS-CoV infection in Calu-3 cells (IC50=0.6µM); inhibition of MERS-CoV infection in HFL cells (IC50=13.9µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24473083]HR2P has low or no in vitro toxic effect. HR1 domain 24473083 Nat Commun. 2014;5:3067. Lu L, Liu Q, Zhu Y, Chan KH, Qin L, Li Y, Wang Q, Chan JF, Du L, Yu F, Ma C, Ye S, Yuen KY, Zhang R, Jiang S. Structure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitor. DRAMP29983 LTQINTTLLDLTYEMLSLQQVVKALNESYIDLKEL 35 MERS-S (1252-1286) K9N5Q8##R9UQ53 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibit MERS-CoV fusion and entry by using a pseudotyped-virus system [Ref.24067982]MERS-COV(Middle East respiratory syndrome coronavirus): inhibition of MERS-CoV PsV infection in 293T/Huh7 cells (EC50~3.013µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 24067982 J Virol. 2013 Dec;87(24):13134-40. Gao J, Lu G, Qi J, Li Y, Wu Y, Deng Y, Geng H, Li H, Wang Q, Xiao H, Tan W, Yan J, Gao GF. Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus. DRAMP29984 RIQQIEQKIHHIEQRIQQIEQRISGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARIL 59 T21N36 A1YNW7 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=81.8±5.69nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented gp41 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z. Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. DRAMP29985 RIQQIEQKIHHIEQRIQQIEQRAIEAQQHLLQLTVWGIKQLQARIL 46 T21N23 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=38.9±35.8nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented gp41 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z. Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. DRAMP29986 RIQQIEQKIHHIEQRIQQIEQLLQLTVWGIKQLQARIL 38 T21N17 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: function as potent inhibitors of viral infection by forming a coiled-coil structure covalently stabilized by interchain disulfide bonds [Ref.31932193]HIV-1(human immunodeficiency virus 1): inhiition of cell-cell fusion between TZM-bl cells and HL2/3 cells(IC50=251±41.1nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented gp41 31932193 Bioorg Med Chem. 2020 Feb 15;28(4):115214. Lai W, Wang C, Yan J, Liu H, Zhang W, Lin B, Xi Z. Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection. DRAMP29987 LHQNIVDVQYMYGLS 15 HCV gp (696–710), E2-79 Q99IB8 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release. [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM Envelope protein 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W. A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. DRAMP29988 GLLHLHQNIVDVQYM 15 HCV gp (692–706), E2-78 Q99IB8 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release. [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM Envelope protein 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W. A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. DRAMP29989 FGCTWMNSTGFTKTC 15 HCV gp (552–566), E2-43 Q99IB8 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release. [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM Envelope protein 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W. A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. DRAMP29990 QGSWFGCTWMNSTGF 18 HCV gp (548–562), E2-42 Q99IB8 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits HCV entry at the post-attachment step and block cell-to-cell transmission, inhibit the late steps of HCV life cycle, such as HCV package and release. [Ref.28638089]HCV(Hepatitis C virus): inhibition of HCVcc infection in Huh7.5/CD81 cells (IC50=1~5nM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.28638089]have no effect on the viability of Huh7.5-CD81 cells at concentrations of 10 nM Envelope protein 28638089 A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, Zhang L, Tan W. A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2. DRAMP29991 VEPGQLKLNWFKK 13 P7(DENV-2 gp (662-674)) P14340 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: might be involved in blocking viral entry via occupying the binding site in the receptor on the host cell(β3 integrin). [Ref.29709564]DENV-2(dengue virus serotype 2): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(65 ± 6% inhibition at 40 μM,55± 12% inhibition at 20 μM,41± 13% inhibition at 10 μM,IC50=12.86±5.96µM);##DENV-1(dengue virus serotype 1): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(65 ± 12% inhibition at 40 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.29709564]No toxic effect on HUVEC(Human umbilical vein endothelial cells) at concentrations up to 100 µM β3 integrin 29709564 Antiviral Res. 2018 Jul;155:20-27. Cui X, Wu Y, Fan D, Gao N, Ming Y, Wang P, An J. Peptides P4 and P7 derived from E protein inhibit entry of dengue virus serotype 2 via interacting with β3 integrin. DRAMP29992 CKIPFEIMDLEKRHV 15 P4(DENV-2 gp (613-627)) P14340 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: might be involved in blocking viral entry via occupying the binding site in the receptor on the host cell(β3 integrin). [Ref.29709564]DENV-2(dengue virus serotype 2): inhibition of virus entry in HUVECs(human umbilical vein endothelial cells)(70 ± 9% inhibition at 40 μM,44 ± 10% inhibition at 20 μM,40± 6% inhibition at 10 μM,IC50=19.08±2.52µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.29709564]No toxic effect on HUVEC(Human umbilical vein endothelial cells) at concentrations up to 100 µM β3 integrin 29709564 Antiviral Res. 2018 Jul;155:20-27. Cui X, Wu Y, Fan D, Gao N, Ming Y, Wang P, An J. Peptides P4 and P7 derived from E protein inhibit entry of dengue virus serotype 2 via interacting with β3 integrin. DRAMP29993 GNHILSLVQNAPYGLYFIHFSW 22 MHV (1096–1117)[Y1117W] P11224 Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]MHV(murine hepatitis virus): inhibition of virus infection in L2 cells(22% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on L2 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29994 GYFVQDDGEWKFTGSSYYY 19 MHV (1144–1162) P11224 Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]MHV(murine hepatitis virus): inhibition of virus infection in L2 cells(98% inhibition at 30 Μm, IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on L2cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29995 AACEVAKNLNESLIDLQELGKYEQYIKW 28 AAC-SARS-CoV (1170–1194) Q19QX0 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(42% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29996 GVFVFNGTSWFITQRNFFS 19 SARS-CoV (1075–1093) Q19QX0 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(83% inhibition at 30 μM,IC50~2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29997 GYHLMSFPQAAP-HGVVFLHVTW 22 SARS-CoV (1028–1049)[Y1049W] Q19QX0 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(90% inhibition at 30 μM,IC50~2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29998 ATAGWTFGAGAALQIPFAMQMAY 23 SARS-CoV (864-886) Q19QX0 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(39% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP29999 TLKPIFKLPLGINITNFR 18 SARS-CoV-S (215-232), peptide 9626 P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Presumably inhibit virus entry by binding to Spike protein, hACE2, or an unknown co-receptor. [Ref.19853613]SARS-COV: inhibition of SARS-CoV/HIV PsV virus infection in 293T/ACE2 cells (IC50=11µM); inhibition of SARS-CoV/HIV PsV virus entry in 293T/ACE2 cells(80% at 50µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented not found 19853613 J Mol Biol. 2009 Dec 11;394(4):600-5. Guo Y, Tisoncik J, McReynolds S, Farzan M, Prabhakar BS, Gallagher T, Rong L, Caffrey M. Identification of a new region of SARS-CoV S protein critical for viral entry. DRAMP30000 MWKTPTLKYFGGFNFSQIL 19 SARS-CoV (770-788)[Y771W] Q19QX0 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: inhibits viral entry through coiled coil interactions. [Ref.16616792]SARS-CoV: inhibition of virus infection in Vero-E6 cells(58% inhibition at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxic at a concentration of 30 μM on Vero-E6 cells cell membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. DRAMP30001 QNQSANQFQKEISQINEVLTTTNTSLGKLQDDVNQNNQSLNTLQKE 46 N46eg(SARS-CoV (902-947)[K2N,I4S,N9Q,A11E,Q16N,S18V,S23N,A25S,V32D,A37N,A39S,V44Q,Q46E]) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding to the HR2 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry. [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=5.07 ± 0.17 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. membrane 18983873 Antiviral Res. 2009 Jan;81(1):82-7. Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK. Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. DRAMP30002 QKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQ 46 N46(SARS-CoV (902-947)) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding to the HR2 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry. [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=3.97 ± 1.40 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. membrane 18983873 Antiviral Res. 2009 Jan;81(1):82-7. Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK. Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. DRAMP30003 GINASVVNIQKEIDRLNEVAKNLNESLIDL 30 P4(SARS-CoV (1153–1182)) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry. [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=0.80 ± 0.21 μM);inhibition of SARS-CoV infection in Vero-E6 cells (IC50=3.17 ± 0.24 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. membrane 18983873 Antiviral Res. 2009 Jan;81(1):82-7. Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK. Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. DRAMP30004 GINASVVNIQKEIDRLNEVAKNL 23 P6(SARS-CoV (1153–1175)) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry. [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=1.04 ± 0.22 μM); inhibition of SARS-CoV infection in Vero-E6 cells (IC50=2.28 ± 0.81 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. membrane 18983873 Antiviral Res. 2009 Jan;81(1):82-7. Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK. Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors. DRAMP30005 GINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 37 P1(SARS-CoV (1153-1189)) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding to the HR1 region and blocking the formation of a 6-helix bundle during the fusion step of virus entry, thus inhibiting virus entry. [Ref.18983873]SARS-CoV:inhibition of cell fusion in Hela cells (IC50=0.62 ± 0.20 μM);inhibition of SARS-CoV infection in Vero-E6 cells (IC50=3.04 ± 0.06 μM).##[Ref.15043961]SARS-CoV:inhibition of the cytopathic effect in Vero E6 cells(IC50~19 μM/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18983873]No discernable cytotoxicity on HeLa or VeroE6 cells at the concentrations of 25 μM. membrane 18983873##15043961 Antiviral Res. 2009 Jan;81(1):82-7.##Lancet. 2004 Mar 20;363(9413):938-47. Liu IJ, Kao CL, Hsieh SC, Wey MT, Kan LS, Wang WK.##Liu S, Xiao G, Chen Y, He Y, Niu J, Escalante CR, Xiong H, Farmar J, Debnath AK, Tien P, Jiang S. Identification of a minimal peptide derived from heptad repeat (HR) 2 of spike protein of SARS-CoV and combination of HR1-derived peptides as fusion inhibitors.##Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. DRAMP30006 AWDFGSVGGVFNSLGKGIHQIFGAAFKSL 29 ZIKV Ep (424-452) Q32ZE1 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. [Ref.28232248]Zika virus (ZIKV):inhibition of Zika virus (ZIKV) infection in Vero cells (IC50=1.32μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30007 AWDFGSIGGVFNSIGRAVHQVFGGAFRTL 29 JEV Ep (424–452) P0DOH7 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=7.66 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30008 AWDFGSIGGVFNSIGRAVHQVF 22 JEV Ep (424–445) P0DOH7 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevented JEV infection in mice by reducing viral load and the inflammatory response in the brain, thereby improving the survival rate. [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=3.93 nM);##Zika virus (ZIKV):inhibition of Zika virus (ZIKV) infection in Vero cells (IC50=3.27μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30009 AALGDTAWDFGSIGGVFNSIGRAVHQVFGGAFRTL 35 JEV Ep (418–452) P0DOH7 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=58.07 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30010 SIGGVFNSIGRAVHQVFGGAFRTL 24 JEV Ep (428–452) P0DOH7 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=94.10 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30011 STLGKAFSTTLKGAQRLAALGDTAWDFG 28 JEV Ep (401–428) P0DOH7 Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from protein E stem may inhibit virus infection by blocking virus entry. [Ref.28232248]Japanese encephalitis virus (JEV):inhibition of JEV infection in BHK-21 (baby hamster kidney) cells (IC50=3790.71 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 28232248 Antiviral Res. 2017 May;141:140-149. Chen L, Liu Y, Wang S, Sun J, Wang P, Xin Q, Zhang L, Xiao G, Wang W. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. DRAMP30012 AGVSGHGQHGVHG 13 Alloferon-1 [H1A] P83412 Herpesviridae, Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit the replication of DNA and RNA viruses. [Ref.21766388]Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=358.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 187.50 µg/ml. Not found 21766388 J Pept Sci. 2011 Nov;17(11):715-9. Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D. Further studies on the antiviral activity of alloferon and its analogues. DRAMP30013 RGVSGHGQHGVHG 13 Alloferon-1 [H1R] P83412 Herpesviridae, Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit the replication of DNA and RNA viruses. [Ref.21766388]HHV-1 McIntyre strain:inhibition of virus replication in Vero cells(IC50=321.10 µg/ml);##HHV-1:inhibition of virus replication in Vero cells(IC50=277.50 µg/ml);inhibition of virus replication in HEp-2 cells(IC50=602.18 µg/ml);##Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=577.73 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=167.71 µg/ml);##CVB2:inhibition of virus replication in LLC-MK2 cells(IC50=355.18 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 143.75 µg/ml. Not found 21766388 J Pept Sci. 2011 Nov;17(11):715-9. Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D. Further studies on the antiviral activity of alloferon and its analogues. DRAMP30014 KGVSGHGQHGVHG 13 Alloferon-1 [H1K] P83412 Herpesviridae, Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit the replication of DNA and RNA viruses. [Ref.21766388]HHV-1 McIntyre strain:inhibition of virus replication in Vero cells(IC50=147.09 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=241.90 µg/ml);##HHV-1:inhibition of virus replication in Vero cells(IC50=9.19 µg/ml);inhibition of virus replication in HEp-2 cells(IC50=12.98 µg/ml);##Coxsackie virus 971 PT(971 PT CVB2):inhibition of virus replication in LLC-MK2 cells(IC50=157.73 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=107.04 µg/ml);##CVB2:inhibition of virus replication in LLC-MK2 cells(IC50=190.67 µg/ml);inhibition of virus replication in Hep-2 cells(IC50=74.00 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.21766388]No cytotoxicity against Vero cells,LLC-MK2 cells and Hep-2 cells up to 218.75 µg/ml. Not found 21766388 J Pept Sci. 2011 Nov;17(11):715-9. Kuczer M, Midak-Siewirska A, Zahorska R, Luczak M, Konopińska D. Further studies on the antiviral activity of alloferon and its analogues. DRAMP30015 GQGKAHNGRLITANP 15 DENV Envelope glycoprotein (340 – 354) Q5UB51##P17763 Flaviviridae Not found Synthetic construct(derived from DENV Envelope glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry. [Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(83%±3.72% inhibition at 50 μM,IC50=33 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. E protein 30508603 Virus Res. 2019 Jan 15;260:142-150. John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P. In vitro analysis of synthetic peptides in blocking the entry of dengue virus. DRAMP30016 DRGWGNGCGLFG 12 DENV Envelope glycoprotein (98-109) Q5UB51##P17763 Flaviviridae Not found Synthetic construct(derived from DENV Envelope glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry. [Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(88%±3.89% inhibition at 50 μM,IC50=10 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. E protein 30508603 Virus Res. 2019 Jan 15;260:142-150. John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P. In vitro analysis of synthetic peptides in blocking the entry of dengue virus. DRAMP30017 LEHGSCVTTMAKDKPTL 17 DENV Envelope glycoprotein (25-41) Q5UB51##P17763 Flaviviridae Not found Synthetic construct(derived from DENV Envelope glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts as inhibitors by binding to the E protein, suppressing its conformational changes, and preventing its binding to the cellular receptor, thereby inhibiting viral entry. [Ref.30508603]DENV-1:inhibition of virus infection in Vero cells(58%±2.55% inhibition at 50 μM,IC50=10 μM);##DENV-2:inhibition of virus infection in Vero cells(IC50=10 μM);##DENV-3:inhibition of virus infection in Vero cells(60% inhibition at 20μM);##DENV-4:inhibition of virus infection in Vero cells(55% inhibition at 20μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30508603]<20% cytotoxicity against Vero and C6/36 cells at 200 μM. E protein 30508603 Virus Res. 2019 Jan 15;260:142-150. John AM, Jittmittraphap A, Chattanadee S, Alwin Prem Anand A, Shenbagarathai R, Leaungwutiwong P. In vitro analysis of synthetic peptides in blocking the entry of dengue virus. DRAMP30018 RRRRRRRXPLSPPLRNTHPQAMQWNSTTF 29 7R-Ahx-HBV Large envelope protein (96-116) P03138 Hepadnaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=6.5 ± 1.5 μM;EC90=41.4 ±8.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L [Ref.21144865]HepG2.2.15:LC50=515.9± 43.8 μM. DNA 21144865 Antiviral Res. 2011 Jan;89(1):109-14. Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X. Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. DRAMP30019 RRRRRRRXLDPAFR 14 7R-Ahx-HBV Large envelope protein (19-24) P03138 Hepadnaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=3.0 ± 1.0 μM;EC90=10.9 ± 3.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L [Ref.21144865]No cytotoxicity was observed at 1mM of peptide concentration against HepG2.2.15. DNA 21144865 Antiviral Res. 2011 Jan;89(1):109-14. Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X. Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. DRAMP30020 RRRRRRRXPTSNHSPTSCPPTCPGYRWMCLRRF 33 7R-Ahx-HBV Large envelope protein (219-243) P03138 Hepadnaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=12.8 ± 2.0 μM;EC90=85.6 ± 9.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L [Ref.21144865]HepG2.2.15:LC50=457.9 ± 41.0 μM. DNA 21144865 Antiviral Res. 2011 Jan;89(1):109-14. Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X. Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. DRAMP30021 RRRRRRRXGSLLGRMKGA 18 7R-Ahx-P3 Hepadnaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can efficiently enter cells and inhibit the envelopment of HBV nucleocapsids and subsequent secretion of viral particles. [Ref.21144865]HBV:inhibition of cell proliferation in HepG2.2.15 cells(EC50=2.5 ±1.0 μM;EC90=8.6± 3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 8 is 6-aminocaproic acid. L [Ref.21144865]HepG2.2.15:LC50=828.7 ± 50.3 μM. DNA 21144865 Antiviral Res. 2011 Jan;89(1):109-14. Pan XB, Wei L, Han JC, Ma H, Deng K, Cong X. Artificial recombinant cell-penetrating peptides interfere with envelopment of hepatitis B virus nucleocapsid and viral production. DRAMP30022 EEQAKTFLDKFNHEAEDLFYQSSGLGKGDFR 31 P6(ACE2 (4-26)-G-ACE2 (333-339)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=0.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30023 EEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEE 36 P5(ACE2 (4-39)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30024 EEQAKTFLDKFNHEAEDLFYQSS 23 P4(ACE2 (4-26)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(IC50=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30025 NHEAEDLFY 9 P3(ACE2 (15-23)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(30% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30026 DKFNHEAED 9 P2(ACE2 (12-20)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(40% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30027 EEQAKTFLDK 10 P1(ACE2 (4-13)) Q9BYF1 Coronaviridae Not found Synthetic construct(derived from angiotensin-converting enzyme 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2), peptide derived from ACE2 could bind with spike glycoprotein and inhibits virus entry. [Ref.16510163]SARS-CoV:inhibition of pseudovirus infection in HeLa cells(25% inhibition at 100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry spike glycoprotein 16510163 Virology. 2006 Jun 20;350(1):15-25. Han DP, Penn-Nicholson A, Cho MW. Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. DRAMP30028 HAKFWW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP30029 HCAFWW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=49 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP30030 EEHEKYHSNW 10 NL1 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30031 ASCDKCQLKG 10 NL2 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30032 HGQVDCSPGIWQLDCTH 17 NL3 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=1000 µM);inhibition of strand transfer catalyzed by integrase(IC50=1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30033 VHVASGY 7 NL4 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30034 PAETGQET 8 NL5 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30035 TAYFLLKLAGRW 12 NL-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=21±7 µM);inhibition of strand transfer catalyzed by integrase(IC50=2.7±1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30036 GRWPVKT 7 NL7 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30037 HTDNGSNF 8 NL8 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30038 ACWWAGIKQEF 11 NL-9 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=95±9 µM);inhibition of strand transfer catalyzed by integrase(IC50=56±5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30039 FGIPYNPQSQ 10 NL10 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30040 ESMNKELKKI 10 NL11 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30041 VRDQAEHLKT 10 NL12 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30042 FIHNFKRK 8 NL13 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30043 GYSAGERIVD 10 NL14 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>2000 µM);inhibition of strand transfer catalyzed by integrase(IC50>2000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30044 WKGPAKLLWK 10 NL15 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30045 VPRRKAKI 8 NL16 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30046 AAYFLLKLAGRW 12 NL6-T1A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=100±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=47±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30047 TAAFLLKLAGRW 12 NL6-Y3A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=193±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=119±11 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30048 TAYALLKLAGRW 12 NL6-F4A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30049 TAYFALKLAGRW 12 NL6-L5A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=115±21 µM);inhibition of strand transfer catalyzed by integrase(IC50=51±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30050 TAYFLAKLAGRW 12 NL6-L6A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30051 TAYFLLALAGRW 12 NL6-K7A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=113±15 µM);inhibition of strand transfer catalyzed by integrase(IC50=56±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30052 TAYFLLKAAGRW 12 NL6-L8A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50=106±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30053 TAYFLLKLAARW 12 NL6-G10A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=118±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=19±6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30054 TAYFLLKLAGAW 12 NL6-R11A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=83±15 µM);inhibition of strand transfer catalyzed by integrase(IC50=80±8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30055 TAYFLLKLAGRA 12 NL6-W12A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30056 AAWWAGIKQEF 11 NL9-C2A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=277±47 µM);inhibition of strand transfer catalyzed by integrase(IC50=311±19 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30057 ACAWAGIKQEF 11 NL9-W3A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=33±6 µM);inhibition of strand transfer catalyzed by integrase(IC50=34±8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30058 ACWAAGIKQEF 11 NL9-W4A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30059 ACWWAAIKQEF 11 NL9-G6A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=90±10 µM);inhibition of strand transfer catalyzed by integrase(IC50=43±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30060 ACWWAGAKQEF 11 NL9-I7A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30061 ACWWAGIAQEF 11 NL9-K8A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=62±13 µM);inhibition of strand transfer catalyzed by integrase(IC50=55±7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30062 ACWWAGIKAEF 11 NL9-Q9A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30063 ACWWAGIKQAF 11 NL9-E10A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30064 ACWWAGIKQEA 11 NL9-F11A No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=245±13 µM);inhibition of strand transfer catalyzed by integrase(IC50=206±12 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30065 TASFLLKLAGRW 12 NL6-1 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=186±23 µM);inhibition of strand transfer catalyzed by integrase(IC50=11±2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30066 TAYFLLILAGRW 12 NL6-2 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=4.1±0.7 µM);inhibition of strand transfer catalyzed by integrase(IC50=3.0±1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30067 TAYFLLKLAGRL 12 NL6-3 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=315±30 µM);inhibition of strand transfer catalyzed by integrase(IC50=38±2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30068 ASWWAGIKQEF 11 NL9-1 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=294±41 µM);inhibition of strand transfer catalyzed by integrase(IC50=163±15 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30069 ACGWAGIKQEF 11 NL9-2 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=46±5 µM);inhibition of strand transfer catalyzed by integrase(IC50=16±2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30070 ACWGAGIKQEF 11 NL9-3 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30071 ACWWAGIRQEF 11 NL9-4 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30072 TAYFLL 6 NL6-4 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=500 µM);inhibition of strand transfer catalyzed by integrase(IC50=500 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30073 YFLLKL 6 NL6-5 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=20 µM);inhibition of strand transfer catalyzed by integrase(IC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30074 KLAGRW 6 NL6-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30075 ACWWAG 6 NL9-5 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30076 WAGIKQ 6 NL9-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30077 IKQEF 5 NL9-7 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>100 µM);inhibition of strand transfer catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30078 tayfllklagrw 12 DNL-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=65±8 µM);inhibition of strand transfer catalyzed by integrase(IC50=13±1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30079 WRGALKLLFYAT 12 RNL-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=96±2 µM);inhibition of strand transfer catalyzed by integrase(IC50=16±4 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30080 wrgalkllfyat 12 RDNL-6 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.5±1 µM);inhibition of strand transfer catalyzed by integrase(IC50=4.0±1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30081 acwwagikqef 11 DNL-9 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30082 FEQKIGAWWCA 11 RNL-9 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30083 feqkigawwca 11 RDNL-9 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 integrase (IN) is essential for viral replication. Following reverse transcription of the RNA into DNA by HIV-1 reverse transcriptase, IN integrates the viral DNA into the host genome.The peptide could inbibit integrase(By inhibiting the two steps of IN catalysis: 3′-processing and strand transfer). [Ref.16854053]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1000 µM);inhibition of strand transfer catalyzed by integrase(IC50>1000 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 16854053 J Med Chem. 2006 Jul 27;49(15):4477-86. Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. Sequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. DRAMP30084 DFRELNKRTQDFWEVQLGIP 20 4277(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is very low. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30085 SPAIFQSSMTKILEPFRKQN 20 4285(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=35 µM);inhibition of strand transfer catalyzed by integrase(IC50=270 µM);inhibition of disintegration catalyzed by integrase(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30086 FRKQNPDIVIYQYMD 15 4286’-1(derived from the DNA-polymerase domain of HIV-1 RT (14-mer) ) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=119 µM);inhibition of strand transfer catalyzed by integrase(IC50=97 µM);inhibition of disintegration catalyzed by integrase(IC50>270 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30087 KILEPFRKQNPDIVIYQYMD 20 4286(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=4.8 µM);inhibition of strand transfer catalyzed by integrase(IC50=4.5 µM);inhibition of disintegration catalyzed by integrase(IC50=9.4 µM);##HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30088 PDIVIYQYMDDLYVGSDLEI 20 4287(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),34(derived from the HIV-1 HXB2 Pol region of the viral genome) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=22 µM);inhibition of strand transfer catalyzed by integrase(IC50=54 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM);##HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=6±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=10±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=28±2 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=23±2 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=41±2 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=20 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=5 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. DRAMP30089 DIQKLVGKLNWASQIYPGIK 20 4295(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30090 IAEIQKQGQGQWTYQIYQEP 20 4302(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30091 KQLTEAVQKITTEAnti-SIVIWGK 20 4306(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),53(derived from the HIV-1 HXB2 Pol region of the viral genome) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=7±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=4±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=51±7 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=31±7 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=29±1 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=15 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=10 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. DRAMP30092 TPKFKLPIQKETWETWWTEY 20 4308(derived from DNA-polymerase domain of HIV-1 RT (20-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30093 ETWETWWTEYWQATWIPEWE 20 4309(derived from DNA-polymerase domain of HIV-1 RT (20-mers)),56(derived from the HIV-1 HXB2 Pol region of the viral genome) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication. [Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=6±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=13±2 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=9±2 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=126±3 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=27±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=25 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=5 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. DRAMP30094 GYVTNRGRQKVVTLTDTTNQ 20 4315(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is very low No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30095 VVTLTDTTNQKTELQAIYLA 20 4316(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30096 KTELQAIYLALQDSGLEVNI 20 4317(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30097 LQDSGLEVNIVTDSQYALGI 20 4318(derived from the RNase H domain of HIV-1 RT (20-mes)),65(derived from the HIV-1 HXB2 Pol region of the viral genome) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=11±1 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=2±1 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50>167 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=36±14 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=18±3 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=4±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50>167 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=20 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. DRAMP30098 VTDSQYALGIIQAQPDQSES 20 4319(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is low. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30099 IQAQPDQSESELVNQIIEQL 20 4320(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50>120 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30100 ELVNQIIEQLIKKEKVYLAW 20 4321(derived from the RNase H domain of HIV-1 RT (20-mes)),64(derived from the HIV-1 HXB2 Pol region of the viral genome) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=6.9 µM);inhibition of strand transfer catalyzed by integrase(IC50=5 µM);inhibition of disintegration catalyzed by integrase(IC50>100 µM);##HIV-1:the level of peptide binding to HIV integrase is high.##[Ref.16879966]HIV:inhibition of 3′-processing catalyzed by wild-type integrase(IC50=15±2 µM);inhibition of strand transfer catalyzed by wild-type integrase(IC50=14±4 µM);inhibition of 3′-processing catalyzed by soluble mutant integrase(IC50=113±11 µM);inhibition of strand transfer catalyzed by soluble mutant integrase(IC50=83±5 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=136±5 µM);inhibition of strand transfer catalyzed by C130S integrase(IC50=7±1 µM);inhibition of 3′-processing catalyzed by C130S integrase(IC50=45 µM);inhibition of strand transfer catalyzed by C130A integrase(IC50=15 µM).##NOTE:soluble mutant,C130S,C130S integrase are mutant IN. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559##16879966 J Biol Chem. 2005 Jun 10;280(23):21987-96.##Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.##Zawahir Z, Neamati N. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.##Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. DRAMP30101 NQIIEQLIKKEKVY 14 4321’-1( derived from the RNase H domain of HIV-1 RT (15-mer)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>240 µM);inhibition of strand transfer catalyzed by integrase(IC50>240 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30102 IKKEKVYLAWVPAHKGIGN 19 4322(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50>120 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30103 EQVDKLVSAGIRKVLFLDGI 20 4324(derived from the RNase H domain of HIV-1 RT (20-mes)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:the level of peptide binding to HIV integrase is high. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30104 ESELVSQIIEQLIKK 15 5628(derived from RNase H domain of HIV-1 RT (15-mers)) No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Reverse Transcriptase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RNase H domain of HIV-1 RT inhibits integrase-associated activities (3′-end processing and strand transfer) and inhibit virus replication. [Ref.15790559]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>120 µM);inhibition of strand transfer catalyzed by integrase(IC50=60 µM);inhibition of disintegration catalyzed by integrase(IC50>120 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 15790559 J Biol Chem. 2005 Jun 10;280(23):21987-96. Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A. Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. DRAMP30105 LQQLLFIHFRIGCQH 15 Vpr 15 No entry found Retroviridae Not found Synthetic construct(HIV-1 gene product) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:inhibition of strand transfer catalyzed by integrase(IC50=5.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30106 TNWLWYIKIFIMIV 14 Env4-4 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:inhibition of strand transfer catalyzed by integrase(IC50=1.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30107 LQQLLF 6 Vpr-1 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 gene products(Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>11 µM);inhibition of strand transfer catalyzed by integrase(IC50=68±1.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30108 LQQLLFRRRRRRRR 14 Vpr-1 R8 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 gene products(Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=6.1±1.1 µM);inhibition of strand transfer catalyzed by integrase(IC50>11 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30109 IHFRIGRRRRRRRR 14 Vpr-2 R8 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 gene products(Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.70±0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.83±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30110 LQQLLFIHFRIGRRRRRRRR 20 Vpr-3 R8 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 gene products(Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.004±0.0001 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.008±0.001 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30111 EAIIRILQQLLFIHFRIGRRRRRRRR 26 Vpr-4 R8 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 gene products(Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: IN is an essential enzyme for the stable infection of host cells because it catalyzes the insertion of viral DNA inside the pre-integration complex (PIC) into the genome of host cells in two successive reactions, designated as strand transfer and 3′-end-processing. The peptide could inhibit the activity of integrase and thus inhibit virus replication. [Ref.20586421]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=0.005±0.002 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.006±0.006 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20586421 J Med Chem. 2010 Jul 22;53(14):5356-60. Suzuki S, Urano E, Hashimoto C, Tsutsumi H, Nakahara T, Tanaka T, Nakanishi Y, Maddali K, Han Y, Hamatake M, Miyauchi K, Pommier Y, Beutler JA, Sugiura W, Fuji H, Hoshino T, Itotani K, Nomura W, Narumi T, Yamamoto N, Komano JA, Tamamura H.  Peptide HIV-1 integrase inhibitors from HIV-1 gene products. DRAMP30112 TYGDTWAGVEAIIRI 15 Vpr 49-63 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50>>150 µM);inhibit the activity of Rnase H(IC50>>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30113 TWAGVEAIIRILQQL 15 Vpr 53-67 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.88 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=0.88 µM);inhibit the activity of Rnase H(IC50=6.9 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM);inhibition of strand transfer catalyzed by integrase(IC50=144 µM);inhibition of disintegration catalyzed by integrase(IC50=27 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase,Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30114 VEAIIRILQQLLFIH 15 Vpr 57-71 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of Rnase H(IC50=2 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=7.8 µM);inhibition of strand transfer catalyzed by integrase(IC50=16 µM);inhibition of disintegration catalyzed by integrase(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase,Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30115 IRILQQLLFIHFRIG 15 Vpr 61-75 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.7 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=1.3 µM);inhibit the activity of Rnase H(IC50=5.25 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=1.3 µM);inhibition of strand transfer catalyzed by integrase(IC50=1 µM);inhibition of disintegration catalyzed by integrase(IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase,Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30116 QQLLFIHFRIGCQHS 15 Vpr 65-79 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=33 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=43 µM);inhibit the activity of Rnase H(IC50=16.5 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50=76 µM);inhibition of strand transfer catalyzed by integrase(IC50=14 µM);inhibition of disintegration catalyzed by integrase(IC50=10 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase,Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30117 FIHFRIGCQHSRIGI 15 Vpr 69-83 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50>>200 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50>>200 µM);inhibit the activity of Rnase H(IC50>>200 µM);##Inhibition of 3′-end processing catalyzed by integrase(IC50>>200 µM);inhibition of strand transfer catalyzed by integrase(IC50>>200 µM);inhibition of disintegration catalyzed by integrase(IC50>>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase,Reverse Transcriptase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30118 HFPRIWLHSLGQHIY 15 Vpr 33-47 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 viral protein R (Vpr)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and thus inhibit the replication of HIV-1. [Ref.17490682]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=187 µM);inhibition of strand transfer catalyzed by integrase(IC50=41 µM);inhibition of disintegration catalyzed by integrase(IC50=73 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 17490682 J Mol Biol. 2007 Jun 22;369(5):1230-43. Gleenberg IO, Herschhorn A, Hizi A. Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). DRAMP30119 QLLIRMIYKNILFYLVPGPGHGAEPERRNIKYL 33 I33 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide bound tightly to the integrase(IN) and inhibited both in vitro IN activities, containing 3′ end processing and strand transfer. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=9 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30120 RMIYKNILFYLVPGPGHGAEPERRNIKYL 29 I29 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=85 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30121 QLLIRMI 7 LCD278B No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30122 AEPERRNIKYL 11 EBR24 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30123 LFYLVPGPGH 10 EBR26 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30124 YQLLIRMIYKNI 12 EBR28 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=5 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50=40 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30125 YALLIRMIYKNI 12 EBR28[Q2A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=8 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30126 YQALIRMIYKNI 12 EBR28[L3A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=165 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30127 YQLAIRMIYKNI 12 EBR28[L4A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=14 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30128 YQLLARMIYKNI 12 EBR28[I5A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=45 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30129 YQLLIAMIYKNI 12 EBR28[R6A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=34 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30130 YQLLIRAIYKNI 12 EBR28[M7A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=70 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30131 YQLLIRMAYKNI 12 EBR28[I8A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=35 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30132 YQLLIRMIAKNI 12 EBR28[Y9A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=40 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30133 YQLLIRMIYANI 12 EBR28[K10A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=11 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30134 YQLLIRMIYKAI 12 EBR28[N11A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=7 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30135 YQLLIRMIYKNA 12 EBR28[I12A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=11 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30136 YQLLIRMIY 9 LCE41 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=5 µM);inhibition of HIV-1 infection in HeLa CD4-β-Gal cells(IC50=55 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30137 YQLLIRMI 8 LCE40 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=120 µM);no inhibition of HIV-1 infection up to 100 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30138 QLLIRMIYKNI 11 LCD278C No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50=21 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30139 YQLLIRPIYKNI 12 ProEBR28 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30140 LSELDDRADALQAGASQFETSAAKLKRKYWWKN 33 C35 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Binding of both viral DNA and host chromosomal DNA are critical steps in IN-catalyzed reactions. The peptide interacted with the catalytic domain of IN interfering with the binding of the DNA substrate and inhibit the replication of virus. [Ref.12054767]HIV-1:Inhibition of 3′-end processing catalyzed by integrase(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12054767]P4 cells: Cell viability estimated by the MTT assay was decreased by about 5% at peptide concentrations higher than 100 μM. Integrase 12054767 J Mol Biol. 2002 Apr 19;318(1):45-58. de Soultrait VR, Caumont A, Parissi V, Morellet N, Ventura M, Lenoir C, Litvak S, Fournier M, Roques B.  A novel short peptide is a specific inhibitor of the human immunodeficiency virus type 1 integrase. DRAMP30141 TGEKVWDRGNVTLLCDCP 18 P11(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=439.7 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=162.1 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=484.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=208.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30142 LPAFCQAIGWGDPITHWS 18 P19(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=369.5 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=46.0 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=194.3 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=71.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30143 FCQAIGWGDPITHWSHGQ 18 P20(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=347.6 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=70.1 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=125.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=111.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30144 AIGWGDPITHWSHGQNRW 18 P21(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=832.9 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=44.9 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=529.1 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=371.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30145 PITHWSHGQNRWPLSCPQ 18 P23(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=508.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30146 HGQNRWPLSCPQYVYGSV 18 P25(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=304.4 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30147 SWFASTGGRDSKIDVWSL 18 P34(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=237.4 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=411.2 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=118.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30148 SDRDTVVELSEWGVPCAT 18 P45(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=141.2 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=48.8 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=505.5 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=43.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30149 DTVVELSEWGVPCATCIL 18 P46(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=428.8 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=39.9 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=462.8 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=24.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30150 VELSEWGVPCATCILDRR 18 P47(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=330.8 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=58.6 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=140.3 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=20.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30151 RFPFHRCGAGPKLTKDLE 18 P59(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=529.6 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30152 LVRRRSELMGRRNPVCPG 18 P97(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=537.6 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30153 LQEVDAGNFIPPPRWLLL 18 P109(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=687.1 μM);inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=37.5 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=294.8 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=60.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30154 WVNQLAVLGLPAVDAAVA 18 P124(derived from E2 envelope protein of GB virus C) No entry found Retroviridae Not found Synthetic construct(derived from E2 envelope protein of GB virus C) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner. [Ref.20718496]HIV-1:inhibition of gp41-induced cell-cell fusion in CEM-174 cells(IC50=332.7 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=94.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20718496 J Med Chem. 2010 Aug 26;53(16):6054-63.  Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I. Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection. DRAMP30155 SAnti-VSVGMKPSPRP 12 VMI5 No entry found Retroviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:binding with vif proteins. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30156 SNQGGSPLPRSV 12 VMI7 No entry found Retroviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=7.43 μM);##The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30157 LPLPAPSFHRTT 12 VMI9 No entry found Retroviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=4.84 μM);####The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30158 SPYPSWSTPAGR 12 VMI16 No entry found Retroviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:binding with vif proteins. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30159 KPKQIKPPLPSV 12 vif 155-166 No entry found Retroviridae Not found Synthetic construct(derived from the proline-enriched C terminus of Vif) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibition of Vif-Vif bingding(IC50=17.39 μM);####The peptide is able to effectively inhibit HIV-1 replication At the concentration of 50 μM. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12480936]No significant cytotoxicity on H9 cells up to 50 μM. Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30160 WQVMIVWQVDRMRIR 15 vif 5-19 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30161 RHHYESTHPRISSEV 15 vif 41-55 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30162 ESTHPRISSEVHIPL 15 vif 45-59 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30163 HTGERDWHLGQGVSI 15 vif 73-87 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30164 RDWHLGQGVSIEWRK 15 vif 77-91 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30165 LGQGVSIEWRKKRYS 15 vif 81-95 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30166 RYSTQVDPDLADQLI 15 vif 93-107 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30167 QVDPDLADQLIHLYY 15 vif 97-111 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30168 DLADQLIHLYYFDCF 15 vif 101-115 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30169 QLIHLYYFDCFSESA 15 vif 105-119 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30170 LYYFDCFSESAIRKA 15 vif 109-123 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30171 ESAIRKAILGHIVSP 15 vif 117-131 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30172 RKAILGHIVSPRCEY 15 vif 121-135 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30173 VSPRCEYQAGHNKVG 15 vif 129-143 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30174 CEYQAGHNKVGSLQY 15 vif 133-147 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30175 AGHNKVGSLQYLALA 15 vif 137-151 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30176 KVGSLQYLALAALIT 15 vif 141-155 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30177 LQYLALAALITPKKI 15 vif 145-159 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30178 ALAALITPKKIKPPL 15 vif 149-163 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30179 LITPKKIKPPLPSVT 15 vif 153-167 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30180 KKIKPPLPSVTKLTE 15 vif 157-171 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30181 PPLPSVTKLTEDRWN 15 vif 161-175 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30182 SVTKLTEDRWNKPQK 15 vif 165-179 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30183 LTEDRWNKPQKTKGH 15 vif 169-183 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30184 RWNKPQKTKGHRGSH 15 vif 173-187 No entry found Retroviridae Not found Synthetic construct(derived from HIV-1 Vif protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication. [Ref.12480936]HIV-1:inhibit vif-vif binding. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Vif proteins 12480936 J Biol Chem. 2003 Feb 21;278(8):6596-602. Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. DRAMP30185 PTGERVWDRGNVTLLCDCPN 20 P4 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=15.07 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=18.28 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30186 WDRGNVTLLCDCPNGPWVWV 20 P4-7 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=2.59 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=2.66 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30187 WDRGNVTLLCDCPNGPWVWV 20 P4-7 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(NL4-3):inhibition of HIV replication(IC50=3.0 μM);##HIV-1(YU-2):inhibition of HIV replication(IC50=5.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30188 GPWVWVPAFCQAVGWGDPIT 20 P6 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=16.80 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=3.57 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30189 TLLCDCPNGPWVWVPAFCQA 20 P6-1 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=2.36 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=1.29 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30190 LCDCPNGPWVWVPAFCQAVG 20 P6-2 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=3.33 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=1.32 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30191 LCDCPNGPWVWVPAFCQAVG 20 P6-2 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(NL4-3):inhibition of HIV replication(IC50=2.3 μM);##HIV-1(YU-2):inhibition of HIV replication(IC50=2.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30192 DCPNGPWVWVPAFCQAVGWG 20 P6-3 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=4.00 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=2.00 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30193 PNGPWVWVPAFCQAVGWGDP 20 P6-4 No entry found Retroviridae Not found Synthetic construct(derived from region of GB virus C glycoprotein E2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The possible mechanism of action is that the peptide could inhibit membrane fusion and inhibit HIV-1 replication in cells. [Ref.21543477]HIV-1(92UG024):inhibition of HIV replication in TZM-bl cells(IC50=11.88 μM);##HIV-1(RU570):inhibition of HIV replication in TZM-bl cells(IC50=8.04 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21543477 J Virol. 2011 Jul;85(14):7037-47. Koedel Y, Eissmann K, Wend H, Fleckenstein B, Reil H.  Peptides derived from a distinct region of GB virus C glycoprotein E2 mediate strain-specific HIV-1 entry inhibition. DRAMP30194 RGTKALTEVIPLTEEAEC 18 PepA No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =35 ± 5 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30195 GTKALTEVIPLTEEAEC 17 P1 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =7.5±2.3 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=78.2 nM,associated with Pep-1).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30196 ATKALTEVIPLTEEAEC 17 P2 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =28 ±11 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30197 GAKALTEVIPLTEEAEC 17 P3 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =10.3 ± 2.1 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30198 GTAALTEVIPLTEEAEC 17 P4 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =15 ± 2.9 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30199 GTKGLTEVIPLTEEAEC 17 P5 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =20 ± 3.7 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30200 GTKAATEVIPLTEEAEC 17 P6 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =5.7 ± 2.3 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=170 nM,associated with Pep-1).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30201 GTKALAEVIPLTEEAEC 17 P7 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =13.5 ± 2.1 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30202 GTKALTAVIPLTEEAEC 17 P8 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =57 ± 19 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=290 nM,associated with Pep-1).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30203 GTKALTEAIPLTEEAEC 17 P9 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =15 ±7.3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30204 GTKALTEVAPLTEEAEC 17 P10 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =7.3 ± 2.9 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=140 nM,associated with Pep-1).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30205 GTKALTEVIALTEEAEC 17 P11 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =7 ± 1.4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30206 GTKALTEVIPATEEAEC 17 P12 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =22 ± 3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30207 GTKALTEVIPLAEEAEC 17 P13 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =10.2 ± 2.5 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30208 GTKALTEVIPLTAEAEC 17 P14 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1: inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 3 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30209 GTKALTEVIPLTEAAEC 17 P15 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 2.2 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30210 GTKWLTEVWPLC 12 P16 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =14 ± 4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30211 GTKAWTEVWPLC 12 P17 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =35 ± 11 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30212 GTKALTEVIPLTC 13 P18 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50>1000 nM,associated with Pep-1);inhibition of polymerase activity of HIV-1 RT(Ki =53± 12 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30213 GTKAATEVIPLTC 13 P19 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =49 ± 9 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30214 GTKWLTEWIPLC 12 P24 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=2.3 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =0.7 ± 0.05 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30215 KWLTEWIPLTAEAEC 15 P26 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50>1000 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =1.8± 0.7 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30216 GTKWLTEWIPLTAEC 15 P27 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50<0.32 nM,associated with Pep-1); inhibition of polymerase activity of HIV-1 RT(Ki =0.05 ± 0.01 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30217 GTKWATEWAPLTAEAEC 17 P28 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =2 ± 0.6 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30218 KWLTEWIPLTAEC 13 P29 No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =1 ± 0.4 μM).##NOTE:Ki: inhibition constants No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30219 GTKWLTEWIPLTAEAEC 17 PAW No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =0.7 ± 0.2 μM);inhibition of PHA-P-activated PBMCs infected with HIV-1-LAI(EC50=1.8 nM,associated with Pep-1). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30220 GAKTETLVIPETELEAC 17 Pscr No entry found Retroviridae Not found Synthetic construct(derived from Pep-A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HIV-1 reverse transcriptase (RT) plays an essential multifunctional role in the replication of the virus, by catalyzing the synthesis of double-stranded DNA from the single strand retroviral RNA genome.The peptide could inhibit the activity of reverse transcriptase. [Ref.18952602]HIV-1:inhibition of polymerase activity of HIV-1 RT(Ki =61 ± 12 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 18952602 J Biol Chem. 2009 Jan 2;284(1):254-264. Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. DRAMP30221 LEAIPMSIPPEVKFNKPFVF 20 VIRIP No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=14.79±2.56 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30222 AEAIPMSIPPEVKFNKPFVF 20 VIRIP[A1] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30223 LAAIPMSIPPEVKFNKPFVF 20 VIRIP[A2] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30224 LEAAPMSIPPEVKFNKPFVF 20 VIRIP[A4] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30225 LEAIAMSIPPEVKFNKPFVF 20 VIRIP[A5] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=23.50±5.19 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30226 LEAIPASIPPEVKFNKPFVF 20 VIRIP[A6] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=13.00±1.04 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30227 LEAIPMSAPPEVKFNKPFVF 20 VIRIP[A8] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=23.46±0.28 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30228 LEAIPMSIAPEVKFNKPFVF 20 VIRIP[A9] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=16.33±4.34 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30229 LEAIPMSIPAEVKFNKPFVF 20 VIRIP[A10] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=9.72±1.66 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30230 LEAIPMSIPPAVKFNKPFVF 20 VIRIP[A11] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=11.00±4.75 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30231 LEAIPMSIPPEAKFNKPFVF 20 VIRIP[A12] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=10.64±2.23 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30232 LEAIPMSIPPEVAFNKPFVF 20 VIRIP[A13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=4.73±0.61 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30233 LEAIPMSIPPEVKANKPFVF 20 VIRIP[A14] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=4.62±1.32 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30234 LEAIPMSIPPEVKFAKPFVF 20 VIRIP[A15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=17.41±3.66 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30235 LEAIPMSIPPEVKFNAPFVF 20 VIRIP[A16] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=10.81±0.68 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30236 LEAIPMSIPPEVKFNKAFVF 20 VIRIP[A17] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=12.72±10.17 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30237 LEAIPMSIPPEVKFNKPAVF 20 VIRIP[A18] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30238 LEAIPMSIPPEVKFNKPFAF 20 VIRIP[A19] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30239 LEAIPMSIPPEVKFNKPFVA 20 VIRIP[A20] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30240 LEAIPMSIPPEVKFNKPFVF 20 N-Ac-VIRIP No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30241 LEAIPMSIPPEVKFNKPFVF 20 VIRIP-amide No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30242 LEAIPMSIPPEVKFNKPFVF 20 N-Ac-VIRIP-amide No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30243 LEAIPMSIPPEVAFAKPFVF 20 VIRIP[A13,A15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=3.45±0.44 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30244 LEAIPMSIPPEVFFNKPFVF 20 VIRIP[F13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.66±0.06 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30245 LEAIPMCIPPECAFNKPFVF 20 VIRIP[A13,C7,C12] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=1.00±0.21 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys7 and Cys12 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30246 LEAIPCSIPPCVAFNKPFVF 20 VIRIP[A13,C6,C11] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.18±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30247 LEAIPCSIPpCVAFNKPFVF 20 VIRIP[A13,C6,C11,p10] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.94±0.54 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30248 LEAIPCSIPPCVGFGKPFVF 20 VIRIP[C6,C11,G13,G15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.73±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30249 LEAIPCSIPPCVLFNKPFVF 20 VIRIP[C6,C11,L13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.84±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30250 LEAIPCSIPPCVFFNKPFVF 20 VIRIP[C6,C11,F13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.93±0.05 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30251 LEAIPCSIPPCFAFNKPFVF 20 VIRIP[A13,C6,C11,F12] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.27±0.04 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30252 LEAIPMSIPPEFLFGKPFVF 20 VIRIP[F12,L13,G15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=1.34±0.42 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30253 LEAIPCSIPPCVFFGKPFVF 20 VIRIP[C6,C11,F13,G15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.28±0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30254 LEAIPCSIPPCFLFGKPFVF 20 VIRIP[C6,C11,F12,L13,G15] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.39±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30255 LEAIPCSIPpCVFFNKPFVF 20 VIRIP[C6,C11,p10,F13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.33±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30256 LEAIPCSIPpCFLFNKPFVF 20 VIRIP[C6,C11,p10,F12,L13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.20±0.04 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys6 and Cys11 Mixed(D-Pro10) [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30257 LEAIPMGIPpEVXFNKPFVF 20 VIRIP[G7,p10,L-Tic13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.28±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 13 is L-tetrahydro-isoquinoline-3-carboxylic acid(Tic). Mixed(D-Pro10) [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30258 LEKIPMSIPpEVXFNKPFVF 20 VIRIP[K3,p10,L-Tic13] No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50=0.41±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 13 is L-tetrahydro-isoquinoline-3-carboxylic acid(Tic). Mixed(D-Pro10) No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30259 KVINPEPIVEPFMSKPFALF 20 scrambled VIRIP No entry found Retroviridae Not found Synthetic construct(derived from α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit HIV-1 entry by binding to the gp41 FP and preventing its insertion into the target cell membrane. [Ref.17448989]HIV-1:inhibition of virus infection in P4-CCR5 clls(IC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17448989]No cytotoxicity against P4-CCR5 cells up tp 1000 µM. membrane 17448989 Cell. 2007 Apr 20;129(2):263-75. Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. DRAMP30260 YTSLIHSLIEEGQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138G] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=1.3± 0.5 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=65± 8.8 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=141±26 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=185±68 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30261 YTSLIHSLIEEAQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138A] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.6 ± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=3.6± 1.7 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=3.5 ±0.9 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=3.2 ± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30262 YTSLIHSLIEEVQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138V] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.4 ± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=31 ± 14 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=22 ± 3.5 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=23 ± 5.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30263 YTSLIHSLIEELQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138L] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.7± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=13± 6 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=2.9 ±0.7 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=2.2± 0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30264 YTSLIHSLIEEIQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138I] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.5 ± 0.1 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=4.9± 2 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=2.9 ±0.8 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=2.4 ± 0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30265 YTSLIHSLIEEMQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138M] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.7± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=4.4± 0.1 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=1.7±0.5 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=1.2± 0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30266 YTSLIHSLIEEPQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138P] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=446± 167 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30267 YTSLIHSLIEETQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138T] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=0.9± 0.2 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=39± 8.5 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=161±35 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=124±43nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30268 YTSLIHSLIEEFQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138F] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=9.4± 2.6 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=203± 89 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50=393 ± 119 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50=478 ± 116 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30269 YTSLIHSLIEEYQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138Y] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=25 ±9nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50=516 ±223 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30270 YTSLIHSLIEEWQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138W] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=29± 14 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30271 YTSLIHSLIEENQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138N] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=19± 4 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30272 YTSLIHSLIEEQQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138Q] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=34± 11 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30273 YTSLIHSLIEEDQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138D] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=210± 94 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30274 YTSLIHSLIEEEQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138E] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=283± 80 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30275 YTSLIHSLIEEHQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138H] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=210± 85 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30276 YTSLIHSLIEEKQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138K] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=708±145 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30277 YTSLIHSLIEERQNQQEKNEQELLELDKWASLWNWF 36 T-20S[138R] No entry found Retroviridae Not found Synthetic construct(derived from Enfuvirtide) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1WT:inhibition of virus replication in HeLa cells(EC50=362± 114 nM);##HIV-1V38A:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1N43D/S138A:inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30278 WMEWDREINNYTSLIHSLIEEAQNQQEKNEQELL 34 C34S[138A] No entry found Retroviridae Not found Synthetic construct(derived from C34) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=2.0± 0.4 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=1.7± 0.3 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=2.0 ±0.6 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=1.3 ±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30279 WMEWDREINNYTSLIHSLIEELQNQQEKNEQELL 34 C34S[138L] No entry found Retroviridae Not found Synthetic construct(derived from C34) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=1.5± 0.4 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=1.2± 0.6 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=0.5 ±0.2 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=0.4±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30280 WMEWDREINNYTSLIHSLIEETQNQQEKNEQELL 34 C34S[138T] No entry found Retroviridae Not found Synthetic construct(derived from C34) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=2.6± 0.2 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=4.8± 1.3 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=32 ± 5.5 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=24 ±6.6nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30281 WMEWDREINNYTSLIHSLIEEWQNQQEKNEQELL 34 C34S[138W] No entry found Retroviridae Not found Synthetic construct(derived from C34) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50>1000 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50>1000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30282 WMEWDREINNYTSLIHSLIEEPQNQQEKNEQELL 34 C34S[138P] No entry found Retroviridae Not found Synthetic construct(derived from C34) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide prevents interactions between the C-HR and the N-terminal HR (N-HR) of gp41, thus interfering with conformational changes that are required for viral fusion. [Ref.19073606]HIV-1 NL4-3:inhibition of virus replication in HeLa cells(EC50=46±11 nM);##HIV-1(NL4-3V38A):inhibition of virus replication in HeLa cells(EC50=436± 125 nM);##HIV-1(NL4-3N43D):inhibition of virus replication in HeLa cells(EC50=250 ± 80 nM);##HIV-1(NL4-3N43D/S138A):inhibition of virus replication in HeLa cells(EC50=176±50 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 19073606 J Biol Chem. 2009 Feb 20;284(8):4914-20. Izumi K, Kodama E, Shimura K, Sakagami Y, Watanabe K, Ito S, Watabe T, Terakawa Y, Nishikawa H, Sarafianos SG, Kitaura K, Oishi S, Fujii N, Matsuoka M. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. DRAMP30283 TTWEEWDREINEYTSRIESLIRESQEQQEKNEQELREL 38 2429 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion. [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.012 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.021μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.056 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.037 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.167 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK. Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus. DRAMP30284 MTWMAWDRAIANYAALIHALIEAAQNQQEKNEAALLEL 38 2638 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion. [Ref.17640899]HIV IIIB:inhibition of virus infection on CEM4 cells(IC50=0.061 μg/ml);##HIV 098:inhibition of virus infection on CEM4 cells(IC50=0.079μg/ml);##HIV 098-T20:inhibition of virus infection on CEM4 cells(IC50=0.079 μg/ml);##HIV 098-T1249:inhibition of virus infection on CEM4 cells(IC50=0.120 μg/ml);##HIV 098-T651:inhibition of virus infection on CEM4 cells(IC50=0.250 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 17640899 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7.  Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, Wring SA, Tvermoes NA, Matthews TJ, Greenberg ML, Delmedico MK. Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus. DRAMP30285 AEAMSQVTN 9 p2(gag) peptide[Δ10-14] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=5 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30286 AAAMSQVTN 9 p2(gag) peptide[Δ10-14,E2A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=100 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30287 AEAMAQVTN 9 p2(gag) peptide[Δ10-14,S5A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=124 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30288 AEAMSQVTNTATIM 14 p2(gag) peptide No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=10 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30289 AEAASQVTNTATIM 14 p2(gag) peptide[M4A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=142 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30290 AEASQVTNTATIM 13 p2(gag) peptide[ΔM4] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=126 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30291 AEAMSQVANTATIM 14 p2(gag) peptide[T8A] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks the autolysis of HIV-1 virions for the conservation of viral species. [Ref.15113844]HIV:inhibition of protease activity in CEM/LAV-1 cells(IC50=110 μM). Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15113844 J Biochem. 2004 Mar;135(3):447-53.  Misumi S, Morikawa Y, Tomonaga M, Ohkuma K, Takamune N, Shoji S. Blocking of human immunodeficiency virus type-1 virion autolysis by autologous p2(gag) peptide.  DRAMP30292 KIPCGESCVWIPCVTSIFNCKCENKVCYHD 30 Circulin-D (CIRD; Plant defensin) P84642 Retroviridae Not found Chassalia parviflora Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 18008336 Biopolymers. 2008;90(1):51-60. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cyclotides as natural anti-HIV agents. DRAMP30293 AIPCGESCVWIPCISAAIGCSCKNKVCYR 29 Circulin-F (CIRF; Plant defensin) P84644 Retroviridae Not found Chassalia parviflora Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18008336]HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=50-275 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20, Cys8 and Cys22,Cys13 and Cys27. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 18008336 Biopolymers. 2008;90(1):51-60. Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. Cyclotides as natural anti-HIV agents. DRAMP30294 CGESCAXISFCFTEVIGCSCKNKVCYLNSIS 31 Leaf cyclotide, Vhl-1 P84522 Retroviridae Not found Viola hederacea Antimicrobial, Antiviral Not found Not found Not found 1ZA8 Comment: No comments found on DRAMP database [Ref.15824119]HIV-1:inhibition of cytopathic effect(EC50=0.87 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 7 indicates Methionine sulfoxide. The N-terminal and C-terminal cyclized by a amide bond. Disulfide bonds between Cys1 and Cys18, Cys5 and Cys20, Cys11 and Cys25. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15824119 J Biol Chem. 2005 Jun 10;280(23):22395-405. Chen B, Colgrave ML, Daly NL, Rosengren KJ, Gustafson KR, Craik DJ.  Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide. DRAMP30295 VFQFLGRIIAnti-HHVGNFVHGFSHVF 23 Clavanin-B (His-rich; chordates, animals) P80711 Retroviridae Not found Styela clava (Sea squirt) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=7.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20086159]CEM-SS cells:50% Cell death at 37.1 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30296 GLWEKIDKFASII 13 B2(derived from Caerin 3.2) No entry found Retroviridae Not found Synthetic construct(derived from Caerin 3.2) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>65.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30297 GIIDIAKKLFESW 13 B3(derived from Uperin 2.7) No entry found Retroviridae Not found Synthetic construct(derived from Uperin 2.7) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=20.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30298 GWFDIIKKIASEL 13 B4(derived from Uperin 7.1) No entry found Retroviridae Not found Synthetic construct(derived from Uperin 7.1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=10.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:50% Cell death at 38.9 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30299 GIFDKLAKEISIW 13 B5(derived from Brevinin-2DYd) No entry found Retroviridae Not found Synthetic construct(derived from Brevinin-2DYd) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>65.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30300 GIWSDLAEIIKKF 13 B6(derived from Ponericin W3) No entry found Retroviridae Not found Synthetic construct(derived from Ponericin W3) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=11.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30301 GFLDIIEKIAKSW 13 B7(derived from Ranatuerin 3) No entry found Retroviridae Not found Synthetic construct(derived from Ranatuerin 3) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=10.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30302 GWLKKIESIIDAF 13 B8(derived from Cecropin) No entry found Retroviridae Not found Synthetic construct(derived from Cecropin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=29.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >65.8 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30303 ILGPVLGLVSRTLRRVLGIL 20 Maximin H5r3 No entry found Retroviridae Not found Synthetic construct(derived from Maximin H5) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=2.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20086159]CEM-SS cells:50% Cell death at 8.7 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30304 GFNEIVQDIEDFLQNLV 17 GF-17− No entry found Retroviridae Not found Synthetic construct(derived from LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50>25.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >25.1 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30305 GLRSRIWLWVLLMIWQESNRFKRM 24 DRS S9r3 No entry found Retroviridae Not found Synthetic construct(derived from Dermaseptin S9) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20086159]CEM-SS cells:TC50(cause 50% Cell death) >32.1 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30306 GLRRLLGRLLRRLGRLLLR 19 GLR-19 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20086159]HIV-1 IIIB:inhibition the cytopathic effects of HIV-1 infection in CEM-SS cells(EC50=4.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20086159]CEM-SS cells:50% Cell death at 25.7 µM. Not found 20086159 Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. DRAMP30307 GLLSVLGSVAKHVLPHVVPVIAAAL 25 Caerin 1.1 mod 7(Caerin 1.1 [E23A,H24A]) No entry found Retroviridae Not found Sythetic construct(derived from Caerin 1.1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented virion envelope 26026377##33008028 Peptides. 2015 Sep;71:296-303. ##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK. DRAMP30308 GLLSVLGSVAKHVLPHVVPVIAKLH 25 Caerin 1.1 mod 9(Caerin 1.1 [E23K,H24L,L25H]) No entry found Retroviridae Not found Sythetic construct(derived from Caerin 1.1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 17 µM." virion envelope 26026377 Peptides. 2015 Sep;71:296-303. Inhibition of HIV infection by caerin 1 antimicrobial peptides. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA. DRAMP30309 GLLKVLGSVAKKVLPKVVPVIAEKL 25 Caerin 1.1 mod 10(Caerin 1.1 [S4K;H12K,H16K,H24K]) No entry found Retroviridae Not found Sythetic construct(derived from Caerin 1.1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=4 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented virion envelope 26026377 Peptides. 2015 Sep;71:296-303. Inhibition of HIV infection by caerin 1 antimicrobial peptides. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA. DRAMP30310 GLFGVLGSIAKHLLPHVVPVIAEKL 25 Caerin 1.9 sm(Caerin 1.9 [V13L]) No entry found Retroviridae Not found Sythetic construct(derived from Caerin 1.9) Antimicrobial, Antiviral Not found Not found Not found Mechanism: [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.26026377]CD4+ T Lymphocytes:50% cell death at 17.5 µM. virion envelope 26026377##33008028 Peptides. 2015 Sep;71:296-303. ##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK. DRAMP30311 GLFGILGSVAKHVLPHVIPVVAEHL 25 Caerin 1.20 No entry found Retroviridae Not found Litoria caerulea/Litoria splendida Antimicrobial, Antiviral Not found Not found Not found Mechanism: [Ref.26026377]Inhibit the infection of HIV by disrupting the HIV envelope and release viral core protein (p24). [Ref.26026377]Human immunodeficiency virus (HIV): inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L "[Ref.26026377]CD4+ T Lymphocytes:50% cell death at 25 µM;Human endocervical cells End1/E6E7:50% cell death at 22 µM." virion envelope 26026377##33008028 Peptides. 2015 Sep;71:296-303.##Antibiotics (Basel). 2020 Sep 30;9(10):661. Inhibition of HIV infection by caerin 1 antimicrobial peptides.##Caerin 1 Antimicrobial Peptides That Inhibit HIV and Neisseria May Spare Protective Lactobacilli. VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.##Rollins-Smith LA, Smith PB, Ledeczi AM, Rowe JM, Reinert LK. DRAMP30312 GLMDTVKNVAKNLAGHMLDKLKCKITGC 28 Ranatuerin-2P (Ranatuerin 2P; Frogs, amphibians, animals) Q8QFQ4##P82847 Iridoviridae, Herpesviridae Not found Rana pipiens (Northern leopard frog) Antimicrobial, Antiviral Not found Not found Not found 2K10 Comment: No comments found on DRAMP database [Ref.11601906]Frog Virus 3(FV3): inhibition of FV3 infection in fathead minnow(FHM) cells(90% inhibition at 500 µM);##Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells(99% inhibition at 50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys22 and Cys27. L No cytotoxicity information found in the reference(s) presented Not found 11601906 Virology. 2001 Sep 30;288(2):351-7. Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. DRAMP30313 GFLSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC 37 Esculentin-2P (Frogs, amphibians, animals) P82846 Iridoviridae, Herpesviridae Not found Rana pipiens (northern leopard frog) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11601906]##Frog Virus 3: inhibition of FV3 infection in fathead minnow(FHM) cells(90% inhibition at 500 µM);##Channel Catfish virus(CCV): inhibition of CCV infection in catfish ovary(CCO) cells( 90% inhibition at 50 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization of a C-terminal Cys residue (forming a disulfide bond) There is a disulfide bond between Cys31 and Cys37. L No cytotoxicity information found in the reference(s) presented Not found 11601906 Virology. 2001 Sep 30;288(2):351-7.##Eur J Biochem. 2000 Feb;267(3):894-900. Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. DRAMP30314 FVPWFSKFlGRIL 13 Temporin L[Pro3,DLeu9](TL1) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=9.99 μM,IC90=18.69 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=8.86 μM μM,IC90=16.71 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.62 μM μM,IC90=12.14 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=7.76 μM,IC90=30.07 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=7.33 μM,IC90=14.98 μM). [Ref.35216177]showing residual hemolytic activity against human erythrocytes only at concentrations equal or above 50 μM. Linear Free Amidation Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50= 42.18 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30315 FVPWFSKFlPRIL 13 Temporin L[Pro3,DLeu9,Pro10](TL2) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=7.70 μM,IC90=18.76 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=9.83 μM μM,IC90=19.20 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.82 μM μM,IC90=13.98 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=10.56 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=11.31 μM,IC90=24.13 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50= 56.52 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30316 FVPWFSKFlpRIL 13 Temporin L[Pro3,DLeu9,DPro10](TL3) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9,D-Pro10) [Ref.35216177]Vero cells:CC50>100 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30317 FVPWFSKFlXRIL 13 Temporin L[Pro3,DLeu9,Hyp10](TL4) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=7.73 μM,IC90=15.89 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=9.61 μM μM,IC90=19.02 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=6.72 μM μM,IC90=25.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=11.74 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=11.33 μM,IC90=27.65 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation The 'X' at position 10 is hydroxyproline (Hyp). Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50=60.90 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30318 FVPWFSKFlxRIL 13 Temporin L[Pro3,DLeu9,DHyp10](TL5) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation The 'x' at position 10 is D-hydroxyproline (Hyp). Mixed(D-Leu9,D-Hyp10) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30319 FVPWFSKFlxRIL 13 Temporin L[Pro3,DLeu9,DNle10](TL7) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.65 μM,IC90=12.83 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=3.13 μM μM,IC90=11.92 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=1.00 μM μM,IC90=17.41 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=6.21 μM,IC90>50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=8.55 μM,IC90=24.74 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation The 'x' at position 10 is D-norleucine. Mixed(D-Leu9,D-Nle10) [Ref.35216177]Vero cells:CC50= 32.16 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30320 FVPWFSKFlKRIL 13 Temporin L[Pro3,DLeu9,Lys10](TL8) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.49 μM,IC90=10.48 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=1.00 μM μM,IC90=7.99 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.88 μM μM,IC90=12.93 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=40.69 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=4.39 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=2.90 μM,IC90=16.30 μM). [Ref.35216177]About 20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50=22.32 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30321 FVPWFSKFlkRIL 13 Temporin L[Pro3,DLeu9,DLys10](TL9) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.53 μM,IC90=12.71 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=2.80 μM μM,IC90=12.50 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.63 μM μM,IC90=25.33 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=40.64 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=5.39 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=8.29 μM,IC90=29.17 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9,D-Lys10) [Ref.35216177]Vero cells:CC50= 45.92 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30322 FVPWFSKFlWRIL 13 Temporin L[Pro3,DLeu9,Trp10](TL10) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.01 μM,IC90=8.25 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.77 μM μM,IC90=12.50 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.88 μM μM,IC90=27.71 μM);##HPIV-3:inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.91 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.96 μM,IC90=24.17 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50= 35.47 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30323 FVPWFSKFlwRIL 13 Temporin L[Pro3,DLeu9,DTrp10](TL11) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=1.86 μM,IC90=7.89 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.58 μM μM,IC90=9.76 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=4.07 μM μM,IC90=14.85 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=41.18 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.92 μM,IC90=50.00 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=5.10 μM,IC90=17.41 μM). [Ref.35216177]<40% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation Mixed(D-Leu9,D-Trp10) [Ref.35216177]Vero cells:CC50=24.12 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30324 FVPWFSKFlXRIL 13 Temporin L[Pro3,DLeu9,Aic10](TL12) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=0.68 μM,IC90=1.58 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.54 μM μM,IC90=11.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.65 μM μM,IC90=13.85 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=33.83 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=0.74 μM,IC90=20.90 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.62 μM,IC90=13.18 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 12.5 μM. Linear Free Amidation The 'X' at position 10 is 2-aminoindane-2-carboxylic acid. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50=8.28 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30325 FVPWFSKFlXRIL 13 Temporin L[Pro3,DLeu9,Nle10](TL6) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.66 μM,IC90=9.12 μM);##HSV-2:inhibition of HSV-2 replication in Vero cells(IC50=0.92 μM μM,IC90=6.28 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.53 μM μM,IC90=12.15 μM);##HPIV-3:inhibition of replication in Vero cells(IC50=32.35 μM,IC90>50.00 μM);##HCoV-229E:inhibition of replication in Vero cells(IC50=2.08 μM,IC90=13.06 μM);##HCoV-OC43:inhibition of replication in Vero cells(IC50=0.97 μM,IC90=10.04 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=34.58 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=2.66 μM,IC90=9.12 μM). [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM. Linear Free Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50=64.52 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30326 FVPWFSKFlXRILC 14 Temporin L[Pro3,DLeu9,Nle10]-C-CHOL(TL6.1) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=6.4 μM,IC90=11.13 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=3.18 μM μM,IC90=12.03 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=39.1 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=5.55 μM,IC90=10.02 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-Cholesterol-NH2 The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30327 FVPWFSKFlXRILGGC 16 Temporin L[Pro3,DLeu9,Nle10]-GGC-CHOL(TL6.2) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=9.54 μM,IC90=47.95 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=12.12 μM μM,IC90=49.95 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=40.89 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=21.12 μM,IC90=49.90 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free PEG4-Cholesterol-NH2 The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30328 CFVPWFSKFlXRIL 14 CHOL-C-Temporin L[Pro3,DLeu9,Nle10](TL6.3) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=0.89 μM,IC90=2.19 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.76 μM μM,IC90=1.89 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=22.3 μM μM,IC90=31.10 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=2.55 μM,IC90=5.89 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Cholesterol-PEG4 Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30329 CGGFVPWFSKFlXRIL 16 CHOL-CGG-Temporin L[Pro3,DLeu9,Nle10](TL6.4) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.32 μM,IC90=8.21 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=1.02 μM μM,IC90=10.21 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=28.88 μM μM,IC90=49.90 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=6.02 μM,IC90=9.90 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Cholesterol-PEG4 Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30330 FVPWFSKFlXRIL 13 Undecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.5) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50<0.10 μM,IC90<0.10 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50<0.10 μM μM,IC90<0.10 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=10.01 μM μM,IC90=29.18 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50<0.10 μM,IC90<0.10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Undecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30331 FVPWFSKFlXRIL 13 Tridecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.6) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=1.39 μM,IC90=2.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.39 μM μM,IC90=5.86 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=33.36 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=3.39 μM,IC90=6.66 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Tridecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30332 FVPWFSKFlXRIL 13 Pentadecanoic-Temporin L[Pro3,DLeu9,Nle10](TL6.7) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=2.48 μM,IC90=4.86 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.48 μM μM,IC90=7.86 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=37.77 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=3.48 μM,IC90=7.10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Pentadecanoic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30333 FVPWFSKFlXRIL 13 Hexadecenoic-Temporin L[Pro3,DLeu9,Nle10](TL6.8) No entry found Coronaviridae, Herpesviridae, Paramyxoviridae, Orthomyxoviridae Not found Synthetic construct(derived from Temporin-L) Antimicrobial, Antiviral Not found Not found Not found Mechanism: TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction. [Ref.35216177]HSV-1:inhibition of HSV-1 replication in Vero cells(IC50=3.13 μM,IC90=4.96 μM);##SARS-CoV-2:inhibition of replication in Vero cells(IC50=0.77 μM μM,IC90=6.96 μM);##Measles virus(MeV):inhibition of MeV replication in VERO/hSLAM cells(IC50=39.4 μM μM,IC90>50.00 μM);##influenza virus(H1N1,VR-1894):inhibition of replication in MDKC cells(IC50=4.77 μM,IC90=7.11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Palmitic acid Amidation The 'X' at position 10 is norleucine. Mixed(D-Leu9) [Ref.35216177]Vero cells:CC50>100.00 μM membrane 35216177 Int J Mol Sci. 2022 Feb 13;23(4):2060. Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.  Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. DRAMP30334 TLLKKVLKAAAKAALNAVLVGANA 24 Dermaseptin S4 (5-28) No entry found Herpesviridae Not found Synthetic construct(derived from Dermaseptin S4) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=27.07 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=25.27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23161023]Vero cells:CC50=34 μM. Not found 23161023 J Med Virol. 2013 Feb;85(2):272-81. Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K.   In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. DRAMP30335 ALWKTLLKKVLKAAAKAALNAVLVGANA 28 Dermaseptin K4S4 No entry found Herpesviridae Not found Synthetic construct(derived from Dermaseptin S4) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=2.7 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=5.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23161023]Vero cells:CC50=12 μM. Not found 23161023 J Med Virol. 2013 Feb;85(2):272-81. Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K.   In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. DRAMP30336 ALWKTLLKKVLKAAAKAALKAVLVGANA 28 Dermaseptin K4K20S4 No entry found Herpesviridae Not found Synthetic construct(derived from Dermaseptin S4) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=2.1 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=5.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23161023]Vero cells:CC50=25 μM. Not found 23161023 J Med Virol. 2013 Feb;85(2):272-81. Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K.   In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. DRAMP30337 ALWDTLLKKVLKAAAKAALDAVLVGANA 28 Dermaseptin D4D20S4 No entry found Herpesviridae Not found Synthetic construct(derived from Dermaseptin S4) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.23161023]HSV-2 acyclovir-sensitive strain(911411):inhibition the cytopathic effect(CPE) of HSV-2 in Vero cells(EC50=5.41 μM);##HSV-2 acyclovir-resistant strain(ROI2):inhibition of cytopathic effet(CPE) of HSV-2 in Vero cells(EC50=9.63 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23161023]Vero cells:CC50=17.75 μM. Not found 23161023 J Med Virol. 2013 Feb;85(2):272-81. Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K.   In vitro antiviral activity of dermaseptin S(4) and derivatives from amphibian skin against herpes simplex virus type 2. DRAMP30338 RLFFKCIYRFFEHGLKRG 18 M2 AH No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza virus M2 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: M2 AH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 AH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission. [Ref.31375212]H1N1(A/Puerto Rico/8/34):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=870 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31375212]Madin-Darby canine kidney epithelial(MDCK) cells:CC50=70.3 μM membrane 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH.  Envelope-deforming antiviral peptide derived from influenza virus M2 protein. DRAMP30339 RKFFKKIYRFFRKLLKRL 18 M2 MH No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza virus M2 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: M2 MH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 MH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission. [Ref.31375212]H1N1(A/Puerto Rico/8/34):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=53 nM);##H3N2(A/Sydney/5/97):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.058 μM);##H3N2(A/X31):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.016 μM);##H5N2(A/aquatic bird/Korea/w81/2005 ):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.066 μM);##H1N1(A/Swine/Iowa/15/30):inhibition of infection in Madin-Darby canine kidney epithelial(MDCK) cells(IC50=0.053 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31375212]Madin-Darby canine kidney epithelial(MDCK) cells:CC50=19.2 μM membrane 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH.  Envelope-deforming antiviral peptide derived from influenza virus M2 protein. DRAMP30340 RLAAKCAARFAEHGLKRG 18 M2 NH No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza virus M2 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: M2 NH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 NH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission. [Ref.31375212]H1N1:did not exhibit any inhibitory effect. No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31375212]did not show apparent cytotoxicity against Madin-Darby canine kidney epithelial(MDCK) cells up to a concentration of 100 μM. membrane 31375212 Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512. Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH.  Envelope-deforming antiviral peptide derived from influenza virus M2 protein. DRAMP30341 GFSSLFKAGAKYLLKQVGKAGAQQLACKAANNC 33 Brevinin-2GHk(BR2GK) A0A6G6CZ26 Flaviviridae Not found Fejervarya limnocharis Antimicrobial, Antiviral Not found Not found Not found Mechanism: BR2GK directly inactivated ZIKV by disrupting the integrity of the envelope and may also penetrate the host cell membrane to inhibit the middle stage of ZIKV infection. [Ref.34960651]Zika Virus: inhibition of infection of Zika virus in Vero cells(IC50=3.408 ± 0.738 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.34960651]exhibited no significant toxicity to Vero, Hela, and Huh7 cells in the concentration range 0-20 µM. membrane 34960651 Viruses. 2021 Nov 28;13(12):2382.  Xiong W, Li J, Feng Y, Chai J, Wu J, Hu Y, Tian M, Lu W, Xu X, Zou M. Brevinin-2GHk, a Peptide Derived from the Skin of Fejervarya limnocharis, Inhibits Zika Virus Infection by Disrupting Viral Integrity. DRAMP30342 FLPLILPAnti-SIVTALSSFLKQG 20 Hs-1 No entry found Flaviviridae Not found Hypsiboas semilineatus Antimicrobial, Antiviral Not found Not found Not found Mechanism: It was possible to observe that the viral particle lost its ability to infect because of the breakdown on the envelope as the peptide acted directly on the virus. [Ref.29153860]DENV2:reduced the number of lysis plaques by 100% at 125 µg/mL; by 60% at 7.81 μg/mL;##DENV3:reduced the number of lysis plaques by 100% at 125 µg/mL; by 50% at 7.81 μg/mL No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.29153860]No significant cytotoxicity agaisnt Vero cells up to 125μg/ mL. envelope 29153860 Virology. 2018 Jan 15;514:79-87. Monteiro JMC, Oliveira MD, Dias RS, Nacif-Marçal L, Feio RN, Ferreira SO, Oliveira LL, Silva CC, Paula SO. The antimicrobial peptide HS-1 inhibits dengue virus infection. DRAMP30343 GGARDAGKAEWW 12 gg-ww No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide gg-ww could exert its inhibition during the viral entry step of DENV-2 infection by interfering with viral attachment or internalization. [Ref.26248692]dengue virus serotype 2(DENV-2):inhibition the cytopathic effect(CPE) and plaque formation in Vero cells(IC50=77-91 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.26248692]It was not toxic to Vero cells up to 400 μmol/L. membrane 26248692 J Appl Microbiol. 2015 Oct;119(4):1170-80.  Chew MF, Tham HW, Rajik M, Sharifah SH.  Anti-dengue virus serotype 2 activity and mode of action of a novel peptide. DRAMP30344 QEGISRFKICPYHWYKQHMSLLFRRYYHKLDSII 34 CPXV012 No entry found Herpesviridae, Hepadnaviridae, Retroviridae, Phenuiviridae Not found Synthetic construct(derived from the cowpox virus protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Within virus-infected cells, this protein helps to evade the immune system by inhibiting the transporter associated with antigen processing (TAP), thereby interfering with MHC I-dependent antigen presentation. And the peptide is the segment of the CPXV012 protein responsible for blocking TAP. [Ref.32872420]Herpes simplex virus-1(HSV-1):inhibition of HSV-1 infection in MelJuSo(MJS) cells(75.9 ± 5.7% inhibition at 150 µg/mL);##Hepatitis B virus(HBV): decrease of HBeAg and viral DNA infected with HBV-1 in HepRG cells(84.0 ± 3.0% of HBeAg and 73.6 ± 2.3% of viral DNA at 100 µg/mL);##HIV-1:inhibition of virus infection in LC5-RIC reporter cells(82.7 ± 4.9% inhibition at 100 µg/mL);inhibition of virus replication in LC5-RIC reporter cells(62.2 ± 2.4% inhibition at 100 µg/mL);##Rift Valley fever virus(RVFV): inhibition of virus infection in MJS cells(65.5 ± 2.3% inhibition at 160 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32872420]Did not observe any decrease in live cells against Vero and Huh7.5 cells up to 200 µg/mL. envelope(phosphatidylserine) 32872420 Cells. 2020 Aug 29;9(9):1989. Luteijn RD, Praest P, Thiele F, Sadasivam SM, Singethan K, Drijfhout JW, Bach C, de Boer SM, Lebbink RJ, Tao S, Helfer M, Bach NC, Protzer U, Costa AI, Killian JA, Drexler I, Wiertz EJHJ. A Broad-Spectrum Antiviral Peptide Blocks Infection of Viruses by Binding to Phosphatidylserine in the Viral Envelope.  DRAMP30345 TEPSTRGSWKFW 12 P1 No entry found Flaviviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E glycoprotein has been identified as the major antigenic determinant on flavivirus particles and mediates binding and fusion during viral entry,DIII has been proposed to act as the binding region for the cellular receptor. And the peptide could bingding with DIII domain and inhibit the initial step of JEV infection. [Ref.24468276]Japanese encephalitis virus (JEV): inhibition of JEV infection in BHK-21 cells(IC50~100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 24468276 Antiviral Res. 2014 Apr;104:7-14. Zu X, Liu Y, Wang S, Jin R, Zhou Z, Liu H, Gong R, Xiao G, Wang W. Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. DRAMP30346 SENRKVPFYSHS 12 P3 No entry found Flaviviridae Not found Synthetic construct(phage display) Antimicrobial, Antiviral Not found Not found Not found Mechanism: E glycoprotein has been identified as the major antigenic determinant on flavivirus particles and mediates binding and fusion during viral entry,DIII has been proposed to act as the binding region for the cellular receptor. And the peptide could bingding with DIII domain and inhibit the initial step of JEV infection. [Ref.24468276]Japanese encephalitis virus (JEV): inhibition of JEV infection in BHK-21 cells(IC50=1.42 ± 0.41 μM determined by plaque assay,IC50=1.12 ± 0.38 μM determined by qRT-PCR,IC90~100 μM determined by plaque assay and qRT-PCR). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 24468276 Antiviral Res. 2014 Apr;104:7-14. Zu X, Liu Y, Wang S, Jin R, Zhou Z, Liu H, Gong R, Xiao G, Wang W. Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. DRAMP30347 MVDRGWGNHAGLFGKGAnti-SIV 19 DN80 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of DENV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(17±10% inhibition at 49.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30348 AWLVHTQWFLDLPLPWLPGADTQGSNWI 28 DN57 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of DENV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(7±4% inhibition at 30.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30349 AWLVHRQWFLDLPLPWLPG 19 DN81 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of DENV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(25±8% inhibition at 42.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30350 MAILGDTAWDFGSLGGVFTSIGKALHQVFGAIY 33 DN59 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of DENV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]Dengue virus(DENV): inhibition of DENV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM,100.0±0.5% inhibition at 20 μM);##West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(>99% inhibition at <25μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30351 VVDRGWGNGAGLFGKGSID 19 WN82 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of WNV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(4±13% inhibition at 52.5μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30352 TFLVHREWFMDLNLPWSSAGSTVWR 25 WN53 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of WNV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM,56.0±3.0% inhibition at 99μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30353 TFLVHREWFMDLNLPWSSA 19 WN83 No entry found Flaviviridae Not found Synthetic construct(derived from the E polyprotein of WNV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may play roles in protein-protein rearrangements or bilayer membrane interactions during the entry and fusion process and thus inhibit infection of DENV or WNV. [Ref.31351847]West Nile virus(WNV): inhibition of WNV infection in LLCKM-2 monkey kidney epithelial cells(IC50~10μM, 70.0±3.0% inhibition at 128 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31351847]No cytotoxicity against LLCMK-2 monkey kidney epithelial cells at 100 mg/ml. envelope 31351847 Bioorg Med Chem. 2019 Sep 15;27(18):3963-3978.  da Silva-Júnior EF, de Araújo-Júnior JX.  Peptide derivatives as inhibitors of NS2B-NS3 protease from Dengue, West Nile, and Zika flaviviruses. DRAMP30354 GYIEAEVI 8 HIV-1 integrase(82-89) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1 mM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30355 QETAYFLLKLAGRWP 15 HIV-1 integrase(95-109) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30356 STTVKAASWWA 11 HIV-1 integrase(123-133) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>1 mM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30357 HLKTAVQMAVFIHNFKR 17 HIV-1 integrase(171-187) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=3.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30358 AGERIVDIIATDIQ 14 HIV-1 integrase(196-210) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=2.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30359 QETAYFLLKLAGR 13 HIV-1 integrase(95-107) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30360 AGERIVDIIA 10 HIV-1 integrase(196-206) P04587 Retroviridae Not found Synthetic construct(derived from HIV-1 integrase) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit the activity of integrase and thus inhibit virus repliaction. [Ref.12643937]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=30 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented Integrase 12643937 Bioorg Med Chem Lett. 2003 Mar 24;13(6):1175-7. Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization.  DRAMP30361 WNSLKIDNLDV 11 LEDGF 361–370 O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(81% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30362 WASLKIDNLDV 11 LEDGF 361–370[N361A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(76% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30363 WNALKIDNLDV 11 LEDGF 361–370[S362A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(79% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30364 WNSAKIDNLDV 11 LEDGF 361–370[L363A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(71% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30365 WNSLAIDNLDV 11 LEDGF 361–370[K364A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(68% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30366 WNSLKADNLDV 11 LEDGF 361–370[I365A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(65% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30367 WNSLKIANLDV 11 LEDGF 361–370[D366A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(58% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30368 WNSLKIDALDV 11 LEDGF 361–370[N367A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(75% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30369 WNSLKIDNADV 11 LEDGF 361–370[L368A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(75% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30370 WNSLKIDNLAV 11 LEDGF 361–370[D369A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(73% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30371 WNSLKIDNLDA 11 LEDGF 361–370[V370A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(68% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30372 WNSLKIANLAV 11 LEDGF 361–370[D366A,D369A] O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(43% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30373 WIDNLD 6 LEDGF 365–369 O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(30% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30374 WKFALKVDSPDV 12 HRP2 483–493 Q7Z4V5 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the catalytic activity of integrase and thus inhibits integration of viral cDNA. [Ref.20171172]HIV-1:inhibition of integrase catalytic activity(25% inhibition at 100nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Integrase 20171172 Biochem Biophys Res Commun. 2010 Apr 2;394(2):260-5.  Hayouka Z, Levin A, Maes M, Hadas E, Shalev DE, Volsky DJ, Loyter A, Friedler A. Mechanism of action of the HIV-1 integrase inhibitory peptide LEDGF 361-370. DRAMP30375 WEEWDKKIEEYTKKIEELIKKSQNQQ 26 WQ(628-653) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=123.4 ±6.5 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=159.5 ± 9.5 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=126.2 ± 9.2 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=81.2-383.3 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=13.5-686.2 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=34.8-433.1 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=195.1-1128.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30376 MTWEEWDKKIEEYTKKIEELIKKSQNQQ 28 MT-WQ(626-653) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=8.8 ±0.4 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=14.8 ± 2.8 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=6.7 ± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30377 WEEWDKKIEEYTKKIEELIKKSQNQQSM 28 WQ-SM(628-655) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=60.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30378 WEEWDKKIEEYTKKIEELIKKSQNQQSW 28 WQ-SW(628-655) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=47.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30379 WEEWDKKIEEYTKKIEELIKKSQNQQSY 28 WQ-SY(628-655) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=54.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30380 WEEWDKKIEEYTKKIEELIKKSQNQQSDLD 30 WQ-SDLD(628-657) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=44.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30381 WEEWDKKIEEYTKKIEELIKKSQNQQLDL 29 WQ-LDL(628-656) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.7 ±1.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=6.4 ±2.7 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.6± 0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30382 WEEWDKKIEEYTKKIEELIKKSQNQQIDI 29 WQ-IDI(628-656) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.7 ±0.3 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=6.4 ± 1.8 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.2 ± 0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30383 WEEWDKKIEEYTKKIEELIKKSQNQQLDI 29 WQ-LDI(628-656) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=3.6±0.2nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=7.2 ± 1.0 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=3.1 ± 0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30384 WEEWDKKIEEYTKKIEELIKKSQNQQIDL 29 WQ-IDL(628-656) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=1.6 ±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=5.6± 1.2 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=2.5 ± 0.1 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=2.0-90.7 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.8-37.4 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=1.6-22.0 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=8.5-61.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30385 MTWEEWDKKIEEYTKKIEELIKKSQNQQIDL 31 MT-WQ-IDL(626-656) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=0.6±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=1.2± 0.2 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=0.6 ±0.1 nM);##HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=0.5-15.1 nM);##HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.1-9.0 nM);##HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=0.1-4.4 nM);##HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=1.1-11.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30386 EEQKTQLKNKIEIDWTKMELEQDWSKIYKEI 31 MT-WQ-IDL-scrambled P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]HIV-1 IIIB:inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50>500 nM);##HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50>500 nM);## No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30387 TTLLDLTYEMLSLQQVVKALNESYIDLKEL 30 M0 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=4.5 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=17.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30388 EANTTLLDLTYEMLSLQQVVKALNESYIDLKEL 33 M1 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=0.9 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=2.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 27795416 J Virol. 2016 Dec 16;91(1):e01445-16. Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.  Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. DRAMP30389 LQQLLFIHFRIGRRRRRRRR 20 peptide 4 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30390 EAIIRILQQLLFIHFRIGRRRRRRRR 26 peptide 5 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.09 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.04 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30391 ILQQLLFIHFRIGRRRRRRRR 21 peptide 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.10 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30392 RILQQLLFIHFRIGRRRRRRRR 22 peptide 7 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.11 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30393 IRILQQLLFIHFRIGRRRRRRRR 23 peptide 8 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.26 ±0.04 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.11 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30394 IIRILQQLLFIHFRIGRRRRRRRR 24 peptide 9 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.11 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30395 AIIRILQQLLFIHFRIGRRRRRRRR 25 peptide 10 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.08 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.05 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30396 EAIIRILQQLLFIEFRIKRRRRRRRR 26 peptide 11 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.05± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.01 ± 0.001 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30397 EEIIRKLQQLLFIHFRIGRRRRRRRR 26 peptide 12 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.047 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30398 EAIIRILQELLFKHFRIGRRRRRRRR 26 peptide 13 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.14 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.065 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30399 EAIERILKQLLFIHFRIGRRRRRRRR 26 peptide 14 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.23± 0.03 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.15 ± 0.002 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30400 EAEIRIKQQLLFIHFRIGRRRRRRRR 26 peptide 15 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.04 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.031± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30401 EAIIRILQQLEFIHKRIGRRRRRRRR 26 peptide 16 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.71 ± 0.21 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.004µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30402 EEIIRKLQQLLFIEFRIKRRRRRRRR 26 peptide 17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.18 ± 0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.08 ± 0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30403 AQQLLFIHFRIGRRRRRRRR 20 peptide 18 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.004 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.08 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30404 LAQLLFIHFRIGRRRRRRRR 20 peptide 19 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30405 LQALLFIHFRIGRRRRRRRR 20 peptide 20 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.10 ± 0.004 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30406 LQQALFIHFRIGRRRRRRRR 20 peptide 21 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.12 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.07 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30407 LQQLAFIHFRIGRRRRRRRR 20 peptide 22 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.003 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30408 LQQLLAIHFRIGRRRRRRRR 20 peptide 23 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.34 ± 0.06 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.18 ± 0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30409 LQQLLFAHFRIGRRRRRRRR 20 peptide 24 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.33 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.22± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30410 LQQLLFIAFRIGRRRRRRRR 20 peptide 25 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.13 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.06 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30411 LQQLLFIHARIGRRRRRRRR 20 peptide 26 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.25 ± 0.02 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.12± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30412 LQQLLFIHFAIGRRRRRRRR 20 peptide 27 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.11 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.05 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30413 LQQLLFIHFRAGRRRRRRRR 20 peptide 28 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.20 ± 0.03 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.16 ± 0.02µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30414 LQQLLFIHFRIARRRRRRRR 20 peptide 29 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts antiviral activity by inhibiting the activity of integrase. [Ref.20708407]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=0.09 ± 0.01 µM);inhibition of strand transfer catalyzed by integrase(IC50=0.09 ± 0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 20708407 Bioorg Med Chem. 2010 Sep 15;18(18):6771-5. Suzuki S, Maddali K, Hashimoto C, Urano E, Ohashi N, Tanaka T, Ozaki T, Arai H, Tsutsumi H, Narumi T, Nomura W, Yamamoto N, Pommier Y, Komano JA, Tamamura H. Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies. DRAMP30415 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C8- N27 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry. [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=1075±90 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=293±27 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear C8(octanoic acid) Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20605950 FASEB J. 2010 Nov;24(11):4196-202.  Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  DRAMP30416 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C12- N27 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry. [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=473±74 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=182±15 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear C12(dodecanoic acid) Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20605950 FASEB J. 2010 Nov;24(11):4196-202.  Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  DRAMP30417 RQLLSGIVQQQNNLLRAIEAQQHLLQK 27 C16-N27 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry. [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=148±4 nM);inhibition of peptide against virus-cell fusion on CD4-expressing cells(IC50=10±1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear C16(hexadecanoic acid) Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20605950 FASEB J. 2010 Nov;24(11):4196-202.  Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  DRAMP30418 RQLLSGIVQQQNNLLRAIEAQQHLL 25 C16- N25 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry. [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=484±60 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear C16(hexadecanoic acid) Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20605950 FASEB J. 2010 Nov;24(11):4196-202.  Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  DRAMP30419 RQLLSGIVQQQNNLLRAIEAQQH 23 C16- N23 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: N peptide may target an exposed C-helix region of gp41 and can interact with their coiled coil formation within a gp41 dimer,which can inhibit HIV-1 entry. [Ref.20605950]HIV-1:inhibition of peptide against cell-cell fusion between Jurkat E6-1 and HXBc2 cells(IC50=1931±187 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear C16(hexadecanoic acid) Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 20605950 FASEB J. 2010 Nov;24(11):4196-202.  Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.  DRAMP30420 XDLTXEMLSLQQVVKALNESY 21 P21S1 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 1 and 5) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (1) and X (5) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30421 LXLTYXMLSLQQVVKALNESY 21 P21S2 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.90 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 2 and 6) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (2) and X (6) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30422 LDLXYEMXSLQQVVKALNESY 21 P21S3 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 4 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (4) and X (8) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30423 LDLTXEMLXLQQVVKALNESY 21 P21S4 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=7.14 ± 0.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 5 and 9) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (5) and X (9) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30424 LDLTYEMXSLQXVVKALNESY 21 P21S5 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.7±2.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 8 and 12) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (8) and X (12) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30425 LDLTYEMLXLQQXVKALNESY 21 P21S6 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 9 and 13) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (9) and X (13) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30426 LDLTYEMLSLXQVVXALNESY 21 P21S7 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 11 and 15) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (11) and X (15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30427 LDLTYEMLSLQXVVKXLNESY 21 P21S8 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.26±0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=3.03 ± 0.29 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.06± 0.34 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.98± 0.28 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L [Ref.29442512]Calu-3 cell:CC50>100 μM membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30428 LDLTYEMLSLQQVVXALNXSY 21 P21S9 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=14.1 ± 2.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (15) and X (19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30429 LDLTYEMLSLQQVVKXLNEXY 21 P21S10 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.33 ± 0.04 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.97± 0.08 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.82± 0.28 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.89± 0.07 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (16) and X (20) are cross-linked by hydrocarbon stapling. L [Ref.29442512]Calu-3 cell:CC50>100 μM membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30430 LXLTYXMLSLQQVVKALNESY 21 P21L2 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.9 ±1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 2 and 6 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30431 LDLTXEMLXLQQVVKALNESY 21 P21L4 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=8.21 ±0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 5 and 9 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30432 LDLTYEMXSLQXVVKALNESY 21 P21L5 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=4.49 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 8 and 12 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30433 LDLTYEMLSLQXVVKXLNESY 21 P21L8 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=20.6± 3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 12 and 16 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30434 LDLTYEMLSLQQVVXALNXSY 21 P21L9 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.9 ± 1.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 15 and 19 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30435 LDLTYEMLSLQQVVKXLNEXY 21 P21L10 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.55 ± 0.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 16 and 20 are S5((S)-pentenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30436 LDLTYEMLSLQXVVKXLNESY 21 P21R8 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=16.3 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' at position 12 and 16 are R5 amino acids. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30437 LDLTYEZLSLQXVVKXLNESY 21 P21S8Z No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.63 ± 0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.80 ± 0.74 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.15± 0.25 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.49±0.18 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. The 'Z' at position 7 indicates R8 ((R)-octenyl alanine) L [Ref.29442512]Calu-3 cell:CC50>100 μM membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30438 LDLTYEMLSLQXVVKXLNESF 21 P21S8F No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=2.16± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30439 LDLTYEZLSLQXVVKXLNESF 21 P21S8ZF No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.89 ± 0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation ①The 'X' (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②X (12) and X (16) are cross-linked by hydrocarbon stapling.,The 'Z' at position 7 indicates R8 ((R)-octenyl alanine) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30440 LDLTYEMLSLQQVVKALNESY 21 P21 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30441 SLTQINTTLLDLEYEMKKLEEVVKKLEESYIDLKEL 36 HR2P-M2 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion. [Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.75 ± 0.09 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.07±0.21 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.25± 0.18 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.64± 0.16 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.29442512]Calu-3 cell:CC50>100 μM membrane 29442512 J Med Chem. 2018 Mar 8;61(5):2018-2026. Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K. Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors.  DRAMP30442 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNI 36 FP3(FCoV Sgp (1338-1373)) P10033 Coronaviridae Not found Synthetic construct(derived from S protein of FCoV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=14.21 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24312629]Fcwf-4 cell:CC50>200 μM. membrane 24312629  PLoS One. 2013 Dec 3;8(12):e82081. Liu IJ, Tsai WT, Hsieh LE, Chueh LL. Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. DRAMP30443 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNINNTLVNL 43 FP4(FCoV Sgp (1338-1380)) P10033 Coronaviridae Not found Synthetic construct(derived from S protein of FCoV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=1.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24312629]Fcwf-4 cell:CC50>200 μM. membrane 24312629  PLoS One. 2013 Dec 3;8(12):e82081. Liu IJ, Tsai WT, Hsieh LE, Chueh LL. Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. DRAMP30444 FNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNINNTLVNLEWLNRIE 50 FP5(FCoV Sgp (1338-1387)) P10033 Coronaviridae Not found Synthetic construct(derived from S protein of FCoV) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interfere the fusion of the viral envelope with host membrane and thus inhibits viral replication. [Ref.24312629]feline coronavirus(FCoV):inhibition of virus replication in Fcwf-4 cells(IC50=1.33 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24312629]Fcwf-4 cell:CC50>200 μM. membrane 24312629  PLoS One. 2013 Dec 3;8(12):e82081. Liu IJ, Tsai WT, Hsieh LE, Chueh LL. Peptides corresponding to the predicted heptad repeat 2 domain of the feline coronavirus spike protein are potent inhibitors of viral infection. DRAMP30445 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKELK 34 SC34EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.9±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30446 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKEL 33 SC33EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30447 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEKE 32 SC32EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30448 WEEWDKKIEEYTKKIEELIKKSEEQQKKNEK 31 SC31EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30449 WEEWDKKIEEYTKKIEELIKKSEEQQKKNE 30 SC30EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1±0 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30450 WEEWDKKIEEYTKKIEELIKKSEEQQKKN 29 SC29EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.2±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30451 WEEWDKKIEEYTKKIEELIKKSEEQQKK 28 SC28EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=18±3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=13±1.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30452 WEEWDKKIEEYTKKIEELIKKSEEQQK 27 SC27EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=29±2.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21.4±2.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30453 WEEWDKKIEEYTKKIEELIKKSEEQQ 26 SC26EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=44.9±5.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=36.2±4.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30454 WEEWDKKIEEYTKKIEELIKKSEEQ 25 SC25EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=79.8±9.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=41.5±3.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30455 WEEWDKKIEEYTKKIEELIKKSEE 24 SC24EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=107.6±8 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=75.7±11.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30456 WEEWDKKIEEYTKKIEELIKKSE 23 SC23EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=105.1±15.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=94.2±12.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30457 WEEWDKKIEEYTKKIEELIKKS 22 SC22EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=66.9±15.9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=98.6±7.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30458 WEEWDKKIEEYTKKIEELIKK 21 SC21EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=113.2±8 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=105.4±12.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30459 WEEWDKKIEEYTKKIEELIK 20 SC20EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=126.6±10.7 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=202.4±5.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30460 WEEWDKKIEEYTKKIEELI 19 SC19EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=70.7±9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=217.2±16.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30461 WEEWDKKIEEYTKKIEEL 18 SC18EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50>2000 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>2000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30462 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKELK 36 MT-SC34EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.7±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30463 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKEL 35 MT-SC33EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.2±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30464 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEKE 34 MT-SC32EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30465 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNEK 33 MT-SC31EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30466 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKNE 32 MT-SC30EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.8±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30467 MTWEEWDKKIEEYTKKIEELIKKSEEQQKKN 31 MT-SC29EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=0.9±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30468 MTWEEWDKKIEEYTKKIEELIKKSEEQQKK 30 MT-SC28EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.3±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.2±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30469 MTWEEWDKKIEEYTKKIEELIKKSEEQQK 29 MT-SC27EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.4±0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30470 MTWEEWDKKIEEYTKKIEELIKKSEEQQ 28 MT-SC26EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.6±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.1±0.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30471 MTWEEWDKKIEEYTKKIEELIKKSEEQ 27 MT-SC25EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.9±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30472 MTWEEWDKKIEEYTKKIEELIKKSEE 26 MT-SC24EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.8±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.3±0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30473 MTWEEWDKKIEEYTKKIEELIKKSE 25 MT-SC23EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.1±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1.9±0.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30474 MTWEEWDKKIEEYTKKIEELIKKS 24 MT-SC22EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=2.4±0.3 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.2±0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30475 MTWEEWDKKIEEYTKKIEELIKK 23 MT-SC21EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=3.8±0.4 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3.1±1.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30476 MTWEEWDKKIEEYTKKIEELIK 22 MT-SC20EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=3.7±0.5 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3.3±1.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30477 MTWEEWDKKIEEYTKKIEELI 21 MT-SC19EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=5±0.9 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=4.9±1.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30478 MTWEEWDKKIEEYTKKIEEL 20 MT-SC18EK Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50>2000 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>2000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30479 MTWEEWDKKIEEYTKKIEELIKKSQNQQEKN 31 MT-WQ-EKN Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.1±0.1 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30480 WEEWDKKIEEYTKKIEELIKKSQNQQEKN 29 WQ-EKN Q5DP94 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. [Ref.31277353]HIV-1 NL4-3:inhibition of pseudovirus entry in TZM-bl cells(IC50=1.4±0.2 nM);##HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.8±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31277353 Viruses. 2019 Jul 3;11(7):609.  Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors. DRAMP30481 YTSLIREILVESRIQQEKNERELRDIDKWASLWNWF 36 T20v1(T20 [H6R; S7E; L8,26I; I9L; E10V; Q13,21R; N14I; L24R; E25D]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.10 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.12 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=0.29 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30482 YTSLIHSIIEESRNRQEKNEQALLELDKWASLWNWF 36 T20v2(T20 [L8I; Q13,15R; E22A]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.06 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.09 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.05 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30483 YTSLLRSIIEEGRNQQEKNEQALLELDKWASLWNWF 36 T20v3(T20 [I5L, H6R, L8I; S12G; Q13R; E22A]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.13 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.08 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.19 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.08 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.34 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30484 YTSLIRSIIEESRNQQEKNEQKLLEVDKWASLWNWF 36 T20v4(T20 [H6R, L8I, Q13R, E22K, L26V]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.15 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.12 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.04 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.22 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.03 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=1.80 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30485 YTSLLRSLIEESRNLQEKNEQALLEVDKWASLWNWF 36 T20v5(T20 [I5L, H6R, Q13R, Q15L, E22A, L26V]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.17 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.15 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.14 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.29 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.13 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.69 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30486 YTSLLWSIIEEGRNLQEKNEQKLLELDKWASLWNWF 36 T20v6(T20 [I5L, H6W, L8I, S12G, Q13R, Q15L, E22K]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.16 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.14 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.21 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.62 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.59 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.10 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.68 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30487 YTSLIWKVLNDAREQQENNQETLVEIDKWASLWNWF 36 T20v7(T20 [H6W; S7K; L8,24V; I9L; E10N; E11D; S12A; Q13R; N14E; K18N; E20Q; Q21E; L26I]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.37 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.16 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.45 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=1.12 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.23 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.07 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=5.10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30488 YTSLIREIMNKSWGQQRRNEGTLAEIDKWASLWNWF 36 T20v8(T20 [H6R; S7E; L8,26I; I9M; E10N; E11K; Q13W; N14G; E17R; K18R; Q21G; E22T; L24A]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=0.40 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.24 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.31 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.53 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=1.11 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.24 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=10.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30489 YTSLIRELISNARTQQTDNEESLRNVDKWASLWNWF 36 T20v9(T20 [H6R; S7E; E10,22S; E11,25N; S12A; Q13R; N14T; E17T; K18D; Q21E; L24R; L26V]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=1.20 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.34 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=0.41 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=0.82 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=1.09 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.35 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=16.8 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30490 YTSLIWSIIIDGREQQRDNEGVLADLDKWASLWNWF 36 T20v10(T20 [H6W; L8I; E10I;E11D;S12G;Q13R;N14E;E17R;K18D;Q21G;E22V;L24D;E25D]) P04578 Retroviridae Not found Synthetic construct(derived from T20) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.31228294]HIV-1 N43:inhibition of virus infection in U87 cells(IC50=23.3 µg/ml);##HIV-1 JRCSF:inhibition of virus infection in U87 cells(IC50=0.50 µg/ml);##HIV-1 94UG103:inhibition of pseudovirus infection in U87 cells(IC50=3.35 µg/ml);##HIV-1 92BR020:inhibition of pseudovirus infection in U87 cells(IC50=12.0 µg/ml);##HIV-1 IAVI C22:inhibition of pseudovirus infection in U87 cells(IC50=0.45 µg/ml);##HIV-1 92HT021:inhibition of pseudovirus infection in U87 cells(IC50=0.11 µg/ml);##HIV-1 JRCSF-GIA:inhibition of pseudovirus infection in U87 cells(IC50=24.4 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30491 EKINQSLAFIRKSDELLHNV 20 peptide 4(RSV fusion protein(497-515)) P03420 Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50>50 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 31228294 Protein Sci. 2019 Aug;28(8):1501-1512. Chen G, Cook JD, Ye W, Lee JE, Sidhu SS. Optimization of peptidic HIV-1 fusion inhibitor T20 by phage display. DRAMP30492 EKINQSLXFIRXSDXLLHXV 20 peptide 4a(derived from RSV fusion protein(497-515)) No entry found Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.82±0.42 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30493 EKIXQSLXFIXKSDXLLHNV 20 peptide 4bb(derived from RSV fusion protein(497-515)) No entry found Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.74±0.27 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30494 EXINXSLXFIRXSDELLHNV 20 peptide 4ca(derived from RSV fusion protein(497-515)) No entry found Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.59±0.13 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 2 indicates R-pentenylalanine; The 'X' at position 5,8,12 indicates S-pentenylalanine, X(2) and X(5), X(8) and X(12) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30495 XKINQSLXFIRXSDELLHXV 20 peptide 4ef(derived from RSV fusion protein(497-515)) No entry found Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=3.07±1.45 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 1,8 indicates R-octenyl-alanine; The 'X' at position 12,19 indicates S-pentenylalanine, X(1) and X(8), X(12) and X(19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30496 EKIXQSLXFIRXSDELLHXV 20 peptide 4bf(derived from RSV fusion protein(497-515)) No entry found Paramyxoviridae Not found Synthetic construct(derived from RSV fusion protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=2.49±0.09 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 12 indicates R-octenyl-alanine; The 'X' at position 4,8,19 indicates S-pentenylalanine, X(4) and X(8), X(12) and X(19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30497 EKIAQSLXFIRXSDXLLHXV 20 peptide 4a[N500A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=20.41±2.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30498 EKINQSLXFIAXSDXLLHXV 20 peptide 4a[R507A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=175±0.00 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 8,12,15,19 indicates S-pentenylalanine, X(8) and X(12), X(15) and X(19) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30499 AKIXQSLXFIXKSDXLLHNV 20 peptide 4bb[E497A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.16±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30500 EAIXQSLXFIXKSDXLLHNV 20 peptide 4bb[K498A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.60±0.02 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30501 EKAXQSLXFIXKSDXLLHNV 20 peptide 4bb[I499A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.30±0.89 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30502 EKIXASLXFIXKSDXLLHNV 20 peptide 4bb[Q501A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.28±0.43 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30503 EKIXQALXFIXKSDXLLHNV 20 peptide 4bb[S502A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.66±0.26 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30504 EKIXQSAXFIXKSDXLLHNV 20 peptide 4bb[L503A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.95±0.53 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30505 EKIXQSLXAIXKSDXLLHNV 20 peptide 4bb[F505A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.39±0.10 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30506 EKIXQSLXFAXKSDXLLHNV 20 peptide 4bb[I506A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=10.44±2.97 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30507 EKIXQSLXFIXASDXLLHNV 20 peptide 4bb[K508A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=10.93±13.90 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30508 EKIXQSLXFIXKADXLLHNV 20 peptide 4bb[S509A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=82.04±1.56 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30509 EKIXQSLXFIXKSAXLLHNV 20 peptide 4bb[D510A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.10±0.08 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30510 EKIXQSLXFIXKSDXALHNV 20 peptide 4bb[L512A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.88±0.06 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30511 EKIXQSLXFIXKSDXLLANV 20 peptide 4bb[H514A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.52±0.07 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30512 EKIXQSLXFIXKSDXLLHAV 20 peptide 4bb[N515A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=2.71±2.93 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30513 EKIXQSLXFIXKSDXLLHNA 20 peptide 4bb[V516A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=0.60±0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 4,8,11,15 indicates S-pentenylalanine, X(4) and X(8), X(11) and X(15) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30514 EXINXSLXFIRXSDALLHNV 20 peptide 4ca[E511A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts the formation of the postfusion six-helix bundle required for viral cell entry. [Ref.28137809]Respiratory syncytial virus (RSV):inhibition of virus infection in Hep-2 cells(EC50=1.00±0.03 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Free The 'X' at position 2 indicates R-pentenylalanine; The 'X' at position 5,8,12 indicates S-pentenylalanine, X(2) and X(5), X(8) and X(12) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading. DRAMP30515 YTSLIHSLIEESQNQQEKNEQELLEX 26 LP-53 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2949±400 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9968±2224 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=21352±1876 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30516 YTSLIEELIKKSEEQQKKNEEELKX 25 LP-54 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=149±48 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=301±26 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1796±340 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30517 WEQKIEELLKKAEEQQKKNEEELKKX 26 LP-55 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=8±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=12±1 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.11-189.34 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=10.67-137.77 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.19-10.61 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=34 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30518 WEQKIEELLKKAEEQQKKNEEELKXX 26 LP-56 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=12±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=11±2 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid),The 'X' at position 25 is Lys-AEEA(8-amino-3,6-dioxaoctanoic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30519 WEQKIEELLKKAEEQQKKNEEEX 23 LP-57 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=213±21 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=178±38 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1917±440 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 23 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30520 WEQKIEELLKKAEEQQKKNEX 21 LP-58 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=143000±19911 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=110900±3715 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=107033±9473 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30521 WEQKIEELLKKAEEQQKX 18 LP-59 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>900000 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=240800±23649 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=210477±25537 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 18 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30522 SLIEELIKKSEEQQKKNEEELKKLEX 26 LP-60 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=55±6 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=48±6 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=62±27 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30523 IEELIKKSEEQQKKNEEELKKLEX 24 LP-61 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=85±9 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=43±9 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=126±63 pM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=144 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=193.63±13.92 μM;##MT-4 cell:CC50=164.47±37.69 μM;##HEK293T cell:CC50=140.43± 10.7μM;##PBMC:CC50=46.43± 2.6 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30524 EQKIEELLKKAEEQQKKNEEELKKLEX 27 LP-62 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=15±1 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=5±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=12±1 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 27 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30525 QKIEELLKKAEEQQKKNEEELKKLEX 26 LP-63 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=17±5 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=6±2 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=13±2 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 26 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30526 KIEELLKKAEEQQKKNEEELKKLEX 25 LP-64 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=128±27 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=36±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=25±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.04 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.08-140.75 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.23-0.75 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.10-0.11 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=58 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 25 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30527 IEELLKKAEEQQKKNEEELKKLEX 24 LP-65 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=8±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=7±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.15-88.63 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.23-0.75 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.07-0.04 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=35 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=256.23 ±14.58 μM;##MT-4 cell:CC50=213.4±59.59 μM;##HEK293T cell:CC50=208.43± 22.9μM;##PBMC:CC50=49.95± 2.97 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30528 EELLKKAEEQQKKNEEELKKLEX 23 LP-66 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=1008±248 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=434±71 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1109±193 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 23 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30529 LLEQAEEQQKKNEEELKKLEX 21 LP-67 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=3417±419 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=627±154 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1527±565 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30530 AEEQQKKNEEELKKLEX 17 LP-68 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>250000 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>250000 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>250000 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 17 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30531 IEELLKKAEEQQKKNEEELKX 21 LP-69 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=239±16 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=125±27 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=157±29 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.31 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=2.01-1815.67 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=9.83-152.28 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.56-11.91 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=1391 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 21 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30532 INNYTSLIEELIKKSEEQQKKNEEELKKLEX 31 LP-70 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=25±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=21±4 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=30±10 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30533 IEEYTKKIEEILKKSEEQQKKNEEELKKLEX 31 LP-71 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=27±2 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=25±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=55±5 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30534 VRYLEANIEELLKKAEEQQKKNEEELKKLEX 31 LP-72 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=23±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=28±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=24±9 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30535 VEELEKKIEELLKKAEEQQKKNEEELKKLEX 31 LP-73 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=33±6 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=19±3 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=42±2 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30536 WEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEX 38 LP-74 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=110±10 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=59±11 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=59±32 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 38 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30537 EMTWEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEX 41 LP-75 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=100±22 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=65±8 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=86±26 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 41 is Lys-C16(palmitic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30538 WQEWEQKITALLEQAQIQQEKNEYELQKLDKX 32 LP-46 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=88±4 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=50±8 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=44±7 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 31 is Lys-C16(palmitic acid). L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30539 WEQKITALLEQAQIQQEKNEYELQKLDKX 29 LP-48 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=83±9 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=47±6 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=37±4 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid). L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30540 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELLX 35 C34-C16 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=247±28 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=65±25 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=109±13 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 35 is Lys-C16(palmitic acid). L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30541 WMEWDREINNYTSLIHSLIEESQNQQEKNEQELLGSGX 38 C34-Chol P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=316±62 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24±2 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=37±5 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 38 is Cys-Chol(cholesterol) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30542 YTSLIEELIKKSEEQQKKNEEELKKLEK 28 P-50 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=35.6±1.3 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=191.1±57.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=21.8±3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30543 LEANIEELLKKAEEQQKKNEEELKKLEK 28 P-51 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=10.2±0.7 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24.9±2.9 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=45.4±10.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30544 WEQKIEELLKKAEEQQKKNEEELKKLEK 28 P-52 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.9±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=1.9±0.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1.9±0.4 nM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=20541 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.30089693]TZM-bl cell:CC50=916.6 ±42.46 μM;##MT-4 cell:CC50=770.63±131.46 μM;##HEK293T cell:CC50=649.07± 37.03μM;##PBMC:CC50=91.19± 20.46 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30545 YTSLIEELIKKSEEQQKKNEEELKK 25 P-54 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30546 WEQKIEELLKKAEEQQKKNEEELKK 25 P-55 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=14.2±1.8 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=16.9±2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=32.3±9.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30547 WEQKIEELLKKAEEQQKKNEEEK 23 P-57 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30548 WEQKIEELLKKAEEQQKKNEK 21 P-58 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30549 WEQKIEELLKKAEEQQKK 18 P-59 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30550 SLIEELIKKSEEQQKKNEEELKKLEK 26 P-60 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>750 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=591.4±65.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30551 EQKIEELLKKAEEQQKKNEEELKKLEK 27 P-62 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=25.3±2.6 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=44.2±2.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=22.1±3.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30552 QKIEELLKKAEEQQKKNEEELKKLEK 26 P-63 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=16.1±2.5 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=24±2.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=24.4±2.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30553 KIEELLKKAEEQQKKNEEELKKLEK 25 P-64 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=7.6±1.3 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.3±0.6 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=10.4±2.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30554 IEELLKKAEEQQKKNEEELKKLEK 24 P-65 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=17.9±2.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=25.7±1.3 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=25.8±1.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30555 IEELLKKAEEQQKKNEEELKK 21 P-69 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50>7508 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50>750 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50>750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30556 INNYTSLIEELIKKSEEQQKKNEEELKKLEK 31 P-70 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=8.5±0.5 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=36.5±6.4 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=49.7±5.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30557 IEEYTKKIEEILKKSEEQQKKNEEELKKLEK 31 P-71 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2.1±0.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.1±3.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=38.7±7.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30558 VRYLEANIEELLKKAEEQQKKNEEELKKLEK 31 P-72 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=4.1±0.9 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=16.2±3.4 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=15.9±1.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30559 VEELEKKIEELLKKAEEQQKKNEEELKKLEK 31 P-73 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=2±0.2 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=5.6±0.7 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=8.2±1.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30560 WEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEK 38 P-74 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.4±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=0.8±0.1 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=1.4±0.4 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30561 EMTWEEWEKKIEEYTKKIEEILKKSEEQQKKNEEELKKLEK 41 P-75 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=0.4±0.1 nM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=0.9±0.2 nM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=0.6±0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30562 ILPWKWPWWPWPP 13 Indolicidin [R12P][R13P] No entry found Retroviridae Not found Synthetic construct(derived from Indolicidin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=16 µM);inhibition of strand transfer catalyzed by integrase(IC50=13 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidtion L No cytotoxicity information or data found in the reference(s) presented in this entry HIV Integrase 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP.  Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. DRAMP30563 LPWKWPWWPWPP 12 Indolicidin (2-13)[R12P][R13P] No entry found Retroviridae Not found Synthetic construct(derived from Indolicidin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=185 µM);inhibition of strand transfer catalyzed by integrase(IC50=215 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidtion L No cytotoxicity information or data found in the reference(s) presented in this entry HIV Integrase 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP.  Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. DRAMP30564 ILPWKWPWWPWP 12 Indolicidin (1-12)[R12P] No entry found Retroviridae Not found Synthetic construct(derived from Indolicidin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=180 µM);inhibition of strand transfer catalyzed by integrase(IC50=80 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidtion L No cytotoxicity information or data found in the reference(s) presented in this entry HIV Integrase 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP.  Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. DRAMP30565 ILPWGWPWWPWPP 13 Indolicidin [K5G;R12P;R13P] No entry found Retroviridae Not found Synthetic construct(derived from Indolicidin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50>333 µM);inhibition of strand transfer catalyzed by integrase(IC50>333 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidtion L No cytotoxicity information or data found in the reference(s) presented in this entry HIV Integrase 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP.  Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. DRAMP30566 ILAWKWAWWAWPP 13 Indolicidin [P3,7,10A,R12,13P] No entry found Retroviridae Not found Synthetic construct(derived from Indolicidin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 integrase plays a crucial role in the HIV-1 virus replication cycle. The peptide can inhibit the activity of integrase and thus inhibit virus replication. [Ref.15482931]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=54 µM);inhibition of strand transfer catalyzed by integrase(IC50=41 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidtion L No cytotoxicity information or data found in the reference(s) presented in this entry HIV Integrase 15482931 Bioorg Med Chem Lett. 2004 Nov 15;14(22):5595-8. Krajewski K, Marchand C, Long YQ, Pommier Y, Roller PP.  Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin. DRAMP30567 LLEYSI 6 peptide 1 from hydrolysate of oyster No entry found Retroviridae Not found Crassostrea gigas(hydrolysate of oyster) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=20 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30568 LLEYSL 6 peptide 2 from hydrolysate of oyster No entry found Retroviridae Not found Crassostrea gigas(hydrolysate of oyster) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=15 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30569 LLEYS 5 peptide derived from hydrolysate of oyster No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=120 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30570 LEYSI 5 peptide derived from hydrolysate of oyster No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=550 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30571 LLEY 4 peptide derived from hydrolysate of oyster No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=5100 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30572 LEYS 4 peptide derived from hydrolysate of oyster No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HIV-1 protease is a virally encoded protease that serves to cleave the gag and gag-pol polyprotein precursor into mature, functional proteins. This specific proteolysis occurs late in the viral life cycle and is essential for the maturation of the infectious virus. The peptide inhibits HIV-1 protease and thus acts antiviral activity. [Ref.9918775]HIV-1:inhibition of HIV-1 protease(IC50=4800 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HIV-1 protease 9918775 Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. Lee TG, Maruyama S.  Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. DRAMP30573 FVFLM 5 FM5 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30574 PFVFLM 6 PM6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30575 KPFVFLM 7 KM7 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30576 NKPFVFLM 8 NM8 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30577 PFVYLI 6 PI6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30578 PFVFLE 6 PE6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30579 EFVFLM 6 EM6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30580 PEVFLM 6 PEM6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30581 PFVFLR 6 PR6 No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30582 CPFVFLM 7 CPM No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=8.96 ± 2.23 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells between H9/HIV-1IIIB cells and MT-2 cells(IC50=67.20 ± 4.05 μM);##HIV-1:inhibition of pseudovirus infection(IC50=5.95 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) L [Ref.22406118]MT-2 cells:CC50>200 μM. Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30583 CPFVFLE 7 CPE No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=55.84 ± 3.31μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50=115.58 ± 6.28 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) L [Ref.22406118]MT-2 cells:CC50>200 μM. Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30584 CPFVFLR 7 CPR No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50=74.07± 22.84 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50=73.98 ± 7.44 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) L [Ref.22406118]MT-2 cells:CC50>200 μM. Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30585 CPEVFLM 7 CPEM No entry found Retroviridae Not found Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) L [Ref.22406118]MT-2 cells:CC50>200 μM. Not found 22406118 Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.  Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. DRAMP30586 IWNHGNITLGEWYNQTKDLQQKFYEIIMDIEQNNV 35 T1562(FIV envelope protein (724-758)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.318 μM,EC90=1.236 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30587 WNHGNITLGEWYNQTKDLQQKFYEIIMDIEQNNVQ 35 T1568(FIV envelope protein (725-759)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.259 μM,EC90=0.971 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30588 GNITLGEWYNQTKDLQQKFYEIIMDIEQNNVQG 33 T1967(FIV envelope protein (728-760)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=2.454 μM,EC90>2.518 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50=2.053 μM,EC90>2.518 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30589 NITLGEWYNQTKDLQQKFYEIIMDIEQNNVQGK 33 T1968(FIV envelope protein (729-761)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.586 μM,EC90=2.067 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.473 μM,EC90>2.473 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30590 ITLGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGI 35 T1569(FIV envelope protein (730-764)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.026 μM,EC90=0.117 μM);inhibition of virus infection in FCD4-E cells(EC50=0.055 μM,EC90=0.106 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.356 μM,EC90>2.356 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30591 TLGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKG 33 T1969(FIV envelope protein (731-763)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.435 μM,EC90=1.413 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30592 LGEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQ 35 T1577(FIV envelope protein (732-766)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.050 μM,EC90=0.162 μM);inhibition of virus infection in FCD4-E cells(EC50=0.098 μM,EC90=0.177 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50=1.933 μM,EC90>2.342 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30593 GEWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQL 35 T1971(FIV envelope protein (733-767)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.012 μM,EC90=0.033 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.342 μM,EC90>2.342 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.12186891]No cytotoxic effects against HeLa cells at the concentration of 23 μM. Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30594 EWYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQ 35 T1972(FIV envelope protein (734-768)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.012 μM,EC90=0.054 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.304 μM,EC90>2.304 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.12186891]No cytotoxic effects against HeLa cells at the concentration of 23 μM. Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30595 WYNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQK 35 T1578(FIV envelope protein (735-769)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.020 μM,EC90=0.090 μM);inhibition of virus infection in FCD4-E cells(EC50=0.053 μM,EC90=0.157 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30596 YNQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKW 35 T1588(FIV envelope protein (736-770)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=0.030 μM,EC90=0.125 μM);inhibition of virus infection in FCD4-E cells(EC50=0.168 μM,EC90=0.4236 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30597 NQTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWE 35 T1988(FIV envelope protein (737-771)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=1.990 μM,EC90>2.322 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.322 μM,EC90>2.322 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30598 QTKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWED 35 T1989(FIV envelope protein (738-772)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50>2.321 μM,EC90>2.321 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30599 TKDLQQKFYEIIMDIEQNNVQGKKGIQQLQKWEDW 35 T1589(FIV envelope protein (739-773)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50=1.145 μM,EC90>2.290 μM);##HIV-1:inhibition of cell-cell fusion between CEM4/IIIb cells and MOLT4 cells(EC50>2.321 μM,EC90>2.321 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30600 FYEIIMDIEQNNVQGKKGIQQLQKWEDWVGWIGNI 35 T1566(FIV envelope protein (746-780)) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12186891]Feline immunodeficiency virus (FIV):inhibition of cell-cell fusion between FIV/CrFK cells and HeLa cells(EC50>2.346 μM,EC90>2.346 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 12186891 J Virol. 2002 Sep;76(18):9079-86. Medinas RJ, Lambert DM, Tompkins WA. C-Terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread.  DRAMP30601 XTWXEWDREINNYTSLIHSLIEESQNQQEKNEQELLE 37 T649v P04582 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.9±0.4 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50>3000 nM);##HIV-1 V38A/N42T:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=15.8±1.9 nM);##HIV-1 V38E/N42S:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=44.4±6.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free The 'X' at position 1 indicates Norleucine. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. DRAMP30602 XTWXEWDXEINNYTSLIHSLIEESQNQQEKNEQELLE 37 SAH-gp41(626-662)A P04582 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.1±0.3 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=339±162 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free The 'X' at position 1 indicates Norleucine,the 'X' at position 4,8 indicates S-2-(4'-pentenyl) alanine. X(4) and X (5) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. DRAMP30603 XTWMEWDREINNYTSLIHSLIEESQNQXEKNXQELLE 37 SAH-gp41(626-662) B P04582 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=4.5±1.4 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=1958±259 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free The 'X' at position 1 indicates Norleucine,the 'X' at position 28,32 indicates S-2-(4'-pentenyl) alanine. X(28) and X (32) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. DRAMP30604 XTWXEWDXEINNYTSLIHSLIEESQNQXEKNXQELLE 37 SAH-gp41(626-662) A,B P04582 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein. [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.5±0.2 nM);##HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=87±30 nM);##HIV-1 V38A/N42T:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=10.7±2.2 nM);##HIV-1 V38E/N42S:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=16.1±3.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free The 'X' at position 1 indicates Norleucine,the 'X' at position 4,8.28,32 indicates S-2-(4'-pentenyl) alanine. X(4) and X (5), X(28) and X (32) are cross-linked by hydrocarbon stapling. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20660316 Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. DRAMP30605 AEEASKKAEEASKKAEEASKKAEEASKKAEEASKKXX 37 AAS No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=4.47±1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=2.38±0.9 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30606 VEEVSKKVEEVSKKVEEVSKKVEEVSKKVEEVSKKXX 37 VVS No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=74.5±6.8 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30607 FEEFSKKFEEFSKKFEEFSKKFEEFSKKFEEFSKKXX 37 FFS No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=3.11±0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30608 YEEYSKKYEEYSKKYEEYSKKYEEYSKKYEEYSKKXX 37 YYS No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=6.26±2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=19.8±1.6 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30609 LEELSKKLEELSKKLEELSKKLEELSKKLEELSKKXX 37 LLS No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.24±0.08 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=4.04±0.4 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30610 IEEISKKIEEISKKIEEISKKIEEISKKIEEISKKXX 37 IIS No entry found Coronaviridae, Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.10±0.02 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=1.96±0.28 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=6.38±1.06 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=88.8±28 μM;##MDCK cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30611 IEEIYKKIEEIYKKIEEIYKKIEEIYKKIEEIYKKXX 37 IIY No entry found Coronaviridae, Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.52±0.4 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=3.15±1.79 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=12.9±5.55 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM;##MDCK cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30612 IEEIWKKIEEIWKKIEEIWKKIEEIWKKIEEIWKKXX 37 IIW No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=10.6±2.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30613 IEEIHKKIEEIHKKIEEIHKKIEEIHKKIEEIHKKXX 37 IIH No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=1.68±0.47 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30614 IEEIQKKIEEIQKKIEEIQKKIEEIQKKIEEIQKKXX 37 IIQ No entry found Coronaviridae, Orthomyxoviridae, Filoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.11±0.02 μM);inhibition of pseudovirus infection in Huh-7 cells(IC50=0.13±0.1 μM);##A/Puerto Rico/8/34 (H1N1):inhibition of virus infection in MDCK cells(EC50=1.73±0.81 μM);##A/Hong Kong/8/68 (H3N2):inhibition of virus infection in MDCK cells(EC50=0.70±0.09 μM);##HIV-1 inhibition of cell-cell fusion in TZM-bl cells(EC50=3.63 ±0.54 μM);##Ebola virus (EboV):inhibition of pseudovirus infection in TZM-bl cells(EC50=1.02 ± 0.54 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM;##MDCK cell:CC50>100 μM;##TZM-bl cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30615 IEEIKKKIEEIKKKIEEIKKKIEEIKKKIEEIKKKXX 37 IIK No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=0.45±0.13 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50=4.54±0.6 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30616 IEEIEKKIEEIEKKIEEIEKKIEEIEKKIEEIEKKXX 37 IIE No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with both MERS-CoV and IAV NHR trimeric coiled coils to prevent virus–cell membrane fusion. [Ref.30192544]MERS-CoV:inhibition of cell-cell fusion between 293T / MERS / EGPF cells and Huh-7 cells(EC50=2.93±0.95 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at 36 indicates β-alanine,the 'X' at 37 indicates Lys-C16(palmitic acid). L [Ref.30192544]Huh-7 cell:CC50>100 μM. membrane 30192544  J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K.  De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.  DRAMP30617 LWGEIWNTVKGLI 13 Eval418 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=2.48 μg/ml);inhibition of viral attachment in Vero cells(IC50=3.70 μg/ml);inhibition of viral entry in Vero cells(IC50=31.71 μg/ml). [Ref.29290802]the cell viability of erythrocytes was also more than 95% at concentrations of Eval418 of 10 μg/mL or less. Linear Free Amidation L [Ref.29290802]Vero cell:CC50=68.50μg/mL; the cell viability of the peptide-treated Vero cells was greater than 95% after treatment with Eval418 at 10 μg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30618 LWGHIWNFVHGLI 13 Eval418-FH2 No entry found Herpesviridae Not found Synthetic construct(derived from Eval418) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=1.50 μg/ml);inhibition of viral attachment in Vero cells(IC50=1.43 μg/ml);inhibition of viral entry in Vero cells(IC50=8.63 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cell:CC50=27.60 μg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30619 LWHHIWNFVHGLI 13 Eval418-FH3 No entry found Herpesviridae Not found Synthetic construct(derived from Eval418) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=1.01 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.86 μg/ml);inhibition of viral entry in Vero cells(IC50=4.23 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cell:CC50=26.83 μg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30620 LWHHIWNTVHHLI 13 Eval418-FH4 No entry found Herpesviridae Not found Synthetic construct(derived from Eval418) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=0.87 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.63 μg/ml);inhibition of viral entry in Vero cells(IC50=4.37 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cell:CC50=27.58 μg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30621 LWHHIWHTVHHLI 13 Eval418-FH5 No entry found Herpesviridae Not found Synthetic construct(derived from Eval418) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]HSV-1:inhibition of viral inactivation in Vero cells(IC50=0.86 μg/ml);inhibition of viral attachment in Vero cells(IC50=0.67 μg/ml);inhibition of viral entry in Vero cells(IC50=2.88 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cell:CC50=106.68 μg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30622 LWGEIWNTVKGLI 13 Eval418 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=2.48 µg/mL); inhibition of viral attachment in Vero cells(IC50=3.70 µg/mL); inhibition of viral entry in Vero cells(IC50=31.71 µg/mL). [Ref.29290802]The hemolysis rate of human erythrocytes was less than 50% when the concentration of Eval418 was as high as 200 μg/mL. Linear Free Amidation L [Ref.29290802]Vero cells: CC50 = 68.50 µg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30623 LWGHIWNFVHGLI 13 Eval418-FH2 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=1.50 µg/mL); inhibition of viral attachment in Vero cells(IC50=1.43 µg/mL); inhibition of viral entry in Vero cells(IC50=8.63 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cells: CC50 = 27.60 µg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30624 LWHHIWNFVHGLI 13 Eval418-FH3 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=1.01 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.86 µg/mL); inhibition of viral entry in Vero cells(IC50=4.23 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cells: CC50 = 26.83 µg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30625 LWHHIWNTVHHLI 13 Eval418-FH4 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=0.87 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.63 µg/mL); inhibition of viral entry in Vero cells(IC50=4.37 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cells: CC50 = 27.58 µg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30626 LWHHIWHTVHHLI 13 Eval418-FH5 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.29290802]Herpes simplex virus type 1(HSV-1): inhibition of viral inactivation in Vero cells(IC50=0.86 µg/mL); inhibition of viral attachment in Vero cells(IC50=0.67 µg/mL); inhibition of viral entry in Vero cells(IC50=2.88 µg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.29290802]Vero cells: CC50 = 106.68 µg/mL. Not found 29290802 Theranostics. 2018 Jan 1;8(1):199-211. Zeng Z, Zhang R, Hong W, Cheng Y, Wang H, Lang Y, Ji Z, Wu Y, Li W, Xie Y, Cao Z. Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1. DRAMP30627 WQCLTLTHRGFVLLTITVLR 20 IN-1 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit integrase and thus inhibit virus replication. [Ref.18201721]HIV-1:Inhibition of 3′-processing catalyzed by integrase(IC50=38 µM);inhibition of strand transfer catalyzed by integrase(IC50=12 µM).##[Ref.19850483]HIV-1:inhibition of integrase catalytic activity(77% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(70% inhibition at 62.5μM);inhibition of intergration(63% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18201721]No cytotixic against HeLa cells and H9 T-lymphocyte cultured cells up to ~62.5 μM. Integrase 18201721##19850483 J Mol Biol. 2008 Feb 29;376(4):971-82. ##Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. Armon-Omer A, Levin A, Hayouka Z, Butz K, Hoppe-Seyler F, Loya S, Hizi A, Friedler A, Loyter A. ##Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A. Correlation between shiftide activity and HIV-1 integrase inhibition by a peptide selected from a combinatorial library.##Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. DRAMP30628 WQCLTLTHRG 10 IN(1-10) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit integrase and thus inhibit virus replication. [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(73% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(68% inhibition at 62.5μM);inhibition of intergration(64% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A.  Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. DRAMP30629 WFVLLTITVLR 11 IN(11-20) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit integrase and thus inhibit virus replication. [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(24% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(29% inhibition at 62.5μM);inhibition of intergration(23% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A.  Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. DRAMP30630 WQSLTLTHRG 10 IN(1-10)[C3S] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can inhibit integrase and thus inhibit virus replication. [Ref.19850483]HIV-1:inhibition of integrase catalytic activity(62% inhibition at 62.5μM);inhibition of virus replication in TZM-bl cells(60% inhibition at 62.5μM);inhibition of intergration(51% inhibition at 62.5μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 19850483 Bioorg Med Chem. 2009 Nov 15;17(22):7635-42. Maes M, Levin A, Hayouka Z, Shalev DE, Loyter A, Friedler A.  Peptide inhibitors of HIV-1 integrase: from mechanistic studies to improved lead compounds. DRAMP30631 VSGHGQHGVHG 11 Alloferon (3-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database "[Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=500 µM);##HHV-1 clinical strain:inhibition of virus replication in Hep-2 cells(IC50=117 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=38 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=250 µM);inhibition of virus replication in LLC-MK2 cells(IC50=93 µM)." No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 165 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30632 SGHGQHGVHG 10 Alloferon (4-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=186 µM);inhibition of virus replication in Hep-2 cells(IC50=310 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=173 µM);inhibition of virus replication in Hep-2 cells(IC50=450 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=210 µM);inhibition of virus replication in LLC-MK2 cells(IC50=180 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 420 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30633 GHGQHGVHG 9 Alloferon (5-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Hep-2 cells(IC50=360 µM);##HHV-1 clinical strain:inhibition of virus replication in Hep-2 cells(IC50=290 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in LLC-MK2 cells(IC50=230 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 448 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30634 HGQHGVHG 8 Alloferon (6-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=179 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=117 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=78 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=190 µM);inhibition of virus replication in LLC-MK2 cells(IC50=410 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 468 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30635 GQHGVHG 7 Alloferon (7-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=215 µM);inhibition of virus replication in HEp-2 cells(IC50=840 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=168 µM);inhibition of virus replication in Vero cells(IC50=280 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);inhibition of virus replication in LLC-MK2 cells(IC50=190 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=870 µM);inhibition of virus replication in LLC-MK2 cells(IC50=170 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 775 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30636 QHGVHG 6 Alloferon (8-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=1300 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=950 µM);inhibition of virus replication in Hep-2 cells(IC50=280 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=170 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=500 µM);inhibition of virus replication in LLC-MK2 cells(IC50=210 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 380 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30637 HGVHG 5 Alloferon (9-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=300 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=400 µM);##Coxsackie virus B2(clinical strain):inhibition of virus replication in Hep-2 cells(IC50=350 µM);inhibition of virus replication in LLC-MK2 cells(IC50=290 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=350 µM);inhibition of virus replication in LLC-MK2 cells(IC50=180 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 826 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30638 GVHG 4 Alloferon (10-13) P83412 Herpesviridae, Picornaviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=500 µM);##HHV-1 clinical strain:inhibition of virus replication in Vero cells(IC50=1500 µM);##Coxsackie virus 971 PT B2:inhibition of virus replication in HEp-2 cells(IC50=1040 µM);inhibition of virus replication in LLC-MK2 cells(IC50=540 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero, Hep-2 and LLC-MK2 cells up to 1174 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30639 HGVSGHGQHGV 11 Alloferon (1-11) P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=178 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 260 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30640 HGVSGHGQHG 10 Alloferon (1-10) P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=520 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 350 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30641 HGVSGHGQ 8 Alloferon (1-8) P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=310 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 447 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30642 HGVSGHG 7 Alloferon (1-7) P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=550 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 504 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30643 FGVSGHGQHGVHG 13 Alloferon [H1F] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=160 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 290 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30644 YGVSGHGQHGVHG 13 Alloferon [H1Y] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 315 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30645 WGVSGHGQHGVHG 13 Alloferon [H1W] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22883213]No cytotoxic against Vero cells up to 282 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30646 XGVSGHGQHGVHG 13 Alloferon [H1Phg] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 indicates Phenylglycine. L [Ref.22883213]No cytotoxic against Vero cells up to 350 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30647 XGVSGHGQHGVHG 13 Alloferon [H1Phe(p-Cl)] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=110 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 indicates 4-Chloro-phenylalanine. L [Ref.22883213]No cytotoxic against Vero cells up to 255 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30648 XGVSGHGQHGVHG 13 Alloferon [H1Phe(p-OME)] P83412 Herpesviridae Not found Synthetic construct(derived from Alloferon-1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22883213]Herpesvirus 1 McIntire (HHV-1MC):inhibition of virus replication in Vero cells(IC50=220 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 indicates 4-Methoxy-phenylalanine. L [Ref.22883213]No cytotoxic against Vero cells up to 312 µM. Not found 22883213 Chem Biol Drug Des. 2013 Feb;81(2):302-9. Kuczer M, Majewska A, Zahorska R. New alloferon analogues: synthesis and antiviral properties. DRAMP30649 EMTWEEWEKKIEEYTKKIEEILXX 24 LP-11 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=931±68 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=201±41 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=253±40 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid),The 'X' at position 23 is Lys-PEG8. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30650 EMTWEEWEKKVEELEKKIEELLXX 24 LP-19 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=296±45 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=95±18 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=92±11 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 24 is Lys-C16(palmitic acid),The 'X' at position 23 is Lys-PEG8. L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30651 YTSLIHSLIEESQNQQEKNEQELLELDX 28 LP-40 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=361±60 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=392±73 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=384±33 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=800.8 ± 62.29 μM;##MT-4 cell:CC50=366.3± 119.08 μM;##HEK293T cell:CC50=408± 40.1μM;##PBMC:CC50=212.6± 25.71 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30652 YTSLIEELIKKSEEQQKKNEEELKKLEX 28 LP-50 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21±3 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=7±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=23±2 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.06-136.12 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.09-5.81 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.06 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=106.4 ± 2.72 μM;##MT-4 cell:CC50=138.37± 6.55 μM;##HEK293T cell:CC50=166.77± 35.33μM;##PBMC:CC50=40.01± 4.63 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30653 LEANIEELLKKAEEQQKKNEEELKKLEX 28 LP-51 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=21±10 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=6±1 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=27±5 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.02-12.07 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.09-0.84 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.03-0.06 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=434.03±90.38 μM;##MT-4 cell:CC50=135.07±32.3 μM;##HEK293T cell:CC50=130.07± 15.27μM;##PBMC:CC50=46.83±4.65 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30654 WEQKIEELLKKAEEQQKKNEEELKKLEX 28 LP-52 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide acts by binding to the heptad repeat 1 (HR1) region of gp41 and preventing the interaction of the HR1 and HR2 domains, which is required for virus–cell fusion.(By similar) [Ref.30089693]HIV-1 HXB2:inhibition of cell-cell fusion in TZM-bl cells(IC50=13±1 pM);##HIV-1 NL4-3:inhibition of pseudovirus infection in TZM-bl cells(IC50=4±0 pM);##HIV-1 JRCSF:inhibition of virus infection in TZM-bl cells(IC50=5±1 pM);##HIV-1(3 A, 13 B, 7 C, 1 G, 1 A/C, 5 A/E, 6 B/C pseudovirus subtypes):inhibition of pseudovirus infection in TZM-bl cells(IC50=17 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50<0.01 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.01-1.86 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.06-0.34 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.01-0.04 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C16(palmitic acid) L [Ref.30089693]TZM-bl cell:CC50=112.9 ± 2.21 μM;##MT-4 cell:CC50=94.06± 4.97 μM;##HEK293T cell:CC50=88.86± 6.68μM;##PBMC:CC50=114.8± 12.68 μM. membrane 30089693 J Virol. 2018 Sep 26;92(20):e01088-18. Chong H, Zhu Y, Yu D, He Y. Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus. DRAMP30655 WEQKIEELLKKAEEQQKKNEEELKKLEX 28 LP-80 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=2.66±0.76 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=7.12±0.28 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=13.00±4.55 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=5 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.003±0.001 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.007-4.006 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.288-0.299 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.034-0.155 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=13.4 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 28 is Lys-C18(stearic acid) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30656 WEQKIEELLKKAEEQQKKNEEELKKLEKX 29 LP-83 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=0.49±0.03 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=4.54±1.42 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=4.75±0.83 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=2.91 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.002±0 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.002-0.041 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.02-0.032 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.004-0.006 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=8.55 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 29 is Cys-Chol(cholesterol) L [Ref.30867304]Human PBMC:CC50=40.27 µM;##Human embryonic kidney HEK293T cells:CC50=25.31 µM;##TZM-bl cells:CC50=12.34 μM;##MT-4 cells:CC50=19.65 μM;##C8166 cells:CC50=19.19 μM;##U937 cells:CC50=9.97 μ membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30657 LEANIEELLKKAEEQQKKNEEELKKLEKX 29 LP-86 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=0.43±0.03 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=4.78±0.69 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=7.24±1.36 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=4.91 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.003±0 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.003-0.17 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.014-0.026 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.005-0.006 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=12.27 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 29 is Cys-Chol(cholesterol) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30658 WEQKIEELLKKAEEQQKKNEEELKX 25 LP-93 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=6.27±1.26 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=6.55±1.97 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=7.57±0.62pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=9.89 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.006±0.001 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.012-2.17 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=1.244-3.514 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.013-0.773 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=14.51pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 25 is Lys-Chol(cholesterol) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30659 IEELLKKAEEQQKKNEEELKKLEX 24 LP-94 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=1.75±0.23 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=5.90±1.80 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=15.69±1.97 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=6.54 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.004±0.002 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.004-2.295 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=0.019-0.027 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.011-0.018 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=27.36 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 24 is Lys-Chol(cholesterol) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30660 IEELLKKAEEQQKKNEEELKX 21 LP-95 P03377 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide had extremely potent activity to block HIV envelope-mediated cell-cell fusion,showing a greatly increased potency relative to its inhibition on virus infection. Besides, it efficiently bounds to both the cellular and viral membranes to exert their antiviral activities. [Ref.30867304]HIV-1 NL4-3(X4):inhibition of virus replication in TZM-bl cells(IC50=199.92±32.69 pM);##HIV-1 JR-CSF(R5):inhibition of virus replication in TZM-bl cells(IC50=24.36±0.15 pM);##HIV-1 89.6(R5X4):inhibition of virus replication in TZM-bl cells(IC50=4781.17±699.33 pM);##HIV-1 pseudovirus:inhibition of pseudovirus infection in TZM-bl cells(IC50=148.88 pM);##T-20 sensitive HIV-1(NL4-3D36G):inhibition of virus infection in TZM-bl cells(IC50=0.067±0.026 nM);##T-20 resistant HIV-1 NL4-3(WT,I37T,V38A,V38 M,Q40H,N43K,G36S/V38 M,I37T/N43K,V38A/N42T):inhibition of virus infection in TZM-bl cells(IC50=0.39-408.556 nM);##HIV-2(ROD,ST):inhibition of virus infection in TZM-bl cells(IC50=2.857-13.512 nM);##SIV(239,PBJ):inhibition of virus infection in TZM-bl cells(IC50=0.556-0.862 nM);##HIV-1(1A,2B,1C,1G,1A/C,1A/E,1B/C subtype):inhibition of cell-cell fusion between HEK293T cells and TZM-bl cells(IC50=29.84 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'X' at position 21 is Lys-Chol(cholesterol) L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity. DRAMP30661 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=1.5 ± 0.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30662 XEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 42 X- C41(C41 N teminus-PEG conjugation) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=7.2 ± 0.7 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30663 XEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 42 X- C41(C41 N teminus-PEG conjugation) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=11.2± 1.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30664 EWDXEINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [R4X](R4C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.1± 1.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 4 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30665 EWDXEINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [R4X](R4C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=8.7± 1.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 4 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30666 EWDREINNYTXLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S11X](S11C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.4± 0.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 11 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30667 EWDREINNYTXLIHSLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S11X](S11C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.9± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 11 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30668 EWDREINNYTSLIHXLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S15X](S15C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.1± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 15 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30669 EWDREINNYTSLIHXLIEESQNQQEKNEQELLELDKWASLW 41 C41 [S15X](S15C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.0± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 15 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30670 EWDREINNYTSLIHSLIXESQNQQEKNEQELLELDKWASLW 41 C41 [E18X](E18C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.5± 1.0 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 18 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30671 EWDREINNYTSLIHSLIXESQNQQEKNEQELLELDKWASLW 41 C41 [E18X](E18C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.9± 0.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 18 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30672 EWDREINNYTSLIHSLIEESQXQQEKNEQELLELDKWASLW 41 C41 [N22X](N22C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=4.2± 0.9 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 22 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30673 EWDREINNYTSLIHSLIEESQXQQEKNEQELLELDKWASLW 41 C41 [N22X](N22C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.1± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 22 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30674 EWDREINNYTSLIHSLIEESQNQQEKNEXELLELDKWASLW 41 C41 [Q29X](Q29C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.2± 0.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 29 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30675 EWDREINNYTSLIHSLIEESQNQQEKNEXELLELDKWASLW 41 C41 [Q29X](Q29C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=5.5± 0.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 29 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30676 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWX 42 C41 -X(C41 C teminus-PEG conjugation) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=10.9± 2.2 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 42 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30677 EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWX 42 C41 -X(C41 C teminus-PEG conjugation) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50=43.3± 14.8 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 42 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30678 EWDREINNYTSLIHSLIEEXQNQQEKNEQELLELDKWASLW 41 C41 [S20X](S20C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50>400 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 20 indicates PEG750-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30679 EWDREINNYTSLIHSLIEEXQNQQEKNEQELLELDKWASLW 41 C41 [S20X](S20C) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide have been shown to be effective inhibitors to prevent virus–host cell membrane fusion. [Ref.22770564]HIV-1:inhibition of cell-cell fusion between CHO-WT cells and K652 cells(IC50>400 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 20 indicates PEG2000-Cys. L No cytotoxicity information or data found in the reference(s) presented in this entry envelope glycoprotein(gp41) 22770564 Bioconjug Chem. 2012 Aug 15;23(8):1648-60. Danial M, van Dulmen TH, Aleksandrowicz J, Pötgens AJ, Klok HA. Site-specific PEGylation of HR2 peptides: effects of PEG conjugation position and chain length on HIV-1 membrane fusion inhibition and proteolytic degradation. DRAMP30680 RMKQIEDKIEEIESKQKKIENEIARIKKLLQLTVWDIKQLQARIL 45 IQN17[G572D] No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=15±5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30681 RMKQIEDKIEEIESKIKKIENEIARIKKLLQLTVWGIKQLQARIL 45 IIN17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.14±0.05 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30682 KIEEIESKQKKIENEIARIKKLLQLTVWGIKQLQARIL 38 IQ22N17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=1.4±0.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30683 KIEEIESKIKKIENEIARIKKLLQLTVWGIKQLQARIL 38 II22N17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=0.16±0.01 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30684 KQKKIENEIARIKKLLQLTVWGIKQLQARIL 31 IQ15N17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=5.5±1..5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30685 KIKKIENEIARIKKLLQLTVWGIKQLQARIL 31 II15N17 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HIV-1 entry by inhibiting the fusion between virus and cell membrane. [Ref.11572974]HIV-1:inhibition of cell-cell fusion between 293T cells and HOS-CD4/fusion cells(IC50=2.1±0.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 11572974 Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11187-92. Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. DRAMP30686 ALWKTMLKKLGTMALHAGKAALGAAADTI 29 Dermaseptin-S1 (1-29) P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=1.7 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50=20 µM;293TT(embryonic human culture cells):CC50=40 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30687 ALWTTMLKKLGKMALHAGKAALGAAADTI 29 Dermaseptin-S1 (1-29)[K4T,T12K] P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=1.3 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50=20 µM;293TT(embryonic human culture cells):CC50=40 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30688 ALWKTMLKKLGTMALHAGK 19 Dermaseptin-S1 (1-19) P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=9 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50=80 µM;293TT(embryonic human culture cells):CC50=80 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30689 ALXKTMLKKLGTMAL 15 Dermaseptin-S1 (1-15)[W31NAL] P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=2.7 µM). [Ref.20718719]human red cells:HC50=75 µM. Linear Free Amidation The 'X' at position 3 indicates Nal (3-[1-naphthyl]alanine). L [Ref.20718719]Vero cells:CC50=50 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30690 ALHKTMLKKLGTMAL 15 Dermaseptin-S1 (1-15)[W3H] P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=5 µM). [Ref.20718719]human red cells:HC50=100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50>100 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30691 KALXKTMLKKLGTMAL 16 K-Dermaseptin-S1 (1-15)[W31NAL] P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=5 µM). [Ref.20718719]human red cells:HC50=80 µM. Linear Free Amidation The 'X' at position 4 indicates Nal (3-[1-naphthyl]alanine). L [Ref.20718719]Vero cells:CC50=50 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30692 ALWKTMLKKLGTMA 14 Dermaseptin-S1 (1-14) P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=10.5 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50=85 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30693 ALWKTMLKKLGTM 13 Dermaseptin-S1 (1-13) P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=10 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50=100 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30694 ALWKTMLKKLGT 12 Dermaseptin-S1 (1-12) P24302 Herpesviridae Not found Synthetic construct(derived from Dermaseptin-S1) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.20718719]HSV-1:inhibition of virus infection in Vero cells(IC50=100 µM). [Ref.20718719]human red cells:HC50>100 µM. Linear Free Amidation L [Ref.20718719]Vero cells:CC50>100 µM;293TT(embryonic human culture cells):CC50>100 µM. Not found 20718719 APMIS. 2010 Sep 1;118(9):674-80. Savoia D, Donalisio M, Civra A, Salvadori S, Guerrini R. In vitro activity of dermaseptin S1 derivatives against genital pathogens. DRAMP30695 EMTWEEWEKKIEEYTKKIEEILKKSQNQQIDL 32 HP23-E6-IDL No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: It was a fusion inhibitor and inhibits cell-cell fusion [Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=338 pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=1.14 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=813 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=748-1543 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=349-1423 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=699-4937 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. membrane 30901967 Molecules. 2019 Mar 21;24(6):1134. Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. DRAMP30696 EMTWEEWEKKIEEYIKKIEEILKKSQNQQIDL 32 YIK(625-656) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: It was a fusion inhibitor and inhibits cell-cell fusion [Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=275pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=1.12 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=640 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=627-1423 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=460-1490 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=856-5286 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. membrane 30901967 Molecules. 2019 Mar 21;24(6):1134. Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. DRAMP30697 EMTWEEWEKKIEEYIKKIEEILKKSQNQQIDLGSGX 36 YIK-C16(625-656) No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: It was a fusion inhibitor and inhibits cell-cell fusion [Ref.30901967]HIV-1IIIB(X4 virus):inhibition of virus infection in MT-2 cells(IC50=76 pM);inhibition of cell-cell fusion between H9/IIIB cells and MT-2 cells(IC50=0.55 nM);##HIV-1Bal(R5 virus):inhibition of virus infection in MT-2 cells(IC50=61 pM);##HIV-1 NL4-3 D36G(6 T-20 resistant strains, WT,V38A,V38A/N42D,V38E/N42S,V38A/N42T,N42T/N43K):inhibition of virus infection in MT-2 cells(IC50=40-179 pM);##HIV-1 LAI (7 T2635-Resistant Strains,WT,A6V,Q66R,K90E,K154Q,Q79E/N126K,K90E/N126K):inhibition of virus infection in MT-2 cells(IC50=65-106 pM);##HIV-1 NL4-3 (5 HP23-Resistant Strains,WT,E49K,E49K/N126K,D36G/E49K/N126K,L34S/D36G/E49K/E136G):inhibition of virus infection in MT-2 cells(IC50=65-188 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 36 indicates PEG4-Lys-C16(Palmitic Acid). L [Ref.30901967]No cytotoxicity against MT-2 or M7 cells at the concentrations as high as 8 μM. membrane 30901967 Molecules. 2019 Mar 21;24(6):1134. Su S, Rasquinha G, Du L, Wang Q, Xu W, Li W, Lu L, Jiang S. A Peptide-Based HIV-1 Fusion Inhibitor with Two Tail-Anchors and Palmitic Acid Exhibits Substantially Improved In Vitro and Ex Vivo Anti-HIV-1 Activity and Prolonged In Vivo Half-Life. DRAMP30698 PACQDFLGAMIHLKAKTNISIR 22 3(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(28% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30699 LKAKTNISIREGPTLGNWAR 20 4(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(24% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30700 EGPTLGNWAREIWATLFKKA 20 5(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(100% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30701 EIWATLFKKATRQCRRGRIW 20 6(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(100% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30702 TRQCRRGRIWKRWNETITGP 20 7(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(94% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30703 SGCANNTCYNAnti-VSVIVPDYQC 20 9(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(24% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30704 YLDRVDTWLQGKINISLCLT 20 11(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(9% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30705 GKINISLCLTGGKMLYNKVT 20 12(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(10% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30706 GGKMLYNKVTKQLSYCTDPL 20 13(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30707 KQLSYCTDPLQIPLINYTFG 20 14(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(15% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30708 PNQTCMWNTSQIQDPEIPKC 20 16(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30709 QIQDPEIPKCGWWNQMAYYN 20 17(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(2% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30710 FHCQRTQSQPGSWFRAISSWKQ 22 20(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(4% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30711 GSWFRAISSWKQRNRWEWRPDF 22 21(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30712 KQRNRWEWRPDFKSKKVKISLPC 23 22(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30713 KSKKVKISLPCNSTKNLTFA 20 23(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(10% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30714 CNSTKNLTFAMRSSGDYGEV 20 24(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(25% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30715 MRSSGDYGEVTGAWIEFGCH 20 25(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(27% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30716 TGAWIEFGCHRNKSNLHTEA 20 26(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30717 RNKSNLHTEARFRIRCRAnti-WNV 20 27(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(2% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30718 RFRIRCRAnti-WNVGSDTSLIDTC 20 28(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(40% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30719 GSDTSLIDTCGNTPNVSGAN 20 29(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(12% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30720 PVDCTMYSNKMYNCSLQNGF 20 31(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(8% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30721 MYNCSLQNGFTMKVDDLIVH 20 32(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(33% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30722 TMKVDDLIVHFNMTKAVEMV 20 33(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(25% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30723 FNMTKAVEMVNIAGNWSCTS 20 34(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(15% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30724 NIAGNWSCTSDLPSSWGYMN 20 35(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(22% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30725 CTSDLPSSWGYMNCNCTNSSSS 22 36(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(5% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30726 CNCTNSSSSYSGTKMACPSNRG 22 37(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30727 SGTKMACPSNRGILRNWYNP 20 38(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(52% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30728 RGILRNWYNPFAGLRQSLEQ 20 39(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30729 VAGLRQSLEQYQVVKQPDYL 20 40(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(48% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30730 YQVVKQPDYLLVPEEVMEYK 20 41(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(38% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30731 PDYLLVPEEVMEYKPRRKRAAI 22 42(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(54% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30732 YKPRRKRAAIHVMLALATVLSI 22 43(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(52% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30733 HVMLALATVLSIAGAGTGATAI 22 44(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(58% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30734 AGAGTGATAIGMVTQYHQVL 20 45(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30735 GMVTQYHQVLATHQEAIEKV 20 46(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(43% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30736 ATHQEAIEKVTGALKINNLR 20 47(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(44% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30737 TGALKINNLRLVTLEHQVLV 20 48(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(73% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30738 LVTLEHQVLVIGLKVEAMEK 20 49(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(45% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30739 IGLKVEAMEKFLYTAFAMQE 20 50(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(74% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30740 FLYTAFAMQELGCNQNQFFC 20 51(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(18% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30741 LGCNQNQFFCKIPLELWTRY 20 52(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(21% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30742 NMTINQTIWNHGNITLGEWY 20 54(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(4% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30743 HGNITLGEWYNQTKDLQQKF 20 55(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(35% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30744 NQTKDLQQKFYEIIMDIEQN 20 56(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(68% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30745 YEIIMDIEQNNVQGKTGIQQ 20 57(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(37% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30746 NVQGKTGIQQLQKWEDWVRW 20 58(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(96% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30747 LQKWEDWVRWIGNIPQYLKG 20 59(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(98% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30748 IGNIPQYLKGLLGGILGIGL 20 60(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(60% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30749 LLGGILGIGLGVLLLILCLP 20 61(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(88% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30750 GVLLLILCLPTLVDCIRNCI 20 62(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(32% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30751 TLVDCIRNCIHKILGYTVIA 20 63(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(9% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30752 HKILGYTVIAMPEVEGEEIQ 20 64(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(8% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30753 MPEVEGEEIQPQMELRRNGR 20 65(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(7% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30754 PQMELRRNGRQCGMSEKEEE 20 66(derived from FIV envelope glycoprotein ) P16090 Retroviridae Not found Synthetic construct(derived from FIV envelope glycoprotein (gE)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The machanism might be peptide bound the surface of FIV permissive cells and were highly active in blocking FIV infection when administered before the virus. [Ref.8661378]Feline immunodeficiency virus (FIV):inhibition of virus replication in Crandell feline kidney (CrFK) fibroblastoid cells(6% inhibition at 16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Syncytium formation 8661378 Virology. 1996 Jun 15;220(2):274-84.  Lombardi S, Massi C, Indino E, La Rosa C, Mazzetti P, Falcone ML, Rovero P, Fissi A, Pieroni O, Bandecchi P, Esposito F, Tozzini F, Bendinelli M, Garzelli C. Inhibition of feline immunodeficiency virus infection in vitro by envelope glycoprotein synthetic peptides. DRAMP30755 NFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSD 35 T-106 P69353 Paramyxoviridae Not found Synthetic construct(derived from Respiratory syncytial virus(RSV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Respiratory syncytial virus(RSV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30756 YTPNDITLNNSVALDPIDISIELNKAKSDLEESKE 35 T-189 P69353 Paramyxoviridae Not found Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Human parainfluenza virus type 3(HPIV3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30757 TPNDITLNNSVALDPIDISIELNKAKSDLEESKEW 35 T-190 P69353 Paramyxoviridae Not found Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30758 PNDITLNNSVALDPIDISIELNKAKSDLEESKEWI 35 T-191 P69353 Paramyxoviridae Not found Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30759 NDITLNNSVALDPIDISIELNKAKSDLEESKEWIR 35 T-192 P69353 Paramyxoviridae Not found Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30760 DITLNNSVALDPIDISIELNKAKSDLEESKEWIRR 35 T-193 P69353 Paramyxoviridae Not found Synthetic construct(derived from Human parainfluenza virus type 3(HPIV-3) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]Human parainfluenza virus type 3(HPIV-3):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30761 DAVYLHRIDLGPPISLERLDVGTNLQNAIAKLEDA 35 T-253 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30762 AVYLHRIDLGPPISLERLDVGTNLQNAIAKLEDAK 35 T-254 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50>100 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30763 VYLHRIDLGPPISLERLDVGTNLQNAIAKLEDAKE 35 T-255 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=85.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30764 YLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKEL 35 T-256 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=90.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30765 LHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELL 35 T-257 P69353 Paramyxoviridae, Retroviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MeV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.5 μg/ml);inhibition of cell-cell fusion in HEp2 cell(EC50=0.068 μg/ml);##Human parainfluenza virus type 3(HPIV-3):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##Respiratory syncytial virus(RSV):inhibition of cell-cell fusion in HEp2 cell(EC50>25 μg/ml);##HIV-1 LAI:inhibition of cell-cell fusion in HEp2 cell(EC50>50 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30766 HRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLE 35 T-258 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=2.2 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30767 RIDLGPPISLERLDVGTNLGNAIAKLEDAKELLES 35 T-259 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30768 IDLGPPISLERLDVGTNLGNAIAKLEDAKELLESS 35 T-260 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=4.9 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30769 DLGPPISLERLDVGTNLGNAIAKLEDAKELLESSD 35 T-261 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=5.7 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30770 LGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQ 35 T-262 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=6.5 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30771 GPPISLERLDVGTNLGNAIAKLEDAKELLESSDQI 35 T-263 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=10.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30772 PPISLERLDVGTNLGNAIAKLEDAKELLESSDQIL 35 T-264 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=1.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30773 PISLERLDVGTNLGNAIAKLEDAKELLESSDQILR 35 T-265 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=3.1 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30774 ISLERLDVGTNLGNAIAKLEDAKELLESSDQILRS 35 T-266 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=13.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30775 SLERLDVGTNLGNAIAKLEDAKELLESSDQILRSM 35 T-267 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=12.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30776 LERLDVGTNLGNAIAKLEDAKELLESSDQILRSMK 35 T-268 P69353 Paramyxoviridae Not found Synthetic construct(derived from measles virus(MV) fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.8700906]measles virus(MV):protection of HEp2 cell from viral cytopathic effect(CPE)(EC50=7.3 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.8700906]No significant cytotoxic against HEp2 cells(CC50>100 μM). Not found 8700906 Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2186-91. Lambert DM, Barney S, Lambert AL, Guthrie K, Medinas R, Davis DE, Bucy T, Erickson J, Merutka G, Petteway SR Jr. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion.  DRAMP30777 DDSVVCAAMSYSYA 14 P1(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30778 DDSVVCAAMSYSFA 14 P2(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(29% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30779 DDSVVCAAMSYSHA 14 P3(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30780 DDSVVSAAMSYSYA 14 P4(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±9% inhibition at 1 µM; 47±1% inhibition at 3 µM; 89±6% inhibition at 10 µM; IC50=3.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30781 DDSVVSAAMSYSFA 14 P5(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30782 DDSVVAAMSYSYA 13 P7(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30783 DDSVVAAMSYSFA 13 P8(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30784 DDSVVAAMSYSHA 13 P9(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30785 ADLEVVAATYVLVA 14 P10(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 6±11% inhibition at 1 µM;27±5% inhibition at 3 µM; 75±1% inhibition at 10 µM; IC50=6.3µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30786 ADLEVVAATFVLVA 14 P11(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(-2±7% inhibition at 1 µM; 29±5% inhibition at 3 µM; 83±5% inhibition at 10 µM; IC50=5.72 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30787 ADLEVVAATHVLVA 14 P12(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 11±16% inhibition at 1 µM; 77±3% inhibition at 3 µM; 95±1% inhibition at 10 µM; IC50=2.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30788 ADLEVVAATYV 11 P13(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30789 KKKKVVAATYVLVA 14 P15(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(30% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30790 DDDEVVAATYVLVA 14 P17(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30791 ADLEVVAATYVDDD 14 P19(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30792 ADLEVVAATYVDVA 14 P20(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 18±21% inhibition at 1 µM; 75±1% inhibition at 3 µM; 96±1% inhibition at 10 µM; IC50=2.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30793 ADLEVVAATYVLDA 14 P21(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30794 ADLEVVAATYVLVD 14 P22(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(38% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30795 ADLEVVAATYVDDA 14 P23(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(20% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30796 ADLEVVAATYVLDD 14 P24(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 5±4% inhibition at 1 µM; 26±4% inhibition at 3 µM; 65±3% inhibition at 10 µM; IC50=7.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30797 ADLEVVAATYVDVD 14 P25(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30798 KKKKVVAATYVKKA 14 P27(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30799 KKKKVVAATYFFFA 14 P30(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30800 KKKKVVAATYFLVA 14 P31(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30801 KKKKVVAATYVLVF 14 P33(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30802 KKKKVVAATYVLFA 14 P34(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30803 KKKKVVAATYKKVA 14 P37(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30804 AKLKVVAATYVLKK 14 P38(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30805 KKKKVVAATYKKKK 14 P42(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30806 ADLEVVAATYVKKK 14 P44(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30807 ADLEVVAATYKKKK 14 P45(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30808 ADLEVVAATYAAAA 14 P47(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30809 KDLKVVAATYVKKK 14 P48(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(21% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30810 KKKKAVAATYVLV 13 P49(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(59% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30811 KKKKVAAATYVLV 13 P50(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±1% inhibition at 1 µM; 51±10% inhibition at 3 µM; 74±1% inhibition at 10 µM; IC50=3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30812 KKKKVVAAAYVLV 13 P51(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30813 KKKKVVAATAVLV 13 P52(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30814 KKKKVVAATYVAV 13 P54(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(21% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30815 KKKKVVAATYVLA 13 P55(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30816 KKKKVLAATYVLV 13 P57(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30817 KKKKVVLATYVLV 13 P58(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 21±8% inhibition at 1 µM; 30±5% inhibition at 3 µM; 61±15% inhibition at 10 µM; IC50=7.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30818 KKKKVVAALYVLV 13 P60(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30819 KKKKVVAATYLLV 13 P61(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30820 KKKKVVAATYVLL 13 P62(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(25% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30821 KKKKFVAATYVLV 13 P63(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 32±7% inhibition at 1 µM; 35±8% inhibition at 3 µM; 61±6% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30822 KKKKVFAATYVLV 13 P64(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30823 KKKKVVFATYVLV 13 P65(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(34% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30824 KKKKVVAFTYVLV 13 P66(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(23% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30825 KKKKVVAAFYVLV 13 P67(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30826 KKKKVVAATFVLV 13 P68(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(28% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30827 KKKKVVAATYFLV 13 P69(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30828 KKKKVVAATYVFV 13 P70(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30829 KKKKVVAATYVLF 13 P71(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30830 KKKKEVAATYVLV 13 P72(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30831 KKKKVVAETYVLV 13 P75(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30832 KKKKVVAAEYVLV 13 P76(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30833 KKKKVVAATEVLV 13 P77(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30834 KKKKVKAATYVLV 13 P82(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(25% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30835 KKKKVVKATYVLV 13 P83(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 26±12% inhibition at 1 µM; 37±10% inhibition at 3 µM; 63±2% inhibition at 10 µM; IC50=6.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30836 KKKKVVAKTYVLV 13 P84(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30837 KKKKTVAATYVLV 13 P89(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(27% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30838 KKKKVTAATYVLV 13 P90(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 15±12% inhibition at 1 µM; 44±3% inhibition at 3 µM; 77±6% inhibition at 10 µM; IC50=4.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30839 KKKKVVTATYVLV 13 P91(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30840 KKKKVVATTYVLV 13 P92(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30841 KKKKVVAATTVLV 13 P93(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2223% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30842 KKKKVVAATYVLT 13 P96(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30843 KKKKVVGATYVLV 13 P99(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30844 KKKKVVAGTYVLV 13 P100(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(30% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30845 KKKKVVAAGYVLV 13 P101(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30846 KKKKVVAATGVLV 13 P102(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(26% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30847 KKKKVVAATYVGV 13 P104(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30848 KKKKVVAATYVLG 13 P105(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(13% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30849 KKKKVVAATYVLV 13 P106(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(17% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30850 KKKKPVAATYVLV 13 P107(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(24% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30851 KKKKVPAATYVLV 13 P108(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30852 KKKKVVAATYVPV 13 P113(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(10% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30853 KKKKVVLATLVLV 13 P116(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(5% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30854 KKKKLVLPFLFFV 13 P119(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(6% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30855 KKKKLLAPFLFFV 13 P120(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30856 KKKKLLLAFLFFV 13 P121(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30857 KKKKLLLPTLFFV 13 P122(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30858 KKKKLVLATYVLV 13 P126(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30859 KKKKLVAAFYVLV 13 P128(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30860 KKKKLVAATYVFV 13 P129(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30861 KKKKLVAATYVLF 13 P130(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30862 KKKKVLAPTYVLV 13 P132(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(1% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30863 KKKKVVLAFYVLV 13 P138(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(10% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30864 KKKKVVAPFYVLV 13 P140(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30865 KKKKVVAPTLVLV 13 P141(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30866 KKKKVVAPTYFLV 13 P142(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30867 KKKKVVAPTYVLF 13 P144(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30868 KKKKVVAAFLVLV 13 P145(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(20% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30869 KKKKVVAAFYFLV 13 P146(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(7% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30870 KKKKVVAAFYVLF 13 P148(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30871 KKKKVVAATLVLF 13 P151(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30872 KKKKVLLPFLFFF 13 P154(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(2% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30873 KKKKLVLPFLFFF 13 P155(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(12% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30874 KKKKLLAPFLFFF 13 P156(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30875 KKKKLLLAFLFFF 13 P157(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30876 KKKKLLLPFYFFF 13 P159(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(24% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30877 KKKKLLLPFLFLF 13 P161(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30878 KKKKLLLPFLFFF 13 P162(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(19% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30879 KKKKVVLPFLFFF 13 P163(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( -2±1% inhibition at 1 µM; 29±4% inhibition at 3 µM; 69±9% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30880 KKKKLVAPFLFFF 13 P164(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(15% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30881 KKKKLLAAFLFFF 13 P165(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 29±5% inhibition at 1 µM; 28±9% inhibition at 3 µM; 61±17% inhibition at 10 µM; IC50=7.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30882 KKKKLLLATLFFF 13 P166(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(16% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30883 KKKKLLLPTYFFF 13 P167(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30884 KKKKLLLPFLVLF 13 P169(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(4% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30885 KKKKVLAPFLFFF 13 P170(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30886 KKKKVLLPFYFFF 13 P172(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(27% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30887 KKKKLVLAFLFFF 13 P175(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30888 KKKKLVLPTLFFF 13 P176(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(29% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30889 KKKKLVLPFYFFF 13 P177(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(14% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30890 KKKKLVLPFLLFF 13 P178(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(18% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30891 KKKKLVLPFLFVF 13 P179(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 14±6% inhibition at 1 µM; 34±11% inhibition at 3 µM; 55±11% inhibition at 10 µM; IC50=8.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30892 KKKKLLAPFLVFF 13 P180(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(9% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30893 KKKKLLLAFYFFF 13 P181(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30894 KKKKLLLAFLFLF 13 P182(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(8% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30895 KKKKLLLPTLVFF 13 P183(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(3% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30896 KKKKLLLPFYFLF 13 P185(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)(22% inhibition at 3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30897 AKDLEVVTSTYVLVEA 16 P189(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 5±7% inhibition at 1 µM; 74±6% inhibition at 3 µM; 96±3% inhibition at 10 µM; IC50=2.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30898 AKDLEVVCSTYVLVEA 16 P190(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 24 ±15% inhibition at 1 µM; 86 ±3% inhibition at 3 µM; 99 ±2% inhibition at 10 µM; IC50=1.8 µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30899 AECVVSCSMSYTKA 14 P197(derived from HCV polyprotein) P26662 Flaviviridae Not found Synthetic construct(derived from Hepatitis C virus(HCV) polyprotein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. The peptide was demonstrated that can indeed block the activity of NS3 and thus inhibit HCV replication [Ref.14694985]Hepatitis C virus(HCV):inhibition of activation of NS3-6K protease(50 nM)( 7±7% inhibition at 1 µM; 29±6% inhibition at 3 µM; 66±3% inhibition at 10 µM; IC50=7 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NS3 protease 14694985 Antivir Chem Chemother. 2003 Sep;14(5):225-33. Portal-Núñez S, González-Navarro CJ, García-Delgado M, Vizmanos JL, Lasarte JJ, Borrás-Cuesta F. Peptide inhibitors of hepatitis C virus NS3 protease.  DRAMP30900 swlrdiwdwicevlsdfk 18 2(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.32 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30901 SWLRDIWDWICEVLSD 16 3(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.98 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30902 SWLRDIWDWICEV 13 5(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30903 SWLRDIWDWICE 12 6(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30904 SWLRDIWDWI 10 7(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30905 SWLRDIWD 8 8(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30906 LRDIWDWICEVLSDFK 16 9(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30907 DIWDWICEVLSDFK 14 10(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30908 WDWICEVLSDFK 12 11(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30909 WICEVLSDFK 10 12(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30910 CEVLSDFK 8 13(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30911 SGSWLRDIWDWICEVLSDFK 20 14(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30912 GSWLRDIWDWICEVLSDFK 19 15(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.51 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30913 SWLRDIWDWICEVLSDFKT 19 16(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30914 SWLRDIWDWICEVLSDFKTW 20 17(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.51 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30915 SWRLIDWDWICEVLSDFK 18 18(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=4.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30916 SWRLDIWDWICESVLDFK 18 19(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30917 VLDLIYSLHKQINRGLKKIVL 21 22(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50>36 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30918 KFDSLVECIWDWIDRLWS 18 23(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.85 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30919 KWLCRIWSWISDVLDDFE 18 25(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30920 SIWRDWVDLICEFLSDWK 18 26(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.40 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30921 SWLRDVWDWICTVLTDFK 18 27(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=3.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30922 SWLRDVWDWVCTILTDFK 18 28(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30923 DWLRIIWDWVCSVVSDFK 18 29(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.55 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30924 SWLWEVWDWVLHVLSDFK 18 30(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30925 TWLRAIWDWVCTALTDFK 18 31(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=7.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30926 SWLRDVWDWVCTVLSDFK 18 32(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=3.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30927 SWLRDIWDWISEVLSDFK 18 33[11S](derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=13.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30928 SWLRDIWDWIREVLSDFK 18 34[11R](derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=12.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30929 SWLRDIWDWIEEVLSDFK 18 35[11E](derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=13.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30930 SWLDDIWDWICEVLSDFE 18 36(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30931 SWLRDIWDWICKVLSDFK 18 38(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=6.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30932 SWLDRIWRWICKVLSRFE 18 39(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=1.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30933 SWLRDIWRWICKVLSRFK 18 40(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.84 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30934 SWLRRIWRWICKVLSRFK 18 41(derived from HCV C5A) P26664 Flaviviridae Not found Synthetic construct(derived from HCV non-structural protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide destabilizes viral structural integrity and has viral membranolytic activity.It interacts with the viral membrane to disrupt its integrity, release viral capsids, and expose the viral genome to exonucleases for degradation. [Ref.18287023]Hepatitis C virus(HCV):inhibition of HCV infection in Huh-7.5.1 cells(IC50=0.89 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 18287023 Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3088-93. Cheng G, Montero A, Gastaminza P, Whitten-Bauer C, Wieland SF, Isogawa M, Fredericksen B, Selvarajah S, Gallay PA, Ghadiri MR, Chisari FV. A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro. DRAMP30935 RTQRRGRTGRGKPGIYR 17 HCVA(1484-1500) P26664 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=27.1±2.4 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=37.1±3.9 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=49.8±4.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30936 STQRRGRTGRGRRGIYR 17 HCVB(1484-1500) P26663 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=24.3±1.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=33.6±3.5 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=47.2±4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30937 RRGRTGRGRRGIYR 14 HCV(1487-1500) P26663 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=0.2±0.01 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=2.7±0.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=21.1±2.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30938 RTGRGRRGIYR 11 HCV(1490-1500) P26663 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=34.6±3.2 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=106±6.1 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=322±9.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30939 RGRRGIYR 8 HCV(1493-1500) P26663 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=313±11.3 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=397±10.6 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30940 RGIYR 5 HCV(1496-1500) P26663 Flaviviridae Not found Synthetic construct(derived from HCV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30941 SQVGD 5 WNV(1968-1972) P06935 Flaviviridae Not found Synthetic construct(derived from WNV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30942 RNPSQVGD 8 WNV(1965-1972) P06935 Flaviviridae Not found Synthetic construct(derived from WNV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=383±12.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=437±13.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30943 RIGRNPSQVGD 11 WNV(1962-1972) P06935 Flaviviridae Not found Synthetic construct(derived from WNV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=417±17.6 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=285±8.1 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=334±12.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30944 RRGRIGRNPSQVGD 14 WNV(1959-1972) P06935 Flaviviridae Not found Synthetic construct(derived from WNV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=169±6.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=156±6.9 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=191±7.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30945 AAQRRGRIGRNPSQVGD 17 WNV(1956-1972) P06935 Flaviviridae Not found Synthetic construct(derived from WNV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=358±13.2 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30946 NQVGD 5 JEV(1971-1975) P27395 Flaviviridae Not found Synthetic construct(derived from JEV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30947 RNPNQVGD 8 JEV(1968-1975) P27395 Flaviviridae Not found Synthetic construct(derived from JEV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50>500 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30948 RVGRNPNQVGD 11 JEV(1965-1975) P27395 Flaviviridae Not found Synthetic construct(derived from JEV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=374±12.8 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=448±14.3 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30949 RRGRVGRNPNQVGD 14 JEV(1962-1975) P27395 Flaviviridae Not found Synthetic construct(derived from JEV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=196±9.4 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50=215±7.2 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50=253±6.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30950 AAQRRGRVGRNPNQVGD 17 JEV(1959-1975) P27395 Flaviviridae Not found Synthetic construct(derived from JEV NS3 helicase protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The intact enzymatic properties of NS3 are necessary for the virus propagation,which possesses numerous enzymatic activities including RNA stimulated nucleoside triphosphatase (NTPase) and RNA helicase activities. The peptides inhibited the NTPase/helicase by a direct interaction with the enzyme highly probably by a competitive mechanism. [Ref.18479669]Hepatitis C virus (HCV): inhibition of HCV helicase activity(IC50=442±17.7 μM);##West Nile virus (WNV): inhibition of WNV helicase activity(IC50>500 μM);##Japanese encephalitis virus (JEV):inhibition of JEV helicase activity(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented NTPase/helicase 18479669 Biochem Pharmacol. 2008 Jul 1;76(1):28-38.  Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. Viral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). DRAMP30951 TTPKFTVAWDWVPKR 15 gB64(gB346-360) P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=85 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30952 KTTSSIEFARLQFTY 15 gB94(496-510) P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=6.5±1.3 µM);inhibition of virus entry in Vero cells(EC50>200 µM);inhibition of virus infection in Vero cells(EC50=165.0±71.9 µM);ability of inactive virus(EC50=125±11.4 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30953 GHRRYFTFGGGYVYF 15 gB122(636-650) P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=15.0±2.2 µM);inhibition of virus entry in Vero cells(EC50=17.6±2.6 µM);inhibition of virus infection in Vero cells(EC50=71.5±17.4 µM);ability of inactive virus(EC50=118±11.6 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30954 Anti-HeVVPLEVYTRHEIK 15 gB131(681-695) P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=18.7±2.70 µM);inhibition of virus entry in Vero cells(EC50=12.2±6.56 µM);inhibition of virus infection in Vero cells(EC50>200 µM);ability of inactive virus(EC50>200 µM);inhibition of virus attachment on Vero cells(EC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.19104014]Not cytotoxic for Vero cells up to 200 µM. Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30955 HRRYFTFGGGYVYF 14 gB122(637-650) P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=31.2 ± 5.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30956 GHRAYFTFGGGYVYF 15 gB122R4A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=26.4 ± 13.5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30957 GHRRAFTFGGGYVYF 15 gB122Y5A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=119.2 ± 26.6 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30958 GHRRYATFGGGYVYF 15 gB122F6A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=67.6 ± 8.1 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30959 GHRRYFTAGGGYVYF 15 gB122F8A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=37.5 ± 4.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30960 GHRRYFTFGAGYVYF 15 gB122G10L P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=25.1 ± 4.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30961 GHRRYFTFGGGYVAF 15 gB122Y14A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=58.0 ± 5.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30962 GHRRYFTFGGGYVYA 15 gB122F15A P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=48.6 ± 6.2 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30963 RYFTFGGGYVYF 12 gB122Δ1-3 P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=34.9 ± 1.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30964 TFGGGYVYF 9 gB122Δ1-6 P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30965 GHRRYFTFGGGY 12 gB122Δ13-15 P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50=91.4± 9.8 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30966 GHRRYFTFG 9 gB122Δ10-15 P06437 Herpesviridae Not found Synthetic construct(derived from HSV-1 B glycoprotein (gB)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19104014]Herpes simplex virus type 1(HSV-1):comprehensive antiviral activity(EC50>100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 19104014 Antimicrob Agents Chemother. 2009 Mar;53(3):987-96. Akkarawongsa R, Pocaro NE, Case G, Kolb AW, Brandt CR. Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection. DRAMP30967 MDVNPTLLFLKVPAQNAISTTFPYT 25 FluA-PB1(1-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=1.80 ±0.49 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30968 VNPTLLFLKVPAQNAISTTFPYT 23 FluA-PB1(3-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=661.77 ±22.08 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30969 PTLLFLKVPAQNAISTTFPYT 21 FluA-PB1(5-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=483.20 ±51.98 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30970 LLFLKVPAQNAISTTFPYT 19 FluA-PB1(7-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30971 FLKVPAQNAISTTFPYT 17 FluA-PB1(9-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30972 KVPAQNAISTTFPYT 15 FluA-PB1(11-25) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30973 MDVNPTLLFLKVPAQNAIST 20 FluA-PB1(1-20) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=33.80 ±5.53 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30974 MDVNPTLLFLKVPAQNAI 18 FluA-PB1(1-18) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=29.45 ±5.16 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30975 MDVNPTLLFLKVPAQN 16 FluA-PB1(1-16) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=45.86 ±4.22 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30976 MDVNPTLLFLKVPA 14 FluA-PB1(1-14) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=34.53±2.19 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30977 MDVNPTLLFLKVP 13 FluA-PB1(1-13) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=138.17 ±7.88 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30978 MDVNPTLLFLKV 12 FluA-PB1(1-12) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=643.93 ±180.75 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30979 MDVNPTLLFLK 11 FluA-PB1(1-11) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=899.53 ±54.31 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30980 MDVNPTLLFL 10 FluA-PB1(1-10) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30981 MDVNPTLLF 9 FluA-PB1(1-9) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30982 MDVNPTLL 8 FluA-PB1(1-8) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30983 MDVNPTL 7 FluA-PB1(1-7) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30984 MDVNPT 6 FluA-PB1(1-6) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30985 MDVNPTLLFLKVPAQ 15 FluA-PB1(1-15) Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=43.32 ±5.31nM);##Influenza B(FluB):inhibition of PA-binding activity and virus replication(IC50>3000nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30986 MNINPYPLFIDVPIQ 15 PB1-1-15 B Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=45.0 ±12.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30987 MNINPTLLFLKVPIQ 15 PB1-1-15 A D2N,V3I,L14I Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=6.69 ±1.73 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30988 MDVNPTLLFIDVPAQ 15 PB1-1-15 A L10I,K11D Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30989 MNINPTLLFLKVPAQ 15 PB1-1-15 A D2N,V3I Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=12.96 ±3.98 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30990 MDVNPYFLFLKVPAQ 15 PB1-1-15 A T6Y,L7F Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=7.51 ±0.71 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=345.0 ±81.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30991 MDVNPTFLFLKVPAQ 15 PB1-1-15 A L7F Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30992 MDVNPYLLFLKVPAQ 15 PB1-1-15 A T6Y Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=21.64 ±1.48 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=107.1 ±31.3 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30993 MDVNPFLLFLKVPAQ 15 PB1-1-15 A T6F Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=2.84 ±0.48 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=750.4 ±249.6 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30994 MDVNPWLLFLKVPAQ 15 PB1-1-15 A T6W Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=3.40 ±0.51 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=628.3 ±389.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30995 MDVNPHLLFLKVPAQ 15 PB1-1-15 A T6H Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=292.16 ±34.04 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30996 MDVNPCLLFLKVPAQ 15 PB1-1-15 A T6C Q6DNS6 Orthomyxoviridae Not found Synthetic construct(derived from INFV A polymerase (PB1)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Influenza virus replication and transcription is performed in the nucleus by the heterotrimeric viral polymerase complex consisting of the PB1, PB2, and PA subunits.The peptide could bind with PA subunit thus inhibit the virus replication. [Ref.19841738]Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50=43.58 ±5.67 nM);##Influenza A(FluA):inhibition of PA-binding activity and virus replication(IC50>3000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PA subunit 19841738 PLoS One. 2009 Oct 20;4(10):e7517. Wunderlich K, Mayer D, Ranadheera C, Holler AS, Mänz B, Martin A, Chase G, Tegge W, Frank R, Kessler U, Schwemmle M. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.  DRAMP30997 GWWYKGRARPVSAVA 15 18-c01 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=3.2 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP30998 RAVWRHSVATPSHSV 15 C18-c03 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=6.5 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=68 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP30999 GAWYKGRARPVSAVA 15 C18-c01W2A No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=53 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31000 GWWYKGRARAVSAVA 15 C18-c01P10A No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=89 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31001 AVASVPRARGKYWWG 15 C18-c01r No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=44 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=17 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31002 DFRRLPGAFWQLRQP 15 C18-p1b No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=52 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=19 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31003 AETVESCLAKPHTEN 15 C18-cp3c No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50=66 μM);##H3N2(A/Aichi/2/68):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Alkylated(C18) Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31004 GWWYKGRARPVSAVA 15 c01 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31005 RAVWRHSVATPSHSV 15 c03 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide has affinity for glycoconjugates on the cell surface. And its binding to the cell resulted in the significant inhibition of influenza virus infections. [Ref.19558186]H1N1(A/PR/8/34):inhibition of virus infection in Madin-Darby canine kidney(MDCK) cells(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented sialylgalactose 19558186 J Med Chem. 2009 Jul 23;52(14):4247-56. Matsubara T, Sumi M, Kubota H, Taki T, Okahata Y, Sato T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library.  DRAMP31006 RRKKAVLLALLAP 13 B12 P08620 Orthomyxoviridae Not found Synthetic construct(derived from FGF-4 signal sequence) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits influenza virus replication by preventing attachment to cells. [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(97 ± 2% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. Jones JC, Settles EW, Brandt CR, Schultz-Cherry S.  Identification of the minimal active sequence of an anti-influenza virus peptide.  DRAMP31007 RRKKVALLAVLLALLA 16 B7NP(B7 without prolines) P08620 Orthomyxoviridae Not found Synthetic construct(derived from FGF-4 signal sequence) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits influenza virus replication by preventing attachment to cells. [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=0.3 ± 0.1 μM). [Ref.21220525]>50% hemolysis agaisnt human red blood cells at 30 μM. Linear Free Free L [Ref.21220525]A549 cells:CD50=126.3± 23.0 μM;##MDCK cells:CD50=105.3 ± 8.0 μM. Not found 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. Jones JC, Settles EW, Brandt CR, Schultz-Cherry S.  Identification of the minimal active sequence of an anti-influenza virus peptide.  DRAMP31008 RRKKALLAVLLALLA 15 B8NP P08620 Orthomyxoviridae Not found Synthetic construct(derived from FGF-4 signal sequence) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits influenza virus replication by preventing attachment to cells. [Ref.21220525]Influenza virus:inhibit hemagglutination of 64 HA units of virus of MDCK cells(EC50=0.4 ± 0.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 21220525  Antimicrob Agents Chemother. 2011 Apr;55(4):1810-3. Jones JC, Settles EW, Brandt CR, Schultz-Cherry S.  Identification of the minimal active sequence of an anti-influenza virus peptide.  DRAMP31009 LFRLIKSLIKRLVSAFK 17 Mucroporin-M1 B9UIY3 Coronaviridae, Orthomyxoviridae, Paramyxoviridae Not found Synthetic construct(derived from Mucroporin) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Mucroporin-M1 may bind to the virus envelope by surface charge interactions and inhibits MeV, SARS-CoV and influenza H5N1 by direct virucidal action. [Ref.21620914]measles virus (MeV):inhibition of MeV infection in Vero cells(EC50=7.15 μg/ml (3.52 μM));##SARS-CoV(pseudoviruse):inhibition of SARS-CoV infection in MDCK cells(EC50=14.46 μg/ml (7.12 μM));##H5N1(pseudovirus):inhibition of H5N1 infection in MDCK cells(EC50=2.10 μg/ml (1.03 μM)). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.21620914]Vero cells:CC50=70.46μg/ ml(34.70μM);##HeLa-ACE2 cells:CC50=61.58 μg/ml (30.31 μM);##MDCK cells:CC50=83.35 μg/ml (41.03 μM). membrane 21620914 Peptides. 2011 Jul;32(7):1518-25. Li Q, Zhao Z, Zhou D, Chen Y, Hong W, Cao L, Yang J, Zhang Y, Shi W, Cao Z, Wu Y, Yan H, Li W.  Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.  DRAMP31010 KAKAKAKAKAKAKAKAKAKAK 21 RJ1 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=53.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>455 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31011 KAAKKAAKAAKKAAKWAKKAA 21 RJ3 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=117.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>467 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31012 AKKAAKKAKKAAKKAKKAAKK 21 RJ5 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=41.0 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=14.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>468 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31013 AKKAAKKAKKAAKKAKKWAKK 21 RJ6 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=47.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>433 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31014 AKKAWKKAKKAAKKAKKWAKK 21 RJ7 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=40.8 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=44.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>412 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31015 ARRAWRRARRAARRARRAARR 21 RJ8 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=18.2 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=22.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>395 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31016 ARRAKRRARRAARRARRKARR 21 RJ9 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=13.0 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=46.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>433 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31017 ARRAKRRARRAKRRARRKKRR 21 RJ10 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide was able to inhibit the entry of HSV-1 into the host cell, probably by blocking heparan sulfate(HS) at the cell surface. [Ref.15498607]herpes simplex virus 1(HSV-1):inhibition of HSV-1 infection in MRC-5 cells(IC50=24.6 μM);##herpes simplex virus 2(HSV-2):inhibition of HSV-2 infection in MRC-5 cells(IC50=54.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.15498607]human fibroblasts(MRC-5 cells):CC50>422 μM. Not found 15498607 Antiviral Res. 2004 Nov;64(2):119-26. Jenssen H, Andersen JH, Mantzilas D, Gutteberg TJ.  A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. DRAMP31018 QLQKWEDWVRWIGNIPQYLKG 21 Peptide 59(FIV ectodomain 767-786) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.03 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31019 QKWEDWVRWIGN 12 C12a(FIV ectodomain 768-779) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.25 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.18 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31020 WEDWVRWIGNIP 12 C12b(FIV ectodomain 770-781) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.04 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.09 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31021 QLQKWEDWVRWI 12 C12c(FIV ectodomain 766-777) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.03 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.04 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31022 WEDWVRWI 8 C8(FIV ectodomain 770-777) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.07 ± 0.02 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.46 ± 0.20 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.05 ± 0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31023 DWVRWI 6 C6a(FIV ectodomain 772-777) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.15 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.07 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31024 WEDWVR 6 C6b(FIV ectodomain 770-775) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31025 WVRWI 5 C5(FIV ectodomain 773-777) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.20 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.11 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31026 WVRW 4 C4a(FIV ectodomain 773-776) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=36 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=24 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31027 VRWI 4 C4b(FIV ectodomain 774-777) P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=7.80 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=4.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31028 AEDWVRWI 8 C8W->A770 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=4.30 ± 0.70 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=2.10± 0.10 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610147]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31029 WADWVRWI 8 C8E->A771 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.16 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.22 ± 0.05 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.12 ± 0.01 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610148]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31030 WEAWVRWI 8 C8D->A772 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.10± 0.02 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.40 ± 0.22 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.03 ± 0.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610149]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31031 WEDAVRWI 8 C8W->A773 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610150]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31032 WEDWARWI 8 C8V->A774 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.07 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.54 ± 0.02 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.15 ± 0.12 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610151]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31033 WEDWVAWI 8 C8G->A775 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.09 ± 0.03 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.38 ± 0.04 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.25 ± 0.06 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610152]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31034 WEDWVRAI 8 C8W->A776 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50>50 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50>50);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50>50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610153]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31035 WEDWVRWA 8 C8I->A777 P16090 Retroviridae Not found Synthetic construct(derived from the Membrane-Proximal Ectodomain of Feline Immunodeficiency Virus) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.12610147]FIV-M2(Feline immunodeficiency virus M2):inhibition of virus replication in MBM cells(IC50=0.15 ± 0.01 µg/ml);##FIV-GL8(Feline immunodeficiency virus GL8):inhibition of virus replication in MBM cells(IC50=0.64± 0.08 µg/ml);##FIV-Pet(Feline immunodeficiency virus Pet):inhibition of virus replication in MBM cells(IC50=0.13 ± 0.04 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12610154]No detectable cytotoxicity on MBM cell viability and proliferation. Not found 12610147 J Virol. 2003 Mar;77(6):3724-33. Giannecchini S, Di Fenza A, D'Ursi AM, Matteucci D, Rovero P, Bendinelli M. Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein. DRAMP31036 TDVILMCFSIDSPDSLENI 19 77-95(wild type) P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=7.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31037 CSIELSDIPLSVDFNTMID 19 77-95(scrambled) P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31038 ADVILMCFSIDSPDSLENI 19 77-95[77A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.56 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31039 TAVILMCFSIDSPDSLENI 19 77-95[78A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.37 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31040 TDAILMCFSIDSPDSLENI 19 77-95[79A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.60 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31041 TDVALMCFSIDSPDSLENI 19 77-95[80A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=11.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31042 TDVIAMCFSIDSPDSLENI 19 77-95[81A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=5.42 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31043 TDVILACFSIDSPDSLENI 19 77-95[82A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.43 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31044 TDVILMAFSIDSPDSLENI 19 77-95[83A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31045 TDVILMCASIDSPDSLENI 19 77-95[84A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.29 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31046 TDVILMCFAIDSPDSLENI 19 77-95[85A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.82 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31047 TDVILMCFSADSPDSLENI 19 77-95[86A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=3.52 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31048 TDVILMCFSIASPDSLENI 19 77-95[87A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.36 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31049 TDVILMCFSIDAPDSLENI 19 77-95[88A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.26 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31050 TDVILMCFSIDSADSLENI 19 77-95[89A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=15.32 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31051 TDVILMCFSIDSPASLENI 19 77-95[90A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.61 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31052 TDVILMCFSIDSPDALENI 19 77-95[91A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.19 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31053 TDVILMCFSIDSPDSAENI 19 77-95[92A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=2.27 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31054 TDVILMCFSIDSPDSLANI 19 77-95[93A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=9.83 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31055 TDVILMCFSIDSPDSLEAI 19 77-95[94A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=18.47 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31056 TDVILMCFSIDSPDSLENA 19 77-95[95A] P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.89 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31057 TDVILMCFSI 10 77-86 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31058 TDVILMCFSIDSP 13 77–89 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31059 TDVILMCFSIDSPDSL 16 77-92 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=10.86 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31060 DVILMCFSIDSPDSLENI 18 78-95 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.23 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31061 VILMCFSIDSPDSLENI 17 79-95 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=16.95 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31062 ILMCFSIDSPDSLENI 16 80-95 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=7.17 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31063 CFSIDSPDSLENI 13 83-95 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31064 ILMCFSIDSPDSLEN 15 80-94 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=1.75 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31065 ILMCFSIDSPDSLE 14 80-93 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=3.50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31066 ILMCFSIDSPDSL 13 80-92 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=12.40 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31067 ILMCFSIDSPDS 12 80-91 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=6.36 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31068 ILMCFSIDSPD 11 80-90 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=4.61 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31069 ILMCFSIDSP 10 80-89 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50=35.77 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31070 ILMCFSIDS 9 80-88 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31071 ILMCFSID 8 80-87 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31072 ILMCFSI 7 80-86 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31073 ILMCFS 6 80-85 P08134 Paramyxoviridae Not found Synthetic construct(derived from RhoA protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.14576104]respiratory syncytial virus(RSV):inhibition of RSV replication in HEp-2 cells(IC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 14576104 Antimicrob Agents Chemother. 2003 Nov;47(11):3470-7. Budge PJ, Lebowitz J, Graham BS.  Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers. DRAMP31074 NGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTA 38 HR1-1(HR1 region 889–926) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: soluble synthesized HR1, HR2 or homologues can bind the exposed HR1 or HR2 region and block the formation of the six-helix bundle, thus inhibiting virus fusion with the target cell. [Ref.15184046]HIV-luc/SARS pseudotyped virus:inhibition of virus infection in 293T cells(EC50=0.14 μM);##SARS-CoV(wild-type):inhibition of virus infection in 293T cells(EC50=3.68 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15184046 Biochem Biophys Res Commun. 2004 Jul 2;319(3):746-52. Yuan K, Yi L, Chen J, Qu X, Qing T, Rao X, Jiang P, Hu J, Xiong Z, Nie Y, Shi X, Wang W, Ling C, Yin X, Fan K, Lai L, Ding M, Deng H. Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein. DRAMP31075 HRILMRIRQMMT 12 p9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=56.47 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50=473.00 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31076 ARILMRIRQMMT 12 1-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=56.12263 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31077 HRALMRIRQMMT 12 3-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=34.18095 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31078 HRIAMRIRQMMT 12 4-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=54.5872 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31079 HRILARIRQMMT 12 5-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=435.4996 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31080 HRILMRARQMMT 12 7-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=150.1405 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31081 HRILMRIAQMMT 12 8-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=60.60846 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31082 HRILMRIRAMMT 12 9-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=34.13563 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31083 HRILMRIRQAMT 12 10-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=57.98146 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31084 HRILMRIRQMAT 12 11-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=120.5239 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31085 HRILMRIRQMMA 12 12-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=89.41235 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50=186.2536 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31086 LMRIRQMMT 9 a-p9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=263.8101 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31087 HRILMRIR 8 b-p9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=43.50202 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31088 LMRIR 5 c-p9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=716.4193 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22743126]MARC-145 cells:CC50>500 μM. PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31089 hrilmrirqmmt 12 D-P9 No entry found Arteriviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase. [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=16.12312 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information found in the reference(s) presented PRRSV polymerase 22743126 Virology. 2012 Oct 10;432(1):73-80. Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P.  Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro. DRAMP31090 AWDFGSIGGVFTSVGKLVHQVFGTAYGVL 29 DV1(419-447) P27909 Flaviviridae Not found Synthetic construct(derived from DENV1 E protein stem) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide shows antiviral activity by inhibiting virus entry. [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90=1.5 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90>6 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90>6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP31091 AWDFGSLGGVFTSIGKALHQVFGAIYGAA 29 DV2(419-447) P29984 Flaviviridae Not found Synthetic construct(derived from DENV2 E protein stem) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide shows antiviral activity by inhibiting virus entry. [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90<0.1 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=0.3 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=0.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP31092 AWDFGSVGGVLNSLGKMVHQIFGSAYTAL 29 DV3(419-447) Q99D35 Flaviviridae Not found Synthetic construct(derived from DENV3 E protein stem) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide shows antiviral activity by inhibiting virus entry. [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90<0.1 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=2 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90=4 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP31093 AWDFGSVGGLFTSLGKAVHQVFGSVYTTM 29 DV4(419-447) P27909 Flaviviridae Not found Synthetic construct(derived from DENV4 E protein stem) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide shows antiviral activity by inhibiting virus entry. [Ref.20881042]Dengue 1 virus(DENV1):inhibition of infection in BHK-21 cells(IC90=5 μM);##Dengue 2 virus(DENV2):inhibition of infection in BHK-21 cells(IC90=6 μM);##Dengue 3 virus(DENV3):inhibition of infection in BHK-21 cells(IC90>6 μM);##Dengue 4 virus(DENV4):inhibition of infection in BHK-21 cells(IC90=6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 20881042 J Virol. 2010 Dec;84(24):12549-54. Schmidt AG, Yang PL, Harrison SC. Peptide inhibitors of flavivirus entry derived from the E protein stem. DRAMP31094 YENQKQIANQFNKAISQIQESLTTTSTA 28 HR1-a(899-926) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18442051]HIV‐luc/SARS Pseudotyped Virus:inhibition of viral-entry in Vero E3 cells(EC50=1.16 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.  DRAMP31095 DVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI 48 GST-removed HR2(1145-1192) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18442051]HIV‐luc/SARS Pseudotyped Virus:inhibition of viral-entry in Vero E3 cells(EC50=2.15 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors.  DRAMP31096 DVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI 48 SARS-Cov-S (1145-1192) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18442051]SARS-CoV PsV: inhibition of HIV-luc/SARS PsV infection in Vero-E6 cells (EC50=2.15μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented not found 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors. DRAMP31097 YENQKQIANQFNKAISQIQESLTTTSTA 28 SARS-Cov-S (899-926) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18442051]SARS-CoV PsV: inhibition of HIV-luc/SARS PsV infection in Vero-E6 cells (EC50=1.16μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented not found 18442051 J Cell Biochem. 2008 Aug 15;104(6):2335-47. Chu LH, Chan SH, Tsai SN, Wang Y, Cheng CH, Wong KB, Waye MM, Ngai SM. Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): in search of potent SARS-CoV entry inhibitors. DRAMP31098 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 64 sHR2-1(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR1 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=43 ± 6.4 μM);##murine coronavirus:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31099 PKEELDKYFKNHTSPDVDLGLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 62 sHR2-2(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR2 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=24 ± 2.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31100 LDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 56 sHR2-3(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR3 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31101 FKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 52 sHR2-4(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR4 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31102 TSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 48 sHR2-5(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR5 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31103 VDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 44 sHR2-6(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR6 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31104 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 40 sHR2-7(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR7 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31105 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 68 sHR2-8(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR8 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=17 ± 3.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31106 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 60 sHR2-9(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR9 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50=34 ± 4.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31107 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLID 56 sHR2-10(derived from SARS-CoV spike protein heptad repeat) P59594 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR10 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31108 DLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKE 39 mHR2(derived from SARS-CoV spike protein heptad repeat) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein heptad repeat) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide exhibits antiviral activity by competitive binding to the HR11 region of the SARS-CoV spike protein, thus blocking the formation of the six-helix bundle and consequently membrane fusion. [Ref.15150417]SARS-CoV:inhibition of virus infection in Vero cells(EC50>50 μM);##murine coronavirus:inhibition of virus infection in Vero cells(EC50=0.9 ± 0.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31109 DLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKE 39 MHV-S (1216-1254) P11224 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM);##MHV(mouse hepatitis virus): inhibition of MHV infection in Vero 118 cells (EC50=0.9±0.1µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31110 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQEL 60 SARS-CoV-S (1134-1185) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=34±4.0µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31111 NQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLIT 46 SARS-CoV-S (935-980) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31112 ELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK 68 SARS-CoV-S (1134-1193) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=17±3.0µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31113 DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 40 SARS-CoV-S (1150-1189) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31114 LDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 56 SARS-CoV-S (1134-1189) P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50>50µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31115 ELDSPKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 64 SARS-CoV (1126-1189)[F5P] P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=43±6.4µM);##MHV(mouse hepatitis virus): inhibition of MHV infection in Vero 118 cells (EC50>50µM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31116 PKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE 60 SARS-CoV (1130-1189)[F1P] P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits virus infection by interfering with six-helix bundle formation(fusion inhibitor). [Ref.15150417]SARS-CoV: inhibition of SARS-CoV infection in Vero 118 cells (EC50=24±2.8µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 15150417 Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60. Bosch BJ, Martina BE, Van Der Zee R, Lepault J, Haijema BJ, Versluis C, Heck AJ, De Groot R, Osterhaus AD, Rottier PJ. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. DRAMP31117 ATCYCRTGRCATRESLSGVCRISGRLYRLCCR 32 HD5[E21R] Q01523 Herpesviridae, Retroviridae Not found Synthetic construct(derived from human alpha defensin(HD5)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells. [Ref.23269800]Herpes simplex virus2(HSV-2):Potential for CaSki cell protection from HSV-2 infection(61.5% ± 7.1% cell protection rates at 25 μg/ml,90.2% ± 4.9% cell protection at 50 μg/ml);neutralization activity against HSV-2 during the preinfection stage(IC50=25 μg/ml);##HIV-1:inhibition of virus infection in JLTRG cells(IC50=3.53 μg/ ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. capsid protein gD 23269800 J Virol. 2013 Mar;87(5):2835-45.  Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J.  Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. DRAMP31118 ATCYCRTGRCATRESLSGVCEIRGRLYRLCCR 32 HD5[S23R] Q01523 Herpesviridae Not found Synthetic construct(derived from human alpha defensin(HD5)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells. [Ref.23269800]Herpes simplex virus2(HSV-2):neutralization activity against HSV-2 during the preinfection stage(IC50=36 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. capsid protein gD 23269800 J Virol. 2013 Mar;87(5):2835-45. Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J.  Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. DRAMP31119 ATCYCRRGRCATRESLSGVCEISGRLYRLCCR 32 HD5[T7R] Q01523 Herpesviridae Not found Synthetic construct(derived from human alpha defensin(HD5)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells. [Ref.23269800]Herpes simplex virus2(HSV-2):neutralization activity against HSV-2 during the preinfection stage(IC50=40 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. capsid protein gD 23269800 J Virol. 2013 Mar;87(5):2835-45.  Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J.  Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. DRAMP31120 ATCYCRTGRCATRESRSGVCEISGRLYRLCCR 32 HD5[L16R] Q01523 Herpesviridae Not found Synthetic construct(derived from human alpha defensin(HD5)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The interaction between peptide and viral capsid proteins may cause aggregation of virions to prevent viruses from normal binding to target cells. Another possibility is that the binding of HD5 derivatives to the virion envelope blocks the epitopes of interaction between viruses and cell receptors, which are necessary for viral adsorption or entry into host cells. [Ref.23269800]Herpes simplex virus2(HSV-2):Potential for CaSki cell protection from HSV-2 infection(51.2% ± 7.2% cell protection at 100 μg/ml);neutralization activity against HSV-2 during the preinfection stage(IC50=67 μg/ml); No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys31,Cys5 and Cys20,Cys10 and Cys30. L [Ref.23269800]No cytotoxicity against CaSki cells up to 100μg/ ml. capsid protein gD 23269800 J Virol. 2013 Mar;87(5):2835-46.  Wang A, Chen F, Wang Y, Shen M, Xu Y, Hu J, Wang S, Geng F, Wang C, Ran X, Su Y, Cheng T, Wang J.  Enhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites. DRAMP31121 PPVYTKDVDISSQISSMNQSLQQSKDYIKEAQKILDTVNPSL 42 HeV F HRC derived peptide(447-488) O89342 Paramyxoviridae Not found Synthetic construct(derived from HeV fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 6HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=75 nM);inhibition of fusion in HeLa cells(IC50=40 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31122 VYTDKVDISSQISSMNQSLQQSKDYIKEAQKILDTV 36 HeV F HRC derived peptide(449-484) O89342 Paramyxoviridae Not found Synthetic construct(derived from HeV fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 7HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=75 nM);inhibition of fusion in HeLa cells(IC50=40 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31123 DITLNNSVALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSIGN 45 HPIV3 F HRC derived peptide(442-486) P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 8HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=20 nM);inhibition of fusion in HeLa cells(IC50=7.5 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=500 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31124 VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI 36 HPIV3 F HRC derived peptide(449-484) P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 9HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=20 nM);inhibition of fusion in HeLa cells(IC50=7.5 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=500 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31125 VANDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI 36 HPIV3 F HRC derived peptide(449-484)[L451N] P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 11HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=100 nM);inhibition of fusion in HeLa cells(IC50=3000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=1100 nM);inhibition of fusion in HeLa cells(IC50=750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31126 VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSD 36 HPIV3 F HRC derived peptide(449-484)[I484D] P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 12HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50=100 nM);inhibition of fusion in HeLa cells(IC50=8000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=500 nM);inhibition of fusion in HeLa cells(IC50=350 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31127 VANDPIDISIELNKAKSDLEESKEWIRRSNQKLDSD 36 HPIV3 F HRC derived peptide(449-484)[L451N,I484D] P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 13HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50=1100 nM);inhibition of fusion in HeLa cells(IC50=750 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31128 VALDPIDISIELNKAKSDLEESKEWIRR 28 HPIV3 F HRC derived peptide(449-476) P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 14HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31129 SIELNKAKSDLEESKEWIRRSNQKLDSI 28 HPIV3 F HRC derived peptide(457-484) P06828 Paramyxoviridae Not found Synthetic construct(derived from HPIV3 fusion (F) protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion. HeV F, once triggered by the receptor-bound G, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 15HB structure that is required for fusion. [Ref.16973588]Henda virus(HeV):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>1000 nM);##human parainfluenza virus 3 (HPIV3):inhibition of virus infection in HeLa cells(IC50>10000 nM);inhibition of fusion in HeLa cells(IC50>10000 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane 16973588 J Virol. 2006 Oct;80(19):9837-49. Porotto M, Doctor L, Carta P, Fornabaio M, Greengard O, Kellogg GE, Moscona A. Inhibition of hendra virus fusion. DRAMP31130 MANAGLQLLGFILAFLGW 18 CL58 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=2.1 ± 0.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22378192]Huh7.5.1 cells:CC50~200 Μm. membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-15.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31131 GLQLLGFILAFLGWIGAI 18 CL58.1 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-16.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31132 LLGFILAFLGWIGAIVST 18 CL58.2 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=4.3 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-17.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31133 FILAFLGWIGAIVSTALP 18 CL58.3 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=8.9± 1.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-18.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31134 AFLGWIGAIVSTALPQWR 18 CL58.4 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=12.5± 1.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-19.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31135 GWIGAIVSTALPQWRIYS 18 CL58.5 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=21.5± 1.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-20.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31136 GAIVSTALPQWRIYSYAG 18 CL58.6 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=23.8 ± 2.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-21.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31137 VSTALPQWRIYSYAGDNI 18 CL58.7 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-22.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31138 ALPQWRIYSYAGDNIVTA 18 CL58.8 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-23.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31139 MANAGLQLLGFILA 14 CL58-4 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-24.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31140 MANAGLQLLGFILAFL 16 CL58-2 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=7.6± 0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-25.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31141 MANAGLQLLGFILAFLGWIG 20 CL58+2 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=17.8 ± 1.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-26.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31142 MANAGLQLLGFILAFLGWIGAI 22 CL58+4 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=4.0 ± 0.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-27.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31143 MANAGLQLLGFILAFLGWIGAIVS 24 CL58+6 O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=5.1 ± 0.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-28.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31144 managlqllgfilaflgw 18 CL58.d O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50=1.8 ± 0.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free D No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-29.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31145 AGALMFAWLLLGLQGIFN 18 CL58.S O95832 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-29.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31146 MASAGMQILGVVLTLLGW 18 CL-6 P56747 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-30.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31147 MANSGLQLLGFSMALLGW 18 CL-7 Q3B794 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-31.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31148 MASTGLELLGMTLAVLGW 18 CL-9 O95484 Flaviviridae Not found Synthetic construct(derived from human claudin-1) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry in a postbinding step. [Ref.22378192]Hepatitis C virus(HCV):inhibition of viral-entry in Huh7.5.1 cells(IC50>25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented membrane protein 22378192 Hepatology. 2012 Aug;56(2):507-32.  Si Y, Liu S, Liu X, Jacobs JL, Cheng M, Niu Y, Jin Q, Wang T, Yang W.  A human claudin-1-derived peptide inhibits hepatitis C virus entry. DRAMP31149 EELRVRLASHLRKLRKRLLRDADDLQKRLAVYEEQAQQIRLQAEAFQARLKSWFEPLVEDM 61 hEP-1 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.67 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22334503]Huh7.5.1 cell:CC50>100 μg/ ml(〜14μM). 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31150 CEELRVRLASHLRKLRKRLLRDADDLQKRLAVY 33 hEP-2 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31151 EELRVRLASHLRKLRKRLLRDADDLQKRLAVY 32 hEP-2/deltaCys P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31152 CEEIRARLSTHLRKMRKRLMRDADDLQKRLAVY 33 mEP-2 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31153 CEEQAQQIRLQAEAFQARLKSWFEPLVEDM 30 hEP-3 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31154 CVRLASHLRKLRKRLLRDADDL 22 hEP-4 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31155 CIRLQAEAFQARLKSWFEPLV 21 hEP-5 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31156 VRLASHLRKLRKRLLRDADDLIRLQAEAFQARLKSWFEPLV 41 hEP-6 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31157 LRVRLASHLRKLRKRLLRDADDLQKRLAVY 30 hEP-7 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31158 EELRVRLASHLRKLRKRLLRDADDL 25 hEP-8 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31159 VRLASHLRKLRKRLLRDADDLQKRLAVY 28 hEP-9 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31160 CVRLASHLRKLRKRLLRDADDLQKRLAVY 29 hEP-10 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31161 CLRVRLASHLRKLRKRLLRDADDL 24 hEP-11 P02649 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31162 CLRKLRKRLLRC 12 hEP-12 P28995 Flaviviridae Not found Synthetic construct(derived from human apolipoprotein E) Antimicrobial, Antiviral Not found Not found Not found Mechanism: hEP peptide blocks the binding of virus to cells, suggesting a role of apoE at the very early stage of HCV entry. [Ref.22334503]hepatitis C virus(HCVpp):inhibition of infection in Huh7.5.1 cells(IC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 22334503 Hepatology. 2012 Aug;56(2):484-91. Liu S, McCormick KD, Zhao W, Zhao T, Fan D, Wang T. Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding. DRAMP31163 YAGAVVNDL 9 H2-(7-15) P10224 Herpesviridae Not found Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=36-60 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31164 AGAVVNDL 8 H2-(8-15) P10224 Herpesviridae Not found Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=283 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31165 GAVVNDL 7 H2-(9-15) P10224 Herpesviridae Not found Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=225 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31166 AVVNDL 6 H2-(10-15) P10224 Herpesviridae Not found Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31167 VVNDL 5 H2-(11-15) P10224 Herpesviridae Not found Synthetic construct(derived from HSV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=760 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31168 YAGAVVNDL 9 Ac-H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31169 YAGAVVNDL 9 H2-(7-15) amide No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=190 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31170 YAGAVVNDL 9 Ac-H2-(7-15) amide No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=76 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31171 VVNDL 5 Ac-H2-(11-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=400 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31172 YAVVNDL 7 [Tyr9]H2-(9-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=340 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31173 YAVVNDL 7 Ac-[Tyr9]H2-(9-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=330 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31174 YGAVVNDL 8 [Tyr8]H2-(8-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=330 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31175 YGAVVNDL 8 Ac-[Tyr8]H2-(8-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31176 AAGAVVNDL 9 [Ala7]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=280 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31177 yAGAVVNDL 9 [D-Tyr7]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Mixed(D-Tyr1) No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31178 yAGAVVNDL 9 Ac-[D-Tyr7]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=165 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free Mixed(D-Tyr1) No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31179 XAGAVVNDL 9 [Tyr7(OMe)]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=88 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 is methoxy Tyrosine. L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31180 XAGAVVNDL 9 Ac[Tyr7(OMe)]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free The 'X' at position 1 is methoxy Tyrosine. L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31181 XAGAVVNDL 9 [desamino-Tyr7]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=33 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 1 is 3-(4-hydroxyphenyl)propionic acid. L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31182 YaGAVVNDL 9 [D-Ala8]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=200 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Mixed(D-Ala2) No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31183 YaGAVVNDL 9 Ac-[D-Ala8]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=230 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free Mixed(D-Ala2) No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31184 YXGAVVNDL 9 [β-Ala8]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=100 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 2 is 3-aminoproprionic acid. L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31185 YAGAVANDL 9 [Ala12]H2-(7-15) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=760 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31186 YTMLVVDDL 9 EBV H2-(7-15) No entry found Herpesviridae Not found Synthetic construct(derived from EBV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=110 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31187 YAGTVINDL 9 VZV H2-(7-15) No entry found Herpesviridae Not found Synthetic construct(derived from VZV ribonucleotide reductase subunit 2) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the activity of ribonucleotide rductase. [Ref.3040743]Herpes simplex virus type 1:inhibition of HSV-1 ribonucleotide reductase activity(IC50=15 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented ribonucleotide reductase 3040743 J Biol Chem. 1987 Sep 15;262(26):12413-6. Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. DRAMP31188 FAVAVKAVAVKAVAVKAVKKAVKKVKKAVKKAVKKKK 37 DC1 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.75 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.78 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=9.20 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31189 FLAAARIAKRVAKKARKLAKRAARKRK 27 D1D6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=0.94 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=1.47 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=8.93 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31190 FRFKIKFRLKFRFKARFKFRAKFRA 25 D4C3 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=1.32 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=3.81 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31191 FAVGLRAIKRALKKLRRGVRKVAKDL 26 D5F No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=5.47 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=8.73 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31192 KRKRAVKRVGRRLKKLARKIARLGVAKLAGLRAVKLF 37 D5C1 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.38 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=5.26 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31193 GAKKGAKKGKKGAKKGAKGAGAKGAGAFKKKK 32 D2B15 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=4.07 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=6.19 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31194 KKKKFVKKVAKKVKKVAKKVAKVAVAV 27 D2A3 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.00 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=3.24 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31195 FLFAFRIFKRVFKKFRKLFKRAF 23 D1A22 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=10.51 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=10.79 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31196 KRKRAVKRVGRRLKKKLARKIARLGVAF 28 D5C No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=7.82 μM);##Feline immunodeficiency virus(FIV-Black):inhibition of reverse transcriptase activity in CrFK cells(IC50=6.84 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=7.48 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31197 KRKRFAKKFLRFLRKVIRFLKRFIRRF 27 D3A15 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.69 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=3.28 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31198 FAIAIKAIKKAIKKIKKAIKKAI 23 D1D2 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=8.71 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=5.87 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31199 FKVKAKVKAKVKAKVKAKKKK 21 D4B No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=2.85 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.12208971]CrFK cell:TC50=0.92 μM. Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31200 AVKRVGRRLKKLARKIARLGVAF 23 D5D No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may facilitate interference with viral assembly or release and reduce the number of infectious progeny virions. [Ref.12208971]Feline immunodeficiency virus(FIV-Petaluma):inhibition of reverse transcriptase activity in CrFK cells(IC50=3.37 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 12208971 J Virol. 2002 Oct;76(19):9952-61. Ma J, Kennedy-Stoskopf S, Jaynes JM, Thurmond LM, Tompkins WA. Inhibitory activity of synthetic peptide antibiotics on feline immunodeficiency virus infectivity in vitro.  DRAMP31201 LPRRLHLEPAFLPYSVKAHECC 22 UL54(1221-1242) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31202 PGGETARKDKFLHMVLPRRL 20 UL54(1206-1225) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31203 EQVLKAVTNVLSPVFPGGET 20 UL54(1191-1210) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=280 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31204 YVREHGVPIHADKYFEQVLK 20 UL54(1176-1195) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31205 PPSAVCNYEVAEDPSYVREH 20 UL54(1161-1180) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31206 RRLHLEPAFLPYSVKAHECC 20 UL54(1223-1242) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31207 LPRRLHLEPAFLPYSVKAHEC 21 UL54(1221-1241) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50=75 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31208 LPRRLHLEPAFLPYSVKAHE 20 UL54(1221-1240) P08546 Herpesviridae Not found Synthetic construct(derived from human cytomegalovirus(HCMV) UL54 protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from C-terminus of UL54 can block the physical interaction between UL54 and UL44,thus inhibits the activity of DNA polymerase. [Ref.12857903]human cytomegalovirus(HCMV):inhibition of phyical interaction between UL54 and UL44(IC50>500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented DNA polymerase 12857903 J Virol. 2003 Aug;77(15):8336-44. Loregian A, Rigatti R, Murphy M, Schievano E, Palu G, Marsden HS. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit. DRAMP31209 ACFPWGNTWCGGK 13 NTW (S-S) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=13.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31210 ACFPWGNTWCGGK 13 NTW (L) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31211 ACFPWGKEYCGGK 13 KEY (S-S) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=22.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31212 ACFPWGKEYCGGK 13 KEY (L) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31213 ACFPWGNQWCGGK 13 NQW (S-S) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=6.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31214 ACFPWGNQWCGGK 13 NQW (L) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=37.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31215 CFPWGC 6 FPWG (S-S) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=50.0 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization of a n-terminal Cys residue (forming a disulfide bond) Cyclization of a C-terminal Cys residue (forming a disulfide bond) Disulfide bond between Cys1 and Cys6 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31216 CFPWGC 6 FPWG (L) No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>150 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31217 ACAPWGNTWCGGK 13 NTW (S-S)[F1A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50>200 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31218 ACFAWGNTWCGGK 13 NTW (S-S)[P2A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=39 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31219 ACFPAGNTWCGGK 13 NTW (S-S)[W3A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=43 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31220 ACFPWANTWCGGK 13 NTW (S-S)[G4A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=7.4 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31221 ACFPWGATWCGGK 13 NTW (S-S)[N5A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=40 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31222 ACFPWGNAWCGGK 13 NTW (S-S)[T6A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=11 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31223 ACFPWGNTACGGK 13 NTW (S-S)[W7A] No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the de novo synthesis catalyzed by the enzyme, which suggests that it likely inhibited the formation of a preinitiation complex between the enzyme and the 3′OH end of the linear poly (C) substrate. [Ref.12951030]Hepatitis C virus(HCV):inhibition of polymerase activity(IC50=80 µM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bond between Cys2 and Cys10 L No cytotoxicity information found in the reference(s) presented RNA-dependent RNA polymerase 12951030 Virology. 2003 Aug 15;313(1):158-69. Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. Identification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. DRAMP31224 MWKTPTLKYFGGFNFSQI 18 SARSWW-I(770-788) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(58% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31225 ATAGWTFGAGAALQIPFAMQMAY 23 SARSWW-II(864-886) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(39% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31226 GYHLMSFPQAAPHGVVFLHVTW 22 SARSWW-III(1028-1049) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(90% inhibition at ~30 μM,IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31227 GVFVFNGTSWFITQRNFFS 19 SARSWW-IV(1075-1093) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(83% inhibition at ~30 μM,IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31228 AACEVAKNLNESLIDLQELGKYEQYIKW 28 SARSWW-Vb(1169-1194) P11224 Coronaviridae Not found Synthetic construct(derived from SARS-CoV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(42% inhibition at ~30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31229 GYFVQDDGEWKFTGSSYYY 19 MHVWW-IV(1144-1162) P11224 Coronaviridae Not found Synthetic construct(derived from MHV spike protein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16616792]SARS-CoV:inhibition of plaque information on Vero E6 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16616792]No cytotoxicity against Vero E6 cells up to 30 μM. membrane 16616792 Virus Res. 2006 Sep;120(1-2):146-55. Sainz B Jr, Mossel EC, Gallaher WR, Wimley WC, Peters CJ, Wilson RB, Garry RF.  Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein DRAMP31230 AAHLIDALYAEFLGGRVLTTPVVHRALFYASAVLRQPFLAGVPSA 45 gH493-537(derived from HSV-1 H glycoprotein) Q9DHD5 Herpesviridae Not found Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry and thus protects cells from infection. [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(50-60% inhibition at 250μM-500μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. mambrane 18572274 Peptides. 2008 Sep;29(9):1461-71. Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M. Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. DRAMP31231 AAHLIDALYAEFLGGRVLTT 20 gH493-512(derived from HSV-1 H glycoprotein) Q9DHD5 Herpesviridae Not found Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry and thus protects cells from infection. [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(60% inhibition at 250μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. mambrane 18572274 Peptides. 2008 Sep;29(9):1461-71. Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M. Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. DRAMP31232 GLASTLTRWAHYNALIRAF 19 gH626-644(derived from HSV-1 H glycoprotein) Q9DHD5 Herpesviridae Not found Synthetic construct(derived from HSV-1 H glycoprotein (gH)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry and thus protects cells from infection. [Ref.18572274]Herpes simplex virus type 1(HSV-1):inhibition of viral-entry in Vero cells(50-60% inhibition at 250μM-500μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18572274]No cytotoxicity against Vero cells up to 500 μM. mambrane 18572274 Peptides. 2008 Sep;29(9):1461-71. Galdiero S, Falanga A, Vitiello M, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M. Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity. DRAMP31233 CCFLNITNSHVSILQERPPLENRVLTGWGL 30 Pcr-400 P14075 Retroviridae Not found Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=0.18 ± 0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented mambrane 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  Lamb D, Mirsaliotis A, Kelly SM, Brighty DW. Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. DRAMP31234 LNITNSHVSILQERPPLENRVL 22 Pcr-Δ8 P14075 Retroviridae Not found Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=5.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented membrane 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  Lamb D, Mirsaliotis A, Kelly SM, Brighty DW. Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. DRAMP31235 CFLNITNSHVSILQERPPLENRV 23 Pcr-Δ7 P14075 Retroviridae Not found Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=0.19± 0.01 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented membrane 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  Lamb D, Mirsaliotis A, Kelly SM, Brighty DW. Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. DRAMP31236 CFLNITNSHVSILQEAPPLENRV 23 Pcr-R416A P14075 Retroviridae Not found Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=1.55 ± 0.08 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented membrane 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  Lamb D, Mirsaliotis A, Kelly SM, Brighty DW. Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. DRAMP31237 CFLNITNSHVSILQEAPPLENAV 23 Pcr-R422A P14075 Retroviridae Not found Synthetic construct(derived from HTLV-1 envelope glycoprotein (gp21)) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide is an effective inhibitor of HTLV-1 envelope-catalyzed membrane fusion and thus inhibits virus entry. [Ref.19114713]:Human T cell leukemia virus type 1(HTLV-1):inhibition of mambrane fusion in 293T cells(IC50=8.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented membrane 19114713 J Biol Chem. 2009 Mar 6;284(10):6575-84.  Lamb D, Mirsaliotis A, Kelly SM, Brighty DW. Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry. DRAMP31238 KQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKK 49 G149-197(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31239 FHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKK 35 G163-197(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31240 VPCSICSNNPTCWAICKRIPNKKPGKK 27 G171-197(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>165 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31241 CSICSNNPTCWAICKRIPNKKPGKK 25 G173-197(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>177 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31242 KQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 41 G149-189(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=12 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31243 KPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 36 G154-189(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=12 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31244 KPNNDFHFEVFNFVPCSICSNNPTCWAICKRI 32 G158-189(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=25 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31245 KQRQNKPPSKPNNDFHFEVFN 21 G149-169(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>190 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31246 KQRQNKPPSKPNNDFHF 17 G149-165(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>240 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31247 KPPSKPNNDFHFEVFNFVP 19 G154-172(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=220 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31248 KPPSKPNNDFHFEVFNFV 18 G154-171(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=14 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31249 KPPSKPNNDFHFEVFNF 17 G154-170(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31250 KPPSKPNNDFHFEVFN 16 G154-169(derived from RSV attachment glycoprotein) P03423 Paramyxoviridae Not found Synthetic construct(derived from RSV attachment glycoprotein) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>510 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Acetylation Amidation The peptide formed two disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31251 KQRQNKPPSKPNNDFHFEVFNFVPBSIBG 29 G149-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 25,28 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31252 KPPSKPNNDFHFEVFNFVPBSIBG 24 G154-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31253 KPNNDFHFEVFNFVPBSIBG 20 G158-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 16,19 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31254 DFHFEVFNFVPBSIBG 16 G162-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=60 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 12,15 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31255 EVFNFVPBSIBG 12 G166-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 8,11 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31256 FVPBSIBG 8 G170-177 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50》500 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 4,7 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31257 KQRQNKPPSKPNNDFHFEVFNFVPB 25 G149-173 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=80 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 25 is S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31258 KPPSKPNNDFHFEVFNFVPBSIAG 24 G154-177[B176A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20 is S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31259 KPPSKPNNDFHFEVFNFVPBSABG 24 G154-177[I175A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=22 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31260 KPPSKPNNDFHFEVFNFVPBAIBG 24 G154-177[S174A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31261 KPPSKPNNDFHFEVFNFVPASIBG 24 G154-177[B173A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 23 is S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31262 KPPSKPNNDFHFEVFNFVABSIBG 24 G154-177[P172A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31263 KPPSKPNNDFHFEVFNFAPBSIBG 24 G154-177[V171A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31264 KPPSKPNNDFHFEVFNAVPBSIBG 24 G154-177[F170A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=22 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31265 KPPSKPNNDFHFEVFAFVPBSIBG 24 G154-177[N169A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31266 KPPSKPNNDFHFEVANFVPBSIBG 24 G154-177[F168A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=90 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31267 KPPSKPNNDFHFEAFNFVPBSIBG 24 G154-177[V167A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=11 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31268 KPPSKPNNDFHFAVFNFVPBSIBG 24 G154-177[E166A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=0.75 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31269 KPPSKPNNDFHAEVFNFVPBSIBG 24 G154-177[F165A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50=5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 20,23 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31270 KQRQNKPPSKPNNDFHFEVANAVPBSIBG 29 G149-177[F168/170A] No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.11487583]Respiratory syncytial virus(RSV):inhibition of the cytopathic effect of RSV in HEp-2 cells(IC50>165 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation The 'B' at position 25,28 are S-acetamidomethyl cysteine. L No cytotoxicity information found in the reference(s) presented Not found 11487583 J Biol Chem. 2001 Oct 19;276(42):38988-94. Gorman JJ, McKimm-Breschkin JL, Norton RS, Barnham KJ.  Antiviral activity and structural characteristics of the nonglycosylated central subdomain of human respiratory syncytial virus attachment (G) glycoprotein. DRAMP31271 DTRACDVIALLCHLNT 16 P1 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P1 significantly inhibited WNV infectivity at a concentration of 1 mM,IC50=67.0 ± 0.1 μM);##Dengue virus serotype 2:inhibition of virus infection in Vero cells(99.3±0.7% inhibition at 200 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17151121]No cytotoxicity against Vero cells up to 500μM. E proteins 17151121 J Virol. 2007 Feb;81(4):2047-55.  Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E. Antiviral peptides targeting the west nile virus envelope protein. DRAMP31272 CDVIALLCHLNT 12 P8 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented E proteins 17151121 J Virol. 2007 Feb;81(4):2047-55.  Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E. Antiviral peptides targeting the west nile virus envelope protein. DRAMP31273 CDVIALLACHLNT 13 P9 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(96.3±2.8% inhibition at 100 μM,IC50=2.60 ± 0.01 μM);inhibition of virus entry in Vero cells(65.2±14.5% inhibition at 100 μM);inhibition of virus attachment to Vero cells(96.3±2.7% inhibition at 1mM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17151121]No cytotoxicity against Vero cells up to 500μM. E proteins 17151121 J Virol. 2007 Feb;81(4):2047-55.  Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E. Antiviral peptides targeting the west nile virus envelope protein. DRAMP31274 CDVIALLCHLNTPSF 15 P10 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented E proteins 17151121 J Virol. 2007 Feb;81(4):2047-55.  Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E. Antiviral peptides targeting the west nile virus envelope protein. DRAMP31275 CDVIALLCHLNTPSFNTTHYRESWY 25 P11 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17151121]west nile virus(WNV):inhibition of virus infection in Vero cells(P10 significantly inhibited WNV infectivity). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented E proteins 17151121 J Virol. 2007 Feb;81(4):2047-55.  Bai F, Town T, Pradhan D, Cox J, Ashish, Ledizet M, Anderson JF, Flavell RA, Krueger JK, Koski RA, Fikrig E. Antiviral peptides targeting the west nile virus envelope protein. DRAMP31276 SSCNMGWDTPAAnti-CCVWFPYWV 20 A4 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(70% inhibition). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented pUL84(nonconventional nuclear localization signal of the essential viral replication factor) 19740994 J Virol. 2009 Nov;83(22):11902-13.  Kaiser N, Lischka P, Wagenknecht N, Stamminger T. Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. DRAMP31277 MAVGLVLCDWWLGEYLLEA 19 A8 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(70% inhibition). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented pUL84(nonconventional nuclear localization signal of the essential viral replication factor) 19740994 J Virol. 2009 Nov;83(22):11902-13.  Kaiser N, Lischka P, Wagenknecht N, Stamminger T. Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. DRAMP31278 PVLQPALSLSCGPEPLLLSC 20 A56 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(40% inhibition). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented pUL84(nonconventional nuclear localization signal of the essential viral replication factor) 19740994 J Virol. 2009 Nov;83(22):11902-13.  Kaiser N, Lischka P, Wagenknecht N, Stamminger T. Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. DRAMP31279 IEVTFVNRRGDGAELWYLSA 20 A110 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide specifically bind to UL84 protein and utilized to inhibit HCMV replication. [Ref.19740994]human cytomegalovirus(HCMV):inhibition of virus replication in HeLa cells(35% inhibition). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented pUL84(nonconventional nuclear localization signal of the essential viral replication factor) 19740994 J Virol. 2009 Nov;83(22):11902-13.  Kaiser N, Lischka P, Wagenknecht N, Stamminger T. Inhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84. DRAMP31280 SFAIKWEYVLLLFLL 15 Peptide 75(710-725)[Δ1] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(91% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31281 FAIKWEYVLLLFLL 14 Peptide 75(710-725)[Δ1-2] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(95% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31282 AIKWEYVLLLFLL 13 Peptide 75(710-725)[Δ1-3] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(92% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31283 IKWEYVLLLFLL 12 Peptide 75(710-725)[Δ1-4] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(88% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31284 KWEYVLLLFLL 11 Peptide 75(710-725)[Δ1-5] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(78% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31285 WEYVLLLFLL 10 Peptide 75(710-725)[Δ1-6] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(82% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31286 VSFAIKWEYVLLLFL 15 Peptide 75(710-725)[Δ16] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(63% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31287 VSFAIKWEYVLLLF 14 Peptide 75(710-725)[Δ15-16] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(49% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31288 VSFAIKWEYVLLL 13 Peptide 75(710-725)[Δ14-16] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(49% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31289 VSFAIKWEYVLL 12 Peptide 75(710-725)[Δ13-16] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(44% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31290 VSFAIKWEYVL 11 Peptide 75(710-725)[Δ12-16] P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(17% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31291 VSFAIKWEYVLLLFLL 16 Peptide 75(710-725) P26663 Flaviviridae Not found Synthetic construct(derived from HCV envelope protein) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits a post-binding step in HCV entry. [Ref.20156485]hepatitis C virus(HCVpp):inhibition of virus infection in Huh-7 human hepatoma cells(EC50=0.3 ± 0.4 μM,EC90=14 ± 12 μM);inhibition of virus infection in primary human hepatocytes(EC50=0.3μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20156485]No cytotoxicity against Huh-7 cells. envelope protein 20156485 Antiviral Res. 2010 May;86(2):172-9. Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.  DRAMP31292 RWMVWRHWFHRLRLPYNPGKNKQNQQWP 28 DN57opt No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein. [Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=8±1 μM,97% inhibition at 20μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20582308]the peptide was found to be mildly toxic to LLC-MK2 cells at 40 µM. E glycoprotein 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF. Structural optimization and de novo design of dengue virus entry inhibitory peptides. DRAMP31293 RQMRAWGQDYQHGGMGYSC 19 DN81opt No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein. [Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=36±6 μM,57% inhibition at 50μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented E glycoprotein 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF. Structural optimization and de novo design of dengue virus entry inhibitory peptides. DRAMP31294 FWFTLIKTQAKQPARYRRFC 20 1OAN1 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide blocks virus:cell binding, interfere with a step during viral entry, alter the surface structure of dengue viral particles, and that they interact directly with dengue virus envelope protein. [Ref.20582308]dengue 2 virus(DENV-2):inhibition of virus infection in LLC-MK2 cells(IC50=7±4 μM,99% inhibition at 50 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.20582308]the peptide showed no toxic to LLC-MK2 cells at 50 µM. E glycoprotein 20582308 PLoS Negl Trop Dis. 2010 Jun 22;4(6):e721.  Costin JM, Jenwitheesuk E, Lok SM, Hunsperger E, Conrads KA, Fontaine KA, Rees CR, Rossmann MG, Isern S, Samudrala R, Michael SF. Structural optimization and de novo design of dengue virus entry inhibitory peptides. DRAMP31295 LLDCWVRLGRYLLRRLKT 18 GBVA1(1-18) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=10 μM,88% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31296 LLDCWVRLGRYLLRRLKTPFTRL 23 GBVA2(1-23) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=15 μM,50% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31297 LLDCWVRLGRYLLRRLKTPFT 21 GBVA3(1-21) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31298 LLDCWVRLGRYLLRRLKTP 19 GBVA4(1-19) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=3 μM,99% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31299 LLDCWVRLGRYLLRRLK 17 GBVA5(1-17) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=5 μM,99% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31300 LDCWVRLGRYLLRRLKTPFTRL 22 GBVA6(2-23) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0 inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31301 CWVRLGRYLLRRLKTPFTRL 20 GBVA7(4-23) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,89% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31302 LDCWVRLGRYLLRRLKTP 18 GBVA8(2-19) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=4 μM,99% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31303 DCWVRLGRYLLRRLKTPF 18 GBVA9(3-20) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,90% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31304 CWVRLGRYLLRRLKTPFT 18 GBVA10(4-21) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2 μM,100% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31305 WVRLGRYLLRRLKTPFTR 18 GBVA11(5-22) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=12 μM,58% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31306 VRLGRYLLRRLKTPFTRL 18 GBVA12(6-23) Q69422 Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM,0 inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31307 CWVRLGRYKLRRLKTPFT 18 GBVA10-1(L9K) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175360 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31308 CWVRLGRYSLRRLKTPFT 18 GBVA10-2(L9S) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=18 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31309 CWVRLGRYALRRLKTPFT 18 GBVA10-3(L9A) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31310 CWVRLGRYVLRRLKTPFT 18 GBVA10-4(L9V) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=16 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31311 CWVRLARYLLRRLKTPFT 18 GBVA10-5(G6A) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=2.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31312 CWVRLVRYLLRRLKTPFT 18 GBVA10-6(G6V) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31313 CWVRLLRYLLRRLKTPFT 18 GBVA10-7(G6L) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31314 CWVRLLRYLLRRLKTLFT 18 GBVA10-8(G6L/P16L) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=1.25 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31315 CWVRLGRYLLRRLKTLFT 18 GBVA10-9(P16L) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: GBVA10-9 can inhibit virus entry at a postattachment step. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=0.16 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23175359]HepG2 cell:LC50=90 μM(4h of treatment);##HeLa cell:LC50=40 μM(4h of treatment);##Huh7.5.1 cell:LC50=90 μM(4h of treatment);LC50=50 μM(24h of treatment). Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31316 CWVRLGRYILRRLKTPFT 18 GBVA10-10(L9I) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31317 CWVRLGRYILRRIKTPFT 18 GBVA10-11(L9I/L13I) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50=0.63 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31318 CWVRIGRYILRRIKTPFT 18 GBVA10-12(L5I/L9I/L13I) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31319 KWVRLGRKLLRRLKKPFK 18 GBVA10-13(C1K/Y8K/T15K/T18K) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175361 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31320 KWVRLGRKLLRRLKKPFT 18 GBVA10-14(C1K/Y8K/T15K) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31321 CWVRLGRKLLRRLKKPFT 18 GBVA10-15(Y8K/T15K) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31322 CWVRLGRKLLRRLKTPFT 19 GBVA10-16(Y8K) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31323 EWVRLGRELLRRLKEPFT 18 GBVA10-17(C1E/Y8E/T15E) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31324 EWVRLGRELLRRLKEPFE 19 GBVA10-18(C1E/Y8E/T15E/T18E) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31325 CWVRLGRELLRRLKEPFT 18 GBVA10-19(Y8E/T15E) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31326 CWVRLGRELLRRLKTPFT 18 GBVA10-20(Y8E) No entry found Flaviviridae Not found Synthetic construct(derived from GBVA non-structutal protein 5A) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits virus entry. [Ref.23175359]hepatitis C virus(Jc1-Luc HCVcc):inhibition of virus entry in Huh7.5.1 cells(IC50>20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information found in the reference(s) presented Not found 23175359 J Virol. 2013 Feb;87(3):1649-57. Liu X, Huang Y, Cheng M, Pan L, Si Y, Li G, Niu Y, Zhao L, Zhao J, Li X, Chen Y, Yang W. Screening and rational design of hepatitis C virus entry inhibitory peptides derived from GB virus A NS5A. DRAMP31327 IPESSELTLQELLGEERR 18 E6ap18 No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=10.5±1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31328 YKFACPECPKRFMRSDHLTLHILLHENKK 29 E6apc1 No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50>1000 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31329 YKFACPECPKRFMRSDHLSKHITLHELLGEERR 33 E6apc2 No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=19.3±2.9μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31330 ALQELLGQWLKDGGPSSGRPPPS 23 E6apn1 No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=36.8±3.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31331 ALQELLGEYIQWLKDGGPSSGRPPPS 26 E6apn2 No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=26.2±4.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31332 YLQELLGE 8 E6apm No entry found Papillomaviridae Not found Synthetic construct(derived from E6-associated protein (E6AP)) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15182185]Human papillomavirus(HPV):inhibition of E6-E6ap interaction(IC50=74.3±1.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information found in the reference(s) presented E6 protein 15182185 Biochemistry. 2004 Jun 15;43(23):7421-31.  Liu Y, Liu Z, Androphy E, Chen J, Baleja JD. Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus. DRAMP31333 FLKGIVGMLGKLF 13 Temporin-Sha[K3] No entry found Herpesviridae Not found Synthetic construct(derived from Temporin-SHa) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30669255]HSV-1:inhibition of HSV-1 replication in human keratinocytes(48% inhibition at 2.5 µM,57% inhibition at 5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.30669255]Significant cytotoxicity was observed on Keratinocyte at the concentration of 10 μM with a cell viability of 74%. Not found 30669255 Viruses. 2019 Jan 18;11(1):77. Roy M, Lebeau L, Chessa C, Damour A, Ladram A, Oury B, Boutolleau D, Bodet C, Lévêque N.  Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1. DRAMP31334 LLGDLLRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES 37 LL-37[F5,6L] No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=18.4 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31335 LLGDLLRKSKEKIGKEFKRIVQR 23 LL-23 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>35.4 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50>35.4 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31336 SKEKIGKEFKRIVQRIKDFLR 21 SK-21 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=10.8 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=22.5 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31337 SKVNGQSGRMEFFWTILK 18 HA-pep25 No entry found Orthomyxoviridae Not found Synthetic construct(derived from influenza viral HA) Antimicrobial, Antiviral Not found Not found Not found Mechanism: Block the HA–cell interactions by binding to the influenza host cell receptor sialyllactose and thus inhibit the viral entry. [Ref.27623031]Influenza A Virus(A/PuertoRico/8/1934):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=34.0 ± 11.5μM);##AInfluenza A Virus(/Vietnam/1203/2004):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=12.0 ± 2.1μM);##influenza A virus(A/Goose/Qinghai/59/2005):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=34.8 ± 1.5μM);##influenza A virus(A/Duck/Anhui/SC702/2013):inhibition of virus entry into Madin Darby canine kidney (MDCK) cells(IC50=51.0 ± 0.6μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA receptor binding domain (RBD) 27623031 ACS Infect Dis. 2016 Mar 11;2(3):187-93 Chen Q, Guo Y Influenza Viral Hemagglutinin Peptide Inhibits Influenza Viral Entry by Shielding the Host Receptor DRAMP31338 GFKRIVQRiKDFLRNLV 17 GF-17d1 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>47.5 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Mixed(D-Ile9) [Ref.18591279]CEM-SS cells:TC50=22.7 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31339 GFKRIVQRiKDFlRNLV 17 GF-17d2 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>47.5μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free Mixed(D-Ile9,D-Leu13) [Ref.18591279]CEM-SS cells:TC50>47.5 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31340 GIKEFKRIVQRIKDFLRNLV 20 GI-20 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.08 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=22.7 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31341 GIKEXKRIVQRIKDFLRNLV 20 GI-20X17 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>40.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 5 is phenylglycine L [Ref.18591279]CEM-SS cells:TC50=7.3 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31342 GIKEWKRIVQRIKDFLRNLV 20 GI-20W17 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=7.4 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=23.6 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31343 GIKQFKRIVQRIKDFLRNLV 20 GI-20Q16 No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.91 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=13.7 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31344 GIKEFKREFQRIKDFLRNLV 20 GI-20EF No entry found Retroviridae Not found Synthetic construct(derived from human cathelicidin LL-37) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=1.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=9.9 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31345 GRFKRFRKKFKKLFKKIS 18 BMAP-18 No entry found Retroviridae Not found Synthetic construct(derived from BMAP-27) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.35 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=8.45 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31346 GRFKRFRKPFKKLFKKIS 18 BMAP-18P9 No entry found Retroviridae Not found Synthetic construct(derived from BMAP-27) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=3.20 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=18.9 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31347 GRFKRXRKKXKKLFKKIS 18 BMAP-18X6X10 No entry found Retroviridae Not found Synthetic construct(derived from BMAP-27) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50=0.68 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 6 and 10 are phenylglycine L [Ref.18591279]CEM-SS cells:TC50=10.2 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31348 GRFKRIRKKLKKLFKKIS 18 BMAP-18I6L10 No entry found Retroviridae Not found Synthetic construct(derived from BMAP-27) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>44.0 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50=2.79 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31349 GRFKRFRKKFKKLFK 15 BMAP-15 No entry found Retroviridae Not found Synthetic construct(derived from BMAP-27) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.18591279]HIV-1IIIB:inhibition the cytopathic effect of HIV in CEM-SS cells(EC50>49.6 μM).(EC50:50% effective concentration for inhibition of virus replication) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.18591279]CEM-SS cells:TC50>49.6 μM.(TC50:the concentration that reduced cell viability by 50%) Not found 18591279 Antimicrob Agents Chemother. 2008 Sep;52(9):3438-40.  Wang G, Watson KM, Buckheit RW Jr.  Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. DRAMP31350 MKTFSVAVAVAIVLAFICTQESSALPVTGVEELVELVSSDDPVADHQELPVELGERLFNIRKKRASPKCTPYCYPTRDGVFCGVRCDF 88 EC-hepcidin1 No entry found Iridoviridae Not found Epinephelus coioides Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.21145974]Singapore grouper iridovirus (SGIV):strongly inhibit the replication of SGIV.(EC-hepcidin1 is more active than EC-hepcidin2) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two pairs of disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-68.  Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW. Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides.  DRAMP31351 MKTFSVAVAVAVVLAFICTQESSALPVTGIEELVEPVSSDNNDNHQGLPVELRERLVNIRKKRAPTDCIPYCYPTGDGFHCGVTCRF 87 EC-hepcidin2 No entry found Iridoviridae Not found Epinephelus coioides Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.21145974]Singapore grouper iridovirus (SGIV):strongly inhibit the replication of SGIV.(EC-hepcidin1 is more active than EC-hepcidin2) No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free There are two pairs of disulfide bonds. L No cytotoxicity information found in the reference(s) presented Not found 21145974 Fish Shellfish Immunol. 2011 Feb;30(2):559-68.  Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW. Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides.  DRAMP31352 GVCRCLCRRGVCRCLCRR 18 RTD-2 (RTD 2, rhesus theta-defensin 2) P82271 Retroviridae Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide binds to gp120 and CD4, thereby inhibiting HIV entry. [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=5.20 ± 1.58 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=1.78± 0.57 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=6.74 ± 1.27 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=3.66 ± 0.69 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=3.02 ± 0.10 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=3.08 ± 1.35 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=5.16 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found in the reference(s) presented gp120,CD4 15210812 J Immunol. 2004 Jul 1;173(1):515-20. Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI. Activity of alpha- and theta-defensins against primary isolates of HIV-1.  DRAMP31353 GFCRCICTRGFCRCICTR 18 RTD-3 (rhesus theta defensin 3) P82270,Q9TU01 Retroviridae Not found Macaca mulatta (Rhesus macaque) Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide binds to gp120 and CD4, thereby inhibiting HIV entry. [Ref.15210812]HIV-1 A:inhibition of infection in JC53-BL cells(IC50=3.26 ± 0.58 µg/ml);##HIV-1 B:inhibition of infection in JC53-BL cells(IC50=1.74± 0.40 µg/ml);##HIV-1 C:inhibition of infection in JC53-BL cells(IC50=4.31 ± 0.90 µg/ml);##HIV-1 CRF01_AE:inhibition of infection in JC53-BL cells(IC50=2.09 ± 0.60 µg/ml);##HIV-1 D:inhibition of infection in JC53-BL cells(IC50=2.31 ± 0.21 µg/ml);##HIV-1 G:inhibition of infection in JC53-BL cells(IC50=3.04 ± 0.64 µg/ml);##HIV-1 BF:inhibition of infection in JC53-BL cells(IC50=0.89 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys3 and Cys16,Cys5 and Cys14,Cys7 and Cys12. L No cytotoxicity information found in the reference(s) presented gp120,CD4 15210812 J Immunol. 2004 Jul 1;173(1):515-20. Wang W, Owen SM, Rudolph DL, Cole AM, Hong T, Waring AJ, Lal RB, Lehrer RI. Activity of alpha- and theta-defensins against primary isolates of HIV-1.  DRAMP31354 RPRLSHKGPMPF 12 Apelin-12 Q9TUI9##K7GLR4 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=63.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 10802050 FEBS Lett. 2000 May 4;473(1):15-8. Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H. Apelin peptides block the entry of human immunodeficiency virus (HIV). DRAMP31355 QRPRLSHKGPMPF 13 Apelin-13 Q9TUI9##A0A484GMR2##A0A5N3XG03##A0A2Y9M6A9##A0A5G2R3Z5##A0A2Y9SZ03##A0A2U4A1K6 Retroviridae Not found Bos taurus (Bovine) Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=26.0 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 10802050 FEBS Lett. 2000 May 4;473(1):15-8. Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H. Apelin peptides block the entry of human immunodeficiency virus (HIV). DRAMP31356 KFRRQRPRLSHKGPMPF 17 Apelin-17 Q9TUI9##K7GLR4 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=4.8 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 10802050 FEBS Lett. 2000 May 4;473(1):15-8. Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H. Apelin peptides block the entry of human immunodeficiency virus (HIV). DRAMP31357 LVQPRGPRSGPGPWQGGRRKFRRQRPRLSHKGPMPF 36 Apelin-36 Q9TUI9##A0A484GMR2##A0A5N3XG03##A0A2Y9M6A9##A0A5G2R3Z5##A0A2Y9SZ03##A0A2U4A1K6 Retroviridae Not found Bos taurus (Bovine) Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.10802050]HIV:Inhibition of HIV infection in NP-2/CD4/APJ cells(IC50=0.3 μg/ml).##[Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 10802050##11090199 FEBS Lett. 2000 May 4;473(1):15-8.##J Virol. 2000 Dec;74(24):11972-6. Zou MX, Liu HY, Haraguchi Y, Soda Y, Tatemoto K, Hoshino H.##Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin peptides block the entry of human immunodeficiency virus (HIV).##Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry. DRAMP31358 RRQRPRLSHKGPMPF 15 Apelin-15 Q9TUI9 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=12μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 11090199 J Virol. 2000 Dec;74(24):11972-6. Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry.  DRAMP31359 RRKFRRQRPRLSHKGPMPF 19 Apelin-19 Q9TUI9 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=4.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 11090199 J Virol. 2000 Dec;74(24):11972-6. Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry.  DRAMP31360 RRQRPRLSHKGPM 13 Apelin-15-(63-75)-peptide Q9TUI9 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 11090199 J Virol. 2000 Dec;74(24):11972-6. Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry.  DRAMP31361 RRQRPRLSHKGPX 13 [Met(O)75]apelin-15-(63-75)-peptide Q9TUI9 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=45 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free The 'X' at position 13 indicates oxidized methionine. L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 11090199 J Virol. 2000 Dec;74(24):11972-6. Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry.  DRAMP31362 RRQRPRLSHKGP 12 Apelin-15-(63-74)-peptide Q9TUI9 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: APJ receptor could help HIV virus enter the target cells. The peptide can bind with APJ receptor and block virus entry, thus inhibiting virus infection. [Ref.11090199]HIV-1:inhibition of HIV-1 infection in CD4 APJ cells(IC50=37 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry APJ receptor 11090199 J Virol. 2000 Dec;74(24):11972-6. Cayabyab M, Hinuma S, Farzan M, Choe H, Fukusumi S, Kitada C, Nishizawa N, Hosoya M, Nishimura O, Messele T, Pollakis G, Goudsmit J, Fujino M, Sodroski J. Apelin, the natural ligand of the orphan seven-transmembrane receptor APJ, inhibits human immunodeficiency virus type 1 entry.  DRAMP31363 RRKKRRQRRR 10 TAT(48-57)[G1R] P04610 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.065 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22319541 Int J Pept. 2012;2012:349427. Keogan S, Passic S, Krebs FC. Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. DRAMP31364 GRKKRRRRRR 10 TAT(48-57)[Q7R] P04610 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.071 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22319541 Int J Pept. 2012;2012:349427. Keogan S, Passic S, Krebs FC. Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. DRAMP31365 RRKKRRRRRR 10 TAT(48-57)[G1R,Q7R] P04610 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.22319541]HIV-1 IIIB:inhibition of virus infection in P4-R5 MAGI cells(EC50=0.025 mg/mL). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 22319541 Int J Pept. 2012;2012:349427. Keogan S, Passic S, Krebs FC. Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat. DRAMP31366 KGEAMHGQVDCSPGIWQLDC 20 #4330 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1:inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(IC50=4 μM);inhibition of reverse transcriptase(DNA-dependent DNA polymerase) activity(IC50=6.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31367 ASCDKCQLKGEAMHG 15 #5649 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(91.5 ± 2.5% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31368 KCQLKGEAMHGQVDC 15 #5650 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(63± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31369 KGEAMHGQVDCSPGI 15 #5651 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(99 ± 6% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31370 MHGQVDCSPGIWQLD 15 #5652 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(79 ± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31371 VDCSPGIWQLDCTHL 15 #5653 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(58 ± 3% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31372 PGIWQLDCTHLEGKI 15 #5654 derived from HIV-1 integrase P04587 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could bind the reverse transcriptase and inhibits its DNA-polymerase activity and thus inhibits virus replication. [Ref.17257575]HIV-1: inhibition of reverse transcriptase(RNA-dependent DNA polymerase) activity(62.5 ± 0.5% residual DNA polymerase activity at 30 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Reverse Transcriptase 17257575 Arch Biochem Biophys. 2007 Feb 15;458(2):202-12. Oz Gleenberg I, Herschhorn A, Goldgur Y, Hizi A. Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase. DRAMP31373 SWLRDLWDWICEVLSDFK 18 NS5A-derived peptide C5A [I6L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.13 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=13.84 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31374 SWLRDIWDWLCEVLSDFK 18 NS5A-derived peptide C5A [I10L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.09 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=1.84±0.16 μM). [Ref.21801309]Human erythrocytes:MHC=6.92 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31375 SWLRDIWDWICELLSDFK 18 NS5A-derived peptide C5A [V13L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.11 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.76±0.19 μM). [Ref.21801309]Human erythrocytes:MHC=3.44 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31376 SWLRDLWDWLCEVLSDFK 18 NS5A-derived peptide C5A [I6L,I10L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.15 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=6.92 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31377 SWLRDLWDWICELLSDFK 18 NS5A-derived peptide C5A [I6L,V13L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=0.78±0.07 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=3.31±0.31 μM). [Ref.21801309]Human erythrocytes:MHC=53.75 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31378 SWLRDIWDWLCELLSDFK 18 NS5A-derived peptide C5A [I10L,V13L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=0.82±0.10 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.58±0.22 μM). [Ref.21801309]Human erythrocytes:MHC=3.44 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31379 SWLRDLWDWLCELLSDFK 18 NS5A-derived peptide C5A [I6L,I10L,V13L] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.20±0.14 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=0.59±0.03 μM). [Ref.21801309]Human erythrocytes:MHC=107.50 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31380 SWLRDIWDWVCEVLSDFK 18 NS5A-derived peptide C5A [I10V] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=1.40±0.117 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=1.86±0.25 μM). [Ref.21801309]Human erythrocytes:MHC=13.93 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31381 SWLRDIWDWACEVLSDFK 18 NS5A-derived peptide C5A [I10A] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50=4.00±0.36 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=2.21±0.28 μM). [Ref.21801309]Human erythrocytes:MHC=14.10 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31382 SWLRDIWDWGCEVLSDFK 18 NS5A-derived peptide C5A [I10G] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50=3.50±0.36 μM). [Ref.21801309]Human erythrocytes:MHC=28.38 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31383 SWLRDIWDWSCEVLSDFK 18 NS5A-derived peptide C5A [I10S] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=28.00 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31384 SWLRDIWDWECEVLSDFK 18 NS5A-derived peptide C5A [I10E] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=214.91 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31385 SWLRDIWDWKCEVLSDFK 18 NS5A-derived peptide C5A [I10K] V5RF15 Flaviviridae, Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits HCV and HIV infection in vitro, which can disrupt the integrity of the viral membrane and capsid core while preserving the integrity of host membranes. [Ref.21801309]HCV: inhibition of HCVcc infection in Huh7.5.1 cells(IC50>5.00 μM);##HIV-1:inhibition of pseudotyped HIV infection in TZM-BL cells(IC50>5.00 μM). [Ref.21801309]Human erythrocytes:MHC=214.81 μM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 21801309 Chem Biol Drug Des. 2011 Nov;78(5):835-43. Li GR, He LY, Liu XY, Liu AP, Huang YB, Qiu C, Zhang XY, Xu JQ, Yang W, Chen YX. Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. DRAMP31386 TRQARRNRRRRWRERQR 17 Rev (34-50) P05866 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found 1ULL Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=1.7±0.25 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31387 TRQARRNRRRRWRERQRAAAAC 22 Rev (34-50) -A4C P05866 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=0.35±0.07 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31388 TRQARRNRRRRWRERQRAAAACYGRKKRRQRRR 33 Rev (34-50) -A4C-RTD P05866##P04612 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=0.37±0.09 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31389 MPKTRRRPRRSQRKRPPTPWP 21 Rex (1-21) P0C207 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31390 MPKTRRRPRRSQRKRPPTPWPYGRKKRRQRRR 32 Rex (1-21) -RTD P0C207##P04612 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=2.5±0.76 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31391 RPRGRRGSRPSGAERRRRRAAAA 23 RSG-P2G4 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from the RNA-binding domain of HIV-1 Rev can act as dual-target inhibitors that inhibit HIV-1 entry and viral production in the early and late phases of replication.  [Ref.20580677]HIV-1 IIIB:inhibition of virus replication in PM1-CCR5 cells(EC50=2.2±0.51 μM);##HIV-1 Bal:inhibition of virus replication in PM1-CCR5 cells(EC50>10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 20580677 Int J Biochem Cell Biol. 2010 Sep;42(9):1482-8. Shimane K, Kodama EN, Nakase I, Futaki S, Sakurai Y, Sakagami Y, Li X, Hattori T, Sarafianos SG, Matsuoka M. Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4. DRAMP31392 RSQKEGLHYTCSSHFPYSQYQFWK 24 CCR5 ECL2 (168-191) P51681 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide binds gp120 and inhibits virus entry. [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=136 ± 49 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=138± 36 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=89±31 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=103±37 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry gp120 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA. Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. DRAMP31393 CSSHFPYSQYQFWK 14 CCR5 ECL2 (178-191) P51681 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide binds gp120 and inhibits virus entry. [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=28 ±7 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=65± 3 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=54±2 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=53±2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry gp120 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA. Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. DRAMP31394 QKEGLHYTCSSHFPYSQYQF 20 CCR5 ECL2 (170-189) P51681 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide binds gp120 and inhibits virus entry. [Ref.22403408]HIV-1 YU2:inhibition of virus infection in TZM-bl cells(IC50=237 ± 31 μM);##HIV-1 BaL26:inhibition of virus infection in TZM-bl cells(IC50=612± 21 μM);##HIV-1 HxB2:inhibition of virus infection in TZM-bl cells(IC50=374±28 μM);##HIV-1 NL4-3:inhibition of virus infection in TZM-bl cells(IC50=600±24 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry gp120 22403408 J Biol Chem. 2012 Apr 27;287(18):15076-86. Dogo-Isonagie C, Lam S, Gustchina E, Acharya P, Yang Y, Shahzad-ul-Hussan S, Clore GM, Kwong PD, Bewley CA. Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. DRAMP31395 RRWYRWW 7 Octa 1 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31396 RRWYRWWRRRWYRWWR 16 MU89 (Octa 1 dp) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=8.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31397 RWWRWWR 7 Hepta 1 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31398 RWWRWWRRWWRWWR 14 MU92 (Hepta 1 dp) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=3.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31399 YRWWRWARRW 10 Deca 1 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31400 YRWWRWARRWYRWWRWARRW 20 MU94 (Deca 1 dp) No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=5 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31401 APKAMRLLRRLLRRLLR 17 N-[RLLR]3 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=7.3 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31402 RRRRRRRWWWRRRRRRRR 18 MU103 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50>20 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31403 RRRRRRRRRRRRRRRWWW 18 MU104 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=9.25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31404 WRKWRKRWWWRKWRKRWW 18 ApoEdpL-W No entry found Herpesviridae, Retroviridae, Rhabdoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The anti-HSV1 activity of apoEdp involves inhibition of virus particle attachment to cells, with this likely being related to the derivation of this peptide from the apoE HSPG/LDLR binding region. [Ref.17681018]HSV-1:inhibition of virus infection in NP-2/CD4/CCR5 cells(IC50=3.1 µM);##HIV-1:inhibition of virus replication(>80% inhibition at 10 µM). [Ref.17681018]15% hemolysis against human red blood cells at 35 μM. Linear Free Free L [Ref.17681018]No significant cytotoxicity against Vero cells up to 40 μM. Not found 17681018 FEBS J. 2007 Sep;274(17):4511-25. Kelly BA, Neil SJ, McKnight A, Santos JM, Sinnis P, Jack ER, Middleton DA, Dobson CB. Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. DRAMP31405 HCKFWW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31406 HCKFWI 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31407 HCKFWF 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31408 HCKFAW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=150 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31409 HCKFWA 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=210 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31410 HCKAWW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31411 ACKFWW 6 No entry found Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may inhibit integrase-mediated 3'-processing and integration, which is useful for inhibiting virus replication. [Ref.8524782]HIV-1:inhibition of integrase-mediated 3'-processing and integration(IC50=51 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry integrase 8524782 Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11456-60. Puras Lutzke RA, Eppens NA, Weber PA, Houghten RA, Plasterk RH. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. DRAMP31412 GWINEKKMQQKIDEKIGKNIIGGMAKAVIHKMAKNEFQCVANVDTLGNCKKHCAKTTGEKGYCHGTKCKCGIELSY 76 Smp76 No entry found Flaviviridae Not found Scorpio maurus palmatu Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.32435168]Dengue Virus(DENV):inhibition of viral infection in Vero/SLAM cells(IC50= 0.01 μg/ml). [Ref.32435168]human red blood cells:HC50>10 μg/ml. Cyclic Free Free Disulfide bonds between Cys39 and Cys63, Cys49 and Cys68, Cys53 and Cys70. L [Ref.32435168]Huh7it-1 cells:CC50>10 μg/ml. Not found 32435168 Int J Pept Res Ther. 2020;26(2):811-821. El-Bitar AMH, Sarhan M, Abdel-Rahman MA, Quintero-Hernandez V, Aoki-Utsubo C, Moustafa MA, Possani LD, Hotta H. Smp76, a Scorpine-Like Peptide Isolated from the Venom of the Scorpion Scorpio maurus palmatus, with a Potent Antiviral Activity Against Hepatitis C Virus and Dengue Virus. DRAMP31413 GFGCPFNQGQCHKHCQSIRRRGGYCDGFLKTRCVCYR 37 BmKDfsin4 No entry found Hepadnaviridae Not found Mesobuthus martensii Antimicrobial, Antiviral Not found Not found Not found Mechanism: BmKDfsin4 had been shown to exhibit powerful inhibitory activity against HBV replication by reducing the production of HBeAg, HBsAg, and HBV DNAin cell culture medium and the production of intracellular HBsAg, HBV core protein, HBx protein, and HBV RT. [Ref.27128943]hepatitic B Virus (HBV): Pharmacological profiles of BmKDfsin4 against HBeAg, HBsAg and HBV DNA on HepG2.2.15 cells(HBeAg: IC50= 3.95 μM; HBsAg: IC50= 2.28 μM; HBV DNA: IC50= 1.26 μM). [Ref.27128943]Human erythrocytes: 50% hemolysis concentration was 66.85 μM. Cyclic Free Free Disulfide bonds between Cys4 and Cys25, Cys11 and Cys33, Cys15 and Cys35. L [Ref.27128943]HepG2.2.15 cells: CC50= 167.82 μM;##HepG2 cells: CC50= 154.24 μM;##L-02 cells: CC50= 103.77 μM. Not found 27128943 Toxins (Basel). 2016 Apr 27;8(5):124. Zeng Z, Zhang Q, Hong W, Xie Y, Liu Y, Li W, Wu Y, Cao Z. A Scorpion Defensin BmKDfsin4 Inhibits Hepatitis B Virus Replication in Vitro. DRAMP31414 LLMVNEATRFQTVSGFV 17 BPIP No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits Mpro, a protein crucial for viral replication. [Ref.35896605]SARS-CoV-2: inhibition of Mpro (IC50= 0.52 nM). [Ref.35896605]BRIP is not hemolytic at 500 nM and slightly hemolytic at 50 µM. Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Mpro 35896605 Sci Rep. 2022 Jul 27;12(1):12802 Kashyap P, Bhardwaj VK, Chauhan M, Chauhan V, Kumar A, Purohit R, Kumar A, Kumar S A ricin-based peptide BRIP from Hordeum vulgare inhibits Mpro of SARS-CoV-2 DRAMP31415 KFFRKKSVKK 10 BF-30 No entry found Orthomyxoviridae Not found Bungarus fasciatus Antimicrobial, Antiviral Not found Not found Not found Mechanism: BF-30 could inhibit the replication of various influenza subtypes by fusing virion membranes and reducing infectivity. [Ref.30447229]Influenza A virus H1N1:inhibition of viral replication in MDCK cells(EC50=5.20±0.9 μM);##influenza A virus H3N2: inhibition of viral replication in MDCK cells(EC50=7.36 ± 1.2 μM);##influenza A virus(oseltamivir-resistant strain): inhibition of viral replication in MDCK cells(EC50=18.91 ± 7.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30447229]MDCK cells:CC50=67.7μM. Not found 30447229 Peptides. 2019 Feb;112:14-22. Xu J, Chen S, Jin J, Ma L, Guo M, Zhou C, Dou J. Inhibition of peptide BF-30 on influenza A virus infection in vitro/vivo by causing virion membrane fusion. DRAMP31416 FLGAILKIGHALAKTVLPMVTNAFKPKQ 28 Figainin 2 A0A2L2DDD0 Not found Boana raniceps (Hypsiboas raniceps) Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.32443921]chikungunya virus (CHIKV):inhibition of viral infection in Huh7 cells(EC50=17 μM);##Dengue Serotype 4 Virus(DENV4):inhibition of viral infection in Huh7 cells(EC50=20.8 μM);##Yellow Fever viral (YFV):inhibition of viral infection in Huh7 cells(EC50=21.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32443921]No cytotoxicity against noninfected Huh7 cells at concentrations as high as 25 µM. Not found 32443921 Biomolecules. 2020 May 20;10(5):790. Santana CJC, Magalhães ACM, Prías-Márquez CA, Falico DA, Dos Santos Júnior ACM, Lima BD, Ricart CAO, de Pilger DRB, Bonotto RM, Moraes CB, Freitas-Júnior LH, Álvares ADCM, Freitas SM, Luz IS, Pires OR Jr, Fontes W, Castro MS. Biological Properties of a Novel Multifunctional Host Defense Peptide from the Skin Secretion of the Chaco Tree Frog, Boana raniceps. DRAMP31417 MRRKVELFTYMRFD 14 TP1 No entry found Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.34314773]RD cells: CC50=683.6 μM. Not found 34314773 Virus Res. 2021 Oct 2;303:198456. Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL. Stability and antiviral activity of SP41 peptide in human serum. DRAMP31418 RRKVELFTYMRFD 13 TP2 No entry found Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.34314773]RD cells: CC50=345 μM. Not found 34314773 Virus Res. 2021 Oct 2;303:198456. Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL. Stability and antiviral activity of SP42 peptide in human serum. DRAMP31419 RKVELFTYMRFD 12 TP3 No entry found Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.34314773]RD cells: CC50=1123 μM. Not found 34314773 Virus Res. 2021 Oct 2;303:198456. Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL. Stability and antiviral activity of SP43 peptide in human serum. DRAMP31420 QMRRKVELFTYMRF 14 TP10 No entry found Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide could associate with the cellular receptors at the surface of cells and prevented the attachment of EV-A71 to the cellular receptors. [Ref.34314773]Enterovirus A71 (EV-A71):inhibition of viral replication into RD cells(IC50=6.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L [Ref.34314773]RD cells: CC50=231 μM. Not found 34314773 Virus Res. 2021 Oct 2;303:198456. Zarif F, Anasir MI, Koh JX, Chew MF, Poh CL. Stability and antiviral activity of SP44 peptide in human serum. DRAMP31421 AKVTMTCSAS 10 KP P01680 Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (96% inhibition at 50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31422 KKVTMTCSAS 10 K10S P01680 Herpesviridae, Picornaviridae, Adenoviridae, Rhabdoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (45% inhibition at 10 µg/ml, 76% inhibition at 50 µg/ml, 89% inhibition at 100 µg/ml);##Coxsackie virus B5:inhibition of viral replication in Vero cells (75% inhibition at 50 µg/ml, 94% inhibition at 100 µg/ml);##Vesicular Stomatitis Virus (VSV):inhibition of viral replication in Vero cells (78% inhibition at 50 µg/ml, 96% inhibition at 100 µg/ml);##Adenovirus:inhibition of viral replication in Vero cells (75% inhibition at 50 µg/ml, 91% inhibition at 100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]20% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31423 KKLVAASQAALGL 13 K13L P02768-2 Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 80% inhibition at 50 µg/ml, 87% inhibition at 100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]30% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31424 DSGEGDFLAEGGGVR 15 D15R P02671 Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (82% inhibition at 10 µg/ml, 85% inhibition at 50 µg/ml, 93% inhibition at 100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31425 GLEEELQFSLGSKINVK 17 G17K P0C0L5 Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 75% inhibition at 50 µg/ml, 88% inhibition at 100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31426 SEETKENEGFTVTAEGK 17 S17K P01024 Adenoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]Adenovirus:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 65% inhibition at 50 µg/ml, 80% inhibition at 100 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31427 LCLRNWDQGHRP 12 L12P A0M8Q8 Herpesviridae, Picornaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30654366]HSV-1:inhibition of viral replication in Vero cells (78% inhibition at 10 µg/ml, 84% inhibition at 50 µg/ml);##Coxsackie virus B5:inhibition of viral replication in Vero cells (60% inhibition at 10 µg/ml, 42% inhibition at 50 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.30654366]<10% cytotoxicity against Vero cells at the concentration of 100μg/ mL. Not found 30654366 Intervirology. 2018;61(4):166-173. Sala A, Ardizzoni A, Ciociola T, Magliani W, Conti S, Blasi E, Cermelli C Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins. DRAMP31428 GKRKSGCA 8 Entry 1 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 114.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31429 GKRKSGAA 8 Entry 6 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 57.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31430 GKRKSXCA 8 Entry 7 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 22.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates phenylglycine(Phg). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31431 GKRKSFCA 8 Entry 8 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 39.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31432 GKRKSXCA 8 Entry 9 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 9.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31433 GKRKSxCA 8 Entry 10 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 38.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'x' at position 6 indicates D-homophenylalanine(D-hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-hPhe6) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31434 GKRKSXAA 8 Entry 11 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 18.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31435 GKRKSXAX 8 Entry 12 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 22.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates homophenylalanine(Phg). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31436 GKRKSXAx 8 Entry 13 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 15.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates D-homophenylalanine(D-Phg). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phg8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31437 GKRKSXAF 8 Entry 14 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 19.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31438 GKRKSXAf 8 Entry 15 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 7.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31439 GKRKSXAX 8 Entry 16 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 25.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 and 8 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31440 GKRKSXAx 8 Entry 17 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 16.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 and 8 indicates homophenylalanine(hPhe/D-hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-hPhe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31441 GKRKSXSf 8 Entry 18 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 5.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31442 AKRKSXSf 8 Entry 19 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 28.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31443 aKRKSXSf 8 Entry 20 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.3 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Ala1, Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31444 PKRKSXSf 8 Entry 21 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 52.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31445 pKRKSXSf 8 Entry 22 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 0.95 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Pro1, Phe8) No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31446 pKRKSXSf 8 Entry 23 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 2.6 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=306.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates L-2-naphthylalanine(l-2Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Pro1, Phe8) [Ref.28539222]BHK-21 cells: CC50>400 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31447 pKRKSXSf 8 Entry 24 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.8 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=293.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Pro1, Phe8) [Ref.28539222]BHK-21 cells: CC50>400 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31448 pRRKSXSf 8 Entry 25 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.8 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=108.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Pro1, Phe8) [Ref.28539222]BHK-21 cells: CC50>400 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31449 rRRKSXSf 8 Entry 26 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 3.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=87.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, Phe8) [Ref.28539222]BHK-21 cells: CC50>400 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31450 rRRKSXSr 8 Entry 27 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 2.3 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=141.1 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates biphenylalanine (L-bPhe). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, 8) [Ref.28539222]BHK-21 cells: CC50>400 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31451 rRRKSXXf 8 Entry 28 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.6 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=23.2 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-1-naphthylalanine(L-1Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, Phe8) [Ref.28539222]BHK-21 cells: CC50=233 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31452 rRRKAXXf 8 Entry 29 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=11.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-1-naphthylalanine(L-1Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, Phe8) [Ref.28539222]BHK-21 cells: CC50=134.1 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31453 rRRKSXXf 8 Entry 30 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.5 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=48.5 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 7 indicates L-2-naphthylalanine(L-2Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, Phe8) [Ref.28539222]BHK-21 cells: CC50=210 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31454 rRRKfXFx 8 Entry 31 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.7 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=4.6 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 8 indicates D-2-naphthylalanine(D-2Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, Phe5, 2Nal8) [Ref.28539222]BHK-21 cells: CC50=86 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31455 rRRKxXFx 8 Entry 32 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The cyclic peptide could inhibit the activity of NS2B-NS3 protease, which is an essential enzyme for the replication of dengue virus. [Ref.28539222]dengue virus 2(DENV2):inhibition of the activity of NS2B-NS3 protease(IC50= 1.1 μM); inhibition of virus-induced cytopathic effects (CPE) in BHK-21 cells(EC50=2.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The 'X' at position 6 indicates homophenylalanine(hPhe), position 5 and 8 indicates D-2-naphthylalanine(D-2Nal). The N-terminal and C-terminal cyclized by a amide bond. Mixed(D-Arg1, 2Nal5, 8) [Ref.28539222]BHK-21 cells: CC50=24 μM. NS2B-NS3 protease 28539222 Bioorg Med Chem Lett. 2017 Aug 1;27(15):3586-3590. Takagi Y, Matsui K, Nobori H, Maeda H, Sato A, Kurosu T, Orba Y, Sawa H, Hattori K, Higashino K, Numata Y, Yoshida Y. Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. DRAMP31456 CGGGGGSLTEINTELLDLEYEMKKLEEVVKKLEESYIDLKEL 42 PIH No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Inhibits MERS-Cov S protein-mediated cell fusion, which is the major pathway of MERS-CoV-induced host infections. [Ref.31099550]MERS-CoV:inhibition of cell-cell fusion between 293T cells and Huh-7 cells(IC50=1.171 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.31099550]PIH displayed no significant cytotoxicity to 293T, Huh-7, and L02 cells even at a high concentration of 100 μM. membrane 31099550 ACS Appl Mater Interfaces. 2019 Jun 5;11(22):19799-19807. Huang X, Li M, Xu Y, Zhang J, Meng X, An X, Sun L, Guo L, Shan X, Ge J, Chen J, Luo Y, Wu H, Zhang Y, Jiang Q, Ning X. Novel Gold Nanorod-Based HR1 Peptide Inhibitor for Middle East Respiratory Syndrome Coronavirus. DRAMP31457 PWLKPGDLDL 10 DET2 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide caused structural abnormalities and alteration of the arrangement of the viral E protein, which interferes with virus binding and entry. [Ref.23630436]dengue virus 2(DENV2):inhibition of viral replication in LLC-MK2 cells(41.5±20.0% inhibition at 200 µM, IC50>500 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23630436]Monkey kidney epithelial cells LLC-MK2: 8% Cell death at 500 µM. E protein 23630436 Int J Med Sci. 2013 Apr 16;10(6):719-29. Alhoot MA, Rathinam AK, Wang SM, Manikam R, Sekaran SD. Inhibition of dengue virus entry into target cells using synthetic antiviral peptides. DRAMP31458 AGVKDGKLDF 10 DET4 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide caused structural abnormalities and alteration of the arrangement of the viral E protein, which interferes with virus binding and entry. [Ref.23630436]dengue virus 2(DENV2):inhibition of viral replication in LLC-MK2 cells(84.6±5.6% inhibition at 500 µM, IC50=35 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.23630436]Monkey kidney epithelial cells LLC-MK2: 5% Cell death at 500 µM. E protein 23630436 Int J Med Sci. 2013 Apr 16;10(6):719-29. Alhoot MA, Rathinam AK, Wang SM, Manikam R, Sekaran SD. Inhibition of dengue virus entry into target cells using synthetic antiviral peptides. DRAMP31459 WLVFFVIFYFFR 12 FP1 (Tkip) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.09360 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31460 WLVFFVIAYFAR 12 FP2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00087 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31461 WLVFFVIFYFFRRRKK 16 FP3 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00003 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31462 RRKKWLVFFVIFYFFR 16 FP4 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.00004 µM);##influenza A virus PR8/Eng09 (H1N1):inhibition of viral replication in MDCK cells(IC50=0.0778 µM);##influenza A virus PR8/Vic (H3N2):inhibition of viral replication in MDCK cells(IC50=0.0535 µM);##influenza A virus PR8/Viet (H5N1):inhibition of viral replication in MDCK cells(IC50=0.1325 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31463 RRKKIFYFFR 10 FP7 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.15483 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31464 WLVFFVRRKK 10 FP8 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=0.63806 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31465 FFVIFYRRKK 10 FP9 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: the mechanism whereby FluPep mediates its antiviral effects is likely to involve inhibiting the binding of HA to sialic acid receptors or through interference with the fusion process by blocking protease cleavage. [Ref.22258859]influenza A virus A/WSN/33 H1N1:inhibition of viral replication in MDCK cells(IC50=1.48175 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry HA 22258859 J Gen Virol. 2012 May;93(Pt 5):980-986. Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA. A novel family of peptides with potent activity against influenza A viruses. DRAMP31466 GYRARPKFKAGKR 13 HPV-31 L1 Cta No entry found Papillomaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(86±3% inhibition at 10 μg/ml); inhibition of pseudovirions infection(91±4% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15170645 J Med Virol. 2004 Jul;73(3):474-80. Bousarghin L, Touzé A, Yvonnet B, Coursaget P. Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. DRAMP31467 TTTPAKRKKTKK 12 HPV-31 L1 Ctb No entry found Papillomaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(12±10% inhibition at 10 μg/ml); inhibition of pseudovirions infection(15±8% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15170645 J Med Virol. 2004 Jul;73(3):474-80. Bousarghin L, Touzé A, Yvonnet B, Coursaget P. Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. DRAMP31468 MLRKRRKRL 9 HPV-16 L2 Ct No entry found Papillomaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.15170645]human papillomavirus(HPV):inhibition of HPV virus-like particle cell entry(78±6% inhibition at 10 μg/ml); inhibition of pseudovirions infection(96±20% inhibition at 10 μg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 15170645 J Med Virol. 2004 Jul;73(3):474-80. Bousarghin L, Touzé A, Yvonnet B, Coursaget P. Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. DRAMP31469 GCKKYRRFRWKFKGKFWFWG 20 Pep19-2.5 No entry found Retroviridae,Herpesviridae, Flaviviridae, Hepadnaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: SALPs block entry of a variety of human pathogenic enveloped viruses, such as HIV-1, HBV, HCV, and HSV 1 and 2 by blocking heparan sulfate on the host cell plasma membrane, which serves as a the docking molecule for these pathogens. [Ref.22457281]HIV-1 BaL:inhibition of viral entry in 293T cells(IC50=8 µg/ml);##HIV-1 NL4-3:inhibition of viral entry in 293T cells(IC50=16 µg/ml);##HSV-1:inhibition of viral entry in Vero cells(IC50=0.42 µg/ml);##Hepatitis C virus (HCV):inhibition of viral entry in 293T cells(IC50=40 µg/ml);##Hepatitis B virus (HBV):inhibition of viral entry in 293T cells(IC50=1 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL. membrane 22457281 J Infect Dis. 2012 Jun;205(11):1654-64. Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U. A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses. DRAMP31470 GKKYRRFRWKFKFGKWFWFG 20 Pep19-4 No entry found Retroviridae,Herpesviridae, Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: SALPs block entry of a variety of human pathogenic enveloped viruses, such as HIV-1, HBV, HCV, and HSV 1 and 2 by blocking heparan sulfate on the host cell plasma membrane, which serves as a the docking molecule for these pathogens. [Ref.22457281]HIV-1 BaL:inhibition of viral entry in 293T cells(IC50=22 µg/ml);##HIV-1 NL4-3:inhibition of viral entry in 293T cells(IC50=10 µg/ml);##HSV-1:inhibition of viral entry in Vero cells(IC50=1.8 µg/ml);##Hepatitis C virus (HCV):inhibition of viral entry in 293T cells(IC50=37 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL. membrane 22457281 J Infect Dis. 2012 Jun;205(11):1654-64. Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U. A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses. DRAMP31471 ATSSANSKA 9 Loop3 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: prevent JEV infection by interfering in virus attachment to the cells. [Ref.22465300]Japanese encephalitis virus(JEV):inhibition of viral replication in BHK-21 cells(IC50=10 ± 1.4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22465300]Did not stimulate significant cytotoxicity in BHK-21 cells even at 200 μM. Envelope protein 22465300 Antiviral Res. 2012 May;94(2):179-83. Li C, Zhang LY, Sun MX, Li PP, Huang L, Wei JC, Yao YL, Isahg H, Chen PY, Mao X. Inhibition of Japanese encephalitis virus entry into the cells by the envelope glycoprotein domain III (EDIII) and the loop3 peptide derived from EDIII. DRAMP31472 SISNALNKLEESNRNLDKVNVKLT 24 C24 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: By binding to the opposite HR region in the F protein, peptides would inhibit fusion from the initial steps (lipid- and contents-mixing), blocking the conformational changes in the fusion protein required for triggering fusion. [Ref.12127571]Newcastle disease virus (NDV):inhibition of syncytium formation between NDV-infected cells(IC50=3.27 μM) No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry F protein 12127571 Int J Biochem Cell Biol. 2002 Oct;34(10):1207-20. San Román K, Villar E, Muñoz-Barroso I. Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus. DRAMP31473 KQNAANILRLKESIAATNEAVAnti-HeV 24 N24 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: By binding to the opposite HR region in the F protein, peptides would inhibit fusion from the initial steps (lipid- and contents-mixing), blocking the conformational changes in the fusion protein required for triggering fusion. [Ref.12127571]Newcastle disease virus (NDV):inhibition of syncytium formation between NDV-infected cells(IC50=22.5 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry F protein 12127571 Int J Biochem Cell Biol. 2002 Oct;34(10):1207-20. San Román K, Villar E, Muñoz-Barroso I. Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus. DRAMP31474 GRRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA 49 HLFcin 1-49 No entry found Papillomaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17481742]human papillomavirus(HPV):inhibition of pseudovirus infection in C33A cells(IC50=0.32±0.18μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys10 and Cys46, Cys20 and Cys37. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17481742 Antiviral Res. 2007 Sep;75(3):258-65. Mistry N, Drobni P, Näslund J, Sunkari VG, Jenssen H, Evander M. The anti-papillomavirus activity of human and bovine lactoferricin. DRAMP31475 FKCRRWQWRMKKLGAPSITCVRRAFA 26 BLfcinB 17-42 No entry found Papillomaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.17481742]human papillomavirus(HPV):inhibition of pseudovirus infection in C33A cells(IC50=0.25±0.24 μM). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys3 and Cys20. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17481742 Antiviral Res. 2007 Sep;75(3):258-65. Mistry N, Drobni P, Näslund J, Sunkari VG, Jenssen H, Evander M. The anti-papillomavirus activity of human and bovine lactoferricin. DRAMP31476 AGDDQGLDKCVPNSKEK 17 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may bind with HA and precent the attachment to target cells. [Ref.22595270]Influenza A virus (A/Roma-ISS/2/08 H1N1):inhibition of viral replication in MDCK cells(EC50=3.7±0.35 pM);##Influenza A virus (A/Parma/24/09 H1N1):inhibition of viral replication in MDCK cells(EC50=3.4±0.14 pM);##Influenza A virus (A/Parma/05/06 H3N2):inhibition of viral replication in MDCK cells(EC50=7.3±0.65 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22595270]MDCK cells:CC50>25 μM. HA 22595270 Pathog Glob Health. 2012 Mar;106(1):12-9. Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F. Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus. DRAMP31477 NGESSADWAKN 11 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may bind with HA and precent the attachment to target cells. [Ref.22595270]Influenza A virus (A/Roma-ISS/2/08 H1N1):inhibition of viral replication in MDCK cells(EC50=225±5.8 fM);##Influenza A virus (A/Parma/24/09 H1N1):inhibition of viral replication in MDCK cells(EC50=50±1.37 fM);##Influenza A virus (A/Parma/05/06 H3N2):inhibition of viral replication in MDCK cells(EC50=22.5±1.16 pM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.22595270]MDCK cells:CC50>25 μM. HA 22595270 Pathog Glob Health. 2012 Mar;106(1):12-9. Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F. Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus. DRAMP31478 AVSKVLHLEGEVNKISALLSTNKAVVSLSNGAnti-VSVLTSKVLDLDNYIDKQLLPIVNK 56 HR1-30a No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from hRSV F protein give strong virus–cell fusion inhibition effect. [Ref.12615056]respiratory syncytial virus(RSV):inhibition of cell fusion in Hep2 cells( IC50=1.68 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry F protein 12615056 Biochem Biophys Res Commun. 2003 Mar 14;302(3):469-75. Wang E, Sun X, Qian Y, Zhao L, Tien P, Gao GF. Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. DRAMP31479 NFYDPLVFPSDEFDASISQVNEKINQSLASIRKSDELLHNVNAGK 45 HR2-30a No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: Peptide derived from hRSV F protein give strong virus–cell fusion inhibition effect. [Ref.12615056]respiratory syncytial virus(RSV):inhibition of cell fusion in Hep2 cells( IC50=2.93 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry F protein 12615056 Biochem Biophys Res Commun. 2003 Mar 14;302(3):469-75. Wang E, Sun X, Qian Y, Zhao L, Tien P, Gao GF. Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. DRAMP31480 NKGCATCSIGAACLVDGPIPDFEIAGAtGLfGLWG 35 Subtilosin-A O07623 Herpesviridae Not found Bacillus subtilis Antimicrobial, Antiviral Not found Not found Not found 1PXQ Mechanism: Subtilosin displays antiviral and virucidal actions against HSV-2. The target of subtilosin inhibitory effect would be late stages of the viral replicative cycle such as viral glycoprotein intracellular transport. [Ref.25087911]herpes simplex virus type 2(HSV-2): inhibition of viral replication in Vero cells(90% inhibition at 25 μg/mL,EC50= 18.2μg/mL). No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal The N-terminal and C-terminal cyclized by a amide bond. Thioether bridges between Cys4 and Phe31,Cys7 and Thr28,Cys13 and Phe22. Mixed(D-Thr28,D-Phe31) [Ref.25087911]Vero cells: CC50=316.8 μg/mL. Not found 25087911 J Appl Microbiol. 2014 Nov;117(5):1253-9. Quintana VM, Torres NI, Wachsman MB, Sinko PJ, Castilla V, Chikindas M. Antiherpes simplex virus type 2 activity of the antimicrobial peptide subtilosin. DRAMP31481 EF 2 EF No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.24612829]dengue virus 2(DENV2):inhibition of viral entry in Vero cells(IC50=96.50 µM); inhibition of viral replication in Vero cells(83.47% inhibition at 200 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24612829]No cytotoxicity against Vero cells up to 500 µM. E protein 24612829 Chem Biol Drug Des. 2014 Aug;84(2):148-57. Panya A, Bangphoomi K, Choowongkomon K, Yenchitsomanus PT. Peptide inhibitors against dengue virus infection. DRAMP31482 KEN 3 KEN No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.24612829]dengue virus 2(DENV2):inhibition of viral entry in Vero cells(IC50=331.9 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24612829]No cytotoxicity against Vero cells up to 500 µM. E protein 24612829 Chem Biol Drug Des. 2014 Aug;84(2):148-57. Panya A, Bangphoomi K, Choowongkomon K, Yenchitsomanus PT. Peptide inhibitors against dengue virus infection. DRAMP31483 SVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPG 41 MLH40 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.25891143]dengue virus 1(DENV1):inhibition of viral infection in Vero cells(IC50=30.35 ± 1.25 μM);##dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=31.41 ± 1.09 μM);##dengue virus 3(DENV3):inhibition of viral infection in Vero cells(IC50=27.95 ± 1.41 μM);##dengue virus 4(DENV4):inhibition of viral infection in Vero cells(IC50=24.45 ± 1.20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25891143 Chem Biol Drug Des. 2015 Nov;86(5):1093-104. Panya A, Sawasdee N, Junking M, Srisawat C, Choowongkomon K, Yenchitsomanus PT. A peptide inhibitor derived from the conserved ectodomain region of DENV membrane (M) protein with activity against dengue virus infection. DRAMP31484 GLLYFAIFFVAAWHIRGR 18 H2-2 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=1.60 ± 0.11 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=2.19 ± 0.16 μM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. Linear Free Amidation L [Ref.26251517]Huh7.5.1 cells: CC50=83.64 ± 6.95 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. Not found 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. DRAMP31485 HGLLYFAIFFVAAWHIRGR 19 H2-3 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=0.54 ± 0.08 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=1.09 ± 0.11 μM);H2-3 peptide inactivated HCV(EC50=82.11 nM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. Linear Free Amidation L [Ref.26251517]Huh7.5.1 cells: CC50=115.99 ± 16.68 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. Not found 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. DRAMP31486 WPFCLLLMAL 10 H3 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.26251517]Hepatitis C Virus(HCV):inhibition of viral infection in Huh7.5.1 cells(EC50=0.52 ± 0.07 μM); inhibition of post-infection in Huh7.5.1 cells(EC50=1.54 ± 0.73 μM). [Ref.26251517]<10% hemolysis even at 400 μM against human erythrocytes. Linear Free Amidation L [Ref.26251517]Huh7.5.1 cells: CC50=47.22 ± 5.29 μM;##Bel7402 cells:CC50~200 μM;##HeLa cells:CC50~200 μM. Not found 26251517 J Biol Chem. 2015 Sep 18;290(38):23254-63. Hong W, Lang Y, Li T, Zeng Z, Song Y, Wu Y, Li W, Cao Z. A p7 Ion Channel-derived Peptide Inhibits Hepatitis C Virus Infection in Vitro. DRAMP31487 LYGNEGCGWAGWLLSPRG 18 SL173 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(80% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. Peptide inhibitors of hepatitis C virus core oligomerization and virus production. DRAMP31488 GWAGWLLSPRGSRPSWGP 18 SL174 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(15% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. Peptide inhibitors of hepatitis C virus core oligomerization and virus production. DRAMP31489 GWAGWLLSPRGSRPS 15 SL175 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.19264632]hepatitis C virus(J6/JFH1):inhibition of viral infection in Huh-7.5 cells(50% inhibition at 20 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 19264632 J Gen Virol. 2009 Jun;90(Pt 6):1319-1328. Kota S, Coito C, Mousseau G, Lavergne JP, Strosberg AD. Peptide inhibitors of hepatitis C virus core oligomerization and virus production. DRAMP31490 MDVNP 5 PB1 (1–5) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=185 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31491 MDVNPTLLFL KVPAQNAIST TFPYT 27 PB1 (1–25) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=122 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31492 TLLFLKVPAQ NAISTTFPYT 21 PB1 (6–25) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=129 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31493 AQNAISTTFPYT 12 PB1 (14–25) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=380 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31494 Anti-MeVVQQTRMD KLTQGRQTYD 21 PB1 (111–130) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=58 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31495 LPVGGNEKKA KLANVVRKMM 21 PB1 (271–290) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=33 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31496 FNESTR 6 PB1 (381–386) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=664 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31497 FNESTRKKIE 10 PB1 (381–390) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=400 ± 8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31498 FNESTRKKIE KIRPLLVEGT 21 PB1 (381–400) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=23 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31499 KIRPLLVEGT 10 PB1 (391–400) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=71 ± 3μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31500 MFNMLSTVLG 10 PB1 (411–420) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=369 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31501 IGVTVI 6 PB1 (525–530) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=833 ± 6 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31502 IGVTVIKNNMI 11 PB1 (525–535) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=416 ± 3μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31503 TLLFLKVP 8 PB1 (6–13) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=102 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31504 TLLFLKVP 8 PB1 (6–13)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=35 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31505 TLLFLKVP 8 Ac-PB1 (6–13) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=33 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31506 TLLFLKVP 8 Ac-PB1 (6–13)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=12 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31507 TLLFLKVPA 9 PB1 (6–14) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=34 ± 2 μM);##Influenza A virus(A/Puerto Rico/8/34 (H1N1)):antiviral activity of the peptide in MDCK cells(ED50=8.9 ± 1.0 μM);##Influenza A virus(A/Aichi/2/68 (H3N2)):antiviral activity of the peptide in MDCK cells(ED50=10.7 ± 0.9 μM);##Influenza A virus(A/Mallard/Pennsylvania/10218/84 (H5N2)):antiviral activity of the peptide in MDCK cells(ED50=8.5 ± 1.1 μM);##Influenza A virus(A/Vladivostok/02/09 of H1N1):antiviral activity of the peptide in MDCK cells(ED50=1.7 ± 0.8 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31508 TLLFLKVPA 9 PB1 (6–14)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=6 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31509 TLLFLKVPA 9 Ac-PB1 (6–14) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=82 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31510 TLLFLKVPA 9 Ac-PB1 (6–14)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=4 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31511 GDPPY 5 PB1 (26–30) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=115 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31512 GDPPY 5 PB1 (26–30)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=100 ± 5 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31513 GDPPY 5 Ac-PB1 (26–30) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=95 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31514 GDPPY 5 Ac-PB1 (26–30)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=254 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31515 LLVEGT 6 PB1 (395–400) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=91 ± 2 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31516 LLVEGT 6 PB1 (395–400)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=794 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31517 LLVEGT 6 Ac-PB1 (395–400) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=297 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31518 LLVEGT 6 Ac-PB1 (395–400)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=744 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31519 KNNMINNDLG 10 PB1 (531–540) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=51 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31520 KNNMINNDLG 10 PB1 (531–540)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=44 ± 1 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31521 KNNMINNDLG 10 Ac-PB1 (531–540) No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=71 ± 3 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31522 KNNMINNDLG 10 Ac-PB1 (531–540)-NH2 No entry found Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide may affect the early stages of the viral life cycle, which includes the synthesis of polymerase subunits and their subsequent assembly into functionally active complex. The peptide could interfere with these processes thus inhibiting virus replication. [Ref.25446335]Influenza A virus(A/California/07/2009 (H1N1)pdm09/):antiviral activity of the peptide in MDCK cells(ED50=109 ± 4 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Acetylation Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 25446335 Antiviral Res. 2015 Jan;113:4-10. Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI. Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments. DRAMP31523 LNLFKKTINGLISDSLVIR 19 AVP-p No entry found Arenaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: that untimely deployment of fusion machinery by the peptide could render virions less able to engage in on-pathway receptor binding or endosomal fusion. [Ref.24850726]Pichinde virus (PICV):inhibition of viral infection in Vero cells(IC50=7.05 ± 2.19 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.24850726]No significant loss of viability was observed in Vero cells or human foreskin fibroblasts (HFF) up to 100 μM. Not found 24850726 J Virol. 2014 Aug;88(15):8556-64. Spence JS, Melnik LI, Badani H, Wimley WC, Garry RF. Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism. DRAMP31524 GREERRQRRRC 11 E50,51TAT-Cd0 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.21029018]Herpes simplex virus type 1(HSV-1):inhibition of viral infection in human corneal epithelial (HCE) cells(EC50~30.0 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 21029018 J Ocul Pharmacol Ther. 2010 Dec;26(6):541-7. Larsen IV, Brandt CR. A cationic TAT peptide inhibits Herpes simplex virus type 1 infection of human corneal epithelial cells. DRAMP31525 NDSRGIDAEEELETKAELVITKLKTPLMRGKVVVGAAGA 39 MDVgHH2L No entry found Paramyxoviridae, Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=43.4 ± 2.0 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=34.0 ± 2.00 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 24412629 J Virol Methods. 2014 Apr;199:11-6. Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ. In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. DRAMP31526 NADIIKSLIRKTIINASKNTASLSILQHLYVLRS 34 MDVgBH3 No entry found Paramyxoviridae, Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=52.9 ± 0.9 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=37.5 ± 1.2 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 24412629 J Virol Methods. 2014 Apr;199:11-6. Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ. In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. DRAMP31527 LGNVNNSISNALDKLEESNSKLDKVNVKLTGTSAL 35 NDVHR2 No entry found Paramyxoviridae, Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: peptides from the hydrophobic fusogenic domains of gB and gH can block virus entry, disrupt cellular membranes by interacting with the cellular factors, or play a role in the glycoprotein conformational changes [Ref.24412629]Newcastle disease virus(NDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=18.9 ± 2.8 μmol/L);##Marek's disease virus(MDV):inhibition of viral infection in chicken embryo fibroblasts(IC50=65.3 ±0.9 μmol/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry membrane 24412629 J Virol Methods. 2014 Apr;199:11-6. Chi XJ, Wang XJ, Wang CY, Cui XJ, Wang XJ. In vitro and in vivo broad antiviral activity of peptides homologous to fusion glycoproteins of Newcastle disease virus and Marek's disease virus. DRAMP31528 TIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFV 43 HRA1 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process. [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=177 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). F protein 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. Deffrasnes C, Hamelin ME, Prince GA, Boivin G. Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. DRAMP31529 AKTIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFVSKN 48 HRA2 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process. [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=2.1 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). F protein 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. Deffrasnes C, Hamelin ME, Prince GA, Boivin G. Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. DRAMP31530 LESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRE 35 HRA3 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process. [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=3240 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). F protein 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. Deffrasnes C, Hamelin ME, Prince GA, Boivin G. Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. DRAMP31531 FNVALDQVFESIENSQALVDQSNRILSSAEKGNTG 35 HRB5 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process. [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=1520 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). F protein 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. Deffrasnes C, Hamelin ME, Prince GA, Boivin G. Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. DRAMP31532 PEDQFNVALDQVFESIENSQALVDQSNRILSSAEKGNTG 39 HRB6 No entry found Paramyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process. [Ref.17967906]Human Metapneumovirus(hMPV):inhibition of viral infection in LLC-MK2 cells(IC50=3310 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.17967906]No cytotoxicity against LLC-MK2 cells at the highest concentrations tested (9 μM). F protein 17967906 Antimicrob Agents Chemother. 2008 Jan;52(1):279-87. Deffrasnes C, Hamelin ME, Prince GA, Boivin G. Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus. DRAMP31533 SWLVNRDWFHDLNLPWTGSSAGTWQ 25 TP1 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: TP1 functions through a mechanism that involves release of the viral genome and interference with cellular TMUV binding [Ref.32456819]Tembusu virus (TMUV):inhibition of viral infection in BHK-21 cells(IC50=14.19 mg/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32456819]No cytotoxicity against BHK-21 cells up to 150mg / L. Not found 32456819 Vet Microbiol. 2020 Jun;245:108708. Zhao D, Zhang L, Han K, Liu Q, Yang J, Huang X, Liu Y, Li Y, Zhao P. Peptide inhibitors of tembusu virus infection derived from the envelope protein.  DRAMP31534 MVALGDTAWDFGSVGGVLTSIGKGIHQVFGSAFKSL 36 TP2 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: TP2 might be an interference factor between TMUV and the cell. [Ref.32456819]Tembusu virus (TMUV):inhibition of viral infection in BHK-21 cells(IC50=7.64 mg/L). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.32456819]No cytotoxicity against BHK-21 cells up to 150mg / L. Not found 32456819 Vet Microbiol. 2020 Jun;245:108708. Zhao D, Zhang L, Han K, Liu Q, Yang J, Huang X, Liu Y, Li Y, Zhao P. Peptide inhibitors of tembusu virus infection derived from the envelope protein.  DRAMP31535 RRRQRRKKRGYGFVNLLFLVVE 22 TAT-Kα2 No entry found Herpesviridae,Paramyxoviridae,Orthomyxoviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: display virucidal activity by disrupting viral envelopes. [Ref.28687749]Vesicular stomatitis virus(VSV):inhibition of viral infection in 293T cells(IC50=2.9 μM);##Respiratory Syncytial Virus(RSV):inhibition of viral infection in Hep2 cells(IC50=3.4 μM);##Newcastle disease virus(NDV):inhibition of viral infection(IC50=0.8 μM);##Parainfluenza virus:inhibition of viral infection(IC50=2.4 μM);##Influenza virus (H1N1) A/Puerto Rico/8/34:inhibition of viral infection(IC50=0.5 μM);##Influenza virus (H5N2) A/bird/Korea/W81/2005:inhibition of viral infection(IC50=0.8 μM);##Influenza virus (H7N3) A/Aquatic bird/Korea/W44/2005:inhibition of viral infection(IC50=1.2 μM);##Influenza virus (H9N2) A/Chicken/Korea/116/2004:inhibition of viral infection(IC50=0.7 μM);##Porcine epidemic diarrhea virus:inhibition of viral infection(IC50=3.5 μM);##Herpes simplex virus:inhibition of viral infection(IC50=5.7 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.28687749]No cytotoxicity against MDCK cells up to 100 μM. Envolope 28687749 Sci Rep. 2017 Jul 7;7(1):4875. Moon HJ, Nikapitiya C, Lee HC, Park ME, Kim JH, Kim TH, Yoon JE, Cho WK, Ma JY, Kim CJ, Jung JU, Lee JS. Inhibition of highly pathogenic avian influenza (HPAI) virus by a peptide derived from vFLIP through its direct destabilization of viruses DRAMP31536 MGRFKRFRKKFKKLFKKLS 19 Bomidin P54228 Flaviviridae,Herpesviridae,Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: bomidin readily disrupted viral membranes (with components similar to those in the endoplasmic reticulum) and bacterial membranes but did not alter the overall structures of the cell membranes [Ref.35663971]Dengue virus 2(DENV2):inhibition of viral infection in Huh7 cells(50% inhibition at 10 μM);##HSV:inhibition of viral infection in Huh7 cells(50% inhibition at 10 μM);##SARS-CoV-2:inhibition of viral infection in Huh7 cells(80% inhibition at 10 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.35663971]Vero E6 cells:CC50=169.6 ± 1.1 µM. membrane 35663971 Front Immunol. 2022 May 19;13:851642. Liu R, Liu Z, Peng H, Lv Y, Feng Y, Kang J, Lu N, Ma R, Hou S, Sun W, Ying Q, Wang F, Gao Q, Zhao P, Zhu C, Wang Y, Wu X.  Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses. DRAMP31537 DHVTPDIAYNPRTYM 15 Pep-RTYM No entry found Flaviviridae Not found Acacia catechu Antimicrobial, Antiviral Not found Not found Not found Mechanism: the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=7.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. Not found 33172110 Viruses. 2020 Nov 6;12(11):1267. Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT. Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. DRAMP31538 DHVTPDIAYNPWAYF 15 Pep-WAYF No entry found Flaviviridae Not found Acacia catechu Antimicrobial, Antiviral Not found Not found Not found Mechanism: the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=15.67 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. Not found 33172110 Viruses. 2020 Nov 6;12(11):1267. Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT.  Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. DRAMP31539 DHVTPDIAYNP 11 Pep-CORE No entry found Flaviviridae Not found Acacia catechu Antimicrobial, Antiviral Not found Not found Not found Mechanism: the biding of peptide to virus particles might disrupt the ability of the virus to bind to the host cell receptor or possibly block the internalization of the virus into the host cells. [Ref.33172110]Dengue virus 2(DENV2):inhibition of viral infection in Vero cells(IC50=20.89 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.33172110]No cytotoxicity against Vero cells up to 1000 μM. Not found 33172110 Viruses. 2020 Nov 6;12(11):1267. Panya A, Sawasdee N, Songprakhon P, Tragoolpua Y, Rotarayanont S, Choowongkomon K, Yenchitsomanus PT.  Synthetic Bioactive Peptide Derived from the Asian Medicinal Plant Acacia catechu Binds to Dengue Virus and Inhibits Cell Entry. DRAMP31540 KKR 3 Cmpd 2 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(IC50=41.0 ± 3.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Phenylacetyl Free L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 viral serine protease 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM.  SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  DRAMP31541 KKR 3 Cmpd 11 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(IC50=3.6 ± 0.9 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Phenylacetyl Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 viral serine protease 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM.  SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  DRAMP31542 GKR 3 Cmpd 12 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(40% inhibition at 100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Phenylacetyl Free L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 viral serine protease 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM.  SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  DRAMP31543 GKR 3 Cmpd 13 No entry found Flaviviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide inhibits the NS2B-NS3 protease and thus inhibits virus replication. [Ref.35123179]Zika virus(ZIKV):inhibition the activity of Zika virus NS2B-NS3 protease(40% inhibition at 100 μM). No hemolysis information or data found in the reference(s) presented in this entry Linear Phenylacetyl Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry NS2B-NS3 viral serine protease 35123179 Bioorg Med Chem. 2022 Mar 1;57:116631. Colarusso S, Ferrigno F, Ponzi S, Pavone F, Conte I, Abate L, Beghetto E, Missineo A, Amaudrut J, Bresciani A, Paonessa G, Tomei L, Montalbetti C, Bianchi E, Toniatti C, Ontoria JM.  SAR evolution towards potent C-terminal carboxamide peptide inhibitors of Zika virus NS2B-NS3 protease.  DRAMP31544 ALWKTLLKKVLKAAAK 16 Dermaseptin S4 (1-16)[M4K] P80280 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: exerts a selective activity on viral particles and disturbs their organization by breaking the viral membrane, leading to the exposure of HIV-1 core and its dissociation.  [Ref.15780876]human immunodeficiency virus type 1 (HIV-1):Inhibition of viral infection in Vero P4-CCR5 cells(IC50=28 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.15780876]P4-CCR5 cells:CC50>100 μM. viral membrane 15780876 Virology. 2005 Apr 10;334(2):264-75.  Lorin C, Saidi H, Belaid A, Zairi A, Baleux F, Hocini H, Bélec L, Hani K, Tangy F. The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro.  DRAMP31545 GIGDPVTCLKSGAICAnti-HPVFCPRRYKQIGTCGLPGTKCCKKP 41 Beta-defensin 2(BD-2, hBD-2, SAP1) O15263 Retroviridae Not found Homo sapiens Antimicrobial, Antiviral Not found Not found Not found 1FD4 Mechanism: No mechanism information found in the reference(s). [Ref.16254366]HIV-1 BaL:inhibition of viral infection in TZM-bl cells(80% Inhibition at 100 µg/ml, 68% Inhibition at 50 µg/ml, 55% Inhibition at 25 µg/ml, 45% Inhibition at 12.5 µg/ml, 32% Inhibition at 6.2 µg/ml, 28% Inhibition at 3.1 µg/ml, 18% Inhibition at 1.6 µg/ml, 20% Inhibition at 0.8 µg/ml,);##HIV-1 IIIB:inhibition of viral infection in TZM-bl cells(95% Inhibition at 100 µg/ml, 87% Inhibition at 50 µg/ml, 75% Inhibition at 25 µg/ml, 62% Inhibition at 12.5 µg/ml, 55% Inhibition at 6.2 µg/ml, 35% Inhibition at 3.1 µg/ml, 28% Inhibition at 1.6 µg/ml, 25% Inhibition at 0.8 µg/ml,). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Free Disulfide bonds between Cys8 and Cys37, Cys15 and Cys30, Cys20 and Cys38. L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 16254366 J Virol. 2005 Nov;79(22):14318-29.  Sun L, Finnegan CM, Kish-Catalone T, Blumenthal R, Garzino-Demo P, La Terra Maggiore GM, Berrone S, Kleinman C, Wu Z, Abdelwahab S, Lu W, Garzino-Demo A. Human beta-defensins suppress human immunodeficiency virus infection: potential role in mucosal protection.  DRAMP31546 QSHLSLCRWCCNCCRSNKGC 20 Hepcidin TH2-3 I3KHK3 Picornaviridae Not found Oreochromis mossambicus Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=25.1±1.5 µg/ml, IC90=78.5±7.6 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Cyclic Free Cyclization(Cys7 and Cys20) Disulfide bonds between Cys7 and Cys20, Cys10 and Cys13, Cys11 and Cys14. L [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=120.2±2.5 µg/ml. Not found 30012343 Peptides. 2018 Aug;106:91-95. Huang HN, Pan CY, Chen JY.  Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. DRAMP31547 FIHHIIGGLFSVGKHIHSLIHGH 23 Tilapia piscidin 3, TP3 L0CMD2 Picornaviridae Not found Oreochromis niloticus Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.30012343]Foot-and-Mouth Disease virus(FMDV):Inhibition of viral replication in BHK-21 cells(IC50=2.5±0.2 µg/ml, IC90=25.0±3.2 µg/ml). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L [Ref.30012343]Baby Hamster Kidney cells BHK-21:CC50=39.0±1.2 µg/ml. Not found 30012343 Peptides. 2018 Aug;106:91-95. Huang HN, Pan CY, Chen JY.  Grouper (Epinephelus coioides) antimicrobial peptide epinecidin-1 exhibits antiviral activity against foot-and-mouth disease virus in vitro. DRAMP31548 AKKAAKKAKKAAKKIEKAAKK 21 RJ5-I15E16 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=112 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31549 AKKAKKKAKKAAKKIKKKAKK 21 RJ9-I15 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=11 µM); inhibition of viral infection in MRC-5 cells(IC50=119 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31550 ARRARRRARRAARRARRGARR 21 RJ8-R5G18 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=1.9 µM); inhibition of viral infection in MRC-5 cells(IC50=4.8 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=96 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31551 ARRARRRARRAARRARRWARR 21 RJ8-R5W18 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=9.2 µM); inhibition of viral infection in MRC-5 cells(IC50=2.8 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=162 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31552 KAAKKAAKWAKKAAKWAKKAA 21 RJ2-W9,16 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=111 µM); inhibition of viral infection in MRC-5 cells(IC50=32 µM);##Herpes simplex virus 2(HSV-2):inhibition of viral infection in MRC-5 cells(IC50=48 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31553 KYAKKAAKYAKKAAKYAKKAA 21 RJ2-Y2,9,16 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=146 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31554 AAKAWKKAKAWKKAKWWKKAA 21 RJ2-A1,4,8; K3,6,7,9,13; W5,11,17 No entry found Herpesviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Comment: No comments found on DRAMP database [Ref.16923027]Herpes simplex virus 1(HSV-1):inhibition of viral entry into Vero cells(IC50=238 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L [Ref.16923027]No cytotoxicity against Human fibroblasts MRC-5 cells up to 448 µM. Not found 16923027 Chem Biol Drug Des. 2006 Jul;68(1):58-66. Jenssen H, Gutteberg TJ, Rekdal Ø, Lejon T. Prediction of activity, synthesis and biological testing of anti-HSV active peptides.  DRAMP31555 WNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQ 36 CHR-1, Env GP (623-658) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The peptide can interact with the viral NHR to form stable heterologous 6-HBs, resulting in inhibition of fusion between the viral and target cell membranes. [Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=17.27 ± 0.31 nM; IC90=26.41 ± 0.55 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry cell membrane 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides DRAMP31556 REINNYTSLIHSLIEESQNQQEKNEQELLELDKWAS 36 CHR-3, Env GP (633-668) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: CHR-3 interacts with N46 to form unstable 6-HB [Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=1,470.00 ± 20.0 nM; IC90=2,380.00 ± 35.00 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides DRAMP31557 HSLIEESQNQQEKNEQELLELDKWASLWNWFNITNW 36 CHR-5, Env GP (643-678) P04578 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: CHR-5 can bind to LUVs of POPC [Ref.17276993]human immunodeficiency virus (HIV):inhibition of cell-cell fusion in MT-2 cells(IC50=2,185.00 ± 15.00 nM; IC90=2,858.00 ± 6.00 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Not found 17276993 J Biol Chem. 2007 Mar 30;282(13):9612-9620. Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S. HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides DRAMP31558 STSQKAnti-SIVAYTM 12 SARS-CoV S (668–679), SP-10 P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: block the binding of S protein to ACE2. [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=1.88 ± 0.52 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry ACE2 16337697 Antiviral Res. 2006 Feb;69(2):70-6. Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY. Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. DRAMP31559 GFLYVYKGYQPI 12 SARS-CoV S (192-203), SP-4 P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: block the binding of S protein to ACE2. [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=4.30 ± 2.18 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry ACE2 16337697 Antiviral Res. 2006 Feb;69(2):70-6. Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY. Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. DRAMP31560 FYTTTGIGYQPY 12 SARS-CoV S (483-494), SP-8 P59594 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: block the binding of S protein to ACE2. [Ref.16337697]SARS-CoV:Inhibition of pseudovirus infection in Vero cells(IC50=6.99 ± 0.71 nM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry ACE2 16337697 Antiviral Res. 2006 Feb;69(2):70-6. Ho TY, Wu SL, Chen JC, Wei YC, Cheng SE, Chang YH, Liu HJ, Hsiang CY. Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction. DRAMP31561 IHAEIKNSLKIDNLDVNRCIEAL 23 LEDGF/p75 (355-377) O75475 Retroviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: The LEDGF/p75 peptide modestly inhibited IN catalysis and was dependent on IN–DNA assembly. The peptide was also effective at disrupting LEDGF/p75–IN complex formation. [Ref.18331842]Human immunodeficiency virus (HIV): Inhibition of integrase activity (3' end processing)(IC50=165±28 µM); inhibition of integrase activity(strand transfer)(IC50=153±28 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Free L No cytotoxicity information or data found in the reference(s) presented in this entry Integrase 18331842 FEBS Lett. 2008 Apr 30;582(10):1425-30. Al-Mawsawi LQ, Christ F, Dayam R, Debyser Z, Neamati N. Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis. DRAMP31562 IEEQAKTFLDKFQAnti-HeVEEIYWQS 23 Peptide1(ACE2 (21-43)[N13Q,A16V,D18E,L19I,F20Y,Y21W]) Q9BYF1 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=11 ± 1 nM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31563 QDKHEEDYQMYNKGDKED 18 Peptide2 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=18 ± 2 nM, 95% inhibition at 0.39 µM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31564 DKFNHEAEDLFYQSSLASWNYNT 23 Peptide3 Q9BYF1 Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=6 ± 4 nM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31565 IDENARSYIDKFQHDAEEMWYQ 22 Peptide4 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=32 ± 2 nM, 95% inhibition at 0.39 µM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31566 IYALLENAEDYNLVN 15 Peptide5 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=9 ± 4 nM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31567 SRDKHEEHEKENDRGQ 16 Peptide6 No entry found Coronaviridae Not found Synthetic construct Antimicrobial, Antiviral Not found Not found Not found Mechanism: antagonizes the SARS-CoV-2 S-RBD:ACE2 interaction and inhibits the virus entry. [Ref.34328726]SARS-CoV-2:Inhibition of virus entry in HEK293T/ACE2 cells (via inhibition of SRBD:ACE2 interaction)(IC50=10 ± 5 nM, 100% inhibition at 25 µM). No hemolysis information or data found in the reference(s) presented in this entry Linear Free Amidation L No cytotoxicity information or data found in the reference(s) presented in this entry Spike protein 34328726 J Med Chem. 2022 Feb 24;65(4):2836-2847.  Sadremomtaz A, Al-Dahmani ZM, Ruiz-Moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-Velázquez MA, de Jong D, de Jonge J, Smit J, Dömling A, van Goor H, Groves MR. Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein DRAMP31568 KWKLFKKIGPGKFLHSAKKF 20 CA-MA3 Not available Not found Ceropin-Magainin hybrid peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=75 µM); A549 (IC50>100 µM); K562 (IC50>100 µM); MDA-MB-361 (IC50>100 µM) Human erythrocytes: Hemolysis 0% (100 μM) Linear Free Amidation L NIH-3T3 fibroblast: IC50>100 μM Not available 10675500 Biochim Biophys Acta. 2000 Feb 15;1463(2):209-18. Shin SY, Kang JH, Jang SY, Kim Y, Kim KL, Hahm KS. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells DRAMP31569 KWKFKKIPKFLHLAKKF 17 P18 Not available Not found Ceropin A Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=3.5 µM); Jurkat (IC50=4 µM); MDA-MB-361 (IC50=8 µM) Human erythrocytes: hemolysis: 0%=100 µM; hemolysis: 0%=50 µM; hemolysis: 0%=25.0 µM; hemolysis: 0%=12.5 µM; hemolysis: 0%=6.25 µM; hemolysis: 0%=3.125 µM; hemolysis: 0%=1.56 µM; hemolysis: 0%=0.78 µM Linear Free Amidation L NIH 3T3: IC50=75 µM Not available 12005420 J Pept Res. 2001 Dec;58(6):504-14. Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs DRAMP31570 PAWFKARRWAWRMKKLAA 18 L2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (IC50=144 µM); MT-1 (IC50>254 µM); HT-29 (IC50>440 µM) Human red blood cells: EC50>440 µM Linear Free Free L Fibroblas: IC50>440 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31571 PAWRKAFRWAWRMKKLAA 18 L3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=141 µM); MT-1 (IC50=18 µM); Meth A (IC50=32 µM) Human red blood cells: EC50>440 µM Linear Free Free L Fibroblas: IC50=163 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31572 PAWFKARRWAWRMLKKAA 18 L4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=16 µM); Meth A (IC50=31 µM); HT-29 (IC50=57 µM) Human red blood cells: EC50>440 µM Linear Free Free L Fibroblas: IC50=299 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31573 PAWRKAFRWAWRMLKKAA 18 L5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=14 µM); A549 (IC50=3 ± 1 μM(pH=7.4); IC50=4 ± 1 μM(pH=5.5)); Meth A (IC50=6.6 µM); MT-1 (IC50=8 µM) Human red blood cells: EC50=33 µM Linear Free Free L Fibroblas: IC50=17 µM; CHO: IC50=5 ± 1 μM(pH=7.4); IC50=5 ± 1 μM(pH=5.5) Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31574 PAWRKAFRWAARMLKKAA 18 L6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (IC50=11 µM); MT-1 (IC50=12 µM); HT-29 (IC50=15 µM) Human red blood cells: EC50=278 µM Linear Free Free L Fibroblas: IC50=46 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31575 PAWRKAFRAAWRMLKKAA 18 L7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=11 µM); HT-29 (IC50=16 µM); Meth A (IC50=16 µM) Human red blood cells: EC50=382 µM Linear Free Free L Fibroblas: IC50=46 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31576 PAWAKAFRAAARMKLKAA 18 L8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (IC50=110 µM); HT-29 (IC50=180 µM); MT-1 (IC50=87 µM) Human red blood cells: EC50>489 µM Linear Free Free L Fibroblas: IC50>489 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31577 PAWRKAARWAWRMLKKAA 18 L9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=32 µM); Meth A (IC50=35 µM); HT-29 (IC50=52 µM) Human red blood cells: EC50>455 µM Linear Free Free L Fibroblas: IC50=289 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31578 PAARKAFRWAWRMLKKAA 18 L10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=20 µM); Meth A (IC50=24 µM); HT-29 (IC50=35 µM) Human red blood cells: EC50>463 µM Linear Free Free L Fibroblas: IC50=190 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31579 PAARKAARWAWRMLKKGA 18 L11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (IC50=116 µM); HT-29 (IC50=248 µM); MT-1 (IC50=75 µM) Human red blood cells: EC50>480 µM Linear Free Free L Fibroblas: IC50>480 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31580 PAWRKAFRWAKRMLKKAA 18 L12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=10 µM); HT-29 (IC50=25 µM); Meth A (IC50=7.9 µM) Human red blood cells: EC50>451 µM Linear Free Free L Fibroblas: IC50=31 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31581 PAWRKAFRKAWRMLKKAA 18 L13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (IC50=12 µM); Meth A (IC50=14 µM); HT-29 (IC50=29 µM) Human red blood cells: EC50>451 µM Linear Free Free L Fibroblas: IC50=59 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31582 PAWRKARRWAWRMKKLAA 18 L14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (IC50=125 µM); MT-1 (IC50=141 µM); HT-29 (IC50=423 µM) Human red blood cells: EC50>438 µM Linear Free Free L Fibroblas: IC50>438 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31583 PAWRKARRWARRMKKLAA 18 L15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=178 µM); Meth A (IC50=87 µM); MT-1 (IC50=92 µM) Human red blood cells: EC50>444 µM Linear Free Free L Fibroblas: IC50>444 µM Not available 12366526 J Pept Res. 2002 Oct;60(4):187-97. Yang N, Stensen W, Svendsen JS, Rekdal Ø. Enhanced antitumor activity and selectivity of lactoferrin-derived peptides DRAMP31584 GIGKFLHSAKKWGKAFVGQIMNC 23 MG2d Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (30-40% viablity=100 µM ) Not available Linear Free Amidation L Not available Not available 12417587 J Biol Chem. 2003 Jan 10;278(2):1310-5. Takeshima K, Chikushi A, Lee KK, Yonehara S, Matsuzaki K. Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes DRAMP31585 TRSSRAGLQWPVGRVHRLLRKGGC 24 BF2d Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (80-90% viablity=100 µM ) Not available Linear Free Amidation L Not available Not available 12417587 J Biol Chem. 2003 Jan 10;278(2):1310-5. Takeshima K, Chikushi A, Lee KK, Yonehara S, Matsuzaki K. Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes DRAMP31586 glfdvikkvasviggl 16 Citropin 1.1D Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation D Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31587 GLFDVIKAVASVIGGL 16 Citropin 5 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Lung cancer group (NCI) (IC50=1 μM); Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50>100 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31588 GLFDVIKKVAAVIGGL 16 Citropin 7 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31589 GLFDVIKKVASVIKGL 16 Citropin 11 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31590 GLFDVIKKVASVIKKL 16 Citropin 13 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31591 GLFAVIKKVAAVIKKL 16 Citropin 17 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31592 GLFAVIKKVAAVIRRL 16 Citropin 18 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50>10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31593 GLFAVIKKVAKVIKKL 16 Citropin 19 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Melanoma cancer group (NCI) (IC50=1 μM); Ovarian cancer group (NCI) (IC50=1 μM); Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31594 GLFKVIKKVASVIGGL 16 Citropin 22 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50>10 μM); Leukemia group (NCI) (IC50>10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31595 GLFKVIKKVAKVIKKL 16 Citropin 23 Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Breast cancer group (NCI) (IC50=10 μM); CNS cancer group (NCI) (IC50=10 μM); Colon cancer group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Ovarian cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM); Leukemia group (NCI) (IC50>10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31596 LGGIVSAVKKIVDFLG 16 Citropin retro Not available Not found Amphibian skin secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNS cancer group (NCI) (IC50=10 μM); Lung cancer group (NCI) (IC50=10 μM); Melanoma cancer group (NCI) (IC50=10 μM); Prostate cancer group (NCI) (IC50=10 μM); Renal cancer group (NCI) (IC50=10 μM); Breast cancer group (NCI) (IC50>10 μM); Colon cancer group (NCI) (IC50>10 μM); Leukemia group (NCI) (IC50>10 μM); Ovarian cancer group (NCI) (IC50>10 μM) Not available Linear Free Amidation L Not available Not available 12631273 Eur J Biochem. 2003 Mar;270(6):1141-53. Doyle J, Brinkworth CS, Wegener KL, Carver JA, Llewellyn LE, Olver IN, Bowie JH, Wabnitz PA, Tyler MJ. nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications DRAMP31597 KLllKLKlKlLK 12 l3,4,8,10K5L7 Not available Not found Diastereomeric peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (LC50=100 µM); D122 (LC50>50 µM) Human erythrocyte: Hemolysis% at 50 μm peptide LC50=0 µM Linear Free Free l=D-Leucine; k=D-Lysine Mix NIH-3T3: LC50>100 µM Not available 12646578 J Biol Chem. 2003 Jun 6;278(23):21018-23. Papo N, Shahar M, Eisenbach L, Shai Y. Designed antimicrobial and antitumor peptides with high selectivity DRAMP31598 KLlRLLkkLlRLlLK 15 l3,10,13K7,8K4R2L9 Not available Not found Diastereomeric peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (LC50=2.5 µM); D122 (LC50=4.5 µM) Human erythrocyte: Hemolysis% at 50 μm peptide LC50=0 µM Linear Free Free l=D-Leucine; k=D-Lysine Mix NIH-3T3: LC50=40 µM Not available 12646578 J Biol Chem. 2003 Jun 6;278(23):21018-23. Papo N, Shahar M, Eisenbach L, Shai Y. Designed antimicrobial and antitumor peptides with high selectivity DRAMP31599 AIGKFLHSAKKFGKAFVGEIMNS 23 Magainin A C0HKN6##P11006 Not found African clawed frog Xenopus laevis skin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H735 (IC50=10.4 µM); NCI-H526 (IC50=11.7 µM); U-937 (IC50=16 µg/ml); RPMI-8402 (IC50=18 µg/ml); Raji (IC50=20 µg/ml); SSKT-1 (IC50=23 µg/ml); Daudi (IC50=30 µg/ml); MLA (IC50=34 µg/ml); K562 (IC50=40 µg/ml); CHP-100 (IC50=45 µg/ml); MCF-7 (IC50=49 µg/ml); PC-3 (IC50=53 µg/ml); NCI-H678 (IC50=6.23 µM); NCI-H889 (IC50=6.56 µM); NCI-H82 (IC50=7.28 µM); NCI-H841 (IC50=9.7 µM) Detectable but low hemolytic activity Linear Beta-alanine Amidation L Not available Not available 1319823 Cancer Res. 1992 Jul 1;52(13):3534-8. Ohsaki Y, Gazdar AF, Chen HC, Johnson BE. Antitumor activity of magainin analogues against human lung cancer cell lines DRAMP31600 LLAGLAANFLPTIICKISYKC 21 PTP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>100 µg/ml); Hep 3B (IC50>100 µg/ml); MCF-7 (IC50>100 µg/ml); PC-3 (IC50>100 µg/ml) Human RBCs: less than 6% hemolysis at 100 μg/ml Cyclic Free Amidation L HEK293: IC50>100 µg/ml Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31601 FAGLAANFLPTIICKISYKC 20 PTP2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>100 µg/ml); Hep 3B (IC50>100 µg/ml); MCF-7 (IC50>100 µg/ml); PC-3 (IC50>100 µg/ml) Human RBCs: less than 6% hemolysis at 100 μg/ml Cyclic Free Amidation L HEK293: IC50>100 µg/ml Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31602 FLKLLKKLAAKFLPTIICKISYKC 24 PTP4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.71 ± 2.12 µg/ml); MCF-7 (IC50=18.10 ± 2.13 µg/ml); Hep 3B (IC50=18.18 ± 3.31 µg/ml); PC-3 (IC50=18.63 ± 0.99 µg/ml) Human RBCs: 45.17% hemolysis at 100 μg/ml Linear Free Amidation L HEK293: IC50=26.15 ± 6.23 µg/ml Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31603 FLKLLKKLAAKFL 13 PTP6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=13.27 ± 4.27 µg/ml); A549 (IC50=13.94 ± 3.96 µg/ml); Hep 3B (IC50=15.07 ± 1.59 µg/ml); MCF-7 (IC50=17.56 ± 6.23 µg/ml) Human RBCs: less than 6% hemolysis at 100 μg/ml Linear Free Amidation L HEK293: IC50=14.00 ± 1.46 µg/ml Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31604 FLGALFKALSKLL 13 PTP7 P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death via apoptosis Tumor cells: PANC-1 (IC50=11 μM ); PC-3 (IC50=5.01±0.42 µg/ml); MCF-7 (IC50=5.25±0.63 µg/ml); Hep 3B (IC50=5.40 ± 0.91 µg/ml); A549 (IC50=8.01 ± 1.32 µg/ml) Human RBCs: less than 6% hemolysis at 100 μg/ml Linear Free Amidation L HEK293: IC50=6.71 ± 0.47 µg/ml; MCF-10A: IC50=8 μM Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31605 FLKLLAGLLKNFA 13 PTP8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=24.58 ± 3.24 µg/ml); PC-3 (IC50=28.90 ± 5.19 µg/ml); Hep 3B (IC50=30.79 ± 3.11 µg/ml); MCF-7 (IC50=32.23 ± 9.12 µg/ml) Human RBCs: less than 6% hemolysis at 100 μg/ml Linear Free Amidation L HEK293: IC50=26.80 ± 5.52 µg/ml Not available 14499271 Peptides. 2003 Jul;24(7):945-53. Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines DRAMP31606 KIFGSLAFL 9 p369–377  Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: N202.A2 (Animals immunized three times with DC pulsed with p369–377 or p773–782 peptide showed ~25–30% tumor growth inhibition, while two immunizations induced ~12–15% tumor growth inhibition and one injection) Not available Linear Free Free L Not available Not available 14991605 Eur J Immunol. 2004 Mar;34(3):752-761. Lustgarten J, Dominguez AL, Cuadros C. The CD8 DRAMP31607 VMAGVGSPYV 10 p773–782  Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available The low-avidity T cell repertoire for a self tumor antigen is functional, can be activated and expanded with the help of costimulation Tumor cells: N202.A2 (Animals immunized three times with DC pulsed with p369–377 or p773–782 peptide showed ~25–30% tumor growth inhibition, while two immunizations induced ~12–15% tumor growth inhibition and one injection) Not available Linear Free Free L Not available Not available 14991605 Eur J Immunol. 2004 Mar;34(3):752-761. Lustgarten J, Dominguez AL, Cuadros C. The CD8 DRAMP31608 FRKSKEKIGKEFKRIVQRIKDFLRNLV 27 HCAP18(109-135) Q1KLX1##P49913 Not found hCAP18 Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SAS-H1 (88 ± 7.2% cytotoxicity=40 mg/ml) Not available Linear Free Free L Not available Not available 15279899 Cancer Lett. 2004 Aug 30;212(2):185-94. Okumura K, Itoh A, Isogai E, Hirose K, Hosokawa Y, Abiko Y, Shibata T, Hirata M, Isogai H. C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells DRAMP31609 HHPHGHHPHGHHPHGHHPHG 20 Ac-(HHPHG)4 -NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Bind to Tropomyosin and Have Antiangiogenic and Antitumor Activities Tumor cells: 3LL (The 50 mg/kg dose in the 3LL model significantly inhibited tumor growth by 48%); B16-F1 (The 50 mg/kg dose in the 3LL model significantly inhibited tumor growth by 48%) Not available Linear Acetylation Amidation L Not available Tropomyosin 15313924 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities DRAMP31610 CVKVKVKVGSGVKVKVKVC 19 V1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=45 µM) Human erythrocytes: 50% Hemolysis=880 µM Cyclic Acetylization Amidation L Not available Not available 15328096 Antimicrob Agents Chemother. 2004 Sep;48(9):3349-57. Frecer V, Ho B, Ding JL. De novo design of potent antimicrobial peptides DRAMP31611 CWMSPRHLGTCGRKKRRQRRRPPQ 24 CIGB-300 (P15-Tat) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available CIGB-300 is a cyclic synthetic peptide that induces apoptosis in malignant cells, elicits antitumor activity in cancer animal models Tumor cells: SiHa (IC50=135±10 µmol/L); HeLa (IC50=136±16 µmol/L); 3LL (IC50=143±4 µmol/L); A549 (IC50=171±12 µmol/L); Ca Ski (IC50=182±6 µmol/L); NCI-H82 (IC50=20±3 µmol/L); PC-3 (IC50=201±16 µmol/L); HL-60 (IC50=30±3 µmol/L); NCI-H125 (IC50=36±9 µmol/L); TC-1 (IC50=71±15 µmol/L); Jurkat (IC50=89±3 µmol/L) Not available Cyclic Free Free L Not available Not available 15466209 Cancer Res. 2004 Oct 1;64(19):7127-9. Perea SE, Reyes O, Puchades Y, Mendoza O, Vispo NS, Torrens I, Santos A, Silva R, Acevedo B, López E, Falcón V, Alonso DF. Antitumor effect of a novel proapoptotic peptide that impairs the phosphorylation by the protein kinase 2 (casein kinase 2) DRAMP31612 GRKKRRQRRRGGWMWVTNLRTD 22 TAT-Ras-GAP317-326 Not available Not found RasGAP-derived peptides Antimicrobial, Anticancer Not found Not found Not found Not available Enhances genotoxin-induced cytotoxicity in tumor cells Tumor cells: HeLa (rendered all the tested cancer cell lines sensitive to doses of cisplatin, adriamycin, and mitoxantrone ); H-Meso-1 (rendered all the tested cancer cell lines sensitive to doses of cisplatin, adriamycin, and mitoxantrone ); MCF-7 (rendered all the tested cancer cell lines sensitive to doses of cisplatin, adriamycin, and mitoxantrone ); U2OS (rendered all the tested cancer cell lines sensitive to doses of cisplatin, adriamycin, and mitoxantrone ) Not available Linear Free Free L Not available Not available 15467750 Oncogene. 2004 Nov 25;23(55):8971-8. Michod D, Yang JY, Chen J, Bonny C, Widmann C. A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells DRAMP31613 ERRP 4 EGFR-related peptide Not available Not found EGFR-related peptide Antimicrobial, Anticancer Not found Not found Not found Not available ERRP inhibits the growth of prostate cancer cells by attenuating EGFR signaling processes Tumor cells: PC-3 (30% Cell viability at 5 µg/ml) Not available Linear Free Free L Not available Not available 15634655 Mol Cancer Ther. 2004 Dec;3(12):1615-21. Marciniak DJ, Rishi AK, Sarkar FH, Majumdar AP. Epidermal growth factor receptor-related peptide inhibits growth of PC-3 prostate cancer cells DRAMP31614 LW 2 Psychrophilin D (1) Not available Not found Anthranilic acid Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (IC50=10.1 µg/ml) Not available Linear Free Free L Not available Not available 15835725 J Antibiot (Tokyo). 2005 Feb;58(2):141-4. Dalsgaard PW, Larsen TO, Christophersen C. Bioactive cyclic peptides from the psychrotolerant fungus Penicillium algidum DRAMP31615 HSHRDFQPVLHLVALNSPLSGGMRG 25 hP1 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (39% inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31616 MRGIRGADFQAFQQARAVGLAGTFR 25 hP2 Not available Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (19% inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31617 TFRAFLSSRLQDLYSIVRRADRAAV 25 hP3 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (No inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31618 AAVPIVNLKDELLFPSWEALFSGSE 25 hP4 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (No inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31619 GSEGPLKPGARIFSFDGKDVLRHPT 25 hP5 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (29% inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31620 HPTWPQKSVWHGSDPNGRRLTESY 24 hP6 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (No inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31621 ETWRTEAPSATGQASSLLGGRLLGQ 25 hP7 P39060 Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (No inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31622 LGQSAASAHHAYIVLAIENSFMTASKKK 28 hP8 Not available Not found Human endostatin peptides Antimicrobial, Anticancer Not found Not found Not found Not available Inhibition of endothelial cell proliferation, migration, and tube formation Tumor cells: BxPC-3 (No inhibition at 7 mg/kg/d) Not available Linear Free Free L Not available α5β1 integrin, metalloproteinases 15867360 Cancer Res. 2005 May 1;65(9):3656-63. Tjin Tham Sjin RM, Satchi-Fainaro R, Birsner AE, Ramanujam VM, Folkman J, Javaherian K. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity DRAMP31623 AXQNXXXPLXXVX 13 Laxaphycin B Not available Not found Terrestrial blue-green alga Anabaena laxa or the marine cyanobacterium Lyngbya Majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CEM/VM-1 (40% inhibition at 1 µM); CEM-VLB (40% inhibition at 1 µM); CEM-WT (40% inhibition at 1 µM); CEM/VM-1 (44% inhibition at 1 µM); CEM-VLB (44% inhibition at 1 µM); CEM-WT (44% inhibition at 1 µM); CEM-WT (50% inhibition at 1 µM) Not available Cyclic X(2/13)=Leu(3-OH); X(5)=N(Me)xiIle; X(6)=Asn(3-OH); X(7/10)=xiThr; X(11)=Unk L Not available Not available 15875779 In Vivo. 2005 May-Jun;19(3):577-82. Gbankoto A, Vigo J, Dramane K, Banaigs B, Aina E, Salmon JM. Cytotoxic effect of Laxaphycins A and B on human lymphoblastic cells (CCRF-CEM) using digitised videomicrofluorometry DRAMP31624 XXXFLXXLGXX 11 Laxaphycin A Not available Not found Terrestrial blue-green alga Anabaena laxa or the marine cyanobacterium Lyngbya Majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CEM/VM-1 (No inhibition at 4 µM); CEM-VLB (No inhibition at 4 µM); CEM-WT (No inhibition at 4 µM) Not available Cyclic X(1)=Abu(2,3-dehydro); X(2)=xiHyp; X(3/11)=Hse; X(6/7)=xiIle; X(10)=Unk L Not available Not available 15875779 In Vivo. 2005 May-Jun;19(3):577-82. Gbankoto A, Vigo J, Dramane K, Banaigs B, Aina E, Salmon JM. Cytotoxic effect of Laxaphycins A and B on human lymphoblastic cells (CCRF-CEM) using digitised videomicrofluorometry DRAMP31625 MWKWFHNVLSSWQLLADKRPARDYNRK 27 Pep27anal1 Not available Not found S. pneumoniae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SNU-601 (IC50=37 µM); Jurkat (IC50=47 µM); OCI-AML-2 (IC50=50 µM); HL-60 (IC50=53 µM); MCF-7 (IC50=55 µM) Human RBCs(0% hemolysis at 0.19 μM, 0.39 μM, 0.78 μM, 1.56 μM, 3.12 μM, 6.25 μM, 12.5 μM) Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP31626 MWKWFHNVLSWWWLLADKRPARDYNRK 27 Pep27anal2 Not available Not found S. pneumoniae Antimicrobial, Anticancer Not found Not found Not found Not available Pep27anal2 can penetrate the plasma membrane, and then induce apoptosis in both caspase-and cytochrome c-independent manner Tumor cells: MCF-7 (IC50<10 µM); HL-60 (IC50=20 µM); Jurkat (IC50=23 µM); SNU-601 (IC50=25 µM); OCI-AML-2 (IC50=29 µM) Human RBCs(18% hemolysis at 12.5 μM), Human RBCs(0% hemolysis at 0.19 μM, 0.39 μM, 0.78 μM, 1.56 μM, 3.12 μM, 6.25 μM) Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP31627 MRKWFHNVLSSGQLLADKWPAWDYNRK 27 Pep27anal3 Not available Not found S. pneumoniae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=38 µM); Jurkat (IC50=50 µM); SNU-601 (IC50=50 µM); HL-60 (IC50=52 µM); OCI-AML-2 (IC50=67 µM) Human RBCs(0% hemolysis at 0.19 μM, 0.39 μM, 0.78 μM, 1.56 μM, 3.12 μM, 6.25 μM, 12.5 μM) Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP31628 MWKEFHNVLSSGQLLADKRWARWYNRW 27 Pep27anal4 Not available Not found S. pneumoniae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=29 µM); SNU-601 (IC50=37 µM); Jurkat (IC50=46 µM); OCI-AML-2 (IC50=50 µM); HL-60 (IC50=51 µM) Human RBCs(0% hemolysis at 0.19 μM, 0.39 μM, 0.78 μM, 1.56 μM, 3.12 μM, 6.25 μM, 12.5 μM) Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP31629 MWKWFHNVLSSGQLLADKWWAWWYNWW 27 Pep27anal5 Not available Not found S. pneumoniae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50>70 µM); Jurkat (IC50>70 µM); MCF-7 (IC50>70 µM); OCI-AML-2 (IC50>70 µM); SNU-601 (IC50>70 µM) Human RBCs(0% hemolysis at 0.19 μM, 0.39 μM, 0.78 μM, 1.56 μM, 3.12 μM, 6.25 μM, 12.5 μM) Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP31630 YSL 3 Tyroserleutide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Enhances the antitumor effects of macrophages and stimulates macrophage secretion of IL-1β, TNF-α, and NO in vitro Tumor cells: BEL-7402 (20.8% cytotoxic at 1 µg/ml); BEL-7402 (33.8% cytotoxic at 10 µg/ml); BEL-7402 (35.6% cytotoxic at 100 µg/ml); BEL-7402 (39.0% cytotoxic at 0.1 µg/ml); B16-F10 (49.4% cytotoxic at 0.1 µg/ml); B16-F10 (51.2% cytotoxic at 1 µg/ml); B16-F10 (53.0% cytotoxic at 10 µg/ml); B16-F10 (61.2% cytotoxic at 100 µg/ml) Not available Linear Free Free L Not available Not available 16091933 Cancer Immunol Immunother. 2006 Jan;55(1):56-60. Yao Z, Qiu S, Wang L, Lu R, Zhou CL, Zhao PP, Li HQ, Gao WY. Tripeptide tyroserleutide enhances the antitumor effects of macrophages and stimulates macrophage secretion of IL-1beta, TNF-alpha, and NO in vitro DRAMP31631 rrrrrrrrGNLWAAQRYGRELRRMSDEFVDSFKK 34 r8-BadBH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induce apoptosis in highly malignant NB-derived cell lines Tumor cells: NGP (>50% apoptosis at 20 µM); SK-N-AS (0% apoptosis at 10 µM); SK-N-AS (10% apoptosis at 20 µM); IMR-5 (15% apoptosis at 10 µM); NGP (20% apoptosis at 10 µM); IMR-5 (20% apoptosis at 20 µM); NB69 (30% apoptosis at 10 µM); NGP (30% apoptosis at 50 µM); SK-N-AS (30% apoptosis at 50 µM); IMR-5 (50% apoptosis at 50 µM); NB69 (80% apoptosis at 20 µM); NB69 (80% apoptosis at 50 µM) Not available Linear Free Free rrrrrrrr=D-isomer homopolymer of eight arginine residues Mix Not available Not available 16568093 Cancer Immunol Immunother. 2006 Jan;55(1):56-60. Yao Z, Qiu S, Wang L, Lu R, Zhou CL, Zhao PP, Li HQ, Gao WY. BH3 peptidomimetics potently activate apoptosis and demonstrate single agent efficacy in neuroblastoma DRAMP31632 rrrrrrrrGEDIIRNIARHLAQVGDSMDR 29 r8-BidBH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induce apoptosis in highly malignant NB-derived cell lines Tumor cells: IMR-5 (23% apoptosis at 10 µM); NB69 (25% apoptosis at 10 µM); IMR-5 (35% apoptosis at 20 µM); NGP (43% apoptosis at 10 µM); SK-N-AS (45% apoptosis at 20 µM); NGP (46% apoptosis at 20 µM); IMR-5 (55% apoptosis at 50 µM); SK-N-AS (65% apoptosis at 50 µM); NB69 (66% apoptosis at 20 µM); NB69 (68% apoptosis at 50 µM); NGP (79% apoptosis at 50 µM); SK-N-AS (8% apoptosis at 10 µM) Not available Linear Free Free rrrrrrrr=D-isomer homopolymer of eight arginine residues Mix Not available Not available 16568093 Cancer Immunol Immunother. 2006 Jan;55(1):56-60. Yao Z, Qiu S, Wang L, Lu R, Zhou CL, Zhao PP, Li HQ, Gao WY. BH3 peptidomimetics potently activate apoptosis and demonstrate single agent efficacy in neuroblastoma DRAMP31633 rrrrrrrrGEDIIRNIARHAAQVGASMDR 29 r8-BidBH3Alt Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induce apoptosis in highly malignant NB-derived cell lines Tumor cells: IMR-5 (0% apoptosis at 10 µM); NGP (1% apoptosis at 10 µM); SK-N-AS (1% apoptosis at 10 µM); IMR-5 (1% apoptosis at 20 µM); NB69 (1% apoptosis at 20 µM); NB69 (2% apoptosis at 10 µM); NGP (2% apoptosis at 20 µM); SK-N-AS (2% apoptosis at 20 µM); IMR-5 (2% apoptosis at 50 µM); NGP (3% apoptosis at 50 µM); SK-N-AS (3% apoptosis at 50 µM); NB69 (5% apoptosis at 50 µM) Not available Linear Free Free rrrrrrrr=D-isomer homopolymer of eight arginine residues Mix Not available Not available 16568093 Cancer Immunol Immunother. 2006 Jan;55(1):56-60. Yao Z, Qiu S, Wang L, Lu R, Zhou CL, Zhao PP, Li HQ, Gao WY. BH3 peptidomimetics potently activate apoptosis and demonstrate single agent efficacy in neuroblastoma DRAMP31634 LKlLKKLlkKLLkLL 15 D-K6L9 Not available Not found Host Defense lytic Peptide Antimicrobial, Anticancer Not found Not found Not found Not available The exclusive selectivity of the peptide towards cancer derives from its specific binding to surface phosphatidylserine and the killing of the cancer cells via cytoplasmic membrane depolarization Tumor cells: CL-1 (LC50=3 μmol/L); MDA-MB-231 (LC50=3 μmol/L); 22Rv1 (LC50=6 μmol/L) Not available Linear Free Amidation l=D-Leucine; k=D-Lysine Mix Not available surface phosphatidylserine 16707464 Cancer Res. 2006 May 15;66(10):5371-8. Papo N, Seger D, Makovitzki A, Kalchenko V, Eshhar Z, Degani H, Shai Y. Inhibition of tumor growth and elimination of multiple metastases in human prostate and breast xenografts by systemic inoculation of a host defense-like lytic peptide DRAMP31635 YGGFM 5 OGF, 7 Not available Not found The native opioid growth factor Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (0.4% inhibition at 1μM, 1% inhibition at 10μM, 4.5% inhibition at 100μM, 10.8% inhibition at 1000μM); HT-29 (14% inhibition at 1μM, 15.9% inhibition at 10μM, 16.1% inhibition at 100μM, 19.3% inhibition at 1000μM); SW620 (18.9% inhibition at 1μM, 12.7% inhibition at 10μM, 15.3% inhibition at 100μM, 19.1% inhibition at 1000μM); HeLa (2.3% inhibition at 1μM, 11.4% inhibition at 10μM, 12% inhibition at 100μM, 22.3% inhibition at 1000μM); MCF-7 (3.6% inhibition at 1μM, 4.1% inhibition at 10μM, 7.6% inhibition at 100μM, 15.4% inhibition at 1000μM); CaCo-2 (4.2% inhibition at 1μM, 6.4% inhibition at 10μM, 8.4% inhibition at 100μM, 3.2% inhibition at 1000μM); HEp-2 (5.2% inhibition at 1μM, 4.5% inhibition at 10μM, 2.4% inhibition at 100μM, 3.3% inhibition at 1000μM) Not available Linear Free Free L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31636 YX 2 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HeLa (10% inhibition at 10μM, 8.2% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.9% inhibition at 1μM, 16.5% inhibition at 10μM, 28.1% inhibition at 100μM, 58.2% inhibition at 1000μM); HEp-2 (14.2% inhibition at 1μM, 19.7% inhibition at 10μM, 24.9% inhibition at 100μM, 30.4% inhibition at 1000μM); MCF-7 (2.4% inhibition at 10μM, 7.5% inhibition at 1000μM); CaCo-2 (3.5% inhibition at 1μM, 22.7% inhibition at 10μM, 18.9% inhibition at 100μM, 26.4% inhibition at 1000μM); HBL (6.5% inhibition at 1μM, 14% inhibition at 10μM, 7.5% inhibition at 100μM, 14% inhibition at 1000μM); HT-29 (9.8% inhibition at 1μM, 1.6% inhibition at 10μM, 5.4% inhibition at 100μM, 26.5% inhibition at 1000μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31637 YX 2 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: MCF-7 (1.1% inhibition at 10μM, 1.2% inhibition at 100μM, 17.8% inhibition at 1000μM); SW620 (10.5% inhibition at 1μM, 21.9% inhibition at 10μM, 11.8% inhibition at 100μM, 17.9% inhibition at 1000μM); CaCo-2 (3.7% inhibition at 1μM, 16.5% inhibition at 10μM, 8.4% inhibition at 100μM, 14.5% inhibition at 1000μM); HBL (3.9% inhibition at 10μM, 7.3% inhibition at 1000μM); HT-29 (4.9% inhibition at 1μM, 8.9% inhibition at 10μM, 3.4% inhibition at 100μM, 20.8% inhibition at 1000μM); HEp-2 (6.2% inhibition at 1μM, 6.4% inhibition at 10μM, 8.2% inhibition at 100μM, 21.2% inhibition at 1000μM); HeLa (7.5% inhibition at 1μM, 6.1% inhibition at 10μM, 3.1% inhibition at 100μM, 14.8% inhibition at 1000μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31638 YX 2 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HT-29 (0.7% inhibition at 1μM, 8.3% inhibition at 10μM, 10.5% inhibition at 100μM, 21.8% inhibition at 1000μM); MCF-7 (1.6% inhibition at 1μM, 2.6% inhibition at 10μM, 7.7% inhibition at 100μM, 18.7% inhibition at 1000μM); SW620 (10.7% inhibition at 1μM, 10% inhibition at 10μM, 9.4% inhibition at 100μM, 18.7% inhibition at 1000μM); HEp-2 (2.7% inhibition at 1μM, 2% inhibition at 10μM, 18.8% inhibition at 100μM, 26.7% inhibition at 1000μM); CaCo-2 (22.2% inhibition at 1μM, 21.4% inhibition at 10μM, 17.5% inhibition at 100μM, 16% inhibition at 1000μM); HBL (3% inhibition at 1μM, 4.7% inhibition at 10μM, 2.7% inhibition at 100μM, 7.3% inhibition at 1000μM); HeLa (7.2% inhibition at 1μM, 17.1% inhibition at 10μM, 11% inhibition at 100μM, 20.5% inhibition at 1000μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31639 YX 2 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HeLa (10% inhibition at 10μM, 8.2% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.9% inhibition at 1μM, 16.5% inhibition at 10μM, 28.1% inhibition at 100μM, 58.2% inhibition at 1000μM); HEp-2 (14.2% inhibition at 1μM, 19.7% inhibition at 10μM, 24.9% inhibition at 100μM, 30.4% inhibition at 1000μM); MCF-7 (2.4% inhibition at 10μM, 7.5% inhibition at 1000μM); CaCo-2 (3.5% inhibition at 1μM, 22.7% inhibition at 10μM, 18.9% inhibition at 100μM, 26.4% inhibition at 1000μM); HBL (6.5% inhibition at 1μM, 14% inhibition at 10μM, 7.5% inhibition at 100μM, 14% inhibition at 1000μM); HT-29 (9.8% inhibition at 1μM, 1.6% inhibition at 10μM, 5.4% inhibition at 100μM, 26.5% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,S ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31640 YX 2 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: MCF-7 (1.1% inhibition at 10μM, 1.2% inhibition at 100μM, 17.8% inhibition at 1000μM); SW620 (10.5% inhibition at 1μM, 21.9% inhibition at 10μM, 11.8% inhibition at 100μM, 17.9% inhibition at 1000μM); CaCo-2 (3.7% inhibition at 1μM, 16.5% inhibition at 10μM, 8.4% inhibition at 100μM, 14.5% inhibition at 1000μM); HBL (3.9% inhibition at 10μM, 7.3% inhibition at 1000μM); HT-29 (4.9% inhibition at 1μM, 8.9% inhibition at 10μM, 3.4% inhibition at 100μM, 20.8% inhibition at 1000μM); HEp-2 (6.2% inhibition at 1μM, 6.4% inhibition at 10μM, 8.2% inhibition at 100μM, 21.2% inhibition at 1000μM); HeLa (7.5% inhibition at 1μM, 6.1% inhibition at 10μM, 3.1% inhibition at 100μM, 14.8% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,S ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31641 YX 2 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HT-29 (0.7% inhibition at 1μM, 8.3% inhibition at 10μM, 10.5% inhibition at 100μM, 21.8% inhibition at 1000μM); MCF-7 (1.6% inhibition at 1μM, 2.6% inhibition at 10μM, 7.7% inhibition at 100μM, 18.7% inhibition at 1000μM); SW620 (10.7% inhibition at 1μM, 10% inhibition at 10μM, 9.4% inhibition at 100μM, 18.7% inhibition at 1000μM); HEp-2 (2.7% inhibition at 1μM, 2% inhibition at 10μM, 18.8% inhibition at 100μM, 26.7% inhibition at 1000μM); CaCo-2 (22.2% inhibition at 1μM, 21.4% inhibition at 10μM, 17.5% inhibition at 100μM, 16% inhibition at 1000μM); HBL (3% inhibition at 1μM, 4.7% inhibition at 10μM, 2.7% inhibition at 100μM, 7.3% inhibition at 1000μM); HeLa (7.2% inhibition at 1μM, 17.1% inhibition at 10μM, 11% inhibition at 100μM, 20.5% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,S ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31642 YX 2 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HeLa (10% inhibition at 10μM, 8.2% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.9% inhibition at 1μM, 16.5% inhibition at 10μM, 28.1% inhibition at 100μM, 58.2% inhibition at 1000μM); HEp-2 (14.2% inhibition at 1μM, 19.7% inhibition at 10μM, 24.9% inhibition at 100μM, 30.4% inhibition at 1000μM); MCF-7 (2.4% inhibition at 10μM, 7.5% inhibition at 1000μM); CaCo-2 (3.5% inhibition at 1μM, 22.7% inhibition at 10μM, 18.9% inhibition at 100μM, 26.4% inhibition at 1000μM); HBL (6.5% inhibition at 1μM, 14% inhibition at 10μM, 7.5% inhibition at 100μM, 14% inhibition at 1000μM); HT-29 (9.8% inhibition at 1μM, 1.6% inhibition at 10μM, 5.4% inhibition at 100μM, 26.5% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,R ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31643 YX 2 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: MCF-7 (1.1% inhibition at 10μM, 1.2% inhibition at 100μM, 17.8% inhibition at 1000μM); SW620 (10.5% inhibition at 1μM, 21.9% inhibition at 10μM, 11.8% inhibition at 100μM, 17.9% inhibition at 1000μM); CaCo-2 (3.7% inhibition at 1μM, 16.5% inhibition at 10μM, 8.4% inhibition at 100μM, 14.5% inhibition at 1000μM); HBL (3.9% inhibition at 10μM, 7.3% inhibition at 1000μM); HT-29 (4.9% inhibition at 1μM, 8.9% inhibition at 10μM, 3.4% inhibition at 100μM, 20.8% inhibition at 1000μM); HEp-2 (6.2% inhibition at 1μM, 6.4% inhibition at 10μM, 8.2% inhibition at 100μM, 21.2% inhibition at 1000μM); HeLa (7.5% inhibition at 1μM, 6.1% inhibition at 10μM, 3.1% inhibition at 100μM, 14.8% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,R ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31644 YX 2 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HT-29 (0.7% inhibition at 1μM, 8.3% inhibition at 10μM, 10.5% inhibition at 100μM, 21.8% inhibition at 1000μM); MCF-7 (1.6% inhibition at 1μM, 2.6% inhibition at 10μM, 7.7% inhibition at 100μM, 18.7% inhibition at 1000μM); SW620 (10.7% inhibition at 1μM, 10% inhibition at 10μM, 9.4% inhibition at 100μM, 18.7% inhibition at 1000μM); HEp-2 (2.7% inhibition at 1μM, 2% inhibition at 10μM, 18.8% inhibition at 100μM, 26.7% inhibition at 1000μM); CaCo-2 (22.2% inhibition at 1μM, 21.4% inhibition at 10μM, 17.5% inhibition at 100μM, 16% inhibition at 1000μM); HBL (3% inhibition at 1μM, 4.7% inhibition at 10μM, 2.7% inhibition at 100μM, 7.3% inhibition at 1000μM); HeLa (7.2% inhibition at 1μM, 17.1% inhibition at 10μM, 11% inhibition at 100μM, 20.5% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,R ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31645 YXG 3 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (1.6% inhibition at 1μM, 2.9% inhibition at 10μM, 5.9% inhibition at 100μM, 17.9% inhibition at 1000μM); SW620 (13.6% inhibition at 1μM, 20.4% inhibition at 10μM, 14.4% inhibition at 100μM, 23.4% inhibition at 1000μM); CaCo-2 (2.2% inhibition at 1μM, 4.2% inhibition at 10μM, 6.4% inhibition at 100μM, 6.2% inhibition at 1000μM); HEp-2 (2.7% inhibition at 1μM, 2% inhibition at 10μM, 18.8% inhibition at 100μM, 26.7% inhibition at 1000μM); MCF-7 (21.2% inhibition at 100μM); HT-29 (5.4% inhibition at 1μM, 7.4% inhibition at 10μM, 9.5% inhibition at 100μM, 15.7% inhibition at 1000μM); HeLa (9.8% inhibition at 1μM, 7.3% inhibition at 10μM, 9.9% inhibition at 100μM, 28.2% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,S ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31646 YXG 3 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (1.2% inhibition at 10μM, 3.3% inhibition at 100μM, 19.4% inhibition at 1000μM); HeLa (11% inhibition at 1μM, 11.7% inhibition at 10μM, 11.6% inhibition at 100μM, 28.2% inhibition at 1000μM); MCF-7 (15.6% inhibition at 100μM); SW620 (17% inhibition at 1μM, 13.5% inhibition at 10μM, 13.5% inhibition at 100μM, 25.3% inhibition at 1000μM); HEp-2 (4.6% inhibition at 1μM, 4.9% inhibition at 10μM, 12.6% inhibition at 100μM, 26.4% inhibition at 1000μM); HT-29 (7.6% inhibition at 1μM, 3.8% inhibition at 10μM, 12.4% inhibition at 100μM, 22.4% inhibition at 1000μM); CaCo-2 (8.1% inhibition at 1μM, 6.9% inhibition at 10μM, 8.1% inhibition at 100μM, 8.6% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,S ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31647 YXG 3 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (1.6% inhibition at 1μM, 2.9% inhibition at 10μM, 5.9% inhibition at 100μM, 17.9% inhibition at 1000μM); SW620 (13.6% inhibition at 1μM, 20.4% inhibition at 10μM, 14.4% inhibition at 100μM, 23.4% inhibition at 1000μM); CaCo-2 (2.2% inhibition at 1μM, 4.2% inhibition at 10μM, 6.4% inhibition at 100μM, 6.2% inhibition at 1000μM); HEp-2 (2.7% inhibition at 1μM, 2% inhibition at 10μM, 18.8% inhibition at 100μM, 26.7% inhibition at 1000μM); MCF-7 (21.2% inhibition at 100μM); HT-29 (5.4% inhibition at 1μM, 7.4% inhibition at 10μM, 9.5% inhibition at 100μM, 15.7% inhibition at 1000μM); HeLa (9.8% inhibition at 1μM, 7.3% inhibition at 10μM, 9.9% inhibition at 100μM, 28.2% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,R ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31648 YXG 3 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (1.2% inhibition at 10μM, 3.3% inhibition at 100μM, 19.4% inhibition at 1000μM); HeLa (11% inhibition at 1μM, 11.7% inhibition at 10μM, 11.6% inhibition at 100μM, 28.2% inhibition at 1000μM); MCF-7 (15.6% inhibition at 100μM); SW620 (17% inhibition at 1μM, 13.5% inhibition at 10μM, 13.5% inhibition at 100μM, 25.3% inhibition at 1000μM); HEp-2 (4.6% inhibition at 1μM, 4.9% inhibition at 10μM, 12.6% inhibition at 100μM, 26.4% inhibition at 1000μM); HT-29 (7.6% inhibition at 1μM, 3.8% inhibition at 10μM, 12.4% inhibition at 100μM, 22.4% inhibition at 1000μM); CaCo-2 (8.1% inhibition at 1μM, 6.9% inhibition at 10μM, 8.1% inhibition at 100μM, 8.6% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,R ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31649 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (0.8% inhibition at 1μM, 1.4% inhibition at 10μM, 2.4% inhibition at 100μM, 18.3% inhibition at 1000μM); HEp-2 (1% inhibition at 1μM, 10.1% inhibition at 10μM, 16.8% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.2% inhibition at 1μM, 15.5% inhibition at 10μM, 24.7% inhibition at 100μM, 29% inhibition at 1000μM); MCF-7 (22.8% inhibition at 1000μM); CaCo-2 (3% inhibition at 1μM, 8.4% inhibition at 10μM, 18.5% inhibition at 100μM, 10.6% inhibition at 1000μM); HT-29 (3.3% inhibition at 1μM, 11% inhibition at 10μM, 7.9% inhibition at 100μM, 23.7% inhibition at 1000μM); HeLa (4.9% inhibition at 1μM, 10.2% inhibition at 10μM, 13.3% inhibition at 100μM, 28% inhibition at 1000μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31650 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HEp-2 (13.7% inhibition at 1μM, 25.8% inhibition at 10μM, 34.7% inhibition at 100μM, 44.5% inhibition at 1000μM); HT-29 (16.2% inhibition at 1μM, 6.6% inhibition at 10μM, 5.1% inhibition at 100μM, 14.5% inhibition at 1000μM); CaCo-2 (17.7% inhibition at 1μM, 10.9% inhibition at 10μM, 12.1% inhibition at 100μM, 8.1% inhibition at 1000μM); HBL (2.4% inhibition at 1μM, 4.5% inhibition at 10μM, 11.4% inhibition at 100μM, 23.2% inhibition at 1000μM); SW620 (26.4% inhibition at 1μM, 13.1% inhibition at 10μM, 14.6% inhibition at 100μM, 38.4% inhibition at 1000μM); HeLa (8.5% inhibition at 1μM, 9.5% inhibition at 10μM, 15.4% inhibition at 100μM, 24.1% inhibition at 1000μM); MCF-7 (9.6% inhibition at 100μM, 29.9% inhibition at 100μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31651 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Not available Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31652 YXGFM 5 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HBL (0.8% inhibition at 1μM, 1.4% inhibition at 10μM, 2.4% inhibition at 100μM, 18.3% inhibition at 1000μM); HEp-2 (1% inhibition at 1μM, 10.1% inhibition at 10μM, 16.8% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.2% inhibition at 1μM, 15.5% inhibition at 10μM, 24.7% inhibition at 100μM, 29% inhibition at 1000μM); MCF-7 (22.8% inhibition at 1000μM); CaCo-2 (3% inhibition at 1μM, 8.4% inhibition at 10μM, 18.5% inhibition at 100μM, 10.6% inhibition at 1000μM); HT-29 (3.3% inhibition at 1μM, 11% inhibition at 10μM, 7.9% inhibition at 100μM, 23.7% inhibition at 1000μM); HeLa (4.9% inhibition at 1μM, 10.2% inhibition at 10μM, 13.3% inhibition at 100μM, 28% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31653 YXGFM 5 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: HEp-2 (13.7% inhibition at 1μM, 25.8% inhibition at 10μM, 34.7% inhibition at 100μM, 44.5% inhibition at 1000μM); HT-29 (16.2% inhibition at 1μM, 6.6% inhibition at 10μM, 5.1% inhibition at 100μM, 14.5% inhibition at 1000μM); CaCo-2 (17.7% inhibition at 1μM, 10.9% inhibition at 10μM, 12.1% inhibition at 100μM, 8.1% inhibition at 1000μM); HBL (2.4% inhibition at 1μM, 4.5% inhibition at 10μM, 11.4% inhibition at 100μM, 23.2% inhibition at 1000μM); SW620 (26.4% inhibition at 1μM, 13.1% inhibition at 10μM, 14.6% inhibition at 100μM, 38.4% inhibition at 1000μM); HeLa (8.5% inhibition at 1μM, 9.5% inhibition at 10μM, 15.4% inhibition at 100μM, 24.1% inhibition at 1000μM); MCF-7 (9.6% inhibition at 100μM, 29.9% inhibition at 100μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31654 YXGFM 5 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Not available Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31655 YGGFMX 6 23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available lead to apoptosis Tumor cells: CaCo-2 (11.8% inhibition at 10μM, 47.0% inhibition at 1000μM); MCF-7 (2.2% inhibition at 1μM, 7.1% inhibition at 10μM, 6.9% inhibition at 100μM, 25.9% inhibition at 1000μM); HEp-2 (3.9% inhibition at 10μM, 45.0% inhibition at 1000μM); HBL (4.1% inhibition at 1μM, 70.7% inhibition at 10μM, 34.2% inhibition at 1000μM); HT-29 (9.2% inhibition at 1000μM); HeLa (9.3% inhibition at 1000μM) Not available Linear Free Free X=Cαα -dialkylated glycine (Aaa1 ) L Not available Not available 16722632 J Med Chem. 2006 Jun 1;49(11):3136-42. Horvat S, Mlinarić-Majerski K, Glavas-Obrovac L, Jakas A, Veljković J, Marczi S, Kragol G, Roscić M, Matković M, Milostić-Srb A. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity DRAMP31656 FLGALFKVASKVLPSVKCAITKKC 24 Gaegurin-5 Not available Not found Rana rugosa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=113.31 µg/ml); A498 (IC50=138.06 µg/ml); A549 (IC50=145.72 µg/ml); MCF-7 (IC50=183.74 µg/ml); MKN 45 (IC50=34.96 µg/ml); SK-OV-3 (IC50=38.28 µg/ml); NCI-H630 (IC50=41.85 µg/ml); PC-3 (IC50=43.64 µg/ml); SK-MEL-2 (IC50=47.47 µg/ml) Human erythrocytes: 7% Hemolysis=100 µg/ml Linear Free Free L Not available Not available 16884301 J Med Chem. 2006 Aug 10;49(16):4886-95. Won HS, Seo MD, Jung SJ, Lee SJ, Kang SJ, Son WS, Kim HJ, Park TK, Park SJ, Lee BJ. Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5 DRAMP31657 FLGALFKWASK 11 Gaegurin 5 (1-11)[V8W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H630 (IC50=129.54 µg/ml); MKN 45 (IC50=142.72 µg/ml); HCT 116 (IC50=144.37 µg/ml); SK-OV-3 (IC50=150.45 µg/m); PC-3 (IC50=174.15 µg/ml); MCF-7 (IC50=198.87 µg/ml); A498 (IC50=214.33 µg/ml); A549 (IC50=418.15 µg/ml) Human erythrocytes: 7% Hemolysis=100 µg/ml Linear Free Free L MCF-10a: IC50=434.79 µg/ml Not available 16884301 J Med Chem. 2006 Aug 10;49(16):4886-95. Won HS, Seo MD, Jung SJ, Lee SJ, Kang SJ, Son WS, Kim HJ, Park TK, Park SJ, Lee BJ. Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5 DRAMP31658 FLGWLFKVASK 11 Gaegurin 5 (1-11)[A4W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=106.27 µg/ml); PC-3 (IC50=123.81 µg/ml); HCT 116 (IC50=30.48 µg/ml); SK-MEL-2 (IC50=30.48 µg/ml); A498 (IC50=73.26 µg/ml); NCI-H630 (IC50=75.92 µg/ml); MCF-7 (IC50=77.29 µg/ml); MKN 45 (IC50=82.70 µg/ml); SK-OV-3 (IC50=92.15 µg/ml) Human erythrocytes: 12% Hemolysis=100 µg/ml Linear Free Free L MCF-10a: IC50=311.38 µg/ml Not available 16884301 J Med Chem. 2006 Aug 10;49(16):4886-95. Won HS, Seo MD, Jung SJ, Lee SJ, Kang SJ, Son WS, Kim HJ, Park TK, Park SJ, Lee BJ. Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5 DRAMP31659 ALSKALSKALSKALSKALSKALSK 24 Z44 Not available Not found Xenopus laevis Antimicrobial, Anticancer Not found Not found Not found Not available magainin 2 and synthetic analogues can rapidly and irreversibly lyse hematopoietic tumor and solid tumor Tumor cells: SSKT-1 (IC50=107 µg/ml); Daudi (IC50=115 µg/ml); RPMI-8402 (IC50=60 µg/ml); Raji (IC50=64 µg/ml); MLA (IC50=80 µg/ml); U-937 (IC50=97 µg/ml); K562 (IC50=98 µg/ml) Not available Linear Free Amidation L Not available Not available 1708887 Proc Natl Acad Sci U S A. 1991 May 1;88(9):3792-6. Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation DRAMP31660 AKSKAKSKAKSKAKSKAKSKAKSK 24 Z24 Not available Not found Xenopus laevis Antimicrobial, Anticancer Not found Not found Not found Not available magainin 2 and synthetic analogues can rapidly and irreversibly lyse hematopoietic tumor and solid tumor Tumor cells: MLA (IC50=102 µg/ml); SSKT-1 (IC50=109 µg/ml); K562 (IC50=112 µg/ml); U-937 (IC50=123 µg/ml); Daudi (IC50=143 µg/ml); Raji (IC50=72 µg/ml); RPMI-8402 (IC50=83 µg/ml) Not available Linear Free Amidation L Not available Not available 1708887 Proc Natl Acad Sci U S A. 1991 May 1;88(9):3792-6. Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation DRAMP31661 KILRGVSKKIMRTFLRRILTGKK 23 NK23c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100 µg/ml) Human erythrocytes: 15% Hemolysis=100 µg/ml Linear Free Free L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31662 KILRGVSKKIMRTFLRRISKDILTGKK 27 C7S/NK27 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa ((38.4±10.3)% Cytotoxicity=100 µg/ml) Human erythrocytes: 25% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31663 KILRGVSKKIMRTFLRRISKDILTGKK 27 C7S/NK27 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa ((6.5±17.3)% Cytotoxicity=100 µg/ml) Human erythrocytes: 25% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31664 KILRGVSKKIMRTFLRRISKDILTGKK 27 C7S/NK27-COOH Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa ((38.4±10.3)% Cytotoxicity=100 µg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Free L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31665 KILRGVSKKIMRTFLRRISKDILTGKK 27 C7S/NK27-COOH Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa ((6.5±17.3)% Cytotoxicity=100 µg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Free L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31666 KISKKIMRTFLRRISKDILTGKK 23 NK23a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100 µg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP31667 VXLfPVXLfP 10 Gramicidin S Not available Not found Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (LC50=7.4 µM); A549 (LC50=7.5 µM) Human erythrocytes: 100% Hemolysis=39 µg/ml; 50% Hemolysis=11 µM; Sheep erythrocytes: 50% Hemolysis=21.1±2.6 µM; 100% Hemolysis=100 µM Cyclic Free Free X=Orn; f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97. Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP31668 fCYwOXXTKKrPKPfQwFwLXKKLMYPTYLKKfQWAVXHL 40 Propeptide 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Molt-4 (10.4 % inhibition of cell proliferation at 1 nM); KB (10.6 % inhibition of cell proliferation at 1 nM); PTC (14.2 % inhibition of cell proliferation at 10 nM); PTC (16.5 % inhibition of cell proliferation at 1 nM); PTC (16.8 % inhibition of cell proliferation at 100 nM); KB (18.2 % inhibition of cell proliferation at 10 nM); Molt-4 (18.7 % inhibition of cell proliferation at 10 nM); PTC (21.7 % inhibition of cell proliferation at 1 µM); Mia PaCa-2 (24.2 % inhibition of cell proliferation at 1 nM); PTC (27.9 % inhibition of cell proliferation at 10 µM); MCF-7 (28.2 % inhibition of cell proliferation at 10 nM); MCF-7 (29.7 % inhibition of cell proliferation at 1 nM); KB (30.7 % inhibition of cell proliferation at 100 nM); Molt-4 (34.7 % inhibition of cell proliferation at 100 nM); MCF-7 (35.3 % inhibition of cell proliferation at 100 nM); Mia PaCa-2 (37.8 % inhibition of cell proliferation at 10 nM); KB (43.1 % inhibition of cell proliferation at 1 µM); Mia PaCa-2 (48.2 % inhibition of cell proliferation at 100 nM); Molt-4 (54.3 % inhibition of cell proliferation at 1 µM); MCF-7 (59.4 % inhibition of cell proliferation at 1 µM); Mia PaCa-2 (59.6 % inhibition of cell proliferation at 1 µM); Mia PaCa-2 (84.5 % inhibition of cell proliferation at 10 µM); MCF-7 (85.4 % inhibition of cell proliferation at 10 µM); Molt-4 (94.5 % inhibition of cell proliferation at 10 µM); KB (98.3 % inhibition of cell proliferation at 10 µM) Not available Cyclic Free Amidation f=D-Phenylalanine; w=D-Tryptophan; O=Ornithine; X(6/21)==cycloleucine or 1-aminocyclopentane-1-carboxylic acid; X(7)=penicillamine; r=D-Arginine; Aib=2-Aminoisobutyric acid Mix Not available Not available 17559067 J Pept Sci. 2007 Jul;13(7):458-67. Prasad S, Mathur A, Jaggi M, Mukherjee R. Delivering multiple anticancer peptides as a single prodrug using lysyl-lysine as a facile linker DRAMP31669 LLGMIPLAISAISALSKL 18 Phylloseptin-L1 A0A5Q0MU22##P0DQK9##L0P329 Not found skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae) Antimicrobial, Anticancer Not found Not found Not found Not available Cytolytic Tumor cells: Hep-G2 (LC50=35 μM) Human erythrocytes: LC50=200 μM Linear Free Free L Not available Not available 17561225 Toxicon. 2007 Sep 15;50(4):498-506. Conlon JM, Woodhams DC, Raza H, Coquet L, Leprince J, Jouenne T, Vaudry H, Rollins-Smith LA. Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae) DRAMP31670 FKCRRWQWRMKKLGAPSITCVR 22 Pep1 P24627 Not found Bovine lactoferrin (Lf-B) Antimicrobial, Anticancer Not found Not found Not found 1LFC Pep1 may kill cancer cells by activating an apoptosis-inducing pathway Tumor cells: HL-60 (IC50=77 µM) Not available Linear Free Free L Not available Not available 18425992 J Pept Sci. 2008 Sep;14(9):1032-8. Onishi J, Roy MK, Juneja LR, Watanabe Y, Tamai Y. A lactoferrin-derived peptide with cationic residues concentrated in a region of its helical structure induces necrotic cell death in a leukemic cell line (HL-60) DRAMP31671 RKAFRWAWRMLKKAAPSITCVR 22 mPep1 Not available Not found Bovine lactoferrin (Lf-B) Antimicrobial, Anticancer Not found Not found Not found Not available mPep1 causes necrotic cell death by destroying cellular membrane structure Tumor cells: HL-60 (IC50=8 µM) Not available Linear Free Free L Not available Not available 18425992 J Pept Sci. 2008 Sep;14(9):1032-8. Onishi J, Roy MK, Juneja LR, Watanabe Y, Tamai Y. A lactoferrin-derived peptide with cationic residues concentrated in a region of its helical structure induces necrotic cell death in a leukemic cell line (HL-61) DRAMP31672 KAQIRAMECNIL 12 a5 Not available Not found Cyclin B (285-296) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18656352 Bioorg Med Chem Lett. 2008 Aug 15;18(16):4633-7. Lou H, Gao Y, Zhai M, Qi Y, Chen L, Lv H, Yu J, Li Y. A novel peptide from alpha5 helix of Asterina pectinifera cyclin B conjugated to HIV-Tat(49-57) with cytotoxic and apoptotic effects against human cancer cells DRAMP31673 KAQIRAMECNILGRKKRRQRRR 22 Tat-a5 Not available Not found HIV-Tat (49-57) Antimicrobial, Anticancer Not found Not found Not found Not available Tat-a5 could arrest cancer cells at G2/M phase and make them apoptotic; Tat-a5 would have the potential to inhibit tumor angiogenesis Tumor cells: HCT 116 (~80% Cytotoxicity at 100 µM) Not available Linear Free Free L Not available HIV-Tat 18656352 Bioorg Med Chem Lett. 2008 Aug 15;18(16):4633-7. Lou H, Gao Y, Zhai M, Qi Y, Chen L, Lv H, Yu J, Li Y. A novel peptide from alpha5 helix of Asterina pectinifera cyclin B conjugated to HIV-Tat(49-59) with cytotoxic and apoptotic effects against human cancer cells DRAMP31674 KKKFPWWWPFKKK 13 PST13-RK Not available Not found Derivative of tritrpticin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-361 (IC50=80 µg/ml); A549 (IC50=90 µg/ml) Not available Linear Free Amidation L NIH-3T3 (mouse): IC50=83 µg/ml Not available 18815734 Biotechnol Lett. 2009 Feb;31(2):233-7. Yang ST, Kim JI, Shin SY. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity DRAMP31675 KKKFPWWWPFKKKCKKKFPWWWPFKKKC 28 di-PST13-RK-C Not available Not found Derivative of tritrpticin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-361 (IC50=10 µg/ml); A549 (IC50=15 µg/ml); A549 (IC50=17 µg/ml); MDA-MB-361 (IC50=17 µg/ml) Not available Linear Free Amidation L NIH-3T3 (mouse): IC50=20 µg/ml Not available 18815734 Biotechnol Lett. 2009 Feb;31(2):233-7. Yang ST, Kim JI, Shin SY. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity DRAMP31676 ETFSDLWKLL 10 PNC-28 Not available Not found Antennapedia Antimicrobial, Anticancer Not found Not found Not found Not available PNC-28 may be effective in treating human pancreatic cancer. The penetratin sequence appears to be responsible for the fundamental change in the mechanism of action, inducing rapid necrosis initiated by membrane pore formation. Tumor cells: Mia PaCa-2 (100% Cytotoxicity=75μM) Not available Linear Free Free L Not available Not available 18931881 Ann Surg Oncol. 2008 Dec;15(12):3588-600. Bowne WB, Sookraj KA, Vishnevetsky M, Adler V, Sarafraz-Yazdi E, Lou S, Koenke J, Shteyler V, Ikram K, Harding M, Bluth MH, Ng M, Brandt-Rauf PW, Hannan R, Bradu S, Zenilman ME, Michl J, Pincus MR. The penetratin sequence in the anticancer PNC-28 peptide causes tumor cell necrosis rather than apoptosis of human pancreatic cancer cells DRAMP31677 YKQCHKKGGKKGSG 14 Crotamine (1–9,38–42) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100 µM) Human erythrocytes: 50% Hemolysis>300µM Linear Free Amidation L PBMC: IC50>300µM Not available 18983137 J Med Chem. 2008 Nov 27;51(22):7041-4. Rádis-Baptista G, de la Torre BG, Andreu D. A novel cell-penetrating peptide sequence derived by structural minimization of a snake toxin exhibits preferential nucleolar localization DRAMP31678 FVDLKKIANIINSIF 15 Temporin-CEa Not available Not found skin of the Chinese brown frog, Rana chensinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=12 µM); MCF-7 (IC50=27.84 μM); MCF-7 (IC50=31.78 μM); MCF-7 (IC50=31.91 μM); MCF-7 (IC50=34.5 μM); HeLa (IC50=36.31 μM); BEL-7402 (IC50=36.9 μM); BEL-7402 (IC50=37.1 μM); BCaP-37 (IC50=37.33 μM); BCaP-37 (IC50=38.39 μM); BCaP-37 (IC50=38.5 μM); HeLa (IC50=38.96 μM); BEL-7402 (IC50=38.98 μM); BCaP-37 (IC50=39.42 μM); BEL-7402 (IC50=40.16 μM); HeLa (IC50=40.6 μM); HeLa (IC50=43.87 μM); SMMC-7721 (IC50=44.92 μM); SMMC-7721 (IC50=46.73 μM); SMMC-7721 (IC50=47.73 μM); SMMC-7721 (IC50=50.32 μM); A549 (IC50=52.09 μM); A549 (IC50=52.82 μM); A549 (IC50=53.12 μM); A549 (IC50=53.31 μM); MDA-MB-231 (IC50=54.95 μM); BGC-823 (IC50=55.16 μM); BGC-823 (IC50=56.47 μM); MDA-MB-231 (IC50=57.94 μM); LK-2 (IC50=58.32 μM); NCI-H446 (IC50=59.45 μM); MDA-MB-231 (IC50=60.38 μM); LK-2 (IC50=61.57 μM); BGC-823 (IC50=61.63 μM); LK-2 (IC50=61.73 μM); HO-8910 (IC50=62.84 μM); BGC-823 (IC50=63.2 μM); MDA-MB-231 (IC50=63.26 μM); LK-2 (IC50=63.4 μM); HO-8910 (IC50=64.75 μM); NCI-H446 (IC50=64.81 μM); NCI-H446 (IC50=65.29 μM); HO-8910 (IC50=66.55 μM); HO-8910 (IC50=66.68 μM); NCI-H446 (IC50=67.66 μM); HT-29 (IC50=88.91 μM); HT-29 (IC50>100 μM); HT-29 (IC50>100 μM); HT-29 (IC50>100 μM) Human erythrocytes: LD50=230 μM Linear Free Amidation L Not available Not available 19341344 Zoolog Sci. 2009 Mar;26(3):220-6. Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis DRAMP31679 ILPILSLIGGLL 12 Temporin-CEb Not available Not found skin of the Chinese brown frog, Rana chensinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=56 µM) Human erythrocytes: LD50=112 μM Linear Free Amidation L Not available Not available 19341344 Zoolog Sci. 2009 Mar;26(3):220-6. Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis DRAMP31680 FKCRRWQWRMKK 12 LfcinB P24627 Not found Bovine lactoferrin (Lf-B) Antimicrobial, Anticancer Not found Not found Not found Not available Peptides induce lysis of cancer cells through interactions with the plasma membrane Tumor cells: Ramos (IC50=10 µM); Raji (IC50=13 µM); Kelly (IC50=141 ± 3 µM); HT-29 (IC50=148±8 µM); SU-DHL-4 (IC50=16 µM); KMS-5 (IC50=38 µM); FEMX-I (IC50=40±7 µM); U266B1 (IC50=55 µM); KMM-1 (IC50=57 µM); MT-1 (IC50>160 µM) Not available Linear Free Free L Not available Not available 19527490 BMC Cancer. 2009 Jun 15;9:183. Fadnes B, Rekdal O, Uhlin-Hansen L. The anticancer activity of lytic peptides is inhibited by heparan sulfate on the surface of the tumor cells DRAMP31681 KAAKKAAKAAKKAAKAAKKAA 21 KW5 Not available Not found Bovine lactoferrin (Lf-B) Antimicrobial, Anticancer Not found Not found Not found Not available Peptides induce lysis of cancer cells through interactions with the plasma membrane Tumor cells: FEMX-I (IC50=30±3 µM); HT-29 (IC50=55±14 µM) Not available Linear Free Free L Not available Not available 19527490 BMC Cancer. 2009 Jun 15;9:183. Fadnes B, Rekdal O, Uhlin-Hansen L. The anticancer activity of lytic peptides is inhibited by heparan sulfate on the surface of the tumor cells DRAMP31682 IDWKKLLDAAKQIX 14 Polybia-MPI [L14L-S] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=20.3±1.0µM); HepG2 (IC50=21.2±0.8µM); EJ (IC50=21.6±1.2µM) Not available Linear Free Amidation X=Leu-S L NIH 3T3: 50% Cell death>60 µM Not available 20600424 Peptides. 2010 Oct;31(10):1832-8. Zhang W, Li J, Liu LW, Wang KR, Song JJ, Yan JX, Li ZY, Zhang BZ, Wang R A novel analog of antimicrobial peptide Polybia-MPI, with thioamide bond substitution, exhibits increased therapeutic efficacy against cancer and diminished toxicity in mice. DRAMP31683 GFFGKRKEYFKKFGASFKRRFANLKKRL 28 Ltc-5 [M6R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50>36 µM) Human erythrocytes: 50% Hemolysis>36 µM Linear Free Amidation L Not available Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31684 GKLIKKFGRKAISYAVKKARGKH 23 Ltc-2a (4-26) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50>36 µM) Human erythrocytes: 50% Hemolysis>36 µM Linear Free Free L Not available Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31685 GKMKEYFKKFGASFKRRFANLKKRL 25 Ltc-5 (4-28) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50>36 µM) Human erythrocytes: 50% Hemolysis>36 µM Linear Free Amidation L Not available Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31686 GLFGKLIKKFLRKAISYAVKKARGKH 26 Ltc-2a [G11L] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50=0.7 µM) Human erythrocytes: 50% Hemolysis=3 µM Linear Free Free L Human leukocytes: 50% Cell death=3 µM Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31687 GLFGKLIKKKGRKAISYAVKKARGKH 26 Ltc-2a [F10K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50=18 µM) Human erythrocytes: 50% Hemolysis>36 µM Linear Free Free L Human leukocytes: 50% Cell death>36 µM Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31688 GLFGKLQKKFGRKAISYAVKKARGKH 26 Ltc-2a [I7Q] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (EC50=18 µM) Human erythrocytes: 50% Hemolysis>36 µM Linear Free Free L Human leukocytes: 50% Cell death>36 µM Not available 19563807 FEBS Lett. 2009 Jul 21;583(14):2425-8. Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins DRAMP31689 DDESSKPCCDQCACTKSNPPQCRCSDMRLNSCHSACKSCICALSYPAQCFCVDITDFCYEPCKPSEDDKEN 71 BBI(Bowman-Birk type proteinase inhibitor) Not available Not found Glycine max Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=48.3±3.5µM) Not available Cyclic Free Free L Not available Not available 19885848 Mol Nutr Food Res. 2010 Mar;54(3):396-405. Clemente A, Moreno FJ, Marín-Manzano Mdel C, Jiménez E, Domoney C. The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases DRAMP31690 ACDCRGDCFCGGGGIVRRADRAAVP 25 AP Not available Not found Endostatin derived Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (40% inhibition at 5µg/ml); B16-F10 (50% inhibition at 2.5µg/ml); B16-F10 (75% inhibition at 10µg/ml) Not available Linear Free Free L Not available integrin αvβ3 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7. Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C Position is More Important Than Disulfide Bonds on Antiangiogenic Activity of RGD-4C Modified Endostatin Derived Synthetic Polypeptide DRAMP31691 ACDCRGDCFCGGGGIVRRADRAAVP 25 AP Not available Not found Endostatin derived Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (40% inhibition at 2.5µg/ml); B16-F10 (42% inhibition at 5µg/ml); B16-F10 (52% inhibition at 10µg/ml) Not available Linear Free Free L Not available integrin αvβ3 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7. Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C Position is More Important Than Disulfide Bonds on Antiangiogenic Activity of RGD-4C Modified Endostatin Derived Synthetic Polypeptide DRAMP31692 ACDCRGDCFCGGGGIVRRADRAAVP 25 AP(O) Not available Not found Endostatin derived Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (40% inhibition at 5µg/ml); B16-F10 (50% inhibition at 2.5µg/ml); B16-F10 (75% inhibition at 10µg/ml) Not available Cyclic Free Free L Not available integrin αvβ3 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7. Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C Position is More Important Than Disulfide Bonds on Antiangiogenic Activity of RGD-4C Modified Endostatin Derived Synthetic Polypeptide DRAMP31693 ACDCRGDCFCGGGGIVRRADRAAVP 25 AP(O) Not available Not found Endostatin derived Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (40% inhibition at 2.5µg/ml); B16-F10 (42% inhibition at 5µg/ml); B16-F10 (52% inhibition at 10µg/ml) Not available Cyclic Free Free L Not available integrin αvβ3 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7. Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C Position is More Important Than Disulfide Bonds on Antiangiogenic Activity of RGD-4C Modified Endostatin Derived Synthetic Polypeptide DRAMP31694 IVRRADRAAVPGGGGACDCRGDCFC 25 IC Not available Not found Endostatin derived Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (60% inhibition at 11µg/ml) Not available Linear Free Free L Not available integrin αvβ4 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7. Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C Position is More Important Than Disulfide Bonds on Antiangiogenic Activity of RGD-4C Modified Endostatin Derived Synthetic Polypeptide DRAMP31695 LPFFPPVXPIIG 12 Callyaerin E Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=0.39µM); HeLa (ED50=3.4µM); PC-12 (ED50=3.8µM) Not available Cyclic Free Amidation X=Daa L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56. brahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa DRAMP31696 VPVFPXPLF 9 Callyaerin F Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (ED50>9µM); L5178Y (ED50>9µM); PC-12 (ED50>9µM) Not available Cyclic Free Amidation X=Daa L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56. brahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa DRAMP31697 IIFPXPLXPINAI 13 Callyaerin D Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=3.03µM) Not available Cyclic Free Amidation X(5)= 4-Hydroxyproline; X(8)=Daa L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56. brahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa DRAMP31698 VPVFPPLXPI 10 Callyaerin H Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=0.48µM) Not available Cyclic Free Amidation X=Daa L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56. brahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa DRAMP31699 LPPPPLXPFFF 11 Callyaerin G Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=0.41µM); HeLa (ED50=4.43µM); PC-12 (ED50>8µM) Not available Cyclic Free Amidation X=Daa L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56. brahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa DRAMP31700 CSSRTMHHC 9 Peptide-20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (30% viablity=100 µM); SK-MEL-28 (35-40% viablity=100 µM); B16-F10 (50% viablity=100 µM); HeLa (50% viablity=100 µM); MDA-MB-231 (55% viablity=100 µM); SK-MEL-25 (55-60% viablity=100 µM); HL-60 (90% viablity=100 µM) Not available Cyclic Free Free L Not available cadherin constituent at the tumor cell surface 20802991 J Mol Med (Berl). 2010 Dec;88(12):1255-64. Matsuo AL, Tanaka AS, Juliano MA, Rodrigues EG, Travassos LR. A novel melanoma-targeting peptide screened by phage display exhibits antitumor activity DRAMP31701 KWKSFAKTFKSAKKTVAHTALKAISS 26 L6A/L17A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Tumor cells: A-375 (IC50>83.6 μmol/L); A549 (IC50>83.6 μmol/L); B16 (IC50>83.6 μmol/L); HeLa (IC50>83.6 μmol/L); MCF-7 (IC50>83.6 μmol/L); NCI-H1299 (IC50>83.6 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Human red blood cells: MHC>334.3 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31702 KWKSFLKTFKSAKKTVAHTAAKAISS 26 L17A/L21A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Tumor cells: NCI-H1299 (IC50=37.7 μmol/L); A-375 (IC50>83.6 μmol/L); A549 (IC50>83.6 μmol/L); B16 (IC50>83.6 μmol/L); HeLa (IC50>83.6 μmol/L); MCF-7 (IC50>83.6 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Human red blood cells: MHC>334.4 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31703 KWKSFLKTFKSAKKTVAHTALKAISS 26 L17A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Tumor cells: NCI-H1299 (IC50=16.4 μmol/L); A-375 (IC50>83.6 μmol/L); A549 (IC50>83.6 μmol/L); B16 (IC50>83.6 μmol/L); HeLa (IC50>83.6 μmol/L); MCF-7 (IC50>83.6 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Human red blood cells: MHC>334.4 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31704 KWKSFLKTFKSAKKTVLHTAAKAISS 26 L21A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Tumor cells: NCI-H1299 (IC50=15.6 μmol/L); A-375 (IC50=59.8 μmol/L); B16 (IC50=63.5 μmol/L); HeLa (IC50=64.7 μmol/L); MCF-7 (IC50=70.8 μmol/L); A549 (IC50=71 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Human red blood cells: MHC>334.4 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31705 KWKSFLKTFKSAKKTVLHTAAKAISS 26 L21A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Human red blood cells: MHC>334.4 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31706 KWKSFAKTFKSAKKTVLHTALKAISS 26 L6A Not available Not found PeptideV13K Antimicrobial, Anticancer Not found Not found Not found Not available Peptides killed cancer cells with a fast necrotic mechanism causing cell membrane lysis Tumor cells: NCI-H1299 (IC50=14 μmol/L); A549 (IC50=53 μmol/L); HeLa (IC50=58.6 μmol/L); A-375 (IC50=58.7 μmol/L); MCF-7 (IC50=62.3 μmol/L); B16 (IC50=62.5 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Human red blood cells: MHC>334.4 μmol/L Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP31707 YHWYGYTPQNVIGGGKLlLKlLKKLLKlLKKK 32 EGFR-lytic Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=0.12 µM); MDA-MB-231 (IC50=0.46 µM) Not available Linear Free Free Mix Not available Not available 21351323 J Pept Sci. 2011 Jul;17(7):493-8. Ohara K, Horibe T, Kohno M, Kawakami K. Characterization of antilytic peptide antibody: application for the detection of lytic-based hybrid peptide in serum samples DRAMP31708 VDKPPYLPRPRPPRXXYNX 19 Oncocin [R15,19Orn][I16Tle] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 2000µg/ml); HepG2 (Not active up to 2000µg/ml) Human erythrocytes: Not active up to 600 µg/ml Linear Free Amidation X(15)=Orn; X(16)=L-tert-leucine; X(19)=Orn L Not available Not available 21387510 Chembiochem. 2011 Apr 11;12(6):874-6. Knappe D, Zahn M, Sauer U, Schiffer G, Sträter N, Hoffmann R. Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex DRAMP31709 VDKPPYLPRPRPXRXIYNX 19 Oncocin [P13Hyp][R15Hyp][R19Orn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 2000µg/ml); HepG2 (Not active up to 2000µg/ml) Human erythrocytes: Not active up to 600 µg/ml Linear Free Amidation X(13)= 4-Hydroxyproline; X(15)= 4-Hydroxyproline; X(19)=Orn L Not available Not available 21387510 Chembiochem. 2011 Apr 11;12(6):874-6. Knappe D, Zahn M, Sauer U, Schiffer G, Sträter N, Hoffmann R. Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex DRAMP31710 VDKPPYLPRPRPXRXXYNX 19 Oncocin [P13Hyp,R15Hyp,I16Tle,R19Orn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 2000µg/ml); HepG2 (Not active up to 2000µg/ml) Human erythrocytes: Not active up to 600 µg/ml Linear Free Amidation X(13)= 4-Hydroxyproline; X(15)= 4-Hydroxyproline; X(16)=L-tert-leucine; X(19)=Orn L Not available Not available 21387510 Chembiochem. 2011 Apr 11;12(6):874-6. Knappe D, Zahn M, Sauer U, Schiffer G, Sträter N, Hoffmann R. Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex DRAMP31711 LTFEHYWAQLTS 12 DI Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=0.29 µM); -- (IC50 for MDMX-p53=1.6 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31712 LTFEHYWAQLTS 12 DI Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31713 LTAEHYAAQATS 12 3A Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2>100 µM); -- (IC50 for MDMX-p53>100 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31714 QETFSDLWKLLP 12 P5317-28 Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=4.7 µM); -- (IC50 for MDMX-p53=30 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31715 PRAWEYWLRLME 12 MIP(F3A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=0.57 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31716 PRFWEAWLRLME 12 MIP(Y6A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2>100 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31717 PRFWEYALRLME 12 MIP(W7A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2>100 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31718 PRFWEYWLALME 12 MIP(R9A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=0.02 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31719 PRFWEYWLRAME 12 MIP(L10A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=1.14 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31720 PRFWEYWLRLAE 12 MIP(M11A) Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=0.4 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31721 PRFWEYWLRLME 12 MIP Not available Not found E3 ubiquitin-protein ligase Antimicrobial, Anticancer Not found Not found Not found Not available Inhibits MDM2-p53 Interaction Tumor cells: -- (IC50 for MDM2=0.01 µM); -- (IC50 for MDMX-p53=0.12 µM) Not available Linear Free Free L Not available MDM2 21423613 PLoS One. 2011 Mar 15;6(3):e17898. Shiheido H, Takashima H, Doi N, Yanagawa H. mRNA display selection of an optimized MDM2-binding peptide that potently inhibits MDM2-p53 interaction DRAMP31722 WKKWXKKWK 9 LTX-302 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60/ADR (IC50=10.5 ± 3.1 µM); MCF-7/mdr (IC50=11.0 ± 4.4 µM); A20 (IC50=16.0 ± 3.0 µM); IGROV-1 (IC50=19.6 ± 8.7 µM); AT84 (IC50=21.0 ± 1.7 µM); Kelly (IC50=28 ± 0 µM); IGROV-1/CDDP (IC50=6.4 ± 2.6 µM); MT-1 (IC50=73 ± 2 µM); HT-29 (IC50=75 ± 5 µM); HL-60 (IC50=8.0 ± 1.1 µM); K562 (IC50=8.2 ± 1.3 µM); MCF-7 (IC50=8.9 ± 2.8 µM); K562/Gleevec (IC50=9.0 ± 2.1 µM) Human red blood cells (RBC): IC50>695 μM Linear Free Amidation X=Dip (Diphenylalanine) L HUVEC: IC50=123 ± 9 μM; MRC-5: IC50=122 ± 16 µM Not available 21453492 BMC Cancer. 2011 Mar 31;11:116. Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø. Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells DRAMP31723 XXWXXXWWX 9 LTX-318 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=21.7 ± 2.5 µM); MT-1 (IC50=216 ± 36 µM); AT84 (IC50=23.0 ± 3.6 µM); HT-29 (IC50=248 ± 5 µM); Kelly (IC50=78 ± 7 µM) Human red blood cells (RBC): IC50>695 μM Linear Free Amidation X(1/2/5/6/9)=ornithine; X(4)=Dip (Diphenylalanine) L HUVEC: IC50> 347 μM; MRC-5: IC50=323 ± 33 µM Not available 21453492 BMC Cancer. 2011 Mar 31;11:116. Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø. Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells DRAMP31724 XXWXXXWWX 9 LTX-318 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=14.3 ± 1.2 µM); A20 (IC50=8.3 ± 0.6 µM) Human red blood cells (RBC): IC50>695 μM Linear Free Amidation X(1/2/5/6/9)=ornithine; X(4)=Dip (Diphenylalanine) L HUVEC: IC50> 347 μM; MRC-5: IC50=323 ± 33 µM Not available 21453492 BMC Cancer. 2011 Mar 31;11:116. Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø. Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells DRAMP31725 XXWXXXWWX 9 LTX-318 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=154 ± 29 µM); A20 (IC50=67.7 ± 13.2 µM) Human red blood cells (RBC): IC50>695 μM Linear Free Amidation X(1/2/5/6/9)=ornithine; X(4)=Dip (Diphenylalanine) L HUVEC: IC50> 347 μM; MRC-5: IC50=323 ± 33 µM Not available 21453492 BMC Cancer. 2011 Mar 31;11:116. Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø. Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells DRAMP31726 GIPCGESCVFIPCLTSAIGCSCKSKVCYRN 30 Mram 8 Not available Not found Viola philippica Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (IC50=1.75±0.05µM); HeLa (IC50=15.5±0.06µM); MM96L (IC50=4.91±0.04µM) Not available Cyclic Free Free L HFF-1: IC50=3.19±0.01µM Not available 21723349 Peptides. 2011 Aug;32(8):1719-23. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica DRAMP31727 GSIPCGESCVFIPCISAIIGCSCSNKVCYKN 31 Viphi G Not available Not found Viola philippica Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (IC50=1.03±0.03µM); BGC-823 (IC50=2.91±0.06µM); HeLa (IC50=6.35±0.31µM) Not available Cyclic Free Free L HFF-1: IC50=1.76±0.12µM Not available 21723349 Peptides. 2011 Aug;32(8):1719-23. He W, Chan LY, Zeng G, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola philippica DRAMP31730 AWXLFDDGV 9 Cr-AcACP1 B3EWE7 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Proapoptosis Tumor cells: HEp-2 (IC50=0.8 mM); HCT 15 (IC50=1.0 mM) Human erythrocytes: 5% Hemolysis=1 mM Linear Acetylation Free X=Lys-Acetylation (Lysine with acetylation side group) L NIH 3T3: IC50=4 mM DNA 21882228 J Cell Biochem. 2012 Jan;113(1):184-93. Mandal SM, Migliolo L, Das S, Mandal M, Franco OL, Hazra TK. Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties DRAMP31731 GVGSPYVSRLLGICL 15 p776 P04626##O18735##P06494##P70424 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Disrupting tumor-mediated mechanisms suppressing host immunity Not available Not available Linear Free Free L Not available Not available 21928125 Cancer Immunol Immunother. 2012 Mar;61(3):397-407. Gritzapis AD, Voutsas IF, Baxevanis CN. Ontak reduces the immunosuppressive tumor environment and enhances successful therapeutic vaccination in HER-2/neu-tolerant mice DRAMP31732 LIAHNQVRQV 10 p85 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Disrupting tumor-mediated mechanisms suppressing host immunity Not available Not available Linear Free Free L Not available Not available 21928125 Cancer Immunol Immunother. 2012 Mar;61(3):397-407. Gritzapis AD, Voutsas IF, Baxevanis CN. Ontak reduces the immunosuppressive tumor environment and enhances successful therapeutic vaccination in HER-2/neu-tolerant mice DRAMP31733 GIIKKIIIKKI 11 Cationic Amphiphilic Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=160 µM); HL-60 (IC50>500 µM) Human red blood cells: over the active concentration ranges against bacteria and cancer cells, there is little activity or toxicity against hRBCs Linear Free Amidation L NIH 3T3: low toxic Not available 21955251 Biomacromolecules. 2011 Nov 14;12(11):3839-43. Hu J, Chen C, Zhang S, Zhao X, Xu H, Zhao X, Lu JR. Designed antimicrobial and antitumor peptides with high selectivity DRAMP31734 GIIKKIIIKKIIIKKI 16 Cationic Amphiphilic Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15 µM); HL-60 (IC50=25 µM) Human red blood cells: over the active concentration ranges against bacteria and cancer cells, there is little activity or toxicity against hRBCs Linear Free Amidation L NIH 3T3: low toxic Not available 21955251 Biomacromolecules. 2011 Nov 14;12(11):3839-43. Hu J, Chen C, Zhang S, Zhao X, Xu H, Zhao X, Lu JR. Designed antimicrobial and antitumor peptides with high selectivity DRAMP31735 GIIKKIIIKKIIIKKIIIKKI 21 Cationic Amphiphilic Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50=10 µM); HeLa (IC50=4 µM) Human red blood cells: over the active concentration ranges against bacteria and cancer cells, there is little activity or toxicity against hRBCs Linear Free Amidation L NIH 3T3: low toxic Not available 21955251 Biomacromolecules. 2011 Nov 14;12(11):3839-43. Hu J, Chen C, Zhang S, Zhao X, Xu H, Zhao X, Lu JR. Designed antimicrobial and antitumor peptides with high selectivity DRAMP31736 AAKKWAKAKWAKAKKWAKAA 20 Z10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (EC50>211 µM); Meth A (EC50>211 µM); MT-1 (EC50>211 µM) Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31737 AAWKWAWAKKWAKAKKWAKAA 21 Z9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (EC50=13 µM); MT-1 (EC50=16 µM); Meth A (EC50=9 µM) MRC-5: EC58=14 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31738 AWKKWAKAWKWAKAKWWAKAA 21 Z8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=14 µM); Meth A (EC50=19 µM); HT-29 (EC50=23 µM) MRC-5: EC57=17 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31739 KAAKKAWKAAKKAAKWWKKAA 21 Z4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (EC50=155 µM); HT-29 (EC50=173 µM); MT-1 (EC50=68 µM) MRC-5: EC53=78 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31740 KAAKKAWKAAKKAWKAAKKAA 21 Z7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Meth A (EC50=15 µM); MT-1 (EC50=15 µM); HT-29 (EC50=21 µM) MRC-5: EC56=20 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31741 KAAKKAWKAWKKAAKAAWKKAA 22 Z3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=128 µM); HT-29 (EC50>211 µM); Meth A (EC50>211 µM) Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31742 KAAKKAWKWAKKAAKWAKKAA 21 Z5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=28 µM); Meth A (EC50=42 µM); HT-29 (EC50=67 µM) MRC-5: EC54=27 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31743 KAAKKWAKAAKKAAKAWKKAA 21 Z1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=186 µM); HT-29 (EC50>211 µM); Meth A (EC50>211 µM) Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31744 KAAKKWAKAWKKAAKAWKKAA 21 Z2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=173 µM); HT-29 (EC50>211 µM); Meth A (EC50>211 µM) Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31745 KWWKKAAKAAKKAAKAAKKWA 21 Z6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MT-1 (EC50=16 µM); Meth A (EC50=17 µM); HT-29 (EC50=31 µM) MRC-5: EC55=23 μM Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244. Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ. Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP31746 IELLQARGGCX 11 Peptide-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50=2.17 µM); NCI-H358 (IC50=4.63 mM) Not available Linear Free Amidation X(11)=Pemetrexed L Not available Not available 22076954 J Pept Sci. 2011 Dec;17(12):805-11. Miklán Z, Orbán E, Bánóczi Z, Hudecz F. New pemetrexed-peptide conjugates: synthesis, characterization and in vitro cytostatic effect on non-small cell lung carcinoma (NCI-H358) and human leukemia (HL-60) cells DRAMP31747 IELLQARGGCXGGRRRRRRRR 21 Peptide-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H358 (IC50=2.19 µM); HL-60 (IC50=2.64 µM) Not available Linear Free Amidation X(11)=Pemetrexed L Not available Not available 22076954 J Pept Sci. 2011 Dec;17(12):805-11. Miklán Z, Orbán E, Bánóczi Z, Hudecz F. New pemetrexed-peptide conjugates: synthesis, characterization and in vitro cytostatic effect on non-small cell lung carcinoma (NCI-H358) and human leukemia (HL-60) cells DRAMP31748 RRRRRRRRGGCX 12 Peptide-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50=6.24 µM); NCI-H358 (IC50=8.41 µM) Not available Linear Free Amidation X(12)=Pemetrexed L Not available Not available 22076954 J Pept Sci. 2011 Dec;17(12):805-11. Miklán Z, Orbán E, Bánóczi Z, Hudecz F. New pemetrexed-peptide conjugates: synthesis, characterization and in vitro cytostatic effect on non-small cell lung carcinoma (NCI-H358) and human leukemia (HL-60) cells DRAMP31750 AFGMALKLLKKVL 13 MAC1/2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=16 µM); HeLa (IC50=16±3 µM); CCRF-CEM (IC50=17 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=30±4 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31751 GFGMAXKLLKKVL 13 MAC1/26 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=18 ± 1 µM); HeLa (IC50=8±2 µM); CCRF-CEM (IC50=9±2 µM) Human erythrocytes: IC50=93 μM Linear Free Amidation X(6)=AC6C=cyclohexyl-1-carboxylic acid L HUVEC: IC50=16 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31752 GFGMALKXLKKVL 13 MAC1/25 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=12±2 µM); SW480 (IC50=14 ± 1 µM); HeLa (IC50=7±1 µM) Human erythrocytes: IC50=88 μM Linear Free Amidation X(6)=AC6C=cyclohexyl-1-carboxylic acid L HUVEC: IC50=13±2 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31753 GFGMALKLXKKVL 13 MAC1/24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=11 µM); SW480 (IC50=16 ± 1 µM); HeLa (IC50=8±2 µM) Human erythrocytes: IC50=88 μM Linear Free Amidation X(6)=AC6C=cyclohexyl-1-carboxylic acid L HUVEC: IC50=15±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31754 gfgmalkllkkvl 13 MAC1/1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=11 µM); HeLa (IC50=12±4 µM); SW480 (IC50=19±2 µM) Human erythrocytes: IC50=152 μM Linear Free Amidation D HUVEC: IC50=21±5 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31755 GFGMALKLlKKVL 13 MAC1/16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=32±2 µM); CCRF-CEM (IC50=70 µM); SW480 (IC50> 100 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation l=D-Leu Mix HUVEC: IC50=87±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31756 GFGmALKLLKKVL 13 MAC1/19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=21±4 µM); CCRF-CEM (IC50=43±11 µM); SW480 (IC50=68±2 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation m=D-Met Mix HUVEC: IC50=52±15 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31757 GFGMaLKLLKKVL 13 MAC1/4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15±5 µM); CCRF-CEM (IC50=29 µM); SW480 (IC50=49±9 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation a=D-Ala Mix HUVEC: IC50=56±2 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31758 GfGMALKLLKKVL 13 MAC1/6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=15 µM); SW480 (IC50=29±3 µM); HeLa (IC50=8±2 µM) Human erythrocytes: IC50=177 μM Linear Free Amidation f=D-Phe Mix HUVEC: IC50=21±5 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31759 GFGMALXLLXXVL 13 MAC1/20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10±1 µM); CCRF-CEM (IC50=25±3 µM); SW480 (IC50=35±4 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation X=Ornithine L HUVEC: IC50=33±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31760 GFGMALRLLRRVL 13 MAC1/21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=17±2 µM); CCRF-CEM (IC50=22±4 µM); HeLa (IC50=9±3 µM) Human erythrocytes: IC50=72 μM Linear Free Amidation L HUVEC: IC50=17±2 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31761 GFkMALKLLKKVL 13 MAC1/10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15±6 µM); CCRF-CEM (IC50=16 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation k=D-Lys Mix HUVEC: IC50=23 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31762 GFKMALKLLKKVL 13 MAC1/9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=13±3 µM); CCRF-CEM (IC50=14±4 µM); HeLa (IC50=8±1 µM) Human erythrocytes: IC50=199 μM Linear Free Amidation L HUVEC: IC50=17±2 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31763 GKFMSLLKHILK 12 HAL-2/24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=34 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=74±10 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31764 GKWKKILGHLIR 12 HAL-1/19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50> 100 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31765 GKWKKILGKLIR 12 HAL-1/21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=30±3 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31766 GKWKSLLKHILK 12 HAL-2/1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=14±2 µM); SW480 (IC50> 100 µM); CCRF-CEM (IC50>40 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31767 GKWLSLLKHILK 12 HAL-2/11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=14±3 µM); SW480 (IC50=40 µM) Rat erythrocytes: IC50=65 μM Linear Free Amidation L HUVEC: IC50=42±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31768 GKWMKLLKHILK 12 HAL-2/2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=35±5 µM); HeLa (IC50=6±1 µM); CCRF-CEM (IC50>40 µM) Rat erythrocytes: IC50=87.4 μM Linear Free Amidation L HUVEC: IC50=40±4 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31769 GMWSKLLGHLLR 12 HAL-1/15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=14±2 µM); SW480 (IC50> 40 µM); CCRF-CEM (IC50>40 µM) Rat erythrocytes: IC50=62 μM Linear Free Amidation L HUVEC: IC50=26±6 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31770 GTGLPMSERRKIMLMMR 17 MAC2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=32 µM); HeLa (IC50> 100 µM); SW480 (IC50> 100 µM) Human erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31771 KMWSKILGHLIR 12 HAL-1/17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=35±3 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31772 KNWKKXLKKXIKXVK 15 LL-III/22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=11±7 µM); CCRF-CEM (IC50=25±4 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation X=Aib=1-amino-isobutyric acid L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31773 KNWKKILGKIIKVVK 15 LL-III/10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=9 µM); HeLa (IC50=9±4 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=35±11 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31774 KNWKKILKKIIKVVK 15 LL-III/18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3 µM); CCRF-CEM (IC50=7±2 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=22±8 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31775 LFGMALKLLKKVL 13 MAC1/3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=11±1 µM); CCRF-CEM (IC50=22 µM); HeLa (IC50=9±2 µM) Human erythrocytes: IC50=53 μM Linear Free Amidation L HUVEC: IC50=27±5 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31776 NKWKKILGKIIKVVK 15 LL-III/34 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=37 µM); HeLa (IC50=5±2 µM); CCRF-CEM (IC50=5±3 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=52±7 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31777 VNFKKLLGKLLKVVK 15 LL-III/15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=42 µM); HeLa (IC50=7±1 µM); CCRF-CEM (IC50=9±3 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=≥70 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31778 VNXKKLLGKLLKVVK 15 LL-III/16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=6±1 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation X=Nal=3-(1-naphthyl)alanine L HUVEC: IC50=15±1 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31779 VNWKKXLGKXIKXVK 15 LL-III/19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=28 µM); HeLa (IC50=3±1 µM); CCRF-CEM (IC50=8±2 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation X=Aib=1-amino-isobutyric acid L HUVEC: IC50=38±6 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31780 VNWKKIILGKIIKVVK 16 LL-III/11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=4±1 µM); SW480 (IC50=48 µM); HeLa (IC50=8±1 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=50± μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31781 vnwkkilgkiikvvk 15 LL-III/12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=20 µM); CCRF-CEM (IC50=5±2 µM); HeLa (IC50=6±2 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation D HUVEC: IC50=17±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31782 VNWKKVLAKIIKVVK 15 LL-III/37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=13 µM); CCRF-CEM (IC50=4±1 µM); SW480 (IC50=5±1 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=18±2 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31783 VNWKKILGKIKKVVK 15 LL-III/4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=18 µM); HeLa (IC50=7±1 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 80 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31784 VNWKKLLGKLLKVVK 15 LL-III/23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=15 µM); HeLa (IC50=4 µM); CCRF-CEM (IC50=6 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=12±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31785 vnwkkllgkllkvvk 15 LL-III/25 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=20 µM); CCRF-CEM (IC50=4 µM); HeLa (IC50=4±2 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation D HUVEC: IC50=12±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31786 VNWKKVLGKVVKVVK 15 LL-III/27 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=13±2 µM); CCRF-CEM (IC50=18 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31787 VNWXXILGXIIXVVX 15 LL-III/24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=20 µM); HeLa (IC50=3±1 µM); CCRF-CEM (IC50=5±2 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation X=Ornithine L HUVEC: IC50=20±4 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31788 VNWRRILGRIIRVVR 15 LL-III/17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=9 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=11±4 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31789 VYWKKILGKIIKVVK 15 LL-III/26 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=30 µM); HeLa (IC50=5±1 µM); CCRF-CEM (IC50=6 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=18±1 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP31790 KVKVKVKVpPTKVKVKVK 18 SVS-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=4.9±0.6µM); MDA-MB-436 (IC50=5.6±0.5µM); KB (IC50=6.3±0.7µM); MCF-7 (IC50=8.1±0.8µM) Human erythrocytes: 50% Hemolysis=80.8±12.8µM Linear Free Free p=D-Pro Mix Not available Not available 22413859 J Am Chem Soc. 2012 Apr 11;134(14):6210-7. Sinthuvanich C, Veiga AS, Gupta K, Gaspar D, Blumenthal R, Schneider JP. Anticancer ?-hairpin peptides: membrane-induced folding triggers activity DRAMP31791 kvkvkvkvPptkvkvkvk 18 SVS-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-436 (IC50=3.2±0.4µM); A549 (IC50=3.2±0.6µM); KB (IC50=4.5±0.5µM); MCF-7 (IC50=4.7±0.4µM) Not available Linear Free Free k=D-Lys; v=D-Val; p=D-Pro; t=D-Thr Mix Not available Not available 22413859 J Am Chem Soc. 2012 Apr 11;134(14):6210-7. Sinthuvanich C, Veiga AS, Gupta K, Gaspar D, Blumenthal R, Schneider JP. Anticancer ?-hairpin peptides: membrane-induced folding triggers activity DRAMP31792 KVKVKVKVPPTKVKVKVK 18 SVS-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>100µM); KB (IC50>100µM); MCF-7 (IC50>100µM); MDA-MB-436 (IC50>100µM) Not available Linear Free Free L Not available Not available 22413859 J Am Chem Soc. 2012 Apr 11;134(14):6210-7. Sinthuvanich C, Veiga AS, Gupta K, Gaspar D, Blumenthal R, Schneider JP. Anticancer ?-hairpin peptides: membrane-induced folding triggers activity DRAMP31793 GIPCAESCVWIPCTITALMGCSCKNNVCYNN 31 Chassatide C2 I0B6F2 Not found Chassalia chartacea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=2.4 μM) Human erythrocytes: HD50>25 μM Cyclic Free Free L Not available Not available 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GKT, Lim WH, Nguyen PQT, Tam JP. Novel cyclotides and uncyclotides with highly shortened precursors from Chassalia chartacea and effects of methionine oxidation on bioactivities DRAMP31794 GIPCAESCVWIPCTITALXGCSCKNNVCYNN 31 Chassatide C2A I0B6F2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>15 μM) Human erythrocytes: HD50>25 μM Cyclic Free Free X=MetO (Methionine sulfoxide) L Not available Not available 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GKT, Lim WH, Nguyen PQT, Tam JP. Novel cyclotides and uncyclotides with highly shortened precursors from Chassalia chartacea and effects of methionine oxidation on bioactivities DRAMP31795 IPCGESCVWIPCISGXFGCSCKDKVCYS 28 Chassatide C11A C0HKH6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>15 μM) Human erythrocytes: HD50>25 μM Cyclic Free Free X=MetO (Methionine sulfoxide) L Not available Not available 22467870 J Biol Chem. 2012 May 18;287(21):17598-17607. Nguyen GKT, Lim WH, Nguyen PQT, Tam JP. Novel cyclotides and uncyclotides with highly shortened precursors from Chassalia chartacea and effects of methionine oxidation on bioactivities DRAMP31796 PLLQATLGGGS 11 P7 Not available Not found No information found in the references Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (IC50=1 µM) Not available Linear Free Free L Not available Angiogenic factor FGF2 22481251 J Cancer Res Clin Oncol. 2012 Aug;138(8):1321-8. Yu Y, Gao S, Li Q, Wang C, Lai X, Chen X, Wang R, Di J, Li T, Wang W, Wu X. The FGF2-binding peptide P7 inhibits melanoma growth in vitro and in vivo DRAMP31797 LLRHVVKILEKYL 13 Temporin-La Not available Not found Temporins family Antimicrobial, Anticancer Not found Not found Not found Not available A membrane-disturbing action seems to be the major mechanism for cell death Tumor cells: MEC (24.15Inhibition ratio at 50 µg/ml); HL-7702(L-02) (37.22 Inhibition ratio at 50 µg/ml); A549 (45.62 Inhibition ratio at 50 µg/ml); BGC-823 (48.19 Inhibition ratio at 50 µg/ml); Hep-G2 (50.90 Inhibition ratio at 50 µg/ml); HeLa (52.32 Inhibition ratio at 50 µg/ml); SMMC-7721 (52.77 Inhibition ratio at 50 µg/ml); SW1116 (57.62 Inhibition ratio at 50 µg/ml) Showed no hemolytic activity against rabbit erythrocytes and human erythrocytes at 250 µg/ml Linear Free Free L Showed little effects on the proliferation of the 293T human embryonic kidney cell line, MECs, and human lymphomonocytes at concentrations of less than 50 µg/ml Not available 22641352 J Pept Sci. 2012 Jul;18(7):476-86. Diao Y, Han W, Zhao H, Zhu S, Liu X, Feng X, Gu J, Yao C, Liu S, Sun C, Pan F. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain DRAMP31798 LLRHVVKILSKYL 13 Temporin-Las Not available Not found Temporins family Antimicrobial, Anticancer Not found Not found Not found Not available A membrane-disturbing action seems to be the major mechanism for cell death Tumor cells: MEC (27.99 Inhibition ratio at 50 µg/ml); HL-7702(L-02) (37.00 Inhibition ratio at 50 µg/ml); A549 (50.64 Inhibition ratio at 50 µg/ml); BGC-823 (50.85 Inhibition ratio at 50 µg/ml); Hep-G2 (55.98 Inhibition ratio at 50 µg/ml); HeLa (56.81 Inhibition ratio at 50 µg/ml); SMMC-7721 (59.37 Inhibition ratio at 50 µg/ml); SW1116 (62.73 Inhibition ratio at 50 µg/ml) Showed no hemolytic activity against rabbit erythrocytes and human erythrocytes at 250 µg/ml Linear Free Free L Showed little effects on the proliferation of the 293T human embryonic kidney cell line, MECs, and human lymphomonocytes at concentrations of less than 50 µg/ml Not available 22641352 J Pept Sci. 2012 Jul;18(7):476-86. Diao Y, Han W, Zhao H, Zhu S, Liu X, Feng X, Gu J, Yao C, Liu S, Sun C, Pan F. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain DRAMP31799 RGDLLRHVVKILEKYL 16 RGD-La Not available Not found Arg-Gly-Asp(RGD) tripeptide ana temporins Antimicrobial, Anticancer Not found Not found Not found Not available A membrane-disturbing action seems to be the major mechanism for cell death Tumor cells: MEC (19.76 Inhibition ratio at 50 µg/ml); HL-7702(L-02) (36.25 Inhibition ratio at 50 µg/ml); A549 (47.26Inhibition ratio at 50 µg/ml); Hep-G2 (60.22 Inhibition ratio at 50 µg/ml); BGC-823 (62.49 Inhibition ratio at 50 µg/ml); SMMC-7721 (70.39 Inhibition ratio at 50 µg/ml); SW1116 (72.69 Inhibition ratio at 50 µg/ml); HeLa (73.09 Inhibition ratio at 50 µg/ml) Showed no hemolytic activity against rabbit erythrocytes and human erythrocytes at 250 µg/ml Linear Free Free L Showed little effects on the proliferation of the 293T human embryonic kidney cell line, MECs, and human lymphomonocytes at concentrations of less than 50 µg/ml Not available 22641352 J Pept Sci. 2012 Jul;18(7):476-86. Diao Y, Han W, Zhao H, Zhu S, Liu X, Feng X, Gu J, Yao C, Liu S, Sun C, Pan F. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain DRAMP31800 RGDLLRHVVKILSKYL 16 RGD-Las Not available Not found Arg-Gly-Asp(RGD) tripeptide ana temporins Antimicrobial, Anticancer Not found Not found Not found Not available A membrane-disturbing action seems to be the major mechanism for cell death Tumor cells: MEC (29.33 Inhibition ratio at 50 µg/ml); HL-7702(L-02) (38.13 Inhibition ratio at 50 µg/ml); A549 (52.50 Inhibition ratio at 50 µg/ml); Hep-G2 (73.07 Inhibition ratio at 50 µg/ml); BGC-823 (73.705 Inhibition ratio at 50 µg/ml); HeLa (78.045 Inhibition ratio at 50 µg/ml); SW1116 (81.465 Inhibition ratio at 50 µg/ml); SMMC-7721 (86.175 Inhibition ratio at 50 µg/ml) Showed no hemolytic activity against rabbit erythrocytes and human erythrocytes at 250 µg/ml Linear Free Free L Showed little effects on the proliferation of the 293T human embryonic kidney cell line, MECs, and human lymphomonocytes at concentrations of less than 50 µg/ml Not available 22641352 J Pept Sci. 2012 Jul;18(7):476-86. Diao Y, Han W, Zhao H, Zhu S, Liu X, Feng X, Gu J, Yao C, Liu S, Sun C, Pan F. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain DRAMP31801 PDEDAINDALNKVCSTGRRQRSICKQLLKK 30 N29D Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Lyse cancer cells Tumor cells: SNU-1 (<100% cell viability at 5 µM); SNU-1 (<40% cell viability at 50 µM); U-937 (<60% cell viability at 50 µM); SW480 (>100% cell viability at 5 µM); U-937 (100% cell viability at 5 µM); SW480 (60% cell viability at 50 µM) Not available Linear Free Free L Not available Not available 22783018 Proc Natl Acad Sci U S A. 2012 Jul 24;109(30):12087-92. Lee MO, Kim EH, Jang HJ, Park MN, Woo HJ, Han JY, Womack JE. Effects of a single nucleotide polymorphism in the chicken NK-lysin gene on antimicrobial activity and cytotoxicity of cancer cells DRAMP31802 PDEDAINNALNKVCSTGRRQRSICKQLLKK 30 N29N Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Lyse cancer cells Tumor cells: SNU-1 (<100% cell viability at 5 µM); SNU-1 (<20% cell viability at 50 µM); U-937 (<40% cell viability at 50 µM); SW480 (100% cell viability at 5 µM); U-937 (100% cell viability at 5 µM); SW480 (40% cell viability at 50 µM) Not available Linear Free Free L Not available Not available 22783018 Proc Natl Acad Sci U S A. 2012 Jul 24;109(30):12087-92. Lee MO, Kim EH, Jang HJ, Park MN, Woo HJ, Han JY, Womack JE. Effects of a single nucleotide polymorphism in the chicken NK-lysin gene on antimicrobial activity and cytotoxicity of cancer cells DRAMP31803 KWKSFLKTFKSlKKTVLHTLLKAISS 26 Peptide L12D Not available Not found Acetylation Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=2.63±0.07 µmol/L) Human red blood cells: MHC=20.81±0.03 μmol/L Linear Acetylation Amidation Mix Not available Not available 22837667 Int J Mol Sci. 2012;13(6):6849-6862. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides DRAMP31804 KWKSFLKTFKSLKKTVLHTlLKAISS 26 Peptide L20D Not available Not found Acetylation Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=2.33±0.06 µmol/L) Human red blood cells: MHC=20.81 +0.13 μmol/L Linear Acetylation Amidation Mix Not available Not available 22837667 Int J Mol Sci. 2012;13(6):6849-6862. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides DRAMP31805 KWKSFlKTFKSLKKTVLHTLLKAISS 26 Peptide L6D Not available Not found Acetylation Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=2.23±0.10 µmol/L) Human red blood cells: MHC=10.40±0.08 μmol/L Linear Acetylation Amidation Mix Not available Not available 22837667 Int J Mol Sci. 2012;13(6):6849-6862. Huang YB, He LY, Jiang HY, Chen YX. Role of helicity on the anticancer mechanism of action of cationic-helical peptides DRAMP31806 GLFGKLIKKFARKAISYAVKKARGKH 26 ltc2aG11A Not available Not found Central Asian spider, Lachesana tarabaevi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22885172 Biochim Biophys Acta. 2012 Dec;1818(12):3072-80. Won A, Ruscito A, Ianoul A. Imaging the membrane lytic activity of bioactive peptide latarcin 2a DRAMP31807 KKWXWKK 7 c1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=10±2 μM); Ramos (IC50=22±5 μM) Human red blood cells: EC50=87 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=10±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31808 KKWXWKK 7 c1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=11±2 μM); Ramos (IC50=23±3 μM) Human red blood cells: EC50=87 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=10±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31809 KKWXWKK 7 c5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=10±2 μM); Ramos (IC50=22±5 μM) Human red blood cells: EC50=141 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=26±3 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31810 KKWXWKK 7 c5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=11±2 μM); Ramos (IC50=23±3 μM) Human red blood cells: EC50=141 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=26±3 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31811 KKXWKK 6 c3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=15±2 μM); Ramos (IC50=92±2 μM) Human red blood cells: EC50=256 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=1030±21 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31812 KKXWKK 6 c3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=157±30 μM); Ramos (IC50=16±5 μM) Human red blood cells: EC50=256 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=1030±21 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31813 KKXWKK 6 c7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=15±2 μM); Ramos (IC50=92±2 μM) denotes no detectable activity (IC50 or EC50) within the concentration range tested Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=31±2 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31814 KKXWKK 6 c7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=157±30 μM); Ramos (IC50=16±5 μM) denotes no detectable activity (IC50 or EC50) within the concentration range tested Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=31±2 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31815 KWXKK 5 c4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=12.6±0.6 μM); Ramos (IC50=99±15 μM) Human red blood cells: EC50=110 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=23.5±0.7 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31816 KWXKK 5 c4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=20±2 μM); Ramos (IC50=226±21 μM) Human red blood cells: EC50=110 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=23.5±0.7 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31817 KWXKK 5 c8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=12.6±0.6 μM); Ramos (IC50=99±15 μM) Human red blood cells: EC50=298 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=53±2 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31818 KWXKK 5 c8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=20±2 μM); Ramos (IC50=226±21 μM) Human red blood cells: EC50=298 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=53±2 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31819 KWXWKK 6 c2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=1.71±0.6 μM); Ramos (IC50=7.9±0.3 μM) Human red blood cells: EC50=31 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=13±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31820 KWXWKK 6 c2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=26±2 μM); Ramos (IC50=8±1 μM) Human red blood cells: EC50=31 μM Cyclic lactam lactam X=2-Nal-CH2- L MRC-5: IC50=13±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31821 KWXWKK 6 c6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=1.71±0.6 μM); Ramos (IC50=7.9±0.3 μM) Human red blood cells: EC50=36 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=23±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31822 KWXWKK 6 c6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Ramos (IC50=26±2 μM); Ramos (IC50=8±1 μM) Human red blood cells: EC50=36 μM Cyclic lactam lactam X=p-CF3-Bzl- L MRC-5: IC50=23±1 μM Not available 22933412 J Pept Sci. 2012 Oct;18(10):609-19. Tørfoss V, Isaksson J, Ausbacher D, Brandsdal BO, Flaten GE, Anderssen T, Cavalcanti-Jacobsen Cde A, Havelkova M, Nguyen LT, Vogel HJ, Strøm MB. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid DRAMP31823 FLGALFHALSKLL 13 PTP-7a P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induced cell tissue damage through a new cell lysis mechanism Tumor cells: A549 (IC50=28 µM); PANC-1 (IC50=57 μM ) Human erythrocytes: 6.8% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50=32 μM Not available 22934601 Biomacromolecules. 2012 Oct 8;13(10):3327-33. Chen L, Patrone N, Liang JF. Peptide Self-Assembly on Cell Membranes to Induce Cell Lysis DRAMP31824 FLGALFKALSHLL 13 PTP-7b P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Induced cell tissue damage through a new cell lysis mechanism Tumor cells: A549 (IC50=32 µM); PANC-1 (IC50=77 μM ) Human erythrocytes: 8.8% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50=56 μM Not available 22934601 Biomacromolecules. 2012 Oct 8;13(10):3327-33. Chen L, Patrone N, Liang JF. Peptide Self-Assembly on Cell Membranes to Induce Cell Lysis DRAMP31825 RRRRRNWMWC 10 9R Not available Not found Nullomer derived anticancer peptides (NulloPs): Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: J774A.1 (IC50=12 µM); MDA-MB-231 (IC50=16 µM); LNCaP (IC50=23 µM); HuT 102 (IC50=25 µM); LNCaP (IC50=28 µM); MDA-MB-231 (IC50=29 µM); HuT 102 (IC50=36 µM); HuT 102 (IC50=37 µM); HuT 102 (IC50=39 µM); MDA-MB-231 (IC50=39 µM); LNCaP (IC50=44 µM); J774A.1 (IC50=47 µM); HuT 102 (IC50=93 µM) no hemolytic effect on human RBCs Linear Free Amidation L Not available Not available 23000474 Peptides. 2012 Dec;38(2):302-11. Alileche A, Goswami J, Bourland W, Davis M, Hampikian G. Nullomer derived anticancer peptides (NulloPs): differential lethal effects on normal and cancer cells in vitro DRAMP31826 RRRRRWCMNW 10 9S1R Not available Not found Nullomer derived anticancer peptides (NulloPs): Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=10 µM); MDA-MB-231 (IC50=12 µM); J774A.1 (IC50=17 µM); MDA-MB-231 (IC50=18 µM); J774A.1 (IC50=26 µM); LNCaP (IC50=26 µM); HuT 102 (IC50=36 µM); HuT 102 (IC50=38 µM); HuT 102 (IC50=43 µM); HuT 102 (IC50=43 µM); HuT 102 (IC50=45 µM); LNCaP (IC50=8 µM); LNCaP (IC50=9 µM) significant hemolytic activity Linear Free Amidation L Not available Not available 23000474 Peptides. 2012 Dec;38(2):302-11. Alileche A, Goswami J, Bourland W, Davis M, Hampikian G. Nullomer derived anticancer peptides (NulloPs): differential lethal effects on normal and cancer cells in vitro DRAMP31827 PPPEE 5 Caseinphosphopeptides Not available Not found Bovine milk Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AZ-97 (Inhibition at 24-28 g/l) Not available Linear Free Amidation L Not available Not available 23533710 J Amino Acids. 2013;2013:939804. Pepe G, Tenore GC, Mastrocinque R, Stusio P, Campiglia P. Potential anticarcinogenic peptides from bovine milk DRAMP31828 RYLGYL 6 αs1-casein f(90_95) Not available Not found Bovine milk Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AZ-97 (Inhibition at 12-15 g/l) Not available Linear Free Amidation L Not available Not available 23533710 J Amino Acids. 2013;2013:939804. Pepe G, Tenore GC, Mastrocinque R, Stusio P, Campiglia P. Potential anticarcinogenic peptides from bovine milk DRAMP31829 YPFPG 5 β-Casomorphins 5 f(60_64) Not available Not found Bovine milk Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AZ-97 (Inhibition at 9-11 g/l) Not available Linear Free Amidation L Not available Not available 23533710 J Amino Acids. 2013;2013:939804. Pepe G, Tenore GC, Mastrocinque R, Stusio P, Campiglia P. Potential anticarcinogenic peptides from bovine milk DRAMP31830 CLBKKLFKKILKKL 14 BP325 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=12.0 ± 2.7 µM); CAPAN-1 (IC50=13.7 ± 2.4 µM); E42/02 (IC50>>100 µM); E42/02 (IC50>>100 µM); E42/02 (IC50>>100 µM); E42/02 (IC50>>100 µM) Not available Linear Free Amidation L NIH 3T3: IC50=20.6 ± 3.3 µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63. Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP31831 RWRWRWX 7 C -C8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=4.5µM); MCF-7 (IC50=4.7µM) Human erythrocytes:16% Hemolysis=142µM; 50% Hemolysis=285µM Linear Free Amidation X=Lysine with Octanoylated side group L Human fibroblasts: IC50=31.3µM Not available 24147906 ACS Comb Sci. 2013 Nov 11;15(11):585-92. Albada HB, Prochnow P, Bobersky S, Langklotz S, Bandow JE, Metzler-Nolte N. Short antibacterial peptides with significantly reduced hemolytic activity can be identified by a systematic L-to-D exchange scan of their amino acid residues DRAMP31832 YGRKKRRQRRRREADFFWSLCTA 23 KilerFLIP-E Not available Not found The C-terminal domain of c-FLIP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP (At 20 μM, about 30% Trypan blue-negative cells); PC-3-TR (At 20 μM, about 30% Trypan blue-negative cells); RS4;11 (At 20 μM, 10.4% Trypan blue-negative cells); MV4-11 (At 20 μM, 10.8% Trypan blue-negative cells); HCT 115 (At 20 μM, 40% Trypan blue-negative cells); K562 (At 20 μM, 7.7% Trypan blue-negative cells); PC-3 (At 20 μM, about 50% Trypan blue-negative cells); HCT 116 (At 20 μM, about 70% Trypan blue-negative cells) Not available Linear Free Free L No toxicity was observed in epithelial and endothelial cells (HPDE and HUVEC, respectively) Not available 24176852 Cell Death Dis. 2013 Oct 31;4(10):e894. Pennarun B, Gaidos G, Bucur O, Tinari A, Rupasinghe C, Jin T, Dewar R, Song K, Santos MT, Malorni W, Mierke D, Khosravi-Far R. killerFLIP: a novel lytic peptide specifically inducing cancer cell death DRAMP31833 GIIKKIIKKI 10 Short α-helical peptides Not available Not found Alpha-helical proteins Antimicrobial, Anticancer Not found Not found Not found Not available In addition to rapid membrane-permeabilizing capacities, the peptides can also induce the programmed cell death of cancer cells via both mitochondrial pathway and death receptor pathway, without inducing non-specific immunogenic responses. Tumor cells: HL-60 (100% Cytotoxicity at 5 µM Approx); HeLa (99% Cytotoxicity at 4 µM Approx) Not available Linear Free Amidation L Not available Not available 24246647 Biomaterials. 2014 Feb;35(5):1552-61. Chen C, Hu J, Zeng P, Pan F, Yaseen M, Xu H, Lu JR. Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides DRAMP31834 GIIKKIIKKIIKKI 14 Short α-helical peptides Not available Not found Alpha-helical proteins Antimicrobial, Anticancer Not found Not found Not found Not available In addition to rapid membrane-permeabilizing capacities, the peptides can also induce the programmed cell death of cancer cells via both mitochondrial pathway and death receptor pathway, without inducing non-specific immunogenic responses. Tumor cells: HL-60 (90% Cytotoxicity at 5 µM Approx); HeLa (95% Cytotoxicity at 4 µM Approx) Human erythrocytes: HC50>250 µM Linear Free Amidation L Human keratinocytes HaCat: <5% Killing=40 µM Not available 24246647 Biomaterials. 2014 Feb;35(5):1552-61. Chen C, Hu J, Zeng P, Pan F, Yaseen M, Xu H, Lu JR. Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides DRAMP31835 GIIKKIIKKIIKKIIKKI 18 Short α-helical peptides Not available Not found Alpha-helical proteins Antimicrobial, Anticancer Not found Not found Not found Not available In addition to rapid membrane-permeabilizing capacities, the peptides can also induce the programmed cell death of cancer cells via both mitochondrial pathway and death receptor pathway, without inducing non-specific immunogenic responses. Tumor cells: HL-60 (70% Cytotoxicity at 5 µM Approx); HeLa (80% Cytotoxicity at 4 µM Approx) Not available Linear Free Amidation L Not available Not available 24246647 Biomaterials. 2014 Feb;35(5):1552-61. Chen C, Hu J, Zeng P, Pan F, Yaseen M, Xu H, Lu JR. Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides DRAMP31836 CREKAKKLFKKILKKL 16 BP327 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=74.7±8.8µM); CAPAN-1 (IC50=76.2±0.8µM) Not available Linear Free Amidation L NIH 3T3: IC50=74.5±4.1µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63. Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP31837 RRLFRRILRRL 11 BP308 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=148.2±8.8µM); CAPAN-1 (IC50=97.0±15.4µM) Human erythrocytes: 1±0.1% Hemolysis=150µM Linear Free Amidation L NIH 3T3: IC50=68.0±7.6µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63. Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP31838 RLGDGCTR 8 cyclosaplin Not available Not found somatic seedlings of sandalwood Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=2.06 μg/mL) Not available Cyclic Free Free L Normal fibroblast (L929) cell line: Peptide (0–1000 μg/mL) did not exhibit any cytotoxicity. Not available 24503375 Peptides. 2014 Apr;54:148-58. Mishra A, Gauri SS, Mukhopadhyay SK, Chatterjee S, Das SS, Mandal SM, Dey S. Identification and structural characterization of a new pro-apoptotic cyclic octapeptide cyclosaplin from somatic seedlings of Santalum album L DRAMP31839 FFGRLKSVWSAVKHGWKAAKSR 22 Trichoplaxin Not available Not found Trichoplax adhaerens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=45-50µM) Rat erythrocytes:20% Hemolysis=800µM Linear Free Free L Not available Not available 24530880 Biochim Biophys Acta. 2014 May;1838(5):1430-8. Simunić J, Petrov D, Bouceba T, Kamech N, Benincasa M, Juretić D. Trichoplaxin - a new membrane-active antimicrobial peptide from placozoan Cdna DRAMP31840 HGFQWPGSWTWENGKWTWKGAYQFLKGGGGSRRRRRRRRR 40 APTSTAT3-9R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available With the addition of a cell-penetrating motif, the resulting APTSTAT3-9R aptide was able to suppress the viability and proliferation of cancer cells by blocking STAT3 phosphorylation, thereby inhibiting STAT3 downstream signaling. Tumor cells: A549 (IC50=10-20 μmol/L) Not available Linear Free Free L Not available STAT3 24576829 Cancer Res. 2014 Apr 15;74(8):2144-51. Kim D, Lee IH, Kim S, Choi M, Kim H, Ahn S, Saw PE, Jeon H, Lee Y, Jon S. A Specific STAT3-Binding Peptide Exerts Antiproliferative Effects and Antitumor Activity by Inhibiting STAT3 Phosphorylation and Signaling DRAMP31841 KKCKFFCKVKKKIKSIGFQIPIVSIPFK 28 Cathelicidin-RC1 Not available Not found Lithobates catesbeiana Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (At 200 µg/ml induced 2.5% cell death); HepG2 (At 200 µg/ml induced 4.3% cell death) Human erythrocytes:0% Hemolysis=100µg/ml; 3% Hemolysis=200µg/ml Linear Free Free L L929: At 200 µg/ml induced 1.1% cell death Not available 24675879 PLoS One. 2014 Mar 27;9(3):e93216. Ling G, Gao J, Zhang S, Xie Z, Wei L, Yu H, Wang Y. Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design DRAMP31842 KAQXQKQAW 9 LTX-328 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: FEMX-I (IC50>350 µM) Not available Linear Free Amidation X=Dip=diphenylalanine L Not available Not available 24676901 Cancer Immunol Immunother. 2014 Jun;63(6):601-13. Camilio KA, Berge G, Ravuri CS, Rekdal O, Sveinbjørnsson B. Complete regression and systemic protective immune responses obtained in B16 melanomas after treatment with LTX-315 DRAMP31843 TKPRKTKPRKTKPRKTKPR 19 T Peptide Not available Not found Tuftsin derivative Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (67.2% maximum inhibitory rate at 8 mg/kg); Hep-G2 (69.6% maximum inhibitory rate at 8 mg/kg); HT-29 (70% maximum inhibitory rate at 8 mg/kg) Not available Linear Free Free L Not available Not available 24714081 Anticancer Drugs. 2014 Sep;25(8):857-67. An Y, Li L, Yang D, Jia N, Xu C, Wang Q, Wang S, Yuan S. Anticancer activity of tuftsin-derived T peptide in postoperative residual tumors DRAMP31844 ESFSDWWKLLAE 12 mt_T18S/L22 W/P27A Not available Not found MDM2 Antimicrobial, Anticancer Not found Not found Not found Not available target the p53–MDM4 interaction Tumor cells: MCF-7 (IC50=27 µM) Not available Linear Free Free L Not available MDM2 24830845 Amino Acids. 2014 Aug;46(8):2015-24. Fang Y, Jin R, Gao Y, Gao J, Wang J. Design of p53-derived peptides with cytotoxicity on breast cancer DRAMP31845 ETFADWWKLLAE 12 mt_S20A/L22 W/P27A Not available Not found MDM2 Antimicrobial, Anticancer Not found Not found Not found Not available target the p53–MDM5 interaction Tumor cells: MCF-7 (IC50=8.7 µM) Not available Linear Free Free L Not available MDM2 24830845 Amino Acids. 2014 Aug;46(8):2015-24. Fang Y, Jin R, Gao Y, Gao J, Wang J. Design of p53-derived peptides with cytotoxicity on breast cancer DRAMP31846 ETFSDWWKLLAE 12 mt_L22 W/P27A Not available Not found MDM2 Antimicrobial, Anticancer Not found Not found Not found Not available target the p53–MDM2 interaction Tumor cells: MCF-7 (IC50=16.3 µM) Not available Linear Free Free L Not available MDM2 24830845 Amino Acids. 2014 Aug;46(8):2015-24. Fang Y, Jin R, Gao Y, Gao J, Wang J. Design of p53-derived peptides with cytotoxicity on breast cancer DRAMP31847 LTFSDWWKLLAE 12 mt_E17L/L22 W/P27A Not available Not found MDM2 Antimicrobial, Anticancer Not found Not found Not found Not available target the p53–MDM3 interaction Tumor cells: MCF-7 (IC50=15.1 µM) Not available Linear Free Free L Not available MDM2 24830845 Amino Acids. 2014 Aug;46(8):2015-24. Fang Y, Jin R, Gao Y, Gao J, Wang J. Design of p53-derived peptides with cytotoxicity on breast cancer DRAMP31848 KILRGVAKKIMRTFLRRISKDILTGKK 27 C7A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (Cell viability >40% at 12.5μM approx); HROC40 (Cell viability >45% at 12.5μM approx); HROC107 (Cell viability >50% at 12.5μM approx); HCT 116 (Cell viability >50% at 25μM approx); HROC60 (Cell viability >50% at 25μM approx); HROC18 (Cell viability >55% at 12.5μM approx); HROC24 (Cell viability >55% at 12.5μM approx); HROC32 (Cell viability >55% at 12.5μM approx); HROC24 (Cell viability >60% at 25μM approx); HROC32 (Cell viability >60% at 25μM approx); HROC40 (Cell viability >60% at 25μM approx); HROC60 (Cell viability >70% at 12.5μM approx); HROC113 (Cell viability >80% at 12.5μM approx) Whole blood cells: experiments revealed absent or minimal hemolysis Linear Free Amidation L lymphotoxic effects in vitro Not available 24962950 Oncotarget. 2014 Jun 30;5(12):4467-79. Maletzki C, Klier U, Marinkovic S, Klar E, Andrä J, Linnebacher M. Host defense peptides for treatment of colorectal carcinoma - a comparative in vitro and in vivo analysis DRAMP31849 KILRGVAKKIMRTFLRRILTGKK 23 C7A-Δ Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (Cell viability >50% at 12.5μM approx); HCT 116 (Cell viability >50% at 12.5μM approx.); HROC40 (Cell viability >50% at 25μM approx); HROC60 (Cell viability >50% at 25μM approx); HROC24 (Cell viability >60% at 25μM approx); HROC107 (Cell viability >70% at 12.5μM approx); HROC113 (Cell viability >70% at 12.5μM approx); HROC24 (Cell viability >70% at 12.5μM approx); HROC60 (Cell viability >70% at 12.5μM approx); HROC18 (Cell viability >75% at 12.5μM approx); HROC32 (Cell viability >85% at 12.5μM approx); HROC40 (Cell viability >85% at 12.5μM approx); HROC32 (Cell viability=50% at 12.5μM approx.) Whole blood cells: experiments revealed absent or minimal hemolysis Linear Free Amidation L lymphotoxic effects in vitro Not available 24962950 Oncotarget. 2014 Jun 30;5(12):4467-79. Maletzki C, Klier U, Marinkovic S, Klar E, Andrä J, Linnebacher M. Host defense peptides for treatment of colorectal carcinoma - a comparative in vitro and in vivo analysis DRAMP31850 KILRGVAKKIMRTFLRRISKKILTGKK 27 C7A-D21K Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (Cell viability >40% at 12.5μM approx); HROC24 (Cell viability >50% at 25μM approx); HROC40 (Cell viability >50% at 25μM approx); HROC60 (Cell viability >50% at 25μM approx); HROC18 (Cell viability >55% at 12.5μM approx); HROC24 (Cell viability >55% at 12.5μM approx); HROC60 (Cell viability >60% at 12.5μM approx); HROC107 (Cell viability >65% at 12.5μM approx); HROC113 (Cell viability >65% at 12.5μM approx); HROC32 (Cell viability >80% at 12.5μM approx); HROC40 (Cell viability >80% at 12.5μM approx); HCT 116 (Cell viability=50% at 12.5μM approx.); HROC32 (Cell viability=50% at 12.5μM approx.) Whole blood cells: experiments revealed absent or minimal hemolysis Linear Free Amidation L lymphotoxic effects in vitro Not available 24962950 Oncotarget. 2014 Jun 30;5(12):4467-79. Maletzki C, Klier U, Marinkovic S, Klar E, Andrä J, Linnebacher M. Host defense peptides for treatment of colorectal carcinoma - a comparative in vitro and in vivo analysis DRAMP31851 MICYSHKTPQPSATITCEEKTCYKKSVRKLPAIVAGRGCGCPSKEMLVAIHCCRSDKCNE 60 Toxin F-VIII P01404 Not found venom of the Eastern green mamba, Dendroaspis angusticeps (Elapidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=106±5 μg/mL ); HT-29 (LC50>300 μg/mL); MDA-MB-231 (LC50>300 μg/mL) Human erythrocytes: LC50>1000 μg/mL Linear Free Free L HUVEC: LC50>300 μg/mL Not available 25035794 J Venom Res. 2014 Jun 19;5:16-21. Conlon JM, Prajeep M, Mechkarska M, Arafat K, Attoub S, Adem A, Pla D, Calvete JJ. Peptides with in vitro anti-tumor activity from the venom of the Eastern green mamba, Dendroaspis angusticeps (Elapidae) DRAMP31852 RICYSHKLLQAKTTKTCEENSCYKRSLPKIPLIIIGRGCGCPLTLPFLRIKCCTSDKCN 59 Toxin C13S1C1 P18329 Not found venom of the Eastern green mamba, Dendroaspis angusticeps (Elapidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC50=110±4 μg/mL); A549 (LC50=56±4 μg/mL); MDA-MB-231 (LC50=62±2 μg/mL) Human erythrocytes: LC50>600 μg/mL Linear Free Free L HUVEC: LC50=57±3 μg/mL Not available 25035794 J Venom Res. 2014 Jun 19;5:16-21. Conlon JM, Prajeep M, Mechkarska M, Arafat K, Attoub S, Adem A, Pla D, Calvete JJ. Peptides with in vitro anti-tumor activity from the venom of the Eastern green mamba, Dendroaspis angusticeps (Elapidae) DRAMP31853 LKLSPKTKDTLKKVLKGAIKGAIAIASMA 29 Hymenochirin-1Pa Not available Not found skin secretions of the frog Pseudhymenochirus merlini (Pipidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=1.2±0.2 μM); HT-29 (LC50=12.3±4.7 μM); MDA-MB-231 (LC50=3.1±0.2 μM) Human red blood cells (RBC): LC50=162±13 μM Linear Free Amidation L HUVEC: LC50=7.7±0.7 μM Not available 25241629 Peptides. 2014 Nov;61:114-21. Serra I, Scorciapino MA, Manzo G, Casu M, Rinaldi AC, Attoub S, Mechkarska M, Conlon JM. Conformational analysis and cytotoxic activities of the frog skin host-defense peptide, hymenochirin-1Pa DRAMP31854 LKLSPKTKKTLKKVLKGAIKGAIAIASMA 29 [D9K]Hymenochirin-1Pa Not available Not found skin secretions of the frog Pseudhymenochirus merlini (Pipidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=0.9±0.3 μM); MDA-MB-231 (LC50=2.4±0.1 μM); HT-29 (LC50=3.9±0.4 μM) Human red blood cells (RBC): LC50=192±21 μM Linear Free Amidation L HUVEC: LC50=6.5±0.2 μM Not available 25241629 Peptides. 2014 Nov;61:114-21. Serra I, Scorciapino MA, Manzo G, Casu M, Rinaldi AC, Attoub S, Mechkarska M, Conlon JM. Conformational analysis and cytotoxic activities of the frog skin host-defense peptide, hymenochirin-1Pa DRAMP31855 LKLSPKTKkTLKKVLKGAIKGAIAIASMA 29 [D9k]Hymenochirin-1Pa Not available Not found skin secretions of the frog Pseudhymenochirus merlini (Pipidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=2.5±0.3 μM); MDA-MB-231 (LC50=5.4±0.4 μM); HT-29 (LC50=6.3±1.9 μM) Human red blood cells (RBC): LC50>400 μM Linear Free Amidation k=D-Lys Mix HUVEC: LC50=9.3±0.3 μM Not available 25241629 Peptides. 2014 Nov;61:114-21. Serra I, Scorciapino MA, Manzo G, Casu M, Rinaldi AC, Attoub S, Mechkarska M, Conlon JM. Conformational analysis and cytotoxic activities of the frog skin host-defense peptide, hymenochirin-1Pa DRAMP31856 GIFPIFAKLLGKVIKVASSLISKGRTE 27 Ps-2Pa Not available Not found skin secretions of the frog Pseudhymenochirus merlini (Pipidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC50=11.5±2.6 μM); A549 (LC50=6.0±0.6 μM); MDA-MB-231 (LC50=6.2±0.6 μM) Human erythrocytes: LC50=6.2±1.0 μM Linear Free Free L HUVEC: LC50=68±2 μM Not available 25447194 Regul Pept. 2014 Nov;194-195:69-76. Mechkarska M, Attoub S, Sulaiman S, Pantic J, Lukic ML, Conlon JM. Anti-cancer, immunoregulatory, and antimicrobial activities of the frog skin host-defense peptides pseudhymenochirin-1Pb and pseudhymenochirin-2Pa DRAMP31857 IKIPSFFRNILKKVGKEAVSLIAGALKQS 29 Ps-1Pb Not available Not found skin secretions of the frog Pseudhymenochirus merlini (Pipidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=2.5±0.2 μM); MDA-MB-231 (LC50=6.6±0.3 μM); HT-29 (LC50=9.5±1.3 μM) Human red blood cells (RBC): LC50>403 μM Linear Free Free L HUVEC: LC50=5.6±0.9 μM Not available 25447194 Regul Pept. 2014 Nov;194-195:69-76. Mechkarska M, Attoub S, Sulaiman S, Pantic J, Lukic ML, Conlon JM. Anti-cancer, immunoregulatory, and antimicrobial activities of the frog skin host-defense peptides pseudhymenochirin-1Pb and pseudhymenochirin-2Pa DRAMP31858 VKRFKKFFRKLKKAV 15 B1-Ala Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=8.6 µM); MCF-7 (IC50=8.9 µM) Not available Linear Free Amidation L GES-1: IC50=87.1 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31859 VKRFKKFFRKLKKDV 15 B1-Asp Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=19.9 µM); K562 (IC50=44.7 µM) Not available Linear Free Amidation L GES-1: IC50=120.2 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31860 VKRFKKFFRKLKKEV 15 B1-Glu Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=36.6 µM); MCF-7 (IC50=38.9 µM) Not available Linear Free Amidation L GES-1: IC50=104.5 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31861 VKRFKKFFRKLKKFV 15 B1-Phe Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.3 µM); K562 (IC50=3.7 µM) Not available Linear Free Amidation L GES-1: IC50=107.2 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31862 VKRFKKFFRKLKKGV 15 B1-Gly Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=14.8 µM); MCF-7 (IC50=15.8 µM) Not available Linear Free Amidation L GES-1: IC50=107.2 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31863 VKRFKKFFRKLKKHV 15 B1-His Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.5 µM); MCF-7 (IC50=5.0 µM) Not available Linear Free Amidation L GES-1: IC50=104.7 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31864 VKRFKKFFRKLKKKV 15 B1-Lys Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=5.5 µM); K562/Adr (IC50=5.5 µM); MCF-7 (IC50=8.3 µM); MCF-7/ADM (IC50=8.6 µM) Not available Linear Free Amidation L GES-1: IC50=123.0 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31865 VKRFKKFFRKLKKLV 15 B1-Leu Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=1.1 µM); K562/Adr (IC50=3.3. µM); MCF-7 (IC50=3.6 µM); MCF-7/ADM (IC50=4.4 µM) Not available Linear Free Amidation L GES-1: IC50=77.6 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31866 VKRFKKFFRKLKKQV 15 B1-Gln Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=14.5 µM); K562 (IC50=16.2 µM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31867 VKRFKKFFRKLKKRV 15 B1-Arg Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=5.5 µM); K562 (IC50=8.7 µM) Not available Linear Free Amidation L GES-1: IC50=93.3 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31868 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31869 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31870 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31871 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31872 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31873 VKRFKKFFRKLKKSV 15 B1 Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) Not available Linear Free Amidation L GES-1: IC50=102.3 µM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP31874 VKRFKKFFRKLKKTV 15 B1-Thr Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B3 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=17.0 µM); MCF-7 (IC50=19.1 µM) Not available Linear Free Amidation L GES-1: IC50=109.6 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31875 VKRFKKFFRKLKKVV 15 B1-Val Not available Not found Cathelicidin-BF15 C-terminal amidated derivative B1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=4.9 µM); K562 (IC50=5.0 µM) Not available Linear Free Amidation L GES-1: IC50=64.6 µM Not available 25462264 Eur J Med Chem. 2015 Jan 7;89:540-8. Deng X, Qiu Q, Yang B, Wang X, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides with anti-cancer and drug resistance-reversing activities DRAMP31876 WKX 3 WKX Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM1.S (25% Inhibition=10µM) Not available Linear Picolinoyl Free X=MET-Boro L Not available Not available 25759383 J Biol Chem. 2015 Apr 24;290(17):11008-20. Akopian T, Kandror O, Tsu C, Lai JH, Wu W, Liu Y, Zhao P, Park A, Wolf L, Dick LR, Rubin EJ, Bachovchin W, Goldberg AL. Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity DRAMP31877 IKWKRWWWR 9 GN-11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>200µg/ml) Human erythrocytes:<10% Hemolysis>400µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31878 IWKRWWWKR 9 GN-8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=199µg/ml) Human erythrocytes:<=10% Hemolysis>400µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31879 KKRWWWWWR 9 GN-5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=131µg/ml) Human erythrocytes:<=10% Hemolysis=100µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31880 KWWKIWRWR 9 GN-12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=173µg/ml) Human erythrocytes:<10% Hemolysis>400µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31881 KWWRWRRWW 9 GN-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=106µg/ml) Human erythrocytes:<10% Hemolysis=100µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31882 RIWKIWWKR 9 GN-9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>200µg/ml) Human erythrocytes:<10% Hemolysis>400µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31883 RKRWWWWFR 9 GN-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=97µg/ml) Human erythrocytes:<=10% Hemolysis=100µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31884 RLWKRWWIR 9 GN-14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>200µg/ml) Human erythrocytes:<10% Hemolysis>400µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31885 RWKKWWRWL 9 GN-4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=37µg/ml) Human erythrocytes:<=10% Hemolysis=100µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31886 RWKRWWRWI 9 GN-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=47µg/ml) Human erythrocytes:<=10% Hemolysis=128µg/ml Linear Free Amidation L Not available Not available 25941221 Antimicrob Agents Chemother. 2015 Jul;59(7):4112-20. Mojsoska B, Zuckermann RN, Jenssen H. Antimicrobial activity of GN peptides and their mode of action DRAMP31887 GLFDIWAWWRWRR 13 DM2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>250µg/ml) Human erythrocytes:10% Hemolysis=114.3±26.1µg/ml; 50% Hemolysis>250µg/ml Linear Free Amidation L NL20: 50% Cell death>250µg/ml Not available 25985150 Sci Rep. 2015 May 18;5:9761. Le CF, Yusof MY, Hassan H, Sekaran SD. In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin DRAMP31888 GLFDIWKKLRWRR 13 DM5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=97.0±9.8µg/ml) Human erythrocytes:10% Hemolysis>250µg/ml;50% Hemolysis>250µg/ml Linear Free Amidation L NL20: 50% Cell death=179.2±3.8µg/ml Not available 25985150 Sci Rep. 2015 May 18;5:9761. Le CF, Yusof MY, Hassan H, Sekaran SD. In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin DRAMP31889 GLFDIWKKWRWRR 13 DM4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=93.3±5.1µg/ml) Human erythrocytes:10% Hemolysis>250µg/ml;50% Hemolysis>250µg/ml Linear Free Amidation L NL20: 50% Cell death=160.2±11.8µg/ml Not available 25985150 Sci Rep. 2015 May 18;5:9761. Le CF, Yusof MY, Hassan H, Sekaran SD. In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin DRAMP31890 GLFDIWKWWRWRR 13 DM3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=56.0±9.3µg/ml) Human erythrocytes:10% Hemolysis=52.7±5.5µg/ml; 50% Hemolysis>250µg/ml Linear Free Amidation L NL20: 50% Cell death=68.5±11.0µg/ml Not available 25985150 Sci Rep. 2015 May 18;5:9761. Le CF, Yusof MY, Hassan H, Sekaran SD. In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin DRAMP31891 GLFDKWAWWRWRR 13 DM1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=215.3±19.7µg/ml) Human erythrocytes:10% Hemolysis>250µg/ml; 50% Hemolysis>250µg/ml Linear Free Amidation L NL20: 50% Cell death=221.8±7.8µg/ml Not available 25985150 Sci Rep. 2015 May 18;5:9761. Le CF, Yusof MY, Hassan H, Sekaran SD. In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin DRAMP31892 RTRCRfLRRC 10 Compound 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-12 (IC50=225µg/ml) Not available Cyclic C9 Amidation f=D-Phe Mix Madin-Darby canine kidney cells: IC50=190µg/ml; Human dermal fibroblasts: IC50=164µg/ml Not available 26024044 Sci Rep. 2015 May 29;5:10558. Rabanal F, Grau-Campistany A, Vila-Farrés X, Gonzalez-Linares J, Borràs M, Vila J, Manresa A, Cajal Y. A bioinspired peptide scaffold with high antibiotic activity and low in vivo toxicity DRAMP31893 RTRCXfLRXC 10 Compound 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-12 (IC50=595µg/ml) Not available Cyclic C9 Amidation X=diaminobutyrate; f=D-Phe Mix Madin-Darby canine kidney cells: IC50=472µg/ml; Human dermal fibroblasts: IC50=461µg/ml Not available 26024044 Sci Rep. 2015 May 29;5:10558. Rabanal F, Grau-Campistany A, Vila-Farrés X, Gonzalez-Linares J, Borràs M, Vila J, Manresa A, Cajal Y. A bioinspired peptide scaffold with high antibiotic activity and low in vivo toxicity DRAMP31894 RTXCXfLRXC 10 Compound 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-12 (IC50=629µg/ml) Not available Cyclic C9 Amidation X=diaminobutyrate; f=D-Phe Mix Madin-Darby canine kidney cells: IC50=548µg/ml; Human dermal fibroblasts: IC50=534µg/ml Not available 26024044 Sci Rep. 2015 May 29;5:10558. Rabanal F, Grau-Campistany A, Vila-Farrés X, Gonzalez-Linares J, Borràs M, Vila J, Manresa A, Cajal Y. A bioinspired peptide scaffold with high antibiotic activity and low in vivo toxicity DRAMP31895 GAFLKCGESCVYLPCLTTVVGCSCQNSVCYRD 32 DC1 Not available Not found Hedyotis diffusa Antimicrobial, Anticancer Not found Not found Not found Not available induce apoptosis and inhibit proliferation and migration of prostate cancer cells Tumor cells: PC-3 (IC50=2.24 μM); DU145 (IC50=3.32 μM); LNCaP (IC50=5.03 μM) Not available Linear Free Free L Not available Not available 26064310 Int J Clin Exp Med. 2015 Mar 15;8(3):4059-65. Hu E, Wang D, Chen J, Tao X. Novel cyclotides from Hedyotis diffusa induce apoptosis and inhibit proliferation and migration of prostate cancer cells DRAMP31896 GAVPCGETCVYLPCITPDIGCSCQNKVCYRD 31 DC2 Not available Not found Hedyotis diffusa Antimicrobial, Anticancer Not found Not found Not found Not available induce apoptosis and inhibit proliferation and migration of prostate cancer cells Tumor cells: PC-3 (IC50=2.65 μM); DU145 (IC50=3.11 μM); LNCaP (IC50=4.31 μM) Not available Linear Free Free L Not available Not available 26064310 Int J Clin Exp Med. 2015 Mar 15;8(3):4059-65. Hu E, Wang D, Chen J, Tao X. Novel cyclotides from Hedyotis diffusa induce apoptosis and inhibit proliferation and migration of prostate cancer cells DRAMP31897 GTSCGETCVLLPCLSSVLGCTCQNKRCYKD 30 DC3 Not available Not found Hedyotis diffusa Antimicrobial, Anticancer Not found Not found Not found Not available induce apoptosis and inhibit proliferation and migration of prostate cancer cells Tumor cells: LNCaP (IC50=0.21 μM); DU145 (IC50=0.55 μM); PC-3 (IC50=0.76 μM) Not available Linear Free Free L Not available Not available 26064310 Int J Clin Exp Med. 2015 Mar 15;8(3):4059-65. Hu E, Wang D, Chen J, Tao X. Novel cyclotides from Hedyotis diffusa induce apoptosis and inhibit proliferation and migration of prostate cancer cells DRAMP31898 KGIRDWLRGFNKLRKWFLRLIKGL 24 m3 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=60 mg/ml) Not available Linear Free Free L Not available Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31899 KRKLYKWFAHLIKGL 15 KL15 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CaCo-2 (IC50=50 mg/ml); SW480 (IC50=50 mg/ml) Not available Linear Free Free L H184B5F5/M10: IC50=150 μg/ml, testing time is 24h Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31900 LRLLDRWLRLFNRLLRWLRLLRGL 24 m5 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=100 mg/ml) Not available Linear Free Free L Not available Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31901 LRRLDRWLRLFNRLRRWFLRLLRGL 25 m4 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=110 mg/ml) Not available Linear Free Free L Not available Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31902 RLWRLAWRLYRLWRLTL 17 m2 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=70 mg/ml) Not available Linear Free Free L Not available Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31903 RLYRLYFRLYRLWRRLTL 18 m1 Not available Not found membrane disrupting antimicrobial peptide KL15 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=60 mg/ml) Not available Linear Free Free L Not available Not available 26147829 Cancer Biol Ther. 2015;16(8):1172-83. Chen YC, Tsai TL, Ye XH, Lin TH. Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15 DRAMP31904 HXLLPPVXPLFG 12 Callyaerin C Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=2.92µM); THP-1 (IC50>100µM; IC90>100µM) Not available Cyclic Free Amidation X(2)= 4-Hydroxyproline; X(8)=Daa L MRC-5:IC50>100µM; IC90>100µM Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-25. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity DRAMP31905 IXIILPPLXPII 12 Callyaerin B Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=4.14µM); HeLa (ED50>8µM); PC-12 (ED50>8µM); THP-1 (IC50=5µM; IC90=30µM) Not available Cyclic Free Amidation X(2)= 4-Hydroxyproline; X(9)=Daa L MRC-5:IC50=2µM; IC90=6µM Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-25. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity DRAMP31906 IXVILPPLXPIFG 13 Callyaerin A Not available Not found Callyspongia aerizusa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (ED50=3.61µM); THP-1 (IC50=30µM; IC90=50µM) Not available Cyclic Free Amidation X(2)= 4-Hydroxyproline; X(9)=Daa L MRC-5:IC50=20µM; IC90=40µM Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-25. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity DRAMP31907 FWQRRIRRWRRFWQRRIRRWRR 22 DIM-LF11-318 Not available Not found Human lactoferricin derived Antimicrobial, Anticancer Not found Not found Not found Not available Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserin Tumor cells: A-375 (LC50=9.3±0.8 µM ); SBcl-2 (LC50=9.4±0.5 µM ) Not available Linear Free Amidation L Normal Human Dermal Fibroblasts (NHDF): LC50=13.9±0.4 µM Not available 26239537 Biochim Biophys Acta. 2015 Nov;1848(11 Pt A):2918-31. Riedl S, Leber R, Rinner B, Schaider H, Lohner K, Zweytick D. Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserine DRAMP31908 PFWRIRIRRPRRIRIRWFP 19 R-DIM-P-LF11-322 Not available Not found Human lactoferricin derived Antimicrobial, Anticancer Not found Not found Not found Not available Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserin Tumor cells: SBcl-2 (LC50=10.4±0.7 µM ); A-375 (LC50=23.3±1.7 µM ) Not available Linear Free Amidation L Normal Human Dermal Fibroblasts (NHDF):LC50>101 µM Not available 26239537 Biochim Biophys Acta. 2015 Nov;1848(11 Pt A):2918-31. Riedl S, Leber R, Rinner B, Schaider H, Lohner K, Zweytick D. Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserine DRAMP31909 PFWRRRIRIRRRRIRIRRRWFP 22 R-DIM-LF11-337 Not available Not found Human lactoferricin derived Antimicrobial, Anticancer Not found Not found Not found Not available Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserin Tumor cells: SBcl-2 (LC50=5.0±0.4 µM ); A-375 (LC50=61.8±0.1 µM ) Not available Linear Free Amidation L Normal Human Dermal Fibroblasts (NHDF): LC50=22.8±0.1 µM Not available 26239537 Biochim Biophys Acta. 2015 Nov;1848(11 Pt A):2918-31. Riedl S, Leber R, Rinner B, Schaider H, Lohner K, Zweytick D. Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserine DRAMP31910 RWKRINRQWFFWQRNIRKWR 20 R-DIM-LF11-316 Not available Not found Human lactoferricin derived Antimicrobial, Anticancer Not found Not found Not found Not available Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserin Tumor cells: SBcl-2 (LC50=16.0±0.5 µM ); A-375 (LC50=21.0±1.2 µM ) Not available Linear Free Amidation L Normal Human Dermal Fibroblasts (NHDF): LC50=61.8±0.1 µM Not available 26239537 Biochim Biophys Acta. 2015 Nov;1848(11 Pt A):2918-31. Riedl S, Leber R, Rinner B, Schaider H, Lohner K, Zweytick D. Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserine DRAMP31911 WWRRWWRRWRRWWRRWWR 18 RW-AH Not available Not found Human lactoferricin derived Antimicrobial, Anticancer Not found Not found Not found Not available Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserin Tumor cells: A-375 (LC50=13.9±0.4 µM ); SBcl-2 (LC50=4.6±0.2 µM ) Not available Linear Free Amidation L Normal Human Dermal Fibroblasts (NHDF): LC50=9.6±0.2 µM Not available 26239537 Biochim Biophys Acta. 2015 Nov;1848(11 Pt A):2918-31. Riedl S, Leber R, Rinner B, Schaider H, Lohner K, Zweytick D. Human lactoferricin derived di-peptides deploying loop structures induce apoptosis specifically in cancer cells through targeting membranous phosphatidylserine DRAMP31912 GKPICGETCFKGKCYTPGCTCSYPICKKD 29 Cyclotide mela-3 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50=18.73±1.82µM); MM96L (CC50=2.04±0.26µM) Not available Cyclic Free Free L HFF-1: CC50=5.39±0.33µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31913 GKPICGETCFKGKCYTPGCTCSYPICKKN 29 Cyclotide mela-4 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50=18.73±1.82µM); MM96L (CC50=2.04±0.26µM) Not available Cyclic Free Free L HFF-1: CC50=5.39±0.33µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31914 GKPTCGETCFKGKCYTPGCTCSYPLCKKD 29 Cyclotide mela-2 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.30±0.44µM); HeLa (CC50=19.26±1.37µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=5.86±0.38µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31915 GKYTCGETCFKGKCYTPGCTCSYPICKKD 29 Cyclotide mela-1 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=2.09±0.18µM); HeLa (CC50=9.83±0.78µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=3.07±0.15µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31916 GLPTCGETCFKGKCYTPGCSCSYPICKKD 29 Cyclotide mela-6 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.58±0.48µM); HeLa (CC50=11.42±1.00µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=3.13±0.16µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31917 GLPTCGETCFKGKCYTPGCSCSYPICKKN 29 Cyclotide mela-7 Not available Not found Melicytus latifolius Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.58±0.48µM); HeLa (CC50=11.42±1.00µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=3.13±0.16µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31918 GLPTCGETCTLGKCNTPKCTCNWPICYKD 29 Cyclotide mech-2 Not available Not found Melicytus chathamicus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=21.94±1.90µM); HeLa (CC50=36.92±3.25µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=12.45±0.99µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31919 GLPTCGETCTLGKCNTPKCTCNWPICYKN 29 Cyclotide mech-3 Not available Not found Melicytus chathamicus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=21.94±1.90µM); HeLa (CC50=36.92±3.25µM) Human erythrocytes: 50% Hemolysis>64µM Cyclic Free Free L HFF-1: CC50=12.45±0.99µM Not available 26322745 ACS Chem Biol. 2015 Nov 20;10(11):2491-500. Ravipati AS, Henriques ST, Poth AG, Kaas Q, Wang CK, Colgrave ML, Craik DJ. Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae DRAMP31920 FKKLKKLFSKLWNWK 15 HPRP-A1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.5±0.03 μM); SGC-7901 (IC50=5.2±0.14 μM); B16 (IC50=6.1±0.02 μM); Hep-G2 (IC50=7.7±0.23 μM) Human RBC: MHC=64±6.80 μM Linear Acetylation Amidation L Not available Not available 26405806 PLoS One. 2015 Sep 25;10(9):e0138911. Hao X, Yan Q, Zhao J, Wang W, Huang Y, Chen Y. TAT Modification of Alpha-Helical Anticancer Peptides to Improve Specificity and Efficacy DRAMP31921 FKKLKKLFSKLWNWK 15 HPRP-A1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (IC50=13.3 µM); BGC-823 (IC50=14.1 µM); A549 (IC50=14.8 µM); MCF-7 (IC50=15.7 µM); MDA-MB-231 (IC50=22.9 µM) Human RBC: MHC=64±6.80 μM Linear Acetylation Amidation L Not available Not available 26405806 PLoS One. 2015 Sep 25;10(9):e0138911. Hao X, Yan Q, Zhao J, Wang W, Huang Y, Chen Y. TAT Modification of Alpha-Helical Anticancer Peptides to Improve Specificity and Efficacy DRAMP31922 FKKLKKLFSKLWNWKRKKRRQRRR 24 HPRP-A1-TAT Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=1.8±0.02 μM); B16 (IC50=3.5±0.03 μM); SGC-7901 (IC50=4.8±0.08 μM); Hep-G2 (IC50=5.8±0.36 μM) Human RBC: MHC>500 μM Linear Acetylation Amidation L Not available Not available 26405806 PLoS One. 2015 Sep 25;10(9):e0138911. Hao X, Yan Q, Zhao J, Wang W, Huang Y, Chen Y. TAT Modification of Alpha-Helical Anticancer Peptides to Improve Specificity and Efficacy DRAMP31923 fkklkklfsklwnwk 15 HPRP-A2 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SGC-7901 (IC50=10.42±0.30 μM ); B16 (IC50=19.16±0.38 μM ); PC-3 (IC50=21.38±0.56 μM ); BGC-823 (IC50=8.65 ±0.38 μM ) Human red blood cells: low toxicity Linear Free Free L Not available Not available 26422386 PLoS One. 2015 Sep 30;10(9):e0139578.  Zhao J, Hao X, Liu D, Huang Y, Chen Y. In vitro Characterization of the Rapid Cytotoxicity of Anticancer Peptide HPRP-A2 through Membrane Destruction and Intracellular Mechanism against Gastric Cancer Cell Lines DRAMP31924 fkklkklfsklwnwk 15 HPRP-A2 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Human red blood cells: low toxicity Linear Free Free L Not available Not available 26422386 PLoS One. 2015 Sep 30;10(9):e0139578.  Zhao J, Hao X, Liu D, Huang Y, Chen Y. In vitro Characterization of the Rapid Cytotoxicity of Anticancer Peptide HPRP-A2 through Membrane Destruction and Intracellular Mechanism against Gastric Cancer Cell Lines DRAMP31925 KRFKKFFKKVKKSV 14 Ctn[1-14] Not available Not found Rattlesnake Venom Cathelicidin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa S3 (IC50=1 µM); THP-1 (IC50=25 µM); U-937 (IC50=6.25 µM) Human erythrocytes: nonhemolytic up to 400 μM, and their equimolar mixture at that concentration caused only 7% hemolysis Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available 26465972 J Med Chem. 2015 Nov 12;58(21):8553-63. Falcao CB, Pérez-Peinado C, de la Torre BG, Mayol X, Zamora-Carreras H, Jiménez MÁ, Rádis-Baptista G, Andreu D. Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity DRAMP31926 KRFKKFFKKVKKSVKKRLKKIFKKPMVIGVTIPF 34 Ctn(Crotalicidin) Not available Not found Rattlesnake Venom Cathelicidin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa S3 (IC50 < 1 µM ); U-937 (IC50 < 1 µM ); THP-1 (IC50=1.56 µM ); HL-60 (IC50>12.5 µM ); Jurkat E6.1 (IC50>12.5 µM ) Human erythrocytes: 7% and 33% hemolysis at 100 and 400 μM, respectively Linear Free Free Mix MM6: IC50=3.12 µM Not available 26465972 J Med Chem. 2015 Nov 12;58(21):8553-63. Falcao CB, Pérez-Peinado C, de la Torre BG, Mayol X, Zamora-Carreras H, Jiménez MÁ, Rádis-Baptista G, Andreu D. Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity DRAMP31927 YGFVMPRSGLWFR 13 YR Not available Not found Spirulina (Arthrospira) platensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=104.05 μg/mL); Hep-G2 (IC50=188.23 μg/mL); SGC-7901 (IC50=247.32 μg/mL); HT-29 (IC50=446.72 μg/mL) Not available Linear Free Free L Not available Not available 26584028 Food Funct. 2016 Feb;7(2):781-8. Wang Z, Zhang X. Inhibitory effects of small molecular peptides from Spirulina (Arthrospira) platensis on cancer cell growth DRAMP31928 CTLEW 5 CTLEW Not available Not found walnut residual protein Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=0.60±0.17 mg/mL ); CaCo-2 (IC50=0.65±0.42 mg/mL ) Not available Linear Free Free L IEC-6: IC50>4 mg/mL; spleen lymphocytes: IC50>4 mg/mL. Not available 26593407 BMC Complement Altern Med. 2015 Nov 23;15:413. Ma S, Huang D, Zhai M, Yang L, Peng S, Chen C, Feng X, Weng Q, Zhang B, Xu M. Isolation of a novel bio-peptide from walnut residual protein inducing apoptosis and autophagy on cancer cells DRAMP31929 GIFPIFAKLLGKVIKVASSLISKGRTK 27 Pseudhymenochirin-2Pa [E27K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=2.5±0.5µM); MDA-MB-231 (IC50=4.3±0.2µM); HT-29 (IC50=5.6±0.4µM) Mouse erythrocytes:50% Hemolysis=4±1µM Linear Free Free k=D-Lys L HUVEC: 50% Cell death=5.0±0.4µM Not available 26606380 J Nat Prod. 2015 Dec 24;78(12):3041-8. Manzo G, Scorciapino MA, Srinivasan D, Attoub S, Mangoni ML, Rinaldi AC, Casu M, Flatt PR, Conlon JM. Conformational Analysis of the Host-Defense Peptides Pseudhymenochirin-1Pb and -2Pa and Design of Analogues with Insulin-Releasing Activities and Reduced Toxicities DRAMP31930 IKIPSFFRNILKKVGKkAVSLIAGALKQS 29 Pseudhymenochirin-1Pb [E17k] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=11±2µM); A549 (IC50=2.1±0.7µM); MDA-MB-231 (IC50=3.6±0.5µM) Mouse erythrocytes:50% Hemolysis=19±4µM Linear Free Free k=D-Lys Mix HUVEC: 50% Cell death=5.0±0.5µM Not available 26606380 J Nat Prod. 2015 Dec 24;78(12):3041-8. Manzo G, Scorciapino MA, Srinivasan D, Attoub S, Mangoni ML, Rinaldi AC, Casu M, Flatt PR, Conlon JM. Conformational Analysis of the Host-Defense Peptides Pseudhymenochirin-1Pb and -2Pa and Design of Analogues with Insulin-Releasing Activities and Reduced Toxicities DRAMP31931 FFSMIPKIAGGIASLVKNL 19 Phylloseptin-Pba Not available Not found Phyllomedusa baltea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (IC50=1.8µM); PC-3 (IC50=2.9µM); NCI-H460 (IC50=4.3µM) Horse erythrocytes: 1.4% Hemolysis=8µg/ml; Human erythrocytes: 80% Hemolysis=128µg/ml Linear Free Amidation L HMEC-1: IC50=36.6µM Not available 26633506 Toxins (Basel). 2015 Dec 1;7(12):5182-93. Wan Y, Ma C, Zhou M, Xi X, Li L, Wu D, Wang L, Lin C, Lopez JC, Chen T, Shaw C. Phylloseptin-PBa--A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity DRAMP31932 IRKLKSWKWLRWL 13 B4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 170 µM) Not available Linear Free Free L Not available Not available 26902758 Antimicrob Agents Chemother. 2016 Apr 22;60(5):2757-64. Pearson CS, Kloos Z, Murray B, Tabe E, Gupta M, Kwak JH, Karande P, McDonough KA, Belfort G. Combined Bioinformatic and Rational Design Approach To Develop Antimicrobial Peptides against Mycobacterium tuberculosis DRAMP31933 KLLKLLKKLLKLLK 14 KL1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.3±0.4 μM ) Not available Linear Free Amidation L Not available Not available 27195657 J Med Chem. 2016 Jun 9;59(11):5238-47. Liu X, Cao R, Wang S, Jia J, Fei H. Amphipathicity Determines Different Cytotoxic Mechanisms of Lysine- or Arginine-Rich Cationic Hydrophobic Peptides in Cancer Cells DRAMP31934 KLLKLLKLKKLLKL 14 KL2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=34.5±1.6 μM) Not available Linear Free Amidation L Not available Not available 27195657 J Med Chem. 2016 Jun 9;59(11):5238-47. Liu X, Cao R, Wang S, Jia J, Fei H. Amphipathicity Determines Different Cytotoxic Mechanisms of Lysine- or Arginine-Rich Cationic Hydrophobic Peptides in Cancer Cells DRAMP31935 RLLRLLRLRRLLRL 14 RL2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=4.3±0.2 μM); MCF-7 (IC50=4.5±0.3 μM); A549 (IC50=4.8±0.6 μM) Mice red blood cells: HD50>200 μM Linear Free Amidation L HLF: IC50=21.4±1.3 μM; 293T: IC50=41.6±2.7 μM; HUVEC: IC50=19±1.5 μM Not available 27195657 J Med Chem. 2016 Jun 9;59(11):5238-47. Liu X, Cao R, Wang S, Jia J, Fei H. Amphipathicity Determines Different Cytotoxic Mechanisms of Lysine- or Arginine-Rich Cationic Hydrophobic Peptides in Cancer Cells DRAMP31936 RLLRLLRRLLRLLR 14 RL1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5±0.3 μM ); HeLa (IC50=3.7±0.1 μM); A549 (IC50=4.3±0.2 μM ) Mice red blood cells: HD50=2.9±0.3 μM Linear Free Amidation L HLF: IC50=6.3±0.2 μM; 293T: IC50=9.6±1.4 μM; HUVEC: IC50=8.4±0.6 μM Not available 27195657 J Med Chem. 2016 Jun 9;59(11):5238-47. Liu X, Cao R, Wang S, Jia J, Fei H. Amphipathicity Determines Different Cytotoxic Mechanisms of Lysine- or Arginine-Rich Cationic Hydrophobic Peptides in Cancer Cells DRAMP31937 FKIGGFIKKLWRSKLA 16 ZXR-1 N0EAL3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available  ZXR-1 could internalize into cells by endocytosis, target on mitochondria, and induce cell apoptosis Tumor cells: Hep-G2 (IC50=141.7±12.2 µM); SACC-83 (IC50=27.9±7.7 µM); HeLa (IC50=62.6±8.4 µM); PC-3 (IC50=69.1±1.6 µM); Huh-7 (IC50=77.9±0.9 µM) Not available Linear Free Free L HEK293T: IC50=186.7±13.1 µM; WPMY-1: IC50=283.3±19.0 µM Not available 27207743 Biochim Biophys Acta. 2016 Aug;1858(8):1914-25. Zhou XR, Zhang Q, Tian XB, Cao YM, Liu ZQ, Fan R, Ding XF, Zhu Z, Chen L, Luo SZ. From a pro-apoptotic peptide to a lytic peptide: One single residue mutation DRAMP31938 FKIGGFIKKLWRSLLA 16 ZXR-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available ZXR-2 could cause cell membrane lysis Tumor cells: PC-3 (IC50=14.2±0.5 µM); PC-3 (IC50=14.8±1.6 μM ); Hep-G2 (IC50=7.5±1.2 µM); HeLa (IC50=8.1±1.6 µM); HeLa (IC50=8.1±1.6 μM ); Huh-7 (IC50=8.4±1.1 µm); SACC-83 (IC50=9.9±1.7 µM) Not available Linear Free Free L HEK293T: IC50=6.3±0.7 µM; WPMY-1: IC50=12.4±2.0 µM Not available 27207743 Biochim Biophys Acta. 2016 Aug;1858(8):1914-25. Zhou XR, Zhang Q, Tian XB, Cao YM, Liu ZQ, Fan R, Ding XF, Zhu Z, Chen L, Luo SZ. From a pro-apoptotic peptide to a lytic peptide: One single residue mutation DRAMP31939 XIXIXIXRPVYXPRPRPPHPRL 22 Api796 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>600µg/ml) Human erythrocytes:0% Hemolysis=100-600µg/ml Linear gu=N , N , N ', N'-tetramethylguanidino) Free X=Orn L HEK293: 50% Cell death>600µg/ml Not available 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Schäfer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa DRAMP31940 XIXIXRPVYXPRPRPPHPRL 20 Api795 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>600µg/ml) Human erythrocytes:0% Hemolysis=100-600µg/ml Linear gu=N , N , N ', N'-tetramethylguanidino) Free X=Orn L HEK293: 50% Cell death>600µg/ml Not available 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Schäfer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa DRAMP31941 XWXWXRPVYXPRPRPPHPRL 20 Api793 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=640±150µg/ml) Human erythrocytes:1% Hemolysis=100µg/ml; Human erythrocytes:2% Hemolysis=600µg/ml Linear gu=N , N , N ', N'-tetramethylguanidino) Free X=Orn L HEK293: 50% Cell death=640±50µg/ml Not available 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Schäfer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa DRAMP31942 XWXWXWXRPVYXPRPRPPHPRL 22 Api794 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=230 ± 90µg/ml) Human erythrocytes:2% Hemolysis=100-600µg/ml Linear gu=N , N , N ', N'-tetramethylguanidino) Free X=Orn L HEK293: 50% Cell death=280±30µg/ml Not available 27243004 Front Cell Dev Biol. 2016 May 10;4:39. Bluhm ME, Schneider VA, Schäfer I, Piantavigna S, Goldbach T, Knappe D, Seibel P, Martin LL, Veldhuizen EJ, Hoffmann R. N-Terminal Ile-Orn- and Trp-Orn-Motif Repeats Enhance Membrane Interaction and Increase the Antimicrobial Activity of Apidaecins against Pseudomonas aeruginosa DRAMP31943 KWKSFLKTFKSAEKTVLHTALKAISS 26 V681 [V13E] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=109.68µM); SGC-7901 (IC50=92.04µM) Human erythrocytes:<5% Hemolysis=>500µM Linear Acetylation Amidation L 3T3-L1:50% Cell death>125µM Not available 27363513 Sci Rep. 2016 Jul 1;6:29145. Sun S, Zhao G, Huang Y, Cai M, Shan Y, Wang H, Chen Y. Specificity and mechanism of action of alpha-helical membrane-active peptides interacting with model and biological membranes by single-molecule force spectroscopy DRAMP31944 ATCETPSKHFNGLCIRSSNCASVCHGEHFTDGRCQGVRRRCMCLKPC 47 PaDef defensin Not available Not found Plant defensins Antimicrobial, Anticancer Not found Not found Not found Not available PaDef defensin from avocado (Persea americana) fruit is cytotoxic to MCF-7 cells via the induction of mitochondrial apoptosis Tumor cells: MCF-7 (IC 50=141.62 μg/mL ); K562 (IC50=97.3 μg/mL (18.65 μM)) Not available Linear Free Free L Not available Not available 27470405 Biomed Pharmacother. 2016 Aug;82:620-7. Guzmán-Rodríguez JJ, López-Gómez R, Salgado-Garciglia R, Ochoa-Zarzosa A, López-Meza JE. The defensin from avocado (Persea americana var. drymifolia) PaDef induces apoptosis in the human breast cancer cell line MCF-7 DRAMP31945 TSLDASIWAMMQNA 14 P144 Not available Not found derived from the extracellular sequence of the human TGF-β type III receptor Antimicrobial, Anticancer Not found Not found Not found Not available P144 induced an upregulation of SMAD7 and downregulation of SKI through inhibition of the TGF-β pathway. Tumor cells: U-87MG ATCC (IC50=16.34±1.47 µg/mL); A172 (IC50=21.96±3.68 µg/mL ) Not available Linear Free Free L Not available Transforming Growth Factor beta 27473823 Cancer Lett. 2016 Oct 10;381(1):67-75. Gallo-Oller G, Vollmann-Zwerenz A, Meléndez B, Rey JA, Hau P, Dotor J, Castresana JS. P144, a Transforming Growth Factor beta inhibitor peptide, generates antitumoral effects and modifies SMAD7 and SKI levels in human glioblastoma cell lines DRAMP31946 RECKTESHRFKGPCITKPPCRKACISEKFTDGHCSKILRRCLCTKPC 47 NaD1 (1-7)-NaD2 (8-13)-NaD1 (14-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (22.2±2.4% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31947 RECKTESNTFPGICITKPPCRKACISEKFSGGDCSKILRRCLCTKPC 47 NaD1 (1-29)-NaD2 (30-33)-NaD1 (34-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (20.0±1.4% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31948 RECKTESNTFPGICITKPPCRKACISEKFTDGHCRGFRRRCLCTKPC 47 NaD1 (1-34)-NaD2 (35-40)-NaD1 (41-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (13.7±8.1% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31949 RECKTESNTFPGICITKPPCRKACISEKFTDGHCSKILRRCFCTRPC 47 NaD1 (1-41)-NaD2 (42-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (43.1±7.2% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31950 RECKTESNTFPGICITKPPCRKACLTEGFTDGHCSKILRRCLCTKPC 47 NaD1 (1-24)-NaD2 (25-29)-NaD1 (30-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (44.6±8.5% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31951 RTCESQSHRFKGPCARDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC 47 Class I defensin, NaD2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: U-937 (5.9±1.3% Cell death=10 µM)" Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31952 RTCESQSNTFPGICITKPPCRKACISEKFTDGHCSKILRRCLCTKPC 47 NaD2 (1-7) - NaD1 (8-47) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (7.9±2.4% Cell death=10µM) Not available Cyclic Free Free L Not available Not available 27503651 Antimicrob Agents Chemother. 2016 Sep 23;60(10):6302-12. Bleackley MR, Payne JA, Hayes BM, Durek T, Craik DJ, Shafee TM, Poon IK, Hulett MD, van der Weerden NL, Anderson MA. Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant DRAMP31953 MQFITDLIKKAVDFFKGLFDNK 22 Warnericin RK [G20D] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (LD50=5.39µM) Human erythrocytes:10% Hemolysis=12.36µM Linear Free Free L Not available Not available 27598770 PLoS One. 2016 Sep 6;11(9):e0162007. Loiseau C, Augenstreich J, Marchand A, Harté E, Garcia M, Verdon J, Mesnil M, Lecomte S, Berjeaud JM. Specific Anti-Leukemic Activity of the Peptide Warnericin RK and Analogues and Visualization of Their Effect on Cancer Cells by Chemical Raman Imaging DRAMP31954 MQFITDLIKKAVDVFKGLFGNK 22 Warnericin RK [F14V] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (LD50=8.79µM) Human erythrocytes:10% Hemolysis=12.5µM Linear Free Free L Not available Not available 27598770 PLoS One. 2016 Sep 6;11(9):e0162007. Loiseau C, Augenstreich J, Marchand A, Harté E, Garcia M, Verdon J, Mesnil M, Lecomte S, Berjeaud JM. Specific Anti-Leukemic Activity of the Peptide Warnericin RK and Analogues and Visualization of Their Effect on Cancer Cells by Chemical Raman Imaging DRAMP31955 GIKHILFMAKTKLPRATCTAEIKENCDRKK 30 Saha-CATH1 Not available Not found Sarcophilus harrisii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 500µg/ml) Human erythrocytes:5% Hemolysis=1-500µg/ml Linear Free Free L Not available Not available 27725697 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) DRAMP31956 KREDFLDQIIRDFRNFIYQKYRRLRDEFRKLRDILSG 37 Saha-CATH4 Not available Not found Sarcophilus harrisii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 500µg/ml) Human erythrocytes:5% Hemolysis=1-500µg/ml Linear Free Free L Not available Not available 27725697 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) DRAMP31957 KRIGLIRLIGKILRGLRRLG 20 Saha-CATH5 Not available Not found Sarcophilus harrisii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 500 µg/ml) Human erythrocytes:5% Hemolysis=1-31.25µg/ml; 7% Hemolysis=62.5µg/ml; 12% Hemolysis=125µg/ml; 30% Hemolysis=250µg/ml Linear Free Free L Not available Not available 27725697 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) DRAMP31958 TFKRKNGSRKNGHRPGGYSLIALGNKKVLKAPYMESI 37 Saha-CATH2 Not available Not found Sarcophilus harrisii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 500µg/ml) Human erythrocytes:5% Hemolysis=1-500µg/ml Linear Free Free L Not available Not available 27725697 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Cathelicidins in the Tasmanian devil (Sarcophilus harrisii) DRAMP31959 CGRRKRRRGCRRDSDCPGACICRYwKVCGSGSDGGV 36 MCoAA-01 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=40.12±0.13 μM); MCF-7 (IC50=45.01±0.16 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50=10.83±0.09 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31960 CPKILKKCRRDSDCPGACICRGNGYCGRRKRRRG 34 MCo-polyR-L6 P82409 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=52.89±0.11 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50=34.95±0.03 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31961 CPKILKKCRRDSDCPGACICRGNGYCGSGSDGGV 34 MCoTI-II P82409 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2PO8 Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31962 CPKILKKCRRDSDCPGACICRGNGYCRFwKTW 32 MCo-SST-02 P82409 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=58.89±0.09 μM); MCF-7 (IC50=70.61±0.11 μM); PC-3 (IC50=83.55±0.20 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31963 CPKILKKCRRDSDCPGACICRGNGYCYHLNQPF 33 MCo-PEDF P82409 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=35.22±0.08 μM); PC-3 (IC50=39.11±0.07 μM); MCF-7 (IC50=53.44±0.14 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50=50.16±0.15 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31964 CPKILKKCRRDSDCPGACICRYwKVCGSGSDGGV 34 MCo-SST-01 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=74.13±0.07 μM); PC-3 (IC50=85.44±0.08 μM); MCF-7 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50=17.12±0.05 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31965 CPKILKKCRRDSDCPGACICRYwKVCGYHLNQPFG 35 MCoAA-02 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=19.75±0.07 μM); PC-3 (IC50=35.44±0.13 μM); MCF-7 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50=27.06±0.06 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31966 CRRKRRRCRRDSDCPGACICRGNGYCGSGSDGGV 34 MCo-polyR-L1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31967 CRRKRRRICFPDGR 14 SFTI-polyR-L1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=28.72±0.15 μM); HT-29 (IC50=82.27±0.13 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31968 CTKSIPPICFPDGR 14 SFTI-1 Q4GWU5 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2AB9 Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31969 CTKSIPPICRFwKTW 15 SFTI-SST-02 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=43.29±0.04 μM); MCF-7 (IC50=55.13±0.07 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31970 CTKSIPPICRRKRRR 15 SFTI-polyR-L2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=41.84±0.07 μM); HT-29 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31971 CTKSIPPICYHLNQPF 16 SFTI-PEDF Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free L HUVEC: IC50=27.89±0.11 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31972 CTKSIPPICYwKV 13 SFTI-SST-01 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=45.38±0.03 μM); MCF-7 (IC50=46.07±0.05 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Cyclic Free Free w=D-Tryptophane Mix HUVEC: IC50=18.32±0.05 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31973 RFwKTW 6 SST-02 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Linear Free Free w=D-Tryptophane Mix HUVEC: IC50>100 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31974 RRKRRR 6 polyR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=83.51±0.46 μM); HT-29 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Linear Free Free L HUVEC: IC50=44.64±0.03 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31975 YHLNQPF 7 PEDF Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Linear Free Free L HUVEC: IC50=19.40±0.08 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31976 YwKV 4 SST-01 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 μM); MCF-7 (IC50>100 μM); PC-3 (IC50>100 μM) Human red blood cells: no hemolytic activity(as show in Fig.4) Linear Free Free w=D-Tryptophane Mix HUVEC: IC50=57.54±0.04 μM pigment epithelium-derived factor; somatostatin 27734947 Sci Rep. 2016 Oct 11;6:35019. Peel E, Cheng Y, Djordjevic JT, Fox S, Sorrell TC, Belov K. Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy DRAMP31977 FKAGGFIKKLWRSLLA 16 IL-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=58.4±13.7 μM); HeLa (IC50=73.9±13.6 μM) Not available Linear Free Free L HEK293T: IC50=24.1±3.2 μM; WPMY-1: IC50=43.2±4.9 μM Not available 27778166 Amino Acids. 2017 Jan;49(1):193-202. Fan R, Yuan Y, Zhang Q, Zhou XR, Jia L, Liu Z, Yu C, Luo SZ, Chen L. "Isoleucine/leucine residues at ""a"" and ""d"" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide" DRAMP31978 FKIGGFAKKLWRSLLA 16 IL-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=43.6±7.9 μM); HeLa (IC50=52.0±5.8 μM) Not available Linear Free Free L HEK293T: IC50=40.0±5.5 μM; WPMY-1: IC50=19.4±5.3 μM Not available 27778166 Amino Acids. 2017 Jan;49(1):193-202. Fan R, Yuan Y, Zhang Q, Zhou XR, Jia L, Liu Z, Yu C, Luo SZ, Chen L. "Isoleucine/leucine residues at ""a"" and ""d"" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide" DRAMP31979 FKIGGFIKKAWRSLLA 16 IL-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=74.9±13.3 μM); HeLa (IC50=93.5±19.4 μM) Not available Linear Free Free L HEK293T: IC50=48.5±4.9 μM; WPMY-1: IC50=40.1±6.9 μM Not available 27778166 Amino Acids. 2017 Jan;49(1):193-202. Fan R, Yuan Y, Zhang Q, Zhou XR, Jia L, Liu Z, Yu C, Luo SZ, Chen L. "Isoleucine/leucine residues at ""a"" and ""d"" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide" DRAMP31980 FKIGGFIKKLWRSALA 16 IL-4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=35.5±3.9 μM); HeLa (IC50=54.4±3.0 μM) Not available Linear Free Free L HEK293T: IC50=36.1±4.7 μM; WPMY-1: IC50=19.9±6.3 μM Not available 27778166 Amino Acids. 2017 Jan;49(1):193-202. Fan R, Yuan Y, Zhang Q, Zhou XR, Jia L, Liu Z, Yu C, Luo SZ, Chen L. "Isoleucine/leucine residues at ""a"" and ""d"" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide" DRAMP31981 FKIGGFIKKLWRSLAA 16 IL-5 N0EAL3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=22.0±2.6 μM); HeLa (IC50=28.0±4.6 μM) Not available Linear Free Free L HEK293T: IC50=27.6±2.7 μM; WPMY-1: IC50=12.7±3.1 μM Not available 27778166 Amino Acids. 2017 Jan;49(1):193-202. Fan R, Yuan Y, Zhang Q, Zhou XR, Jia L, Liu Z, Yu C, Luo SZ, Chen L. "Isoleucine/leucine residues at ""a"" and ""d"" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide" DRAMP31982 FIGAIARLLSK 11 BmKn-22 Not available Not found Scorpion venom Antimicrobial, Anticancer Not found Not found Not found Not available BmKn-2 exerts selective cytotoxic effects on human oral cancer cells by inducting apoptosis via a p53-dependent intrinsic apoptotic pathway. BmKn-2 peptide originally derived from a natural source shows great promise as a candidate treatment for oral cancer Tumor cells: HSC-4 (IC50=97 μg/mL) Not available Linear Free Free L Not available Not available 27780132 Biomed Pharmacother. 2016 Dec;84:1042-1050. Satitmanwiwat S, Changsangfa C, Khanuengthong A, Promthep K, Roytrakul S, Arpornsuwan T, Saikhun K, Sritanaudomchai H. The scorpion venom peptide BmKn2 induces apoptosis in cancerous but not in normal human oral cells DRAMP31983 RYRRKKKMKKALQYIKLLKE 20 Peptide 35409 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 44 µg/ml); HepG2 (Not active up to 44 µg/ml) Human erythrocytes: 14% Hemolysis=350µM Linear Free Free L Not available Not available 28066341 Front Microbiol. 2016 Dec 20;7:2006. Barreto-Santamaría A, Curtidor H, Arévalo-Pinzón G, Herrera C, Suárez D, Pérez WH, Patarroyo ME. A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35 DRAMP31984 XXXVXAaXXXX 11 Cyclosporin A Not available Not found Tolypocladium inflatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CaCo-2 (0% Killing=12µM; 20% Killing=17µM); Huh-7 (0% Killing=8µM; 50% Killing=17µM) Not available Cyclic Free Free X(1)=alpha-Aminobutyrate; X(2)=Sarcosine; X(3)=METH-Leu; X(5)=METH-Leu; X(7)=D-Ala; X(8)=METH-Leu; X(9)=METH-Leu; X(10)=METH-Val; X(11)=N-methyl-(4R)-4-[(E)-but-2-enyl]-4-methyl-L-threonyl Mix Vero E6: <10% Killing=5µM, 25% Killing=17µM; Fcwf-4: 0% Killing=4µM, 40% Killing=12µM Not available 28137809 Antimicrob Agents Chemother. 2017 Mar 24;61(4):e02241-16. Gaillard V, Galloux M, Garcin D, Eléouët JF, Le Goffic R, Larcher T, Rameix-Welti MA, Boukadiri A, Héritier J, Segura JM, Baechler E, Arrell M, Mottet-Osman G, Nyanguile O. A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading DRAMP31985 ASVVNKLTGGVAGLLK 16 Bacteriocin TP Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NB4 (IC50=11.479µM); MKN 45 (IC50=4.686µM) Mouse erythrocytes: <10% Hemolysis=160µM; 10% Hemolysis=320µM Linear Free Free L Not available Not available 28254375 Int J Antimicrob Agents. 2017 Apr;49(4):427-436. Xin H, Ji S, Peng J, Han P, An X, Wang S, Cao B. Isolation and characterisation of a novel antibacterial peptide from a native swine intestinal tract-derived bacterium DRAMP31986 FASGIAGMAGKLF 13 Temporin-1Sa [L2,9A;V6A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50>60µM); HepG2 (IC50>600µM) "Rat erythrocytes: 50% Hemolysis>200µM; Human erythrocytes: 50% Hemolysis >100µM" Linear Free Amidation L Not available Not available 28319176 PLoS One. 2017 Mar 20;12(3):e0174024. Raja Z, André S, Abbassi F, Humblot V, Lequin O, Bouceba T, Correia I, Casale S, Foulon T, Sereno D, Oury B, Ladram A. Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent DRAMP31987 ALlVNx 6 Wollamide B [W1A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31988 lLWVNx 6 Wollamide B [W1l, l3W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31989 WAlVNx 6 Wollamide B [L2A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31990 WIlVNx 6 Wollamide B [L2I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31991 WLaVNx 6 Wollamide B [l3a] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31992 WLIVNx 6 Wollamide B [l3I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31993 WLlANx 6 Wollamide B [V4A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31994 WLlIIx 6 Wollamide B [V4I, N5I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31995 WLlINx 6 Wollamide B [V4I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=50µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31996 WLlISx 6 Wollamide B [V4I,N5S] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31997 WLlIXx 6 Wollamide B [V4I, N5TERT BU SER] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31998 WLlVAx 6 Wollamide B [N5A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP31999 WLlVxx 6 Wollamide B [N5D-ORN] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free l=D-Leu; x(5)=D-Orn; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32000 WLxIxx 6 Wollamide B [l3D-Phe(4Cl), V4I, N5D-Orn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(3)=D-4-Cl-Phe; x(5)=D-Orn; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32001 WLxVNx 6 Wollamide B [l3D-Phe(4Cl)] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=60µM) Not available Cyclic Free Free x(3)=D-4-Cl-Phe; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32002 WLxVXx 6 Wollamide B [l3D-Me-Leu, N5Me-Asn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(3)=METH-Leu; x(5)=METH-Asn; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32003 WxlVNx 6 Wollamide B [L2D-Phe(4Cl)] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(2)=D-4-Cl-Phe; l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32004 WXlVXx 6 Wollamide B [L2Me-Leu, N5Me-Asn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(2)=METH-Leu; l=D-Leu; x(5)=METH-Asn; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32005 WXlXNx 6 Wollamide B [L2Me-Leu, V4Me-Val] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(2)=METH-Leu; l=D-Leu; x(5)=METH-Val; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32006 xLlVNx 6 Wollamide B [W1D-Phe(4-Cl)] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100µM) Not available Cyclic Free Free x(1)=D-4-Cl-Phe; l=D-Leu; x(6)=D-Orn Mix Not available Not available 28423019 PLoS One. 2017 Apr 19;12(4):e0176088. Asfaw H, Laqua K, Walkowska AM, Cunningham F, Martinez-Martinez MS, Cuevas-Zurita JC, Ballell-Pages L, Imming P. Design, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent DRAMP32007 KKLFKKILKAL 11 BP100 [Y10A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=21.4±2.7µM); MCF-7 (IC50=23.2±2.4µM); K562 (IC50=27.4±3.5µM); K562/ADM (IC50=31.3±4.0µM) Rabbit erythrocytes: 4% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=77.3±7.4µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32008 KKLFKKILKDL 11 BP100 [Y10D] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=70.7±6.3µM); K562 (IC50=76.3±5.4µM); MCF-7 (IC50=77.9±6.7µM); K562/ADM (IC50=82.5±6.8µM) Rabbit erythrocytes: 11% Hemolysis=160µM Linear Free Amidation L GES-1: IC50>100µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32009 KKLFKKILKEL 11 BP100 [Y10E] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=79.5±6.9µM); MCF-7 (IC50=83.2±6.7µM); K562 (IC50=89.4±7.3µM); K562/ADM (IC50>100µM) Rabbit erythrocytes: 6.5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50>100µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32010 KKLFKKILKGL 11 BP100 [Y10G] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=30.3±4.2µM); MCF-7 (IC50=33.5±3.3µM); K562 (IC50=34.5±4.0µM); K562/ADM (IC50=36.8±3.9µM) Rabbit erythrocytes: 11% Hemolysis=160µM Linear Free Amidation L GES-1: IC50>100µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32011 KKLFKKILKHL 11 BP100 [Y10H] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=10.2±1.7µM); K562 (IC50=7.6±1.8µM); MCF-7 (IC50=8.6±1.3µM); K562/ADM (IC50=9.9±1.4µM) Rabbit erythrocytes: 4% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=72.3±7.4µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32012 KKLFKKILKIL 11 BP100 [Y10I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=21.3±2.1µM); MCF-7 (IC50=21.5±1.9µM); K562 (IC50=23.7±2.3µM); K562/ADM (IC50=24.6±1.6µM) Rabbit erythrocytes: 7.5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=76.9±6.7µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32013 KKLFKKILKLL 11 BP100 [Y10L] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=6.6±1.4µM); MCF-7/ADM (IC50=7.3±0.7µM); K562 (IC50=7.7±1.4µM); K562/ADM (IC50=9.3±1.7µM) Rabbit erythrocytes: 5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=67.4±8.3µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32014 KKLFKKILKQL 11 BP100 [Y10Q] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=53.3±4.5µM); MCF-7 (IC50=53.6±4.2µM); K562 (IC50=57.6±3.9µM); K562/ADM (IC50=58.3±6.2µM) Rabbit erythrocytes: 6.5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=77.9±5.6µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32015 KKLFKKILKRL 11 BP100 [Y10R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/ADM (IC50=57.3±4.5µM); MCF-7 (IC50=59.4±2.9µM); K562 (IC50=60.8±5.3µM); K562/ADM (IC50=71.2±4.7µM) Rabbit erythrocytes: 5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50>100µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32016 KKLFKKILKTL 11 BP100 [Y10T] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=32.2±2.2µM); MCF-7/ADM (IC50=33.7±3.9µM); MCF-7 (IC50=36.9±4.0µM); K562/ADM (IC50=39.5±3.7µM) Rabbit erythrocytes: 5% Hemolysis=160µM Linear Free Amidation L GES-1: IC50=82.8±9.2µM Not available 28474125 Amino Acids. 2017 Aug;49(8):1355-1364 Zhang B, Shi W, Li J, Liao C, Li M, Huang W, Qian H. Design, synthesis and biological evaluation of novel peptides as potential agents with anti-tumor and multidrug resistance-reversing activities DRAMP32017 FRRFFKWFRRFFKFF 15 FR-15 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=2.5 μM); MDA-MB-231 (IC50=3.15 μM); HeLa (IC50=4.9 μM); DLD-1 (IC50=6.7 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32018 FRRFFKWFRRPFKFF 15 FR11P Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=11 μM); DLD-1 (IC50=12.9 μM); Hep-G2 (IC50=4.8 μM); MDA-MB-231 (IC50=7.0 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32019 FRRFFKWPRRFFKFF 15 FR8P Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10.5 μM); DLD-1 (IC50=10.8 μM); Hep-G2 (IC50=4.2 μM); MDA-MB-231 (IC50=6.4 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32020 FRRFFKWPRRPFKFF 15 FR8, 11P Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=15 μM); HeLa (IC50=18.9 μM); DLD-1 (IC50=22 μM); MDA-MB-231 (IC50=27 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32021 FRRPFKWFRRFFKFF 15 FR4P Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=2.5 μM); MDA-MB-231 (IC50=6.3 μM); HeLa (IC50=7.7 μM); DLD-1 (IC50=9.4 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32022 FRRPFKWPRRFFKFF 15 FR4, 8P Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=13.8 μM); DLD-1 (IC50=15.3 μM); MDA-MB-231 (IC50=15.4 μM); Hep-G2 (IC50=5 μM) Not available Linear Free Free L Not available Not available 28483698 Acta Biomater. 2017 Jul 15;57:170-186. Tripathi AK, Kumari T, Tandon A, Sayeed M, Afshan T, Kathuria M, Shukla PK, Mitra K, Ghosh JK. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat DRAMP32023 KKLFKKILKY 10 B7 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: K562 (IC50=73.7±6.1 μM); MCF-7 (IC50=77.3±5.6 μM); MCF-7/ADM (IC50=97.3±11.4 μM); K562/Adr (IC50>100 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50>100 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32024 KKLFKKILKYLK 12 B1 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7 (IC50=15.7±1.5 μM); K562 (IC50=17.9±1.4 μM); MCF-7/ADM (IC50=18.2±1.3 μM); K562/Adr (IC50=19.1±2.1 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=52.3±4.5 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32025 KKLFKKILKYLKK 13 B2 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7 (IC50=30.8±3.4 μM); K562 (IC50=33.6±4.2 μM); MCF-7/ADM (IC50=36.1±6.7 μM); K562/Adr (IC50=39.6±5.7 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=89.6±7.2 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32026 KKLFKKILKYLKKL 14 B3 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7 (IC50=25.3±3.2 μM); MCF-7/ADM (IC50=28.4±3.1 μM); K562 (IC50=47.4±12.5 μM); K562/Adr (IC50>100 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50>100 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32027 KLKKLFKKILKY 12 B9 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7/ADM (IC50=30.6±5.7 μM); MCF-7 (IC50=38.3±2.5 μM); K562 (IC50=60.7±5.4 μM); K562/Adr (IC50=83.7±5.3 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=76.7±6.2 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32028 LKKLFKKILKY 11 B8 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7/ADM (IC50=10.9±1.2 μM); MCF-7 (IC50=7.6±1.4 μM); K562 (IC50=7.7±1.2 μM); K562/Adr (IC50=8.1±0.9 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=64.2±5.6 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32029 LKKLFKKILKYL 12 B4 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7 (IC50=5.9±0.2 μM); MCF-7/ADM (IC50=6.3±0.4 μM); K562 (IC50=6.6±0.5 μM); K562/Adr (IC50=7.7±0.4 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=73.7±4.5 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32030 LKKLFKKILKYLK 13 B5 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: K562 (IC50=26.5±1.5 μM); MCF-7 (IC50=27.3±2.4 μM); MCF-7/ADM (IC50=28.2±2.7 μM); K562/Adr (IC50=28.3±2.3 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=63.6±4.7 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32031 LKKLFKKILKYLKK 14 B6 Not available Not found antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis Tumor cells: MCF-7 (IC50=18.4±1.5 μM); K562 (IC50=19.2±2.3 μM); MCF-7/ADM (IC50=20.7±1.6 μM); K562/Adr (IC50=22.7±2.3 μM) Rabbit red blood cells: very low hemolytic activity even at the concentration of 160 μm(as show in fig.3) Linear Free Free L GES-1: IC50=77.9±5.2 μM Not available 28524273 Chem Biol Drug Des. 2017 Nov;90(5):972-980. Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities DRAMP32032 KAKAKAVSRSARAGLQFPVGRIHRHLK 27 Sphistin (12-38) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100 µg/ml) Crab haemocytes: Not active up to 100 µg/ml Linear Free Free L Not available Not available 28600196 Fish Shellfish Immunol. 2017 Aug;67:561-570. Ma XW, Hou L, Chen B, Fan DQ, Chen YC, Yang Y, Wang KJ. A truncated Sph12-38 with potent antimicrobial activity showing resistance against bacterial challenge in Oryzias melastigma DRAMP32033 IIGPVLGLIGKALGGLL 17 Bombinin H-BO Not available Not found skin secretion of Oriental fire-bellied toad, Bombina orientalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-HEP-1 (IC50=0.99 μM); Huh-7 (IC50=1.81 μM); Hep-G2 (IC50=2.88 μM) Human erythrocytes: Bombinin H-BO was found to lyse 38% of erythrocytes at concentration of 80.0 μm (128 mg/ml), and up to 85% at the concentration of 159.7 μm (256 mg/ml). Linear Free Amidation L Not available Not available 28636781 Chem Biol Drug Des. 2018 Jan;91(1):50-61. Zhou C, Wang Z, Peng X, Liu Y, Lin Y, Zhang Z, Qiu Y, Jin M, Wang R, Kong D. Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis DRAMP32034 kwfrvyrGiyrrr 13 D Tachyplesin [C3,7,12,16Del] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=9.814µM) Sheep erythrocytes: <1% Hemolysis=67µM Linear Free Amidation k=D-Lys; w=D-Trp; f=D-Phe; r=D-Arg; v=D-Val; y=D-Tyr; i=D-Ile Mix Not available Not available 28641565 Protein Pept Lett. 2017;24(7):590-598. Evans HG, Guthrie JW, Jujjavarapu M, Hendrickson N, Eitel A, Park Y, Garvey J, Newman R, Esckilsen D, Heyl DL. D-Amino Acid Analogues of the Antimicrobial Peptide CDT Exhibit Anti- Cancer Properties in A549, a Human Lung Adenocarcinoma Cell Line DRAMP32035 rrryiGryvrfwk 13 Reverse D Tachyplesin [C3,7,12,16Del] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=90.16µM) Sheep erythrocytes: <1% Hemolysis=8.4µM Linear Free Amidation k=D-Lys; w=D-Trp; f=D-Phe; r=D-Arg; v=D-Val; y=D-Tyr; i=D-Ile Mix Not available Not available 28641565 Protein Pept Lett. 2017;24(7):590-598. Evans HG, Guthrie JW, Jujjavarapu M, Hendrickson N, Eitel A, Park Y, Garvey J, Newman R, Esckilsen D, Heyl DL. D-Amino Acid Analogues of the Antimicrobial Peptide CDT Exhibit Anti- Cancer Properties in A549, a Human Lung Adenocarcinoma Cell Line DRAMP32036 RRRYIGRYVRFWK 13 Reverse Tachyplesin [C3,7,12,16Del] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12100µM) Sheep erythrocytes: <1% Hemolysis=540µM Linear Free Amidation L Not available Not available 28641565 Protein Pept Lett. 2017;24(7):590-598. Evans HG, Guthrie JW, Jujjavarapu M, Hendrickson N, Eitel A, Park Y, Garvey J, Newman R, Esckilsen D, Heyl DL. D-Amino Acid Analogues of the Antimicrobial Peptide CDT Exhibit Anti- Cancer Properties in A549, a Human Lung Adenocarcinoma Cell Line DRAMP32037 LVKRFKKFFRKLKKSVLL 18 I-3 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.3±0.3 μM); K562/ADM (IC50=12.9±0.3 μM); K562 (IC50=15.1±1.1 μM); HeLa (IC50=6.5±0.3 μM); MCF-7 (IC50=7.0±0.2 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=80.84±3.9 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32038 LVRRFRRFFRRLRRSVLL 18 I-7 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=14.3±0.2 μM); HeLa (IC50=4.2±0.8 μM); MCF-7 (IC50=5.9±0.1 μM); K562 (IC50=6.9±0.2 μM); K562/ADM (IC50=7.6±0.3 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=85.24±3.4 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32039 VKRFKKFFLKLKSV 14 I-8 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15.4±0.1 μM); MCF-7 (IC50=22.5±3.3 μM); K562 (IC50=24.4±3.3 μM); K562/ADM (IC50=54.8±6.1 μM); MCF-7/Taxol (IC50=65.2±4.2 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=74.58±5.9 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32040 VKRFKKFFRKLKKSVL 16 I-1 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=12.7±2.5 μM); K562/ADM (IC50=19.3±0.8 μM); K562 (IC50=26.5±0.9 μM); MCF-7/Taxol (IC50=31.1±5.1 μM); HeLa (IC50=9.8±1.5 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=50.62±6.1 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32041 VKRFKKFFRKLKKSVLL 17 I-2 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10.2±0.8 μM); MCF-7 (IC50=10.5±1.2 μM); K562 (IC50=20.4±3.3 μM); K562/ADM (IC50=20.7±1.1 μM); MCF-7/Taxol (IC50=30.2±2.4 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=64.15±3.7 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32042 VKRFKLFFRKLKSV 14 I-9 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16.5±0.4 μM); MCF-7 (IC50=31.1±2.2 μM); K562 (IC50=33.4±1.1 μM); MCF-7/Taxol (IC50=43.6±1.1 μM); K562/ADM (IC50=55.6±3.3 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=72.37±2.7 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32043 VRRFRLFFRRLRRSV 15 I-11 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=11.5±0.5 μM); HeLa (IC50=19.0±1.1 μM); K562/ADM (IC50=23.2±1.7 μM); MCF-7/Taxol (IC50=35.7±1.5 μM); K562 (IC50=9.46±0.5 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=70.73±3.5 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32044 VRRFRRFFLRLRRSV 15 I-10 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=13.5±1.4 μM); MCF-7 (IC50=16.2±3.8 μM); MCF-7/Taxol (IC50=21.5±2.7 μM); K562 (IC50=25.6±3.3 μM); K562/ADM (IC50=43.5±4.2 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=70.07±2.1 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32045 VRRFRRFFRRLRRSV 15 I-4 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10.7±0.5 μM); MCF-7 (IC50=16.9±2.1 μM); K562 (IC50=17.9±0.2 μM); K562/ADM (IC50=22.7±0.5 μM); MCF-7/Taxol (IC50=40.6±5.1 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=69.74±2.9 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32046 VRRFRRFFRRLRRSVL 16 I-5 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.5±0.7 μM); MCF-7/Taxol (IC50=16.8±0.8 μM); K562 (IC50=20.4±0.7 μM); HeLa (IC50=3.3±1.1 μM); MCF-7 (IC50=7.5±0.9 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=75.84±6.8 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32047 VRRFRRFFRRLRRSVLL 17 I-6 Not available Not found cationic host defense peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.3±0.3 μM); MCF-7/Taxol (IC50=15.1±1.0 μM); MCF-7 (IC50=3.8±0.4 μM); HeLa (IC50=7.9±0.9 μM); K562 (IC50=8.5±1.1 μM) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Amidation L HUVEC: IC50=82.37±4.4 μM Not available 28664269 Amino Acids. 2017 Sep;49(9):1601-1610. Dai Y, Cai X, Shi W, Bi X, Su X, Pan M, Li H, Lin H, Huang W, Qian H. Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane DRAMP32048 GGVCPKILKKCRRDSDCPGACICRGNGYCGSGSD 34 MCoTI-II Not available Not found Momordica cochinchinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50>>80µM) Not available Cyclic Free Free L Not available Not available 28669767 Biochim Biophys Acta Biomembr. 2017 Oct;1859(10):1986-2000 Strömstedt AA, Park S, Burman R, Göransson U. Bactericidal activity of cyclotides where phosphatidylethanolamine-lipid selectivity determines antimicrobial spectra DRAMP32049 GGVCPKILQRCRRDSDCPGACICRGNGYCGSGSD 34 MCoTI-I Not available Not found Momordica cochinchinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50>>32µM) Not available Cyclic Free Free L Not available Not available 28669767 Biochim Biophys Acta Biomembr. 2017 Oct;1859(10):1986-2000 Strömstedt AA, Park S, Burman R, Göransson U. Bactericidal activity of cyclotides where phosphatidylethanolamine-lipid selectivity determines antimicrobial spectra DRAMP32050 GLPVCGETCTLGTCSTQGCTCSWPICKRN 29 Kalata B7 [Y15S] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50>>40µM) Not available Cyclic Free Free L Not available Not available 28669767 Biochim Biophys Acta Biomembr. 2017 Oct;1859(10):1986-2000 Strömstedt AA, Park S, Burman R, Göransson U. Bactericidal activity of cyclotides where phosphatidylethanolamine-lipid selectivity determines antimicrobial spectra DRAMP32051 FpFw 4 [D-Trp]CJ-15,208 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=16.5±0.7 µM) Not available Cyclic Lactam Lactam p=D-Proline; w=D-Tryptophane Mix Not available Not available 28692379 Cancer Biol Ther. 2017 Aug 3;18(8):571-583. Mukhopadhyay A, Hanold LE, Thayele Purayil H, Gisemba SA, Senadheera SN, Aldrich JV. Macrocyclic peptides decrease c-Myc protein levels and reduce prostate cancer cell growth DRAMP32052 FpFW 4 CJ-15,208 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=10.1±0.9 µM) Not available Cyclic Lactam Not available p=D-Proline Mix Not available Not available 28692379 Cancer Biol Ther. 2017 Aug 3;18(8):571-583. Mukhopadhyay A, Hanold LE, Thayele Purayil H, Gisemba SA, Senadheera SN, Aldrich JV. Macrocyclic peptides decrease c-Myc protein levels and reduce prostate cancer cell growth DRAMP32053 FLGAIAQALTSLLGKL 16 temporin-ITa C0HL49 Not found skin secretions of the Italian stream frog Rana italica (Ranidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC50=100 μM); MDA-MB-231 (LC50=40 μM); A549 (LC50=45 μM) mouse erythrocytes: LC50=22 μM Linear Free α-amidated residue at the C-terminus α-amidated residue at the C-terminus L Not available Not available 28699258 J Pept Sci. 2017 Oct;23(10):769-776. Conlon JM, Musale V, Attoub S, Mangoni ML, Leprince J, Coquet L, Jouenne T, Abdel-Wahab YHA, Flatt PR, Rinaldi AC. Cytotoxic peptides with insulin-releasing activities from skin secretions of the Italian stream frog Rana italica (Ranidae) DRAMP32054 IVPFLLGMVPKLVCLITKKC 20 Brevinin-1ITa C0HL47 Not found skin secretions of the Italian stream frog Rana italica (Ranidae) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=18 μM); HT-29 (LC50=18 μM); MDA-MB-231 (LC50=8 μM) mouse erythrocytes: LC50=7 μM Linear Free Free L Not available Not available 28699258 J Pept Sci. 2017 Oct;23(10):769-776. Conlon JM, Musale V, Attoub S, Mangoni ML, Leprince J, Coquet L, Jouenne T, Abdel-Wahab YHA, Flatt PR, Rinaldi AC. Cytotoxic peptides with insulin-releasing activities from skin secretions of the Italian stream frog Rana italica (Ranidae) DRAMP32055 GXRRLXYKQRXVTYXRGR 18 Cyclic Gomesin [PYA1G, C2,6,11,15SeCys] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (CC50=1.4±0.2µM); MCF-7 (CC50=37.5±3.3µM); HL-60 (CC50=38.5±4.8µM); MM96L (CC50=4.6±0.2µM); CRL-1739 (CC50=51.0±4.6µM); HeLa (CC50>64µM) Human erythrocytes: 32.8±0.5% Hemolysis=64µM Cyclic Free Free X=Se-Cys L HFF-1: CC50=15.6±3.6µM; PBMC: CC50=15.5±0.8µM Not available 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. Troeira Henriques S, Lawrence N, Chaousis S, Ravipati AS, Cheneval O, Benfield AH, Elliott AG, Kavanagh AM, Cooper MA, Chan LY, Huang YH, Craik DJ. Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP32056 KXRRYXYRQRXVTYXRGR 18 Cyclic Gomesin [PYA1K;C2,6,11,15SeCys;L5Y;K8R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=2.3±0.2µM); MCF-7 (CC50=29.0±3.7µM); HL-60 (CC50=33.3±7.4µM); HeLa (CC50=36.2±2.8µM); CRL-1739 (CC50=46.2±7.6µM); K562 (CC50=6.4±0.6µM) Human erythrocytes: 20.9±3.1% Hemolysis=64µM Cyclic Free Free X=Se-Cys L HFF-1: CC50=30.8±2.0µM; PBMC: CC50=9.5±0.5µM Not available 28741926 ACS Chem Biol. 2017 Sep 15;12(9):2324-2334. Troeira Henriques S, Lawrence N, Chaousis S, Ravipati AS, Cheneval O, Benfield AH, Elliott AG, Kavanagh AM, Cooper MA, Chan LY, Huang YH, Craik DJ. Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties DRAMP32057 RRGLFKKLRRKIKKGFKKIFKRLPPVGVGVSIPLAGRR 38 As-CATH4 Not available Not found Alligator sinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (26±0.9% Cell death=200µg/ml); BGC-823 (58±1.5% Cell death=200µg/ml); BGC-823 (58±1.5% Cell death=200µg/ml) Human erythrocytes: 4±0.5% Hemolysis=200µg/ml Linear Free Free L CHO: 55±2.5% Cell death=200µg/ml Not available 28798159 Biochem J. 2017 Aug 10;474(16):2861-2885. Chen Y, Cai S, Qiao X, Wu M, Guo Z, Wang R, Kuang YQ, Yu H, Wang Y. As-CATH1-6, novel cathelicidins with potent antimicrobial and immunomodulatory properties from Alligator sinensis, play pivotal roles in host antimicrobial immune responses DRAMP32058 WDPYFAGVKKLTKAILAVRA 20 Lavracin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (EC50=(50-100)µM); MEC-7 (Not active up to 100 µM) Not available Linear Free Amidation L HDME: Not active up to 100 µM Not available 28799716 Small. 2017 Oct;13(40). Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Müller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G. Rational Design of Membrane-Pore-Forming Peptides. DRAMP32059 WGKFFAGVKKLTKAILAVRA 20 Lavracin [D2G,P3K,Y4F] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (EC50=25µM) Not available Linear Free Amidation L HDME: Not active up to 100 µM Not available 28799716 Small. 2017 Oct;13(40). Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Müller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G. Rational Design of Membrane-Pore-Forming Peptides. DRAMP32060 WDPYFAGVKKLTKAILGEIA 20 Lavracin [A17G,V18E,R19I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (Not active up to 100 µM) Not available Linear Free Amidation L HDME: Not active up to 100 µM Not available 28799716 Small. 2017 Oct;13(40). Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Müller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G. Rational Design of Membrane-Pore-Forming Peptides. DRAMP32061 WGKFFAGVKKLTKAILGEIA 20 Lavracin [D2G,P3K,Y4F,A17G,V18E,R19I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (EC50=25µM) Not available Linear Free Amidation L HDME: Not active up to 100 µM Not available 28799716 Small. 2017 Oct;13(40). Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Müller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G. Rational Design of Membrane-Pore-Forming Peptides. DRAMP32062 IKKILSKIKKLLK 13 L-K6 Not available Not found some cationic antimicrobial peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=23 μM ); MCF-7 (IC50=31 μM ); MCF-7 (IC50=34 μM ); MCF-7 (IC50=38 μM ) Rabbit red blood cells: modest hemolytic activity(as show in Fig.2) Linear Free Free L HUVEC: IC50=65.88±4.5 μM Not available 28811617 Sci Rep. 2017 Aug 15;7(1):8293. Wang C, Dong S, Zhang L, Zhao Y, Huang L, Gong X, Wang H, Shang D. Cell surface binding, uptaking and anticancer activity of L-K6, a lysine/leucine-rich peptide, on human breast cancer MCF-7 cells DRAMP32063 FLSLIPAAISAVSALANHF 19 Phylloseptin-PHa Not available Not found Pithecopus hypochondrialis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (LD50=24.05µM); MDA-MB-435S (LD50=28.48µM); U-251MG (LD50=34.67µM); HCT 116 (LD50=36.64µM); NCI-H157 (LD50=37.61µM); PC-3 (LD50=37.96µM) Horse erythrocytes: 10% Hemolysis=76.5µM; 50% Hemolysis=109.5µM; 50% Hemolysis=52.17µM Linear Free Amidation L Not available Not available 28850103 Molecules. 2017 Aug 29;22(9):1428. Liu J, Wu Q, Li L, Xi X, Wu D, Zhou M, Chen T, Shaw C, Wang L. Discovery of Phylloseptins that Defense against Gram-Positive Bacteria and Inhibit the Proliferation of the Non-Small Cell Lung Cancer Cell Line, from the Skin Secretions of Phyllomedusa Frogs DRAMP32064 FLSLIPKIAGGIAALAKHL 19 Phylloseptin-PT Not available Not found Phyllomedusa baltea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H157 (IC50=6.73µM) Horse erythrocytes: 10% Hemolysis=7.79µM; 50% Hemolysis=22.8µM Linear Free Amidation L Not available Not available 28850103 Molecules. 2017 Aug 29;22(9):1428. Liu J, Wu Q, Li L, Xi X, Wu D, Zhou M, Chen T, Shaw C, Wang L. Discovery of Phylloseptins that Defense against Gram-Positive Bacteria and Inhibit the Proliferation of the Non-Small Cell Lung Cancer Cell Line, from the Skin Secretions of Phyllomedusa Frogs DRAMP32065 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32066 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32067 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32068 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32069 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32070 XXLXAXX 7 Ilamycin B1 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32071 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32072 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32073 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32074 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32075 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32076 XXLXAXX 7 Ilamycin B2 Not available Not found Streptomyces atratus SCSIO ZH16 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=24.6 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32077 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32078 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32079 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32080 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32081 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32082 XXLXAXX 7 Ilamycin C Not available Not found Streptomyces atratus SCSIO ZH21 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50=7.4 µM; HUVEC: IC50=33.8 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32083 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32084 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32085 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32086 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32087 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32088 XXLXAXX 7 Ilamycin D Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-OH-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(8)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32089 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32090 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32091 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32092 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32093 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32094 XXLXAXX 7 Ilamycin E Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50=14.9 µM; HUVEC: IC50=18.6 µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32095 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32096 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.8 µM); MCF-7 (IC50=17.4 µM); CNE2 (IC50=24.5 µM); HeLa (IC50=7.1 µM); HepG2 (IC50=8.9 µm) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32097 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=3.2 µM); HeLa (IC50=3.3 µM); A549 (IC50=3.5 µM); MCF-7 (IC50=4.5 µM); CNE2 (IC50=6.8 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32098 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32099 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CNE2 (IC50=14.9 µM); HeLa (IC50=3.9 µM); MCF-7 (IC50=3.9 µM); HepG2 (IC50=4.9 µM); A549 (IC50=6.2 µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32100 XXLXAXX 7 Ilamycin F Not available Not found Streptomyces atratus SCSIO ZH25 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50µM); CNE2 (IC50>50µM); HeLa (IC50>50µM); HepG2 (IC50>50µM); MCF-7 (IC50>50µM) Not available Cyclic Free Free X(1)=Pre-Trp; X(2)=(2S)-2-Aminohex-4-enoic acid; X(4)=OH-METH-Leu; X(6)=N-Tyr; X(7)=METH-Leu L HL-7702 (L02): IC50>50µM; HUVEC: IC50>50µM Not available 28855504 Nat Commun. 2017 Aug 30;8(1):391. Ma J, Huang H, Xie Y, Liu Z, Zhao J, Zhang C, Jia Y, Zhang Y, Zhang H, Zhang T, Ju J. Biosynthesis of ilamycins featuring unusual building blocks and engineered production of enhanced anti-tuberculosis agents DRAMP32101 FTVAXFI 7 Bacteriocin ASP-1 Not available Not found Bacillus subtilis URID 12.1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=192µg/ml); MCF-7 (IC50=280µg/ml) Human erythrocytes: <5% Hemolysis=128µg/ml; 30% Hemolysis=256µg/ml Cyclic Acetylation Free X=dehydrobutyrine L Not available Not available 28887200 Int J Antimicrob Agents. 2018 Jan;51(1):89-97. Chalasani AG, Roy U, Nema S. Purification and characterization of a novel anti-staphylococcal peptide (ASP-1) from bacillus sp. URID 12.1 DRAMP32102 NPEKALEKLIAIQKAIKGMLNGWFTGVGFRRKR 33 LysAB2 P3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 200 µm) Human erythrocytes: 1.97% Hemolysis=4µM; <10% Hemolysis=256µM Linear Free Free L HaCat: Not active up to 200 µM Not available 28904355 Sci Rep. 2017 Sep 13;7(1):11477. Peng SY, You RI, Lai MJ, Lin NT, Chen LK, Chang KC. Highly potent antimicrobial modified peptides derived from the Acinetobacter baumannii phage endolysin LysAB2 DRAMP32103 FKARRWQWRMKKLGAFKARRWQWRMKKLGAKX 32 LfcinB (17-31)2 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-468 (IC50=11 μM); MDA-MB-231 (IC50=31 μM) Not available Linear Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32104 FKARRWQWRMKKLGAFKARRWQWRMKKLGAKXC 33 LfcinB (17-31)4 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-468 (IC50=5 μM); MDA-MB-231 (IC50=9 μM) Not available Tetrameric Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32105 RRWQWRRRWQWRKX 14 LfcinB (20–25)2 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=130 μM); MDA-MB-468 (IC50>100 μM) Not available Linear Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32106 RRWQWRRRWQWRKXC 15 LfcinB (20–25)4 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=15 μM); MDA-MB-468 (IC50=6 μM) Not available Tetrameric Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32107 RWQWRMKKLGRWQWRMKKLGKX 22 LfcinB (20–30)2 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=14 μM); MDA-MB-468 (IC50=5 μM) Not available Linear Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32108 RWQWRMKKLGRWQWRMKKLGKXC 23 LfcinB (20–30)4 Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-468 (IC50=2 μM); MDA-MB-231 (IC50=6 μM) Not available Tetrameric Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32109 CFKARRWQWRMKKLGAXC 18 LfcinB (17-31)cyc Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50>88 μM); MDA-MB-468 (IC50>88 μM) Not available Linear Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32110 CRRWQWRXC 9 LfcinB (20–25)cyc Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50>200 μM); MDA-MB-468 (IC50>200 μM) Not available Cyclic Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32111 RWQWRMKKLG 10 LfcinB (20–30) Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50>103 μM); MDA-MB-468 (IC50>103 μM) Not available Linear Free Free L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32112 CRWQWRMKKLGXC 13 LfcinB (20–30)cyc Not available Not found Bovine Lactoferricin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=7 μM); MDA-MB-468 (IC50>107 μM) Not available Linear Free Free X=Ahx L Not available Not available 28961215 Molecules. 2017 Sep 29;22(10):1641. Vargas Casanova Y, Rodríguez Guerra JA, Umaña Pérez YA, Leal Castro AL, Almanzar Reina G, García Castañeda JE, Rivera Monroy ZJ. Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines DRAMP32113 GFGCPFNARRCHRHCRSIRRRAGYCAGRLRLTCTCVR 37 HlDFS1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 20 µM); K562 (Not active up to 20 µM); THP-1 (Not active up to 20 µM) Human erythrocytes: <5% Hemolysis=10µM; 18% Hemolysis=20µM; 60% Hemolysis=50µM Cyclic Free Free L HEK293T: Not active up to 20 µM Not available 28969703 Parasit Vectors. 2017 Oct 2;10(1):455. Sun T, Pan W, Song Y, Zhang J, Wang J, Dai J. Functional characterization of two defensins, HlDFS1 and HlDFS2, from the hard tick Haemaphysalis longicornis DRAMP32114 GFGCPLNQGACHRHCRSIRRRGGYCSGIIKQTCTCY 36 HlDFS2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (Not active up to 20 µM); K562 (Not active up to 20 µM); THP-1 (Not active up to 20 µM) Human erythrocytes: <5% Hemolysis=50µM Cyclic Free Free L HEK293T: Not active up to 20 µM Not available 28969703 Parasit Vectors. 2017 Oct 2;10(1):455. Sun T, Pan W, Song Y, Zhang J, Wang J, Dai J. Functional characterization of two defensins, HlDFS1 and HlDFS2, from the hard tick Haemaphysalis longicornis DRAMP32115 ALWKEVLKNAGKAALNEINNLVQ 23 Dermaseptin-PH Not available Not found Phyllomedusa hypochondrialis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=0.69µM); PC-3 (IC50=11.8µM); NCI-H157 (IC50=2.01µM); U-251MG (IC50=2.36µM); MDA-MB-435S (IC50=9.94µM) Horse erythrocytes: 1% Hemolysis=16µM; 3% Hemolysis=64µM; 10% Hemolysis=128µM; 45% Hemolysis=256µM; 100% Hemolysis=512µM Linear Free Amidation L HMEC-1: IC50=4.85µM Not available 29064402 Molecules. 2017 Oct 24;22(10):1805. Huang L, Chen D, Wang L, Lin C, Ma C, Xi X, Chen T, Shaw C, Zhou M. Dermaseptin-PH: A Novel Peptide with Antimicrobial and Anticancer Activities from the Skin Secretion of the South American Orange-Legged Leaf Frog, Pithecopus (Phyllomedusa) hypochondrialis DRAMP32116 GIGSAILSAGKSIIKGLAKGLAEHF 25 Bombinin-BO1 Not available Not found Bombina orientalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-HEP-1 (IC50=0.76µM); HepG2 (IC50=3.75µM); Huh-7 (IC50=3.91µM) Human erythrocytes: 2.89% Hemolysis=26.3µM; Human erythrocytes=38.05% Hemolysis=52.5µM Linear Free Amidation L Not available Not available 29098406 Amino Acids. 2018 Feb;50(2):241-253 Peng X, Zhou C, Hou X, Liu Y, Wang Z, Peng X, Zhang Z, Wang R, Kong D. Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis DRAMP32117 GIGSAILSAGKSIIKGLAKGLA 22 Bombinin-BO1 A0A219CMY0 Not found skin secretion of Oriental fire-bellied toad, Bombina orientalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=0.76 μM); SK-HEP-1 (IC50=3.75 μM); Huh-7 (IC50=3.91 μM) Human Red cells: only 2.89% hemolysis of the red cells at a concentration of 26.3 μM and 38.05% hemolysis at 52.5 μM Linear Free Amidation L Not available Not available 29098406 Amino Acids. 2018 Feb;50(2):241-253 Peng X, Zhou C, Hou X, Liu Y, Wang Z, Peng X, Zhang Z, Wang R, Kong D. Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis DRAMP32118 IIGPVLGLVGKALGGLL 17 Bombinin H-BO1  Not available Not found skin secretion of Oriental fire-bellied toad, Bombina orientalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=3.61 μM); SK-HEP-1 (IC50=8.08 μM); Huh-7 (IC50=8.42 μM) Human Red cells: caused 42.03% hemolysis of the red cells at a concentration of 40.3 μM while reaching 100% hemolysis at 161.1 μM Linear Free Amidation L Not available Not available 29098406 Amino Acids. 2018 Feb;50(2):241-253 Peng X, Zhou C, Hou X, Liu Y, Wang Z, Peng X, Zhang Z, Wang R, Kong D. Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis DRAMP32119 FLSLIPKIATGIAALAKHL 19 PSN-PC Not available Not found Phyllomedusa camba Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H157 (IC50=2.85µM) Horse erythrocytes: 100% Hemolysis=64µM; Horse erythrocytes=50% Hemolysis=23µM Linear Free Amidation L HMEC-1: IC50=51.83µM Not available 29112170 Molecules. 2017 Nov 7;22(11):1896. Wu X, Pan J, Wu Y, Xi X, Ma C, Wang L, Zhou M, Chen T. PSN-PC: A Novel Antimicrobial and Anti-Biofilm Peptide from the Skin Secretion of Phyllomedusa-camba with Cytotoxicity on Human Lung Cancer Cell DRAMP32120 HLRRINKLLTRIGLYRHAFG 20 Lynronne-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (Not active up to 128 µg/ml) Human erythrocytes: 20% Hemolysis=500µg/ml; Sheep erythrocytes: 25% Hemolysis=500µg/ml Linear Free Free L HUVEC: Not active up to 128 µg/ml Not available 29214045 NPJ Biofilms Microbiomes. 2017 Dec 1;3:33. Oyama LB, Girdwood SE, Cookson AR, Fernandez-Fuentes N, Privé F, Vallin HE, Wilkinson TJ, Golyshin PN, Golyshina OV, Mikut R, Hilpert K, Richards J, Wootton M, Edwards JE, Maresca M, Perrier J, Lundy FT, Luo Y, Zhou M, Hess M, Mantovani HC, Creevey CJ, Huws SA. The rumen microbiome: an underexplored resource for novel antimicrobial discovery DRAMP32121 LPRRNRWSKIWKKVVTVFS 19 Lynronne-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=45.9µg/ml) Human erythrocytes: 20% Hemolysis=500µg/ml; Sheep erythrocytes: 10% Hemolysis=500µg/ml; Horse erythrocytes:0% Hemolysis=536µg/ml Linear Free Free L HUVEC: LC50=98.1µg/ml Not available 29214045 NPJ Biofilms Microbiomes. 2017 Dec 1;3:33. Oyama LB, Girdwood SE, Cookson AR, Fernandez-Fuentes N, Privé F, Vallin HE, Wilkinson TJ, Golyshin PN, Golyshina OV, Mikut R, Hilpert K, Richards J, Wootton M, Edwards JE, Maresca M, Perrier J, Lundy FT, Luo Y, Zhou M, Hess M, Mantovani HC, Creevey CJ, Huws SA. The rumen microbiome: an underexplored resource for novel antimicrobial discovery DRAMP32122 NRFTARFRRTPWRLCLQFRQ 20 Lynronne-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=24.4µg/ml) Human erythrocytes: 45% Hemolysis=500µg/ml; Sheep erythrocytes: 0% Hemolysis=500µg/ml Linear Free Free L HUVEC: LC50>128µg/ml Not available 29214045 NPJ Biofilms Microbiomes. 2017 Dec 1;3:33. Oyama LB, Girdwood SE, Cookson AR, Fernandez-Fuentes N, Privé F, Vallin HE, Wilkinson TJ, Golyshin PN, Golyshina OV, Mikut R, Hilpert K, Richards J, Wootton M, Edwards JE, Maresca M, Perrier J, Lundy FT, Luo Y, Zhou M, Hess M, Mantovani HC, Creevey CJ, Huws SA. The rumen microbiome: an underexplored resource for novel antimicrobial discovery DRAMP32123 RLLSLIRKLIT 11 [Arg]1 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=50.0 µmol/L) Human red blood cells: MHC=25.00 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32124 SFLSLIRKLIT 11 [Phe]2 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=50.0 µmol/L) Human red blood cells: MHC=3.12 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32125 SLLPLIRKLIT 11 [Pro]4 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=25.0 µmol/L) Human red blood cells: MHC=12.50 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32126 SLLSLFRKLI 10 [Phe]6 -Dec[Thr]11-Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=50.0 µmol/L) Human red blood cells: MHC=12.50 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32127 SLLSLFRKLIT 11 [Phe]6 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50>50 µmol/L) Human red blood cells: MHC=3.12 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32128 SLLSLIRKLIW 11 [Trp]11 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=25.0 µmol/L) Human red blood cells: MHC=1.56 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32129 SLLSLIRLLIT 11 [Leu]8 -Dec-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50>50 µmol/L) Human red blood cells: MHC=50.00 μmol/L Linear Free Amidation L Not available Not available 30013694 Beilstein J Org Chem. 2018 Jul 6;14:1693-1703. Torres MDT, Andrade GP, Sato RH, Pedron CN, Manieri TM, Cerchiaro G, Ribeiro AO, de la Fuente-Nunez C, Oliveira VX Jr. Natural and redesigned wasp venom peptides with selective antitumoral activity DRAMP32130 FIFHIIKGLFHAGKMIHGLVTRRRHGVEELQDLDQRAFEREKAFA 45 Em-Pis1 Not available Not found Epinephelus coioides; Epinephelus malabaricus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: N2a (65.6% Killing=20µM); A549 (73.5% Killing=20µM) Fish erythrocytes:25% Hemolysis=20µM; Rabbit erythrocytes:47% Hemolysis=20µM Linear Free Free L Not available Not available 30032476 Probiotics Antimicrob Proteins. 2019 Jun;11(2):667-675. Hu B, Pan Y, Li Z, Yuan W, Deng L. EmPis-1L, an Effective Antimicrobial Peptide Against the Antibiotic-Resistant VBNC State Cells of Pathogenic Bacteria DRAMP32131 CIKPHQGQHICNDE 14 VGB Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 4T1 (IC50=0.61 μM); U-87MG ATCC (IC50=0.92 μM) Not available Cyclic Free Free L Not available Not available 30251659 Biochim Biophys Acta Gen Subj. 2018 Dec;1862(12):2688-2700. Sadremomtaz A, Mansouri K, Alemzadeh G, Safa M, Rastaghi AE, Asghari SM. Dual blockade of VEGFR1 and VEGFR2 by a novel peptide abrogates VEGF-driven angiogenesis, tumor growth, and metastasis through PI3K/AKT and MAPK/ERK1/2 pathway DRAMP32132 GALKGCWTKSIPPKPCK 17 PE-BBI Not available Not found skin secretion of Pelophylax esculentus (PE) named PE-BBI Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=35.4 μM); DLD-1 (IC50=50.1 μM ); DKs-8 (IC50=9.8 μM ) Not available Linear Free Amidation L HKE3: IC50=50.2 μM Not available 30267012 Sci Rep. 2018 Sep 28;8(1):14502. Lyu P, Ge L, Ma R, Wei R, McCrudden CM, Chen T, Shaw C, Kwok HF. Identification and pharmaceutical evaluation of novel frog skin-derived serine proteinase inhibitor peptide-PE-BBI (Pelophylax esculentus Bowman-Birk inhibitor) for the potential treatment of cancer DRAMP32133 GIMDTVKNAAKNLAGQLLDKLK  23 R2PLx-22 Not available Not found skin secretions of the pickerel frog (Rana palustris) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (IC50=104.10 μM); MCF-7 (IC50=109.30 μM); PC-3 (IC50=283.90 μM); NCI-H157 (IC50=843.40 μM); MDA-MB-435S (IC50=872.70 μM) Horse erythrocytes: Low haemolytic activity Linear Free Free Mix HMEC-1: IC50=588.20 μM Not available 30279210 Biosci Rep. 2018 Nov 9;38(6):BSR20180710. Chen X, Zhang L, Ma C, Zhang Y, Xi X, Wang L, Zhou M, Burrows JF, Chen T. A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells DRAMP32134 GIMDTVKNAAKNLAGQLLDKLKCKITAC  29 R2PLx  Not available Not found skin secretions of the pickerel frog (Rana palustris) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-435S (IC50=15.44 μM); U-251MG (IC50=16.14 μM); MCF-7 (IC50=20.19 μM); PC-3 (IC50=5.79 μM); NCI-H157 (IC50=5.90 μM) Horse erythrocytes: Moderate haemolytic activity Linear Free Free Mix HMEC-1: IC50=79.50 μM Not available 30279210 Biosci Rep. 2018 Nov 9;38(6):BSR20180710. Chen X, Zhang L, Ma C, Zhang Y, Xi X, Wang L, Zhou M, Burrows JF, Chen T. A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells DRAMP32135 GIMDTVKNAAKNLAGQLLDKLKCSITAC 28 S-24-R2Plx  Not available Not found skin secretions of the pickerel frog (Rana palustris) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-435S (IC50=179.00 μM); U-251MG (IC50=278.30 μM); MCF-7 (IC50=316.90 μM); NCI-H157 (IC50=58.18 μM); PC-3 (IC50=792.60 μM) Horse erythrocytes: Low haemolytic activity Linear Free Free L HMEC-1: IC50=1185.00 μM Not available 30279210 Biosci Rep. 2018 Nov 9;38(6):BSR20180710. Chen X, Zhang L, Ma C, Zhang Y, Xi X, Wang L, Zhou M, Burrows JF, Chen T. A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells DRAMP32136 GCRLYGFKFHGCG 13 I192F Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=20.1 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32137 GCRLYGFKIFGCG 13 H193F Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=26.8 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32138 GCRLYGFKIHGCG 13 Pc Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=30.4 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32139 GCRLYGFKIWGG 12 H193W Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=19.4 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32140 GCRLYGFKWHGCG 13 I192W Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=72.9 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32141 GCRVYGFKIHGCG 13 L187V Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=38.9 µM) Not available Cyclic Free Free L Not available Protein kinase CK2 30307134 Mol Inform. 2019 Mar;38(3):e1800089. Tang S, Zhang N, Zhou Y, Cortopassi WA, Jacobson MP, Zhao LJ, Zhong RG. Structure-based Discovery of Novel CK2α-Binding Cyclic Peptides with Anti-cancer Activity DRAMP32142 PMKKLKLALRLAAKIAPVW 19 P-MerP fragment [F5K,A6L,A9R,V13K,V14I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (Not active up to 100 µM); MCF-7 (Not active up to 100 µM); PC-3 (Not active up to 100 µM) Human erythrocytes: Not active up to 100 µM Linear Free Free L 3T3-L1: Not active up to 100 µM; HUVEC: Not active up to 100 µM Not available 30346140 ACS Infect Dis. 2018 Dec 14;4(12):1727-1736. Cardoso MH, Cândido ES, Chan LY, Der Torossian Torres M, Oshiro KGN, Rezende SB, Porto WF, Lu TK, de la Fuente-Nunez C, Craik DJ, Franco OL. A Computationally Designed Peptide Derived from Escherichia coli as a Potential Drug Template for Antibacterial and Antibiofilm Therapies DRAMP32143 IWLTALKFLGKNLGKLAKQQLAKL 24 LyeTxI-b Not available Not found Lycosa erythrognatha spider venom Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG ATCC (IC50=20.94±5.18 μM ); U-87MG ATCC (IC50=29.20±7.96 μM); SH-SY5Y (IC50=93.80±2.17 μM ) hRBC(human blood red cells): IC50=155±13.04 μM (testing time is 48 h) Linear Free Free L Vero(African green monkey kidney): IC50≥100 μM (testing time is 48 h); PBMC(Peripheral Blood Mononuclear Cells): IC50=4.16±1.94 μM (testing time is 48 h); GM00637: IC50 ≥ 100 μM Not available 30449002 Amino Acids. 2019 Mar;51(3):433-449. Abdel-Salam MAL, Carvalho-Tavares J, Gomes KS, Teixeira-Carvalho A, Kitten GT, Nyffeler J, Dias FF, Dos Reis PVM, Pimenta AMC, Leist M, de Lima ME, de Souza-Fagundes EM. The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells DRAMP32144 HSDGIFTDSYSRYRKQMAVKKYLAAVLGRRYRQRFRNK 38 PACAP  P48144 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (IC50=14.97 ± 1.16 µM ) Human red blood cells: PACAP was not hemolytic for human erythrocytes at concentrations below 75 μM (0% hemolysis). At concentration between 75 μM and 150 μM the hemolytic activity was less than 3%; Fish red blood cells:PACAP was not hemolytic for fish red blood cells at concentrations below 18.75 μM (0% hemolysis). At concentration between 18.75 μM and 150 μM, the hemolytic activity was less than 20% Linear Free Free L Not available Not available 30481557 Fish Shellfish Immunol. 2019 Mar;86:559-570. Lugo JM, Tafalla C, Oliva A, Pons T, Oliva B, Aquilino C, Morales R, Estrada MP. Evidence for antimicrobial and anticancer activity of pituitary adenylate cyclase-activating polypeptide (PACAP) from North African catfish (Clarias gariepinus): Its potential use as novel therapeutic agent in fish and humans DRAMP32145 RRGCFRVCYRGFCFQRCR 18 PM III Not available Not found horseshoe crab Limulus polyphemus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50=2.5±0.1 μM); HeLa (IC50=6.0±0.2 μM); A549 (IC50=7.3±0.5 μM); SK-BR-3 (IC50=9.9±0.1 μM) Human red blood cells (hBRC): HC50=46 µM Linear Free Free L HEK 293T: IC50=7.3±0.4 μM; HEF: IC50=7.0±0.4 μM; NHA: IC50=7.5±0.5 μM Not available 30486233 Mar Drugs. 2018 Nov 26;16(12):466. Marggraf MB, Panteleev PV, Emelianova AA, Sorokin MI, Bolosov IA, Buzdin AA, Kuzmin DV, Ovchinnikova TV. Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III DRAMP32146 FKKLKKLFSKLWNWK 15 HPRP-A1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.5±0.03 μM); SGC-7901 (IC50=5.2±0.14 μM); B16 (IC50=6.1±0.02 μM); Hep-G2 (IC50=7.7±0.23 μM) Human red blood cells: MHC=32 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=24.2 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32147 FKKLKKLFSKLWNWK 15 HPRP-A1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (IC50=13.3 µM); BGC-823 (IC50=14.1 µM); A549 (IC50=14.8 µM); MCF-7 (IC50=15.7 µM); MDA-MB-231 (IC50=22.9 µM) Human red blood cells: MHC=32 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=24.2 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32148 FKKLKKLFSKLWNWKCRGDKGPDC 24 HPRP-A1-iRGD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=14.3 µM); MCF-7 (IC50=14.8 µM); NCI-H460 (IC50=15.2 µM); BGC-823 (IC50=18.5 µM); MDA-MB-231 (IC50=22.5 µM) Human red blood cells: MHC=125 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=26.5 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32149 FKKLKKLFSKLWNWKGGCRGDKGPDC 26 HPRP-A1-GG-iRGD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (IC50=12.9 µM); BGC-823 (IC50=14.8 µM); MDA-MB-231 (IC50=15.2 µM); MCF-7 (IC50=15.8 µM); A549 (IC50=21.6 µM) Human red blood cells: MHC=125 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=31.6 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32150 FKKLKKLFSKLWNWKGGRGD 20 HPRP-A1-GG-RGD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=11.1 µM); MCF-7 (IC50=11.8 µM); BGC-823 (IC50=15.7 µM); NCI-H460 (IC50=19.5 µM); MDA-MB-231 (IC50=27 µM) Human red blood cells: MHC=125 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=29.1 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32151 FKKLKKLFSKLWNWKRGD 18 HPRP-A1-RGD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (IC50=10.8 µM); MCF-7 (IC50=11.8 µM); NCI-H460 (IC50=14.6 µM); MDA-MB-231 (IC50=15.6 µM); A549 (IC50=8.4 µM) Human red blood cells: MHC=125 μM, MHC: the minimum hemolytic concentration is the concentration of peptide that results in 10% hemolysis of human red blood cells (hRBCs). Linear Free Free L HUVEC: IC50=31.6 μM Not available 30592418 Mol Pharm. 2019 Feb 4;16(2):561-572. Hu C, Huang Y, Chen Y. Targeted Modification of the Cationic Anticancer Peptide HPRP-A1 with iRGD To Improve Specificity, Penetration, and Tumor-Tissue Accumulation DRAMP32152 GRFKRFRKKLKRLWHKVGPFVGPILHY 27 ChMAP-28 Not available Not found Goat Antimicrobial Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (IC50=3.39±0.15 μM); B16-F1 (IC50=4.82±1.01 μM); SK-BR-3 (IC50=5.63±1.05 μM); A431 (IC50=6.49±0.09 μM) Human erythrocytes: ChMAP-28 has a low hemolytic activity (hemolysis less than 10%) at a concentration range up to 10 μM. Linear Free Free L HEK293T: IC50=5.09±0.40 μM; HEF: IC50=8.95±2.68 μM Not available 30622471 Front Pharmacol. 2018 Dec 21;9:1501. Emelianova AA, Kuzmin DV, Panteleev PV, Sorokin M, Buzdin AA, Ovchinnikova TV. Anticancer Activity of the Goat Antimicrobial Peptide ChMAP-28 DRAMP32153 RQCKAESNTFTGICIAKPPCRKACIREKFTDGHCSKVLRRCLCTKRC 47 NoD173(Q22K) Not available Not found Nicotiana occidentalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=0.70±0.07 μM); MM170 (IC50=0.87±0.04 μM); PC-3 (IC50=2.86±0.14 μM) Human red blood cells: with ∼12% lysis at the very high concentration (100 µM) Linear Free Free L HUVEC: IC50=6.20±0.07 μM; AHDF: IC50=6.49±0.13 μM Not available 30794440 FASEB J. 2019 May;33(5):6470-6482 Lay FT, Ryan GF, Caria S, Phan TK, Veneer PK, White JA, Kvansakul M, Hulett MD. Structural and functional characterization of the membrane-permeabilizing activity of Nicotiana occidentalis defensin NoD173 and protein engineering to enhance oncolysis DRAMP32154 RQCKAESNTFTGICIAKPPCRQACIREKFTDGHCSKVLRRCLCTKRC 47 NoD173 Not available Not found Nicotiana occidentalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=1.35±0.06 μM); MM170 (IC50=1.75±0.06 μM); PC-3 (IC50=6.31±0.099 μM) Human red blood cells: with ∼12% lysis at the very high concentration (100 µM) Linear Free Free L HUVEC: IC50=12.31±0.08 μM; AHDF: IC50=10.17±0.29 μM Not available 30794440 FASEB J. 2019 May;33(5):6470-6482 Lay FT, Ryan GF, Caria S, Phan TK, Veneer PK, White JA, Kvansakul M, Hulett MD. Structural and functional characterization of the membrane-permeabilizing activity of Nicotiana occidentalis defensin NoD173 and protein engineering to enhance oncolysis DRAMP32155 RQCKRESNTFTGICIAKPPCRQACIREKFTDGHCSKVLRRCLCTKRC 47 NoD173(A5R) Not available Not found Nicotiana occidentalis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=12.41±0.14 μM); MM170 (IC50=3.27±0.12 μM); HeLa (IC50=3.32±0.09 μM) Not available Linear Free Free L HUVEC: IC50=25.15±0.14 μM Not available 30794440 FASEB J. 2019 May;33(5):6470-6482 Lay FT, Ryan GF, Caria S, Phan TK, Veneer PK, White JA, Kvansakul M, Hulett MD. Structural and functional characterization of the membrane-permeabilizing activity of Nicotiana occidentalis defensin NoD173 and protein engineering to enhance oncolysis DRAMP32156 WEQKIEELLKKAEEQQKKNEEELKKLEKC 29 LP-83 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: TZM-bl (50% Cytotoxicity=12.34µM); C8166 (50% Cytotoxicity=19.19µM); MT-4 (50% Cytotoxicity=19.65µM); U-937 (50% Cytotoxicity=9.97µM) Not available Linear Acetylation Chol-NH2 L PBMC: 50% Cytotoxicity=40.27 µM; HEK293T cells: 50% Cytotoxicity=25.31 µM Not available 30867304 J Virol. 2019 May 15;93(11):e02312-18. Zhu Y, Chong H, Yu D, Guo Y, Zhou Y, He Y. Design and Characterization of Cholesterylated Peptide HIV-1/2 Fusion Inhibitors with Extremely Potent and Long-Lasting Antiviral Activity DRAMP32157 NGVQPKYKWWKWWKKWW 17 KT2 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available KT2 interacts with the plasma membrane and is then internalized into cells. Moreover, the KT2 peptide increases membrane permeability and induces cytotoxicity against cancer cells through DNA condensation, the increase of apoptotic factor protein levels, and autophagy suppression. Tumor cells: A431 (34% Cytotoxicity=10 µM); HCT 116 (IC50=50 µM); MDA-MB-231 (Not active up to 10 µM) Not available Linear Free Amidation L Not available Not available 31073999 J Cell Physiol. 2019 Dec;234(12):22116-22129. Maraming P, Klaynongsruang S, Boonsiri P, Peng SF, Daduang S, Leelayuwat C, Pientong C, Chung JG, Daduang J. The cationic cell-penetrating KT2 peptide promotes cell membrane defects and apoptosis with autophagy inhibition in human HCT 116 colon cancer cells DRAMP32158 KWCVYAYVKVKGVLVKYKKCW 21 Arenicin-1 [R1,9,11,16,18,19K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=7.7 µM) Human erythrocytes: 15% Hemolysis=10.1 µM; 50% Hemolysis=63 µM Cyclic Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP32159 INLKKLAARIKKKI 14 Mastoparan-L [A5K,L9R,A10I,I13K,L14I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 µM); MCF-7 (IC50>100 µM); PC-3 (IC50>100 µM) Human erythrocytes: 8% Hemolysis=100 µM Linear Free Amidation L "3T3-L1: 50% Cell death>100 µM ; HUVEC: 50% Cell death>100 µM" Not available 31411881 J Med Chem. 2019 Sep 12;62(17):8140-8151. Oshiro KGN, Cândido ES, Chan LY, Torres MDT, Monges BED, Rodrigues SG, Porto WF, Ribeiro SM, Henriques ST, Lu TK, de la Fuente-Nunez C, Craik DJ, Franco OL, Cardoso MH. Computer-Aided Design of Mastoparan-like Peptides Enables the Generation of Nontoxic Variants With Extended Antibacterial Properties DRAMP32160 KILKRLAAKIKKIL 14 Mastoparan-L [I1K,N2I,A5R,L9K,A10I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50>100 µM); MCF-7 (IC50>100 µM); PC-3 (IC50>100 µM) Human erythrocytes: 3% Hemolysis=100 µM Linear Free Amidation L "3T3-L1: 50% Cell death>100 µM ; HUVEC: 50% Cell death>100 µM" Not available 31411881 J Med Chem. 2019 Sep 12;62(17):8140-8151. Oshiro KGN, Cândido ES, Chan LY, Torres MDT, Monges BED, Rodrigues SG, Porto WF, Ribeiro SM, Henriques ST, Lu TK, de la Fuente-Nunez C, Craik DJ, Franco OL, Cardoso MH. Computer-Aided Design of Mastoparan-like Peptides Enables the Generation of Nontoxic Variants With Extended Antibacterial Properties DRAMP32161 LP 2 CLP Not available Not found marine natural metabolite Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-468 (IC50=67.4 μM); MDA-MB-231 (IC50=73.4 μM) Human red blood cells (RBC): LC50>401 μM Cyclic Lactam Lactam Lactam L MCF-12A: IC50>100 μM Not available 31669320 Chem Biol Interact. 2020 Jan 5;315:108872. Kgk D, Kumari S, G S, Malla RR. Marine natural compound cyclo(L-leucyl-L-prolyl) peptide inhibits migration of triple negative breast cancer cells by disrupting interaction of CD151 and EGFR signaling DRAMP32162 RFRPPIRRPPIRPPFWP 17 Bac5 (1-17)[Y16W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (19% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32163 RFRPPIRRPPIRPPFYR 17 Bac5 (1-17)[P17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (5% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32164 RFRPPIRRPPIRPPFYW 17 Bac5 (1-17)[P17W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (5% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32165 RFRRPIRRPPIRPPFYR 17 Bac5 (1-17)[P4,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (9% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32166 RFRRPIRRPPIRPPWYP 17 Bac5 (1-17)[P4R,F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (32% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32167 RFRRPIRRRPIRPPFWR 17 Bac5 (1-17)[P4,9,17R; Y16W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (10% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32168 RFRRPIRRRPIRPPFYP 17 Bac5 (1-17)[P4,9R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (Not active up to 32 µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32169 RFRRPIRRRPIRPPFYR 17 Bac5 (1-17)[P4,9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (13% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32170 RFRRPIRRRPIRPPWYR 17 Bac5 (1-17)[P4,9,17R; F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (5% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32171 RFRWPIRRPPIRPPFYR 17 Bac5 (1-17)[P4W, P4R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (Not active up to 32 µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32172 RFRWPIRRPPIRPPWYP 17 Bac5 (1-17)[P4W, F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (7% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32173 RFRWPIRRRPIRPPFWR 17 Bac5 (1-17)[P4W; P9,17R; Y16W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (20% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32174 RFRWPIRRRPIRPPFYP 17 Bac5 (1-17)[P4W, P9R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (2% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32175 RFRWPIRRRPIRPPFYR 17 Bac5 (1-17)[P4W; P9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (16% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32176 RFRWPIRRRPIRPPFYW 17 Bac5 (1-17)[P4,17W; P9R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (22% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32177 RFRWPIRRRPIRPPWYR 17 Bac5 (1-17)[P4W, P9R, F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (28% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32178 RRRRPIRRRPIRPPFYR 17 Bac5 (1-17)[F2R;P4,9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (Not active up to 32 µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32179 RRRRPIRRRPIRPPWYP 17 Bac5 (1-17)[F2R; P4,9R; F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (5% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32180 RRRRPIRRRPIRPPWYR 17 Bac5 (1-17)[F2R;P4,9,17R;F15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (5% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32181 RRRRPWRRRPIRPPFYW 17 Bac5 (1-17)[F2R; P4,9R; I6W; P17W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (23% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32182 RWRPPIRRPPIRPPWYP 17 Bac5 (1-17)[F2,15W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (25% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32183 RWRRPIRRPPIRPPFYP 17 Bac5 (1-17)[F2W, P4R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (16% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32184 RWRRPIRRPPIRPPFYR 17 Bac5 (1-17)[F2W; P4,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (11% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32185 RWRRPIRRPPIRPPWYP 17 Bac5 (1-17)[F2,15W; P4R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (17% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32186 RWRRPIRRRPIRPPFWR 17 Bac5 (1-17)[F2W; P4,9,17R; Y16W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (4% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32187 RWRRPIRRRPIRPPFYP 17 Bac5 (1-17)[F2W; P4,9R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (1% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32188 RWRRPIRRRPIRPPFYR 17 Bac5 (1-17)[F2W; P4,9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (1% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32189 RWRRPIRRRPIRPPFYW 17 Bac5 (1-17)[F2W; P4,9R; P17W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (19% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32190 RWRRPIRRRPIRPPWYP 17 Bac5 (1-17)[F2,15W; P4,9R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (9% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32191 RWRRPIRRRPIRPPWYR 17 Bac5 (1-17)[F2,15W; P4,9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (9% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32192 RWRRPWRRRPIRPPFYR 17 Bac5 (1-17)[F2W; P4,9,17R; I6W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (22% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32193 RWRWPIRRPPIRPPFYP 17 Bac5 (1-17)[F2W, P4W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (8% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32194 RWRWPIRRPPIRPPFYR 17 Bac5 (1-17)[F2W, P4W, P17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (14% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32195 RWRWPIRRPPIRPPWYP 17 Bac5 (1-17)[F2,15W; P4W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (10% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32196 RWRWPIRRRPIRPPFWR 17 Bac5 (1-17)[F2W; P4W; P9,17R; Y16W] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (27% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32197 RWRWPIRRRPIRPPWYR 17 Bac5 (1-17)[F2,15W; P4W; P9,17R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (41% Killing=32µM) Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033. Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E. Coli, K. Pneumoniae, and A. Baumannii. DRAMP32198 KSCFRVCYRGICYRRCRG 18 [W2S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-435S (CC50=18.9±0.9 µM ); MM96L (CC50=2.0±0.1 µM ); K562 (CC50=2.7±0.2 µM ); HeLa (CC50=22.5±2.1 µM ); HT-144 (CC50=3.0±0.2 µM ); WM164 (CC50=3.9±0.2 µM ) Human RBCs: CC50>32 µM Cyclic Free Free L HaCaT: CC50=41.4±2.6 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32199 KWCFKVCYKGICYKKCKG 18 [R/K]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50=13.4±1.9 µM ); K562 (CC50=2.5±0.1 µM ); MDA-MB-435S (CC50=3.5±0.4 µM ); WM164 (CC50=4.3±0.3 µM ) Human RBCs: CC50>32 µM Cyclic Free Free L HaCaT: CC50=31.1±2.1 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32200 KWCFRVCSRGSCYRRCRG 18 [Y8S-I11S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50>32 µM ); K562 (CC50>32 µM ); MDA-MB-435S (CC50>32 µM ); MM96L (CC50>32 µM ); WM164 (CC50>32 µM ); HT-144 (CC50>64 µM ) Human RBCs: CC50>32 µM Cyclic Free Free L HaCaT: CC50>64 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32201 KWCFRVCYRGFCYRRCRK 18 [I11F-G18K]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.3±0.1 µM ); K562 (CC50=1.9±0.1 µM ); WM164 (CC50=2.9±0.2 µM ); HT-144 (CC50=3.2±0.1 µM ); HeLa (CC50=5.1±0.3 µM ) Human RBCs: CC50=8.4±1.2 µM Cyclic Free Free L HaCaT: CC50=4.1±0.1 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32202 KWCFRVCYRGICYRRCRG 18 cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.3±0.1 µM ); HT-144 (CC50=1.4±0.1µM ); K562 (CC50=2.0±0.1 µM ); WM164 (CC50=2.7±0.1 µM ); MDA-MB-435S (CC50=2.7±0.3 µM ); MCF-7 (CC50=6.4±0.6 µM ); HeLa (CC50=6.7±0.6 µM ) Human RBCs: CC50=107±21 µM Cyclic Free Free L HaCaT: CC50=7.9±0.5 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32203 KWCFRVCYRGICYRRCRK 18 [G18K]cTI P14213##P69135 Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found 6PIN##1WO0##1MA2 Not available Tumor cells: MM96L (CC50=1.0±0.1 µM ); K562 (CC50=1.7±0.1 µM ); WM164 (CC50=2.7±0.2 µM ); HT-144 (CC50=3.2±0.1 µM ); HeLa (CC50=6.7±1.1 µM ) Human RBCs: CC50=6.9±0.3 µM Cyclic Free Free L HaCaT: CC50>64 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32204 KWCFRVCYRGICYRRCSG 18 [R17S]cTI P69135 Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found 1WO0##1MA2 Not available Tumor cells: HT-144 (CC50=1.2±0.1 µM ); MM96L (CC50=1.8±0.1 µM ); WM164 (CC50=1.8±0.1 µM ); HeLa (CC50=12.2±0.4 µM ); MDA-MB-435S (CC50=4.5±0.3 µM ) Human RBCs: CC50=10.3±0.4 µM Cyclic Free Free L HaCaT: CC50>64 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32205 KWCFRVCYRGICYSRCRG 18 [R14S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=1.7±0.1 µM ); HT-144 (CC50=2.3±0.2 µM ); WM164 (CC50=2.7±0.1 µM ); MDA-MB-435S (CC50=3.5±0.3 µM ); HeLa (CC50=7.5±0.3 µM ) Human RBCs: CC50=5.3±0.3 µM Cyclic Free Free L HaCaT: CC50>64 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32206 KWCFRVCYSGICYRRCRG 18 [R9S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-435S (CC50=5.3±0.6 µM ) Human RBCs: CC50>64 µM Cyclic Free Free L Not available Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32207 KWCFRVCYSGICYSRCSG 18 [R9S-R14S-R17S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: WM164 (CC50=11.1±0.9 µM ); HT-144 (CC50=11.8±0.9 µM ); K562 (CC50=4.8±0.3 µM ) Human RBCs: CC50=15.3±1.4 µM Cyclic Free Free L Not available Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32208 KWCSRVCYRGICSRRCRG 18 [F4S-Y13S]cTI Not available Not found host defense peptide from the horseshoe crab Tachypleus tridentatus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (CC50=13.2±0.9 µM ); MM96L (CC50=17.3±1.0 µM ); HT-144 (CC50=27.8±2.2 µM ); WM164 (CC50=28.2±2.0 µM ); HeLa (CC50>32 µM ); MCF-7 (CC50>32 µM ); MDA-MB-435S (CC50>64 µM ) Human RBCs: CC50>64 µM Cyclic Free Free L HaCaT: CC50>64 µM Not available 31714739 ACS Chem Biol. 2019 Dec 20;14(12):2895-2908. Vernen F, Craik DJ, Lawrence N, Troeira Henriques S. Cyclic Analogues of Horseshoe Crab Peptide Tachyplesin I with Anticancer and Cell Penetrating Properties DRAMP32209 SRSCLIVCQRLF 12 Cm-p5 [E4C, H8C] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (Not active up to 300 µg/ml) Not available Cyclic Free Amidation L Not available Not available 31763531 ACS Omega. 2019 Nov 5;4(21):19081-19095. Vicente FEM, González-Garcia M, Diaz Pico E, Moreno-Castillo E, Garay HE, Rosi PE, Jimenez AM, Campos-Delgado JA, Rivera DG, Chinea G, Pietro RCLR, Stenger S, Spellerberg B, Kubiczek D, Bodenberger N, Dietz S, Rosenau F, Paixão MW, Ständker L, Otero-González AJ. Design of a Helical-Stabilized, Cyclic, and Nontoxic Analogue of the Peptide Cm-p5 With Improved Antifungal Activity. DRAMP32210 AWWRRTVAKVRK 12 EeCentrocin 1 Chain A (1-12)[G1A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>100µM) Human erythrocytes:0% Hemolysis=25 µM; 1.6% Hemolysis=200 µM Linear Free Amidation L MRC-5: IC50>100 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32211 GAWRRTVAKVRK 12 EeCentrocin 1 Chain A (1-12)[W2A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25-200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32212 GWARRTVAKVRK 12 EeCentrocin 1 Chain A (1-12)[W3A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25-200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32213 GWWARTVAKVRK 12 EeCentrocin 1 Chain A (1-12)[R4A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25 µM; 3.6% Hemolysis=200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32214 GWWRATVAKVRK 12 EeCentrocin 1 Chain A (1-12)[R5A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25-200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32215 GWWRRTAAKVRK 12 EeCentrocin 1 Chain A (1-12)[V7A, D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25-200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32216 GWWRRTVAAVRK 12 EeCentrocin 1 Chain A (1-12)[D8A, K9A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25 µM; 5.1% Hemolysis=200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32217 GWWRRTVAKVAK 12 EeCentrocin 1 Chain A (1-12)[D8A, R11A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:0% Hemolysis=25-200 µM Linear Free Free L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32218 GWWRRTVAKVRK 12 EeCentrocin 1 Chain A (1-12)[D8A, N12K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes:2.4% Hemolysis=25 µM; 25.1% Hemolysis=200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32219 GWWRRTVAKVRNAGRK 16 EeCentrocin 1 Chain A (1-16)[D8A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes: 0% Hemolysis=25 µM; 5% Hemolysis=200 µM Linear Free Amidation L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32220 GWWRRTVDKVRNAGRK 16 EeCentrocin 1 Chain A (1-16) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>200µM) Human erythrocytes: 0% Hemolysis=25-200 µM Linear Free Free L MRC-5: IC50>200 µM Not available 31802582 J Pept Sci. 2020 Feb;26(2):e3233 Solstad RG, Johansen C, Stensvåg K, Strøm MB, Haug T. Structure-activity relationship studies of shortened analogues of the antimicrobial peptide EeCentrocin 1 from the sea urchin Echinus esculentus DRAMP32221 SNGYRPAYRPAYRPSYRP 18 Astacidin PcAst-1a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T24 (IC50>100 µM); MEC-1 (Not active up to 100 µM) Not available Linear Free Amidation L Not available Not available 31884202 Dev Comp Immunol. 2020 Apr;105:103574. Rončević T, Čikeš-Čulić V, Maravić A, Capanni F, Gerdol M, Pacor S, Tossi A, Giulianini PG, Pallavicini A, Manfrin C. Identification and functional characterization of the astacidin family of proline-rich host defence peptides (PcAst) from the red swamp crayfish (Procambarus clarkii, Girard 1852) DRAMP32222 SNVYRPPPYRPVYRPLRRPGYRP 23 Astacidin PcAst-1b/c Not available Not found Procambarus clarkii; Procambarus clarkii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T24 (IC50>100 µM); MEC-1 (Not active up to 100 µM) Not available Linear Free Amidation L Not available Not available 31884202 Dev Comp Immunol. 2020 Apr;105:103574. Rončević T, Čikeš-Čulić V, Maravić A, Capanni F, Gerdol M, Pacor S, Tossi A, Giulianini PG, Pallavicini A, Manfrin C. Identification and functional characterization of the astacidin family of proline-rich host defence peptides (PcAst) from the red swamp crayfish (Procambarus clarkii, Girard 1852) DRAMP32223 FYPRPYRPPYLPDPRPFPRPLPAFGHEFRRH 31 Astacidin PcAst-2 Not available Not found Procambarus clarkii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T24 (IC50>100 µM); MEC-1 (Not active up to 100 µM) Not available Linear Free Free L Not available Not available 31884202 Dev Comp Immunol. 2020 Apr;105:103574. Rončević T, Čikeš-Čulić V, Maravić A, Capanni F, Gerdol M, Pacor S, Tossi A, Giulianini PG, Pallavicini A, Manfrin C. Identification and functional characterization of the astacidin family of proline-rich host defence peptides (PcAst) from the red swamp crayfish (Procambarus clarkii, Girard 1852) DRAMP32224 GIKEXLCNMACAQTVCKKSGGPLCDTCQAACKALG 35 Turgencin B Mox1 Not available Not found Synoicum turgens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50=27.4 µM) Not available Cyclic Free Amidation X=MET-OXD L MRC-5: IC50> 50 µM Not available 31940927 Mar Drugs. 2020 Jan 12;18(1):51. Hansen IKØ, Isaksson J, Poth AG, Hansen KØ, Andersen AJC, Richard CSM, Blencke HM, Stensvåg K, Craik DJ, Haug T. Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens DRAMP32225 GIKEXLCNXACAQTVCKKSGGPLCDTCQAACKALG 35 Turgencin B Mox2 Not available Not found Synoicum turgens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50>50.0 µM) Not available Cyclic Free Amidation X=MET-OXD L MRC-5: IC50> 50 µM Not available 31940927 Mar Drugs. 2020 Jan 12;18(1):51. Hansen IKØ, Isaksson J, Poth AG, Hansen KØ, Andersen AJC, Richard CSM, Blencke HM, Stensvåg K, Craik DJ, Haug T. Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens DRAMP32226 GPKTKAACKXACKLATCGKKPGGWKCKLCELGCDAV 36 Turgencin A Not available Not found Synoicum turgens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2058 (IC50=1.4 µM) Not available Cyclic Free Amidation X=MET-OXD L MRC-5: IC50=4.8 µM Not available 31940927 Mar Drugs. 2020 Jan 12;18(1):51. Hansen IKØ, Isaksson J, Poth AG, Hansen KØ, Andersen AJC, Richard CSM, Blencke HM, Stensvåg K, Craik DJ, Haug T. Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens DRAMP32227 ILPWKWPWWPWKK 13 Indolicidin-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=26.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32228 RAWVAWR 7 LysH Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32229 CLBCREKAKKLFKKILKKL 19 BP329 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CAPAN-1 (IC50=33.0 ± 1.0 µM); MCF-7 (IC50=35.2 ± 1.8 µM); 22Rv1 (LC50=50 µM); CL1 (LC50>100 µM) Not available Linear Free Amidation L NIH 3T3: IC50=33.7 ± 1.9 µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63. Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP32230 VXXFPWWWPFLXX 13 Tritrp-Agb Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50=34.6 µM Linear Free Amidation X=Agb=(S)-2-amino-4 guanidinobutyric acid L PBMC: IC50=9.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32231 VXXFPWWWPFLXX 13 Tritrp-Agb Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≤ 6.5 µM) RBC: IC50=34.6 µM Linear Free Amidation X=Agb=(S)-2-amino-4 guanidinobutyric acid L PBMC: IC50=9.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32232 VXXFPWWWPFLXX 13 Tritrp-Agb Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50=34.6 µM Linear Free Amidation X=Agb=(S)-2-amino-4 guanidinobutyric acid L PBMC: IC50=9.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32233 VXXFPWWWPFLXX 13 Tritrp-Agb Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=13.3 µM) RBC: IC50=34.6 µM Linear Free Amidation X=Agb=(S)-2-amino-4 guanidinobutyric acid L PBMC: IC50=9.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32234 VXXFPWWWPFLXX 13 Tritrp-Dab Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dab=2,4-diaminobutyric acid L PBMC: IC50=25.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32235 VXXFPWWWPFLXX 13 Tritrp-Dab Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≤ 6.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dab=2,4-diaminobutyric acid L PBMC: IC50=25.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32236 VXXFPWWWPFLXX 13 Tritrp-Dab Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dab=2,4-diaminobutyric acid L PBMC: IC50=25.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32237 VXXFPWWWPFLXX 13 Tritrp-Dab Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=13.3 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dab=2,4-diaminobutyric acid L PBMC: IC50=25.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32238 VXXFPWWWPFLXX 13 Tritrp-Dap Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dap=2,3-diaminopropionic acid L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32239 VXXFPWWWPFLXX 13 Tritrp-Dap Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≤ 6.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dap=2,3-diaminopropionic acid L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32240 VXXFPWWWPFLXX 13 Tritrp-Dap Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dap=2,3-diaminopropionic acid L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32241 VXXFPWWWPFLXX 13 Tritrp-Dap Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=13.3 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=Dap=2,3-diaminopropionic acid L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32242 VXXFPWWWPFLXX 13 Tritrp-hArg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50=41.3 µM Linear Free Amidation X=hArg=homo-arginine L PBMC: IC50=19.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32243 VXXFPWWWPFLXX 13 Tritrp-hArg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≤ 6.5 µM) RBC: IC50=41.3 µM Linear Free Amidation X=hArg=homo-arginine L PBMC: IC50=19.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32244 VXXFPWWWPFLXX 13 Tritrp-hArg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50=41.3 µM Linear Free Amidation X=hArg=homo-arginine L PBMC: IC50=19.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32245 VXXFPWWWPFLXX 13 Tritrp-hArg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=13.3 µM) RBC: IC50=41.3 µM Linear Free Amidation X=hArg=homo-arginine L PBMC: IC50=19.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32246 VKKFAWWWAFLKK 13 Tritrp-P59A-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=14.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=27.6 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32247 VKKFAWWWPFLKK 13 Tritrp-P5A-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=27.6 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=27.6 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32248 VKKFPWWWAFLKK 13 Tritrp-P9A-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=15.1 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=22.5 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32249 VKKFPWWWPFLKK 13 Tritrp-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=11.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=41.0 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32250 VOOFPWWWPFLOO 13 Tritrp-Orn Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≤ 6.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation O=Ornithine L PBMC: IC50=38.1 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32251 VRRFAWWWPFLRR 13 Tritrp-P5A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found 2I1H Not available Tumor cells: Jurkat (IC50=16.2 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=26.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32252 VRRFPXXXPFLRR 13 Tritrp-W678bTA Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50=12.2 µM Linear Free Amidation X=bTA=β-3-benzothienyl-1-Ala L PBMC: IC50=16.5 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32253 VRRFPXXXPFLRR 13 Tritrp-W678bTA Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=44.8 µM) RBC: IC50=12.2 µM Linear Free Amidation X=bTA=β-3-benzothienyl-1-Ala L PBMC: IC50=16.5 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32254 VRRFPXXXPFLRR 13 Tritrp-W678hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=9.6 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan; bTA L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32255 VRRFPXXXPFLRR 13 Tritrp-W678hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=44.8 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan; bTA L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32256 VRRFPXWWPFLRR 13 Tritrp-W6hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=16.1 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan; bTA L PBMC: IC50=39.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32257 VRRFPAAAPFLRR 13 Tritrp-W678A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32258 VRRFPAAWPFLRR 13 Tritrp-W67A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32259 VRRFPAWAPFLRR 13 Tritrp-W68A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32260 VRRFPAWWPFLRR 13 Tritrp-W6A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=36.5 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32261 VRRFPWXWPFLRR 13 Tritrp-W7hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=15.1 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan; bTA L PBMC: IC50=24.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32262 VRRFPWAAPFLRR 13 Tritrp-W78A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32263 VRRFPWAWPFLRR 13 Tritrp-W7A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=48.2 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32264 VRRFPWWXPFLRR 13 Tritrp-W8hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=10.7 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan; bTA L PBMC: IC50=23.9 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32265 VRRFPWWAPFLRR 13 Tritrp-W8A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=22.8 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=52.1 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32266 VRRFPWWWAFLRR 13 Tritrp-P9A Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found 2I1I Not available Tumor cells: Jurkat (IC50=6.8 µM) RBC: IC50=29.3 µM Linear Free Amidation L PBMC: IC50=12.8 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32267 VRRFPWWYPFLRR 13 Tritrp-W8Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=12.0 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=21.6 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32268 VRRFPWYWPFLRR 13 Tritrp-W7Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=11.4 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=26.4 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32269 VRRFPWYYPFLRR 13 Tritrp-W78Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=25.6 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32270 VRRFPYWWPFLRR 13 Tritrp-W6Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=19.3 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=34.5 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32271 VRRFPYWYPFLRR 13 Tritrp-W68Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=35.4 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32272 VRRFPYYWPFLRR 13 Tritrp-W67Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=32.2 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32273 VRRFPYYYPFLRR 13 Tritrp-W678Y Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32274 RWKLFKKIEKVGRNVRDGLIKAGPAIAVIGQAKSLGK 37 anti-HIV AMPs Molecule 3 Not available Not found Bombyx mori Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HepG2 (20% Killing=100 µg/ml)" Not available Linear Free Free L HEK293T: 40% Killing=100µM Not available 32322274 Int J Microbiol. 2020 Apr 8;2020:2131535. Tincho MB, Morris T, Meyer M, Pretorius A. Antibacterial Activity of Rationally Designed Antimicrobial Peptides DRAMP32275 GFLKKIGKKLEGAVQRTRDATIQTIAVAQAAANVAATAKQ 40 EtCec1-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (Not active up to 1655 µg/ml) Human erythrocytes: Not active up to 1024 µg/ml Linear Free Amidation L Not available Not available 32344933 Microorganisms. 2020 Apr 25;8(5):626 Hirsch R, Wiesner J, Bauer A, Marker A, Vogel H, Hammann PE, Vilcinskas A. Antimicrobial Peptides from Rat-Tailed Maggots of the Drone Fly Eristalis tenax Show Potent Activity against Multidrug-Resistant Gram-Negative Bacteria DRAMP32276 GFLKKVGKKLEGASDLTRDATIQTIAVAQAAANVAATAKQ 40 EtCec3-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (Not active up to 1622 µg/ml) Human erythrocytes: Not active up to 1024 µg/ml Linear Free Amidation L Not available Not available 32344933 Microorganisms. 2020 Apr 25;8(5):626 Hirsch R, Wiesner J, Bauer A, Marker A, Vogel H, Hammann PE, Vilcinskas A. Antimicrobial Peptides from Rat-Tailed Maggots of the Drone Fly Eristalis tenax Show Potent Activity against Multidrug-Resistant Gram-Negative Bacteria DRAMP32277 GWLRDFGKRIERTGQNIRDATIQTIGIAQEAANVAATLK 39 EtCec2-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (Not active up to 535 µg/ml) Human erythrocytes: Not active up to 512 µg/ml Linear Free Amidation L Not available Not available 32344933 Microorganisms. 2020 Apr 25;8(5):626 Hirsch R, Wiesner J, Bauer A, Marker A, Vogel H, Hammann PE, Vilcinskas A. Antimicrobial Peptides from Rat-Tailed Maggots of the Drone Fly Eristalis tenax Show Potent Activity against Multidrug-Resistant Gram-Negative Bacteria DRAMP32278 QFNMQGGGSPRQGFDVNANARFPIWQSQNARNSVHGTASYAQHLGGPYGNSRPNFGGGLQFT 62 EtDip Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (Not active up to 1330 µg/ml) Human erythrocytes: Not active up to 1024 µg/ml Linear Free Free L Not available Not available 32344933 Microorganisms. 2020 Apr 25;8(5):626 Hirsch R, Wiesner J, Bauer A, Marker A, Vogel H, Hammann PE, Vilcinskas A. Antimicrobial Peptides from Rat-Tailed Maggots of the Drone Fly Eristalis tenax Show Potent Activity against Multidrug-Resistant Gram-Negative Bacteria DRAMP32279 GFPCGESCVYIPCFTAAIGCSCKSKVCYKN 30 Hyen D C0HLN8 Not found medicinal herb Hybanthus enneaspermus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (CC50=0.52±0.03 µM ); MCF-7 (CC50=0.75±0.05 µM ); HeLa (CC50=0.88±0.05 µM ) Human red blood cells (hRBCs): HC50=24.56±2.16 µM Cyclic Free Free L HUVEC:CC50=0.62±0.01 µM, testing time is 24h Not available 32414842 J Biol Chem. 2020 Aug 7;295(32):10911-10925. Du Q, Chan LY, Gilding EK, Henriques ST, Condon ND, Ravipati AS, Kaas Q, Huang YH, Craik DJ. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus DRAMP32280 GIPCAESCVYIPCTVTALLGCSCSDKVCYN 30 Hyen L C0HLP6 Not found medicinal herb Hybanthus enneaspermus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (CC50=1.54±0.08 µM ); HeLa (CC50=2.00±0.04 µM ); MCF-7 (CC50=3.34±0.28 µM ) Human red blood cells (hRBCs): HC50>50 µM Cyclic Free Free L HUVEC: CC50=2.06±0.08 µM , testing time is 24h Not available 32414842 J Biol Chem. 2020 Aug 7;295(32):10911-10925. Du Q, Chan LY, Gilding EK, Henriques ST, Condon ND, Ravipati AS, Kaas Q, Huang YH, Craik DJ. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus DRAMP32281 GTHPCQETCVTSTRCSTQGCHCNWPICFKN 30 Hyen C C0HLN7 Not found medicinal herb Hybanthus enneaspermus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50>8 µM ) Not available Cyclic Free Free L Not available Not available 32414842 J Biol Chem. 2020 Aug 7;295(32):10911-10925. Du Q, Chan LY, Gilding EK, Henriques ST, Condon ND, Ravipati AS, Kaas Q, Huang YH, Craik DJ. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus DRAMP32282 GVPCGESCVYIPCFTGIINCSCRDKVCYNN 30 Hyen E C0HLN9 Not found medicinal herb Hybanthus enneaspermus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50=2.64±0.09 µM ); K562 (CC50=2.85±0.09 µM ); MCF-7 (CC50=3.73±0.25 µM ) Human red blood cells (hRBCs): HC50>50 µM Cyclic Free Free L HUVEC: CC50=2.06±0.08 µM , testing time is 24h Not available 32414842 J Biol Chem. 2020 Aug 7;295(32):10911-10925. Du Q, Chan LY, Gilding EK, Henriques ST, Condon ND, Ravipati AS, Kaas Q, Huang YH, Craik DJ. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus DRAMP32283 SIPCAESCVWIPCTVTALLGCSCSDKVCYN 30 Hyen M C0HLP Not found medicinal herb Hybanthus enneaspermus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (CC50=1.16±0.03 µM ); HeLa (CC50=1.34±0.04 µM ); MCF-7 (CC50=2.36±0.16 µM ) Human red blood cells (hRBCs): HC50>50 µM Cyclic Free Free L HUVEC: CC50=1.38±0.03 µM, testing time is 24h Not available 32414842 J Biol Chem. 2020 Aug 7;295(32):10911-10925. Du Q, Chan LY, Gilding EK, Henriques ST, Condon ND, Ravipati AS, Kaas Q, Huang YH, Craik DJ. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus DRAMP32284 ALWKDMLKGIGKLAGKAALGAVKTLV 26 Dermaseptin-PP Not available Not found Phyllomedusa palliata Skin Secretions Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H157 (IC50=1.55 μM); U-251MG (IC50=2.47 μM); MCF-7 (IC50=2.92 μM); PC-3 (IC50=4.15 μM) Horse erythrocytes: Dermaseptin-PP exhibited only a moderate hemolytic effect (<20% at 16 μM with a calculated HC50 of 38.77 μM) Linear Free Free L Not available Not available 32582642 Front Chem. 2020 Jun 5;8:476. Dong Z, Hu H, Yu X, Tan L, Ma C, Xi X, Li L, Wang L, Zhou M, Chen T, Du S, Lu Y. Novel Frog Skin-Derived Peptide Dermaseptin-PP for Lung Cancer Treatment: In vitro/vivo Evaluation and Anti-tumor Mechanisms Study DRAMP32285 FIQHLIPLIPHAIQGIKDIF 20 Kassinatuerin-3  Not available Not found Skin Secretion of the African Frog, Kassina senegalensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (IC50=1.67 μM); NCI-H838 (IC50=10.3 μM); U-251MG (IC50=13.20 μM ); NCI-H157 (IC50=21.54 μM); LNCaP (IC50=3.79 μM); NCI-H23 (IC50=4.52 μM) Human RBCs: Kassinatuerin-3 produced no detectable hemolysis activity up to a concentration of 160 μM Linear Free Amidation L Not available Not available 32630734 Biology (Basel). 2020 Jul 2;9(7):148. Wang H, He H, Chen X, Zhou M, Wei M, Xi X, Ma C, Du Q, Chen T, Shaw C, Wang L. A Novel Antimicrobial Peptide (Kassinatuerin-3) Isolated from the Skin Secretion of the African Frog, Kassina senegalensis DRAMP32286 GLLKRIKXLL 10 Anoplin [T8Beta-Ala] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HeLa (30% Killing=256 µM)" Horse erythrocytes : 0% Hemolysis=256µM Linear Free Amidation X(8)=Beta-Ala L HEK293T: 17% Hemolysis=256µM Not available 32654770 Int J Med Microbiol. 2020 Jul;310(5):151433. Zhong C, Zhu Y, Zhu N, Liu T, Gou S, Zhang F, Yao J, Xie J, Ni J. Synthesis and anti-pseudomonal activity of new ß-Ala modified analogues of the antimicrobial peptide anoplin DRAMP32287 XLLKRIKTLL 10 Anoplin [G1Beta-Ala] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HeLa (20% Killing=256 µM)" Horse erythrocytes : <5% Hemolysis=256µM Linear Free Amidation X(1)=Beta-Ala L HEK293T: 15% Hemolysis=256µM Not available 32654770 Int J Med Microbiol. 2020 Jul;310(5):151433. Zhong C, Zhu Y, Zhu N, Liu T, Gou S, Zhang F, Yao J, Xie J, Ni J. Synthesis and anti-pseudomonal activity of new ß-Ala modified analogues of the antimicrobial peptide anoplin DRAMP32288 XXGXGXXXA 9 Desmethoxymajusculamide C Not available Not found Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=0.02µM); MDA-MB-435 (IC50=0.022µM); NCI-H460 (IC50=0.063µM); N2a (IC50>1.0µM) Not available Cyclic Free Free X(1)=3-amino-2-methylpentanoic acid; X(2)=2-hydroxy-3-methylpentanoate; X(4)=METH-Ile; X(6)=METH-Val; X(7)=METH-Phe; X(8)=4-amino-2,2-dimethyl-3-oxo-pentanoate L Not available Not available 19489598 J Nat Prod. 2009 Jun;72(6):1011-6. Simmons TL, Nogle LM, Media J, Valeriote FA, Mooberry SL, Gerwick WH. Desmethoxymajusculamide C, a cyanobacterial depsipeptide with potent cytotoxicity in both cyclic and ring-opened forms DRAMP32289 XXGXGXXXA 9 Desmethoxymajusculamide C Not available Not found Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=0.016µM); NCI-H460 (IC50=0.094µM); MDA-MB-435 (IC50=0.23µM); N2a (IC50>1.0µM) Not available Cyclic Free Free X(1)=3-amino-2-methylpentanoic acid; X(2)=2-hydroxy-3-methylpentanoate; X(4)=METH-Ile; X(6)=METH-Val; X(7)=METH-Phe; X(8)=4-amino-2,2-dimethyl-3-oxo-pentanoate L Not available Not available 19489598 J Nat Prod. 2009 Jun;72(6):1011-6. Simmons TL, Nogle LM, Media J, Valeriote FA, Mooberry SL, Gerwick WH. Desmethoxymajusculamide C, a cyanobacterial depsipeptide with potent cytotoxicity in both cyclic and ring-opened forms DRAMP32290 XXGXGXXXA 9 Linear Desmethoxymajusculamide C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=0.02µM); MDA-MB-435 (IC50=0.022µM); NCI-H460 (IC50=0.063µM); N2a (IC50>1.0µM) Not available Linear Free Free X(1)=3-amino-2-methylpentanoic acid; X(2)=2-hydroxy-3-methylpentanoate; X(4)=METH-Ile; X(6)=METH-Val; X(7)=METH-Phe; X(8)=4-amino-2,2-dimethyl-3-oxo-pentanoate L Not available Not available 19489598 J Nat Prod. 2009 Jun;72(6):1011-6. Simmons TL, Nogle LM, Media J, Valeriote FA, Mooberry SL, Gerwick WH. Desmethoxymajusculamide C, a cyanobacterial depsipeptide with potent cytotoxicity in both cyclic and ring-opened forms DRAMP32291 XXGXGXXXA 9 Linear Desmethoxymajusculamide C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=0.016µM); NCI-H460 (IC50=0.094µM); MDA-MB-435 (IC50=0.23µM); N2a (IC50>1.0µM) Not available Linear Free Free X(1)=3-amino-2-methylpentanoic acid; X(2)=2-hydroxy-3-methylpentanoate; X(4)=METH-Ile; X(6)=METH-Val; X(7)=METH-Phe; X(8)=4-amino-2,2-dimethyl-3-oxo-pentanoate L Not available Not available 19489598 J Nat Prod. 2009 Jun;72(6):1011-6. Simmons TL, Nogle LM, Media J, Valeriote FA, Mooberry SL, Gerwick WH. Desmethoxymajusculamide C, a cyanobacterial depsipeptide with potent cytotoxicity in both cyclic and ring-opened forms DRAMP32292 RKIKRYLRRMI 11 Ovalbumin (277-287)[V5R, P8R, K11I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HeLa (10% Killing=600 µg/ml)" Mouse erythrocytes: 10% Hemolysis=1660µg/ml Linear Free Free L Not available Not available 32715598 J Pept Sci. 2020 Oct;26(10):e3276. Tan A, Suzuki R, Yokoyama C, Yano S, Konno H. Antimicrobial activity and secondary structure of a novel peptide derived from ovalbumin DRAMP32293 RKIKVYLPRMK 11 Ovalbumin (277-287) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HeLa (10% Killing=572 µg/ml)" Mouse erythrocytes: 10% Hemolysis>1660µg/ml Linear Free Free L Not available Not available 32715598 J Pept Sci. 2020 Oct;26(10):e3276. Tan A, Suzuki R, Yokoyama C, Yano S, Konno H. Antimicrobial activity and secondary structure of a novel peptide derived from ovalbumin DRAMP32294 GIFSKLAGKKIKNLLISGLKG 21 Esculentin (1-21) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (50% Cell death=150 µM) Sheep erythrocytes: 10% Hemolysis=64 µM Linear Free Amidation L HaCat: 20% Killing=64 µM Not available 32722535 Antibiotics (Basel). 2020 Jul 26;9(8):448. Casciaro B, Loffredo MR, Cappiello F, Verrusio W, Corleto VD, Mangoni ML. Frog Skin-Derived Peptides Against Corynebacterium jeikeium: Correlation between Antibacterial and Cytotoxic Activities DRAMP32295 GIFSKLAGKKIKNlLIsGLKG 21 Esculentin (1-21)[L14l,S17s] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (10% Cell death=150 µM) Not available Linear Free Amidation l=D-Leu; s=D-Ser Mix Not available Not available 32722535 Antibiotics (Basel). 2020 Jul 26;9(8):448. Casciaro B, Loffredo MR, Cappiello F, Verrusio W, Corleto VD, Mangoni ML. Frog Skin-Derived Peptides Against Corynebacterium jeikeium: Correlation between Antibacterial and Cytotoxic Activities DRAMP32296 GIFSKLAGKKLKNLLISG 18 Esculentin (1-18) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (20% Killing=64 µM) Sheep erythrocytes: 10% Hemolysis=64 µM Linear Free Amidation L HaCat: 20% Killing=64 µM Not available 32722535 Antibiotics (Basel). 2020 Jul 26;9(8):448. Casciaro B, Loffredo MR, Cappiello F, Verrusio W, Corleto VD, Mangoni ML. Frog Skin-Derived Peptides Against Corynebacterium jeikeium: Correlation between Antibacterial and Cytotoxic Activities DRAMP32297 FIFLPIFRRPVS 12 Granuliberin-SSa Not available Not found Glandirana susurra Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (50.5% Killing=32µg/ml) Not available Linear Free Free L "COS-7: 88.5% Killing=32µg/ml; CPAE: 99.2% Killing=32µg/ml" Not available 32751229 Antibiotics (Basel). 2020 Jul 29;9(8):457. Ogawa D, Suzuki M, Inamura Y, Saito K, Hasunuma I, Kobayashi T, Kikuyama S, Iwamuro S. Antimicrobial Property and Mode of Action of the Skin Peptides of the Sado Wrinkled Frog, Glandirana susurra, against Animal and Plant Pathogens DRAMP32298 GLISTIWNTASNVAGTLTDSVKCKFKKC 28 Ranatuerin-2SSa Not available Not found Glandirana susurra Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (80.3% Killing=32µg/ml) Not available Linear Free Free L "COS-7: 88.5% Killing=32µg/ml; CPAE: 99.2% Killing=32µg/ml" Not available 32751229 Antibiotics (Basel). 2020 Jul 29;9(8):457. Ogawa D, Suzuki M, Inamura Y, Saito K, Hasunuma I, Kobayashi T, Kikuyama S, Iwamuro S. Antimicrobial Property and Mode of Action of the Skin Peptides of the Sado Wrinkled Frog, Glandirana susurra, against Animal and Plant Pathogens DRAMP32299 SLFSLIKAGAKFLGKNMLKQGPQYPACKVSKDSENVNWKS 40 Brevinin-2SSb Not available Not found Glandirana susurra Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (95.3% Killing=32µg/ml) Not available Linear Free Free L "COS-7: 88.5% Killing=32µg/ml; CPAE: 99.2% Killing=32µg/ml" Not available 32751229 Antibiotics (Basel). 2020 Jul 29;9(8):457. Ogawa D, Suzuki M, Inamura Y, Saito K, Hasunuma I, Kobayashi T, Kikuyama S, Iwamuro S. Antimicrobial Property and Mode of Action of the Skin Peptides of the Sado Wrinkled Frog, Glandirana susurra, against Animal and Plant Pathogens DRAMP32300 FALGAVTKVLPKLFCLITRKC 21 Brevinin-1H Not available Not found skin secretion of Amolops hainanensis  Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=2.599 μM); NCI-H157 (IC50=3.37 μM); MDA-MB-435S (IC50=3.47 μM); PC-3 (IC50=5.87 μM) Not available Linear Free Free L Horse blood cells: HC50=53.12 µM Not available 32812694 Chem Biol Drug Des. 2021 Feb;97(2):273-282. Pei X, Gong Z, Wu Q, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M. Characterisation of a novel peptide, Brevinin-1H, from the skin secretion of Amolops hainanensis and rational design of several analogues DRAMP32301 FALGAVTCLIRTKCKVLPKLF 21 Brevinin-1Ha Not available Not found skin secretion of Amolops hainanensis  Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=186.9 μM); MDA-MB-435S (IC50=214.7 μM); NCI-H157 (IC50=278.9 μM); HCT 116 (IC50=342.8 μM) Not available Linear Free Free L Horse blood cells: only over 20% at a concentration of 128 µM Not available 32812694 Chem Biol Drug Des. 2021 Feb;97(2):273-282. Pei X, Gong Z, Wu Q, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M. Characterisation of a novel peptide, Brevinin-1H, from the skin secretion of Amolops hainanensis and rational design of several analogues DRAMP32302 FALGAVTKVLYKLFCLITRKC 21 Brevinin-1HY Not available Not found skin secretion of Amolops hainanensis  Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-435S (IC50=2.243 μM); NCI-H157 (IC50=2.811 μM); HCT 116 (IC50=3.583 μM); PC-3 (IC50=5.425 μM) Not available Linear Free Free L Horse blood cells: The haemolysis at the MIC of Brevinin-1HY (28.48%) was more than threefold at the MIC for the parent peptide Not available 32812694 Chem Biol Drug Des. 2021 Feb;97(2):273-282. Pei X, Gong Z, Wu Q, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M. Characterisation of a novel peptide, Brevinin-1H, from the skin secretion of Amolops hainanensis and rational design of several analogues DRAMP32303 GFQKVKAQAATCNHTVMA 18 B18K Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available may induce cell death through processes involving membrane surface blebs, loss of membrane integrity, PI internalization, LDH release and PS externalization, coupled with coordinated regulation of Src•Erk1/2 signaling and mitochondrial events. Tumor cells: MCF-7 (IC50>131.0 µM ); MCF-7/G11-TR1 (IC50>131.0 µM ); MCF-7/G11-TR5 (IC50>131.0 µM ); MDA-MB-231 (IC50>131.0 µM ); MDA-MB-468 (IC50>131.0 µM ); SK-BR-3 (IC50>131.0 µM ); T-47D (IC50>131.0 µM ); ZR-75-1 (IC50>131.0 µM ) Not available Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available 32872253 . Cancers (Basel). 2020 Aug 28;12(9):2448. Lyu Y, Kopcho S, Alvarez FA, Okeoma BC, Okeoma CM. Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead DRAMP32304 GFQKAKAKALACLAKALA 18 B18KA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available may induce cell death through processes involving membrane surface blebs, loss of membrane integrity, PI internalization, LDH release and PS externalization, coupled with coordinated regulation of Src•Erk1/18 signaling and mitochondrial events. Tumor cells: MDA-MB-468 (IC50=135.6±9.3 µM); SK-BR-3 (IC50=43.5±11.5 µM); MCF-7/G11-TR5 (IC50=56.4±5.0 µM); ZR-75-1 (IC50=58.9±2.0 µM); MCF-7 (IC50=61.8±3.9 µM); MCF-7/G11-TR1 (IC50=61.8±5.1 µM); T-47D (IC50=78.5±20.9 µM); MDA-MB-231 (IC50=83.7±20.1 µM) Not available Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available 32872253 . Cancers (Basel). 2020 Aug 28;12(9):2448. Lyu Y, Kopcho S, Alvarez FA, Okeoma BC, Okeoma CM. Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead DRAMP32305 GFQKVKAQALTCLHTVMA 18 B18KL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available may induce cell death through processes involving membrane surface blebs, loss of membrane integrity, PI internalization, LDH release and PS externalization, coupled with coordinated regulation of Src•Erk1/10 signaling and mitochondrial events. Tumor cells: MCF-7 (IC50>128.5 µM); MCF-7/G11-TR1 (IC50>128.5 µM); MCF-7/G11-TR5 (IC50>128.5 µM); MDA-MB-231 (IC50>128.5 µM); MDA-MB-468 (IC50>128.5 µM); SK-BR-3 (IC50>128.5 µM); T-47D (IC50>128.5 µM); ZR-75-1 (IC50>128.5 µM) Not available Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available 32872253 . Cancers (Basel). 2020 Aug 28;12(9):2448. Lyu Y, Kopcho S, Alvarez FA, Okeoma BC, Okeoma CM. Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead DRAMP32306 GIGKAIAKAIACIAKAIA 18 B18I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available may induce cell death through processes involving membrane surface blebs, loss of membrane integrity, PI internalization, LDH release and PS externalization, coupled with coordinated regulation of Src•Erk1/34 signaling and mitochondrial events. Tumor cells: T-47D (IC50 >148.5 µM); ZR-75-1 (IC50=10.1±1.8 µM); MCF-7/G11-TR1 (IC50=10.8±2.0 µM); MCF-7 (IC50=16.0±1.6 µM); MCF-7/G11-TR5 (IC50=16.1±4.9 µM); MDA-MB-468 (IC50=16.6±1.5 µM); SK-BR-3 (IC50=18.1±4.7 µM); MDA-MB-231 (IC50=18.6±2.4 µM) Not available Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available 32872253 . Cancers (Basel). 2020 Aug 28;12(9):2448. Lyu Y, Kopcho S, Alvarez FA, Okeoma BC, Okeoma CM. Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead DRAMP32307 GLGKALAKALACLAKALA 18 B18L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available may induce cell death through processes involving membrane surface blebs, loss of membrane integrity, PI internalization, LDH release and PS externalization, coupled with coordinated regulation of Src•Erk1/26 signaling and mitochondrial events. Tumor cells: MDA-MB-468 (IC50=12.4±1.4 µM); T-47D (IC50=17.5±6.5 µM); MCF-7/G11-TR5 (IC50=3.8±0.3 µM); ZR-75-1 (IC50=5.2±1.0 µM); MCF-7 (IC50=5.9±0.5 µM); MCF-7/G11-TR1 (IC50=6.2±0.8 µM); MDA-MB-231 (IC50=7.2±0.8 µM); SK-BR-3 (IC50=7.2±1.0 µM) Human red blood cells: EC 50=21.2±3.2 μM, testing time is 24 h Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available 32872253 . Cancers (Basel). 2020 Aug 28;12(9):2448. Lyu Y, Kopcho S, Alvarez FA, Okeoma BC, Okeoma CM. Development of a Cationic Amphiphilic Helical Peptidomimetic (B18L) As A Novel Anti-Cancer Drug Lead DRAMP32308 FLPALAGIAGLLGKIF 16 Temporin-SHe Not available Not found Pelophylax saharicus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (45% Killing=12.5µM; 96% Killing=25µM) Human erythrocytes: 22% Hemolysis=12.5µM; 84% Hemolysis=25µM Linear Free Amidation L Not available Not available 32933215 Int J Mol Sci. 2020 Sep 13;21(18):6713. André S, Raja Z, Humblot V, Piesse C, Foulon T, Sereno D, Oury B, Ladram A. Functional Characterization of Temporin-SHe, a New Broad-Spectrum Antibacterial and Leishmanicidal Temporin-SH Paralog from the Sahara Frog ( Pelophylax saharicus) DRAMP32309 FIGTLIPLALGALTKLFK 18 Figainin 1  A0A2L2DDE6 Not found B. raniceps skin secretion Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: B16-F10 (IC50=10.5 µM (0.020 g/L)); HeLa (IC50=11.1 µM (0.021 g/L)); MCF-7 (IC50=13.7 µM (0.026 g/L)) Human red blood cells: HC50 =10 µM (0.019 g/L) (testing time is 24 h) Linear Free Free L NIH 3T3: IC50=13 µM (0.025 g/L) (testing time is 24 h) Not available 32967114 Antibiotics (Basel). 2020 Sep 21;9(9):625 Santana CJC, Magalhães ACM, Dos Santos Júnior ACM, Ricart CAO, Lima BD, Álvares ADCM, Freitas SM, Pires OR Jr, Fontes W, Castro MS. Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties DRAMP32310 CKKKC 5 C1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HeLa (IC50=25.5±2.9 µg/ml)" Human erythrocytes:HC50=43.9±3.5µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=23.6±6µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32311 CKKKRC 6 C6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=30.4±2.5µg/ml) Human erythrocytes:HC50=71±6.4µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=45.7±13.5µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32312 CKKRKC 6 C5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=21.9±4.5µg/ml) Human erythrocytes:HC50=97±15.4µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=12.9±4.6µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32313 CRKKKC 6 C3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=38.8±4.4µg/ml) Human erythrocytes:HC50=66.5±14.8µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=36.8±2.7µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32314 KKKR 4 L6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.6±0.5µg/ml) Human erythrocytes:HC50=89.7±2.4µg/ml Linear CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=7.5±0.8µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32315 KKRK 4 L5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=6.2±2.7µg/ml) Human erythrocytes:HC50=96.7±1.4µg/ml Linear CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=2.4±0.4µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32316 RKKK 4 L3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8.4±1.7µg/ml) Human erythrocytes:HC50=79.1±6.1µg/ml Linear CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=23.6±3.4µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP32317 WRRRYRRWRRRRRWRRRPRR 20 vCPP 2319 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=5.02±1.04 µM) Human erythrocytes: 50% Hemolysis>200µM Linear Free Amidation L Not available Not available 33015016 Front Bioeng Biotechnol. 2020 Sep 9;8:552035 Cavaco M, Pérez-Peinado C, Valle J, Silva RDM, Correia JDG, Andreu D, Castanho MARB, Neves V. To What Extent Do Fluorophores Bias the Biological Activity of Peptides? A Practical Approach Using Membrane-Active Peptides as Models DRAMP32318 RRIPFWPIPLRWQWPPPWFPPSFPIPRISRKR 32 Del1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (80% killing=32μM) Human erythrocytes:25% Hemolysis=32µM Linear Free Free L "HaCat: 10% Killing=32µM" Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP32319 RRIPFWPPNLPGPRRPPWFLPDFRIPRIPRKR 32 Orc1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (40% Killing=32µM) Human erythrocytes:0% Hemolysis=32µM Linear Free Free L "HaCat: 15% Killing=32µM" Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP32320 RRIRFPFPPFPWQWPPAGFPTFHIPRIPRKQ 31 Cathelicidin Neo1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (32% killing=32μM) Human erythrocytes:0% Hemolysis=32µM Linear Free Free L "HaCat: 12% Killing=32µM" Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP32321 RRIRFRPPRLPRPRPRPWIPPRFPFPRIPGKR 32 Cathelicidin-like peptide Bal1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (95% killing=32μM) Human erythrocytes:0% Hemolysis=32µM Linear Free Free L "HaCat: 0% Killing=32µM" Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP32322 RRIRIRPPRLPRPRPRPWFPPRFPIPRIPGKR 32 Cathelicidin-like peptide Lip1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-1 (90% killing=32μM) Human erythrocytes:0% Hemolysis=32µM Linear Free Free L "HaCat: 10% Killing=32µM" Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP32323 KCAGSIAWAIGSGLFGGAKLIKIKKYIAELGGLQ 34 Pom-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: TZM-bl (IC50=40.16µg/ml) Not available Linear Free Free L Vero E6: 50% Cytotoxicity=438 µM Not available 33113998 Biomolecules. 2020 Oct 23;10(11):1473. González García M, Rodríguez A, Alba A, Vázquez AA, Morales Vicente FE, Pérez-Erviti J, Spellerberg B, Stenger S, Grieshober M, Conzelmann C, Münch J, Raber H, Kubiczek D, Rosenau F, Wiese S, Ständker L, Otero-González A. New Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927) DRAMP32324 KRWHWWRRHWVVW 13 MAD1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OVCAR-3 (IC50=14.2 µM); A549 (IC50=36.2 µM); NCI/ADR-RES (IC50=85.6 µM); T24 (IC50>100 µM) Not available Linear Free Amidation L HUVEC: IC50>100 μM; NL20: IC50=76.9 μM Not available 33184577 Cell Mol Bioeng. 2020 Jun 24;13(5):447-461. Aronson MR, Dahl ES, Halle JA, Simonson AW, Gogal RA, Glick AB, Aird KM, Medina SH. Re-engineering Antimicrobial Peptides into Oncolytics Targeting Drug-Resistant Ovarian Cancers DRAMP32325 LWKRWVGVWRKWL 13 DAP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=11.9 µM); NCI/ADR-RES (IC50=14.0 µM); T24 (IC50=15.3 µM); OVCAR-3 (IC50=8.6 µM) Not available Linear Free Amidation L HUVEC: IC50=19.5 μM; NL20: IC50=19.0 μM Not available 33184577 Cell Mol Bioeng. 2020 Jun 24;13(5):447-461. Aronson MR, Dahl ES, Halle JA, Simonson AW, Gogal RA, Glick AB, Aird KM, Medina SH. Re-engineering Antimicrobial Peptides into Oncolytics Targeting Drug-Resistant Ovarian Cancers DRAMP32326 RWGKWFKKNSHLS 13 DAP2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>100 µM); NCI/ADR-RES (IC50>100 µM); OVCAR-3 (IC50>100 µM); T24 (IC50>100 µM) Not available Linear Free Amidation L HUVEC: IC50>100 μM; NL20: IC50>100 μM Not available 33184577 Cell Mol Bioeng. 2020 Jun 24;13(5):447-461. Aronson MR, Dahl ES, Halle JA, Simonson AW, Gogal RA, Glick AB, Aird KM, Medina SH. Re-engineering Antimicrobial Peptides into Oncolytics Targeting Drug-Resistant Ovarian Cancers DRAMP32327 WKWLKKWIK 9 AMP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OVCAR-3 (IC50=51.1 µM) Not available Linear Free Amidation L Not available Not available 33184577 Cell Mol Bioeng. 2020 Jun 24;13(5):447-461. Aronson MR, Dahl ES, Halle JA, Simonson AW, Gogal RA, Glick AB, Aird KM, Medina SH. Re-engineering Antimicrobial Peptides into Oncolytics Targeting Drug-Resistant Ovarian Cancers DRAMP32328 WKWLKKWIK 9 AMP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=24.3 µM) Not available Linear Free Amidation L Not available Not available 33184577 Cell Mol Bioeng. 2020 Jun 24;13(5):447-461. Aronson MR, Dahl ES, Halle JA, Simonson AW, Gogal RA, Glick AB, Aird KM, Medina SH. Re-engineering Antimicrobial Peptides into Oncolytics Targeting Drug-Resistant Ovarian Cancers DRAMP32329 CGAISLAKLQINES 14 HS3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=80.7±6.9 µM) Not available Linear Free Free L Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32330 CGAISLAPKAQIKES 15 HS1 Q15116 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=19.2±2.3 µM) Not available Linear Free Free L Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32331 CGAISLAPKLQIKES 15 HS2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=93.5±10.7 µM) Not available Linear Free Free L Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32332 GAISAPKLQIND 12 HS7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=4.4±0.4 µM) Not available Linear Free Free L Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32333 GAISLAKLQINeG 13 HS6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=0.71±0.22 µM) Not available Cyclic Acetylization Amidation C,N-terminal lactam peptide; e=D-Glutamic acid Mix Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32334 GAISLAPKLQINE 13 HS4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=5.6±0.15 µM) Not available Linear Free Free L Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32335 GAISLAPKLQINe 13 HS5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CT26 (IC50=1.56±0.35 µM) Not available Linear Free Free e=D-Glutamic acid Mix Not available programmed cell death protein 1 33360579 Bioorg Med Chem. 2021 Jan 15;30:115951. Orafaie A, Sadeghian H, Bahrami AR, Rafatpanah H, Matin MM. Design, synthesis and evaluation of PD-L1 peptide antagonists as new anticancer agents for immunotherapy DRAMP32336 OLeu-V-NMeLeu-FL 16 MSSV Not available Not found Fusarium spp. isolated from Korean potato Antimicrobial, Anticancer Not found Not found Not found Not available MSSV inhibited the proliferation of both bladder cancer 5637 and T24 cells, which was attributed to the G1-phase cell cycle arrest, apoptosis induction, and alteration of mitogen-activated protein kinases (MAPKs) and protein kinase b (AKT) signaling pathways. Tumor cells: 5637 (IC50=20 μg/mL); T24 (IC50=20 μg/mL) Not available Cyclic OLeu=leucic acid component; NMeLeu=N-methylleucine; Mix Not available Not available 33430488 Cancers (Basel). 2021 Jan 7;13(2):191. Song JH, Park J, Park SL, Hwang B, Kim WJ, Lee C, Moon SK. N-Methylsansalvamide, a cytotoxic cyclic depsipeptide from a marine fungus of the genus fusarium DRAMP32337 VKLRSLLCS 9 VS-9 Not available Not found garlic Antimicrobial, Anticancer Not found Not found Not found Not available VS-9 could induce apoptosis and upregulate mRNA levels of caspase 3, caspase 8, caspase 9, and Bax while downregulating Bcl-2, Bcl-xL, and Bcl-w. Tumor cells: Molt-4 (IC50=0.84 mM ); K562 (IC50=1.57 mM ) Not available Linear Free Free L PBMC: IC50>2.0 mM groove of the BH3 domain on target proteins 33595876 Chem Biol Drug Des. 2021 May;97(5):1017-1028. Rasaratnam K, Nantasenamat C, Phaonakrop N, Roytrakul S, Tanyong D. A novel peptide isolated from garlic shows anticancer effect against leukemic cell lines via interaction with Bcl-2 family proteins DRAMP32338 DVNFLLHKIYGNIRY 15 LvHemB1 Not available Not found Litopenaeus vannamei Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: EC109 (49.01% decrease=50μg/mL); HepG2 (53.26% decrease=50μg/mL); HeLa (70.30% decrease=50μg/mL); EJ (78.44% decrease=50μg/mL) Not available Linear Free Free L THLE-3: 30.83% decrease=50μg/mL Not available 33630204 Cell Biol Toxicol. 2022 Feb;38(1):87-110. Liu S, Aweya JJ, Zheng L, Zheng Z, Huang H, Wang F, Yao D, Ou T, Zhang Y. LvHemB1, a novel cationic antimicrobial peptide derived from the hemocyanin of Litopenaeus vannamei, induces cancer cell death by targeting mitochondrial voltage-dependent anion channel 1 DRAMP32339 FFPLIAGLAARFLPKIFCSITKRC 24 Brevinin-1RL1 Not available Not found Frog Skin Secretion Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=10.37±0.40 µM ); MDA-MB-231 (IC50=5.44±0.33 µM ); A549 (IC50=5.81±0.23 µM ); HCT 116 (IC50=5.87±0.15 µM ); B16-F10 (IC50=6.65±0.33 µM ); SMMC-7721 (IC50=6.87±0.51 µM ) Human erythrocytes: Moderate Hemolysis Linear Free Free L NCM460: IC50=16.84±0.56 µM; BEAS-2B: IC50=16.57±0.29 µM; HaCaT: IC50=28.67±0.36 µM Not available 33916789 Molecules. 2021 Apr 3;26(7):2059 Ju X, Fan D, Kong L, Yang Q, Zhu Y, Zhang S, Su G, Li Y. Antimicrobial Peptide Brevinin-1RL1 from Frog Skin Secretion Induces Apoptosis and Necrosis of Tumor Cells DRAMP32340 CIIKKIIKKIIKK 13 IK-13 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=29±6 µM); HeLa (IC50=47±5 µM) Not available Linear Free Free L HDF: IC50>100 µM Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP32341 CIIKKIIKKIIKKII 15 CI-15 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=2.7±0.5 µM); HCT 116 (IC50=7.7±0.2 µM) Not available Linear Free Free L HDF: IC50=83±5 µM Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP32342 CIIRRIIRRIIRR 13 IR-13 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50>100 µM); HeLa (IC50>100 µM) Not available Linear Free Free L HDF: IC50=22±3 µM Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP32343 CLLKKLLKKLLKK 13 LK-13 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=23±2 µM); HeLa (IC50=83±9 µM) Not available Linear Free Free L HDF: IC50>100 µM Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP32344 CLLRRLLRRLLRR 13 LR-13 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=15.6±1.0 µM); HeLa (IC50=26.7±1.3 µM) Not available Linear Free Free L HDF: IC50=24±5 µM Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP32345 KKRKKKAFALKFVVDLI 17 PCC-1 Not available Not found insect-derived peptide Antimicrobial, Anticancer Not found Not found Not found Not available PCC-1 induces cell proliferation inhibition, apoptosis, and cell cycle arrest by downregulating Sp1 expression in the melanoma cell lines SK-MEL-28 and G361. Tumor cells: SK-MEL-28 (IC50=50.8 µM); G-361 (IC50=57.8 µM) Not available Linear Free Amidation L HaCaT: not induce toxicity Not available 34531430 Sci Rep. 2021 Sep 16;11(1):18445. Lee RH, Oh JD, Hwang JS, Lee HK, Shin D. Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32346 VTFVLIAAK 9 C-ori Not available Not found Cordyceps militaris Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=114.9±1.5 µM) Not available Linear Free Free L Not available Not available 34641308 Molecules. 2021 Sep 23;26(19):5767. Chantawannakul J, Chatpattanasiri P, Wattayagorn V, Kongsema M, Noikaew T, Chumnanpuen P. Virtual Screening for Biomimetic Anti-Cancer Peptides from Cordyceps militaris Putative Pepsinized Peptidome and Validation on Colon Cancer Cell Line DRAMP32347 IKIKIKIKIKIK 12 IKIK Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=32.7±4.5 µM); HeLa (IC50=8.9±2.1 µM) Not available Linear Free Free L HDF: IC50=4.4±0.3 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32348 IKIRIKIRIKIR 12 IKIR Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=14.5±2.3 µM); HCT 116 (IC50=20.9±2.0 µM) Not available Linear Free Free L HDF: IC50=38.6±0.2 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32349 IRIKIRIKIRIK 12 IRIK Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15.5±1.2 µM); HCT 116 (IC50=30.1±5.2 µM) Not available Linear Free Free L HDF: IC50=34.5±0.9 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32350 LKLKLKLKLKLK 12 LKLK Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=14.5±1.3 µM); HeLa (IC50=17.7±6.5 µM) Not available Linear Free Free L HDF: IC50>40 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32351 LKLRLKLRLKLR 12 LKLR Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50>40 µM); HeLa (IC50>40 µM) Not available Linear Free Free L HDF: IC50=22.5±1.4 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32352 LRLKLRLKLRLK 12 LRLK Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50>40 µM); HeLa (IC50>40 µM) Not available Linear Free Free L HDF: IC50=24.1±0.7 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32353 LRLRLRLRLRLR 12 LRLR Not available Not found cationic amphiphilic peptides Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=31.8±2.9 µM); HeLa (IC50>40 µM) Not available Linear Free Free L HDF: IC50=22.7±2.4 µM Not available 34715505 Colloids Surf B Biointerfaces. 2022 Jan;209(Pt 2):112165. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity DRAMP32354 FLPLLISALTSLFPKLGK 18 SSTP1 Not available Not found Skin Secretion of Indosylvirana aurantiaca Antimicrobial, Anticancer Not found Not found Not found Not available In IL6Rα-overexpressing cancer cells, SSTP1 induces apoptosis at low concentration through JNK pathway, without causing significant membrane disruption. Tumor cells: HSC-4 (IC50=10.22 μM); MDA-MB-231 (IC50=4.5 μM) Human red blood cell: SSTP1-induced hemolysis at 5 μM was only-0.25% Linear Free Free L HEK293: IC50=21.72 μM, lower cytotoxicity IL6/IL6Rα/gp130 complex 34867962 Front Immunol. 2021 Nov 19;12:740620. Gopalakrishnan S, Uma SK, Mohan G, Mohan A, Shanmugam G, Kumar VTV, J S, Chandrika SK, Vasudevan D, Nori SRC, Sathi SN, George S, Maliekal TT. SSTP1, a Host Defense Peptide, Exploits the Immunomodulatory IL6 Pathway to Induce Apoptosis in Cancer Cells DRAMP32355 GYFCESCRKIIQKLEDMVGPQPNEDTVTQAASQVCDKLKILRGLCKKIMRSFLRRISWDILTGKKPQAICVDIKICKE 78 Antimicrobial peptide NK-lysin Not available Not found Sus scrofa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: YAC-1 (LC90=50 µg/ml) Sheep erythrocytes: 0% Hemolysis=170 µM Cyclic Free Free L Not available Not available 7737114 EMBO J. 1995 Apr 18;14(8):1615-25. Andersson M, Gunne H, Agerberth B, Boman A, Bergman T, Sillard R, Jörnvall H, Mutt V, Olsson B, Wigzell H, et al. NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity DRAMP32356 GEILCNLCTGLINTLENLLTTKRKRQQ 27 EH-APP(1-22)-Melittin (21-26) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LC=50 µM); Jurkat (LC50=8 µM) Human erythrocytes: 50% Hemolysis=10 µM Linear Free Amidation L Not available Not available 8146160 Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2602-6. Leippe M, Andrä J, Müller-Eberhard HJ. Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica DRAMP32357 GFIATLCTKVLDFGIDKLIQLIEDK 25 EH-APP(40-64) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (LC50=60 µM); U-937 (LC50=80 µM) Human erythrocytes: 10% Hemolysis=10 µm Linear Free Free L Not available Not available 8146160 Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2602-6. Leippe M, Andrä J, Müller-Eberhard HJ. Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica DRAMP32358 GIGKFLKKAKKFAKAFVKIINN 22 MSI-136 Not available Not found African clawed frog Xenopus laevis skin Antimicrobial, Anticancer Not found Not found Not found Not available A mechanism which appears to be related to short duration non-receptor-driven contact with target cell membranes. Tumor cells: A549 (IC50=10 µM) Not available Linear Free Amidation L Not available Not available 8319212 Cancer Res. 1993 Jul 1;53(13):3052-7. Baker MA, Maloy WL, Zasloff M, Jacob LS. Anticancer efficacy of Magainin2 and analogue peptides DRAMP32359 gigkflkkakkfakafvkiinn 22 MSI-238 Not available Not found African clawed frog Xenopus laevis skin Antimicrobial, Anticancer Not found Not found Not found Not available A mechanism which appears to be related to short duration non-receptor-driven contact with target cell membranes. Tumor cells: A549 (IC50=6 µM) Not available Linear Free Amidation D Not available Not available 8319212 Cancer Res. 1993 Jul 1;53(13):3052-7. Baker MA, Maloy WL, Zasloff M, Jacob LS. Anticancer efficacy of Magainin2 and analogue peptides DRAMP32360 KWKLFKKIGIGAVLKVLKKG 20 P1 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=3.4 µM); NCI-H128 (IC50=3.5 µM); NCI-H146 (IC50=4.5 µM) Human red blood cells: hemolysis 0.3%(50 μg/mL); hemolysis 1%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 14 and cecropin A-melittin hybrid peptides DRAMP32361 KWKLFKKIGIGKFLHSATTF 20 P2 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=36.2 µM); NCI-H128 (IC50=37.9 µM); NCI-H146 (IC50=47.7 µM) Human red blood cells: hemolysis 0.2%(50 μg/mL); hemolysis 1%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 15 and cecropin A-melittin hybrid peptides DRAMP32362 KWKLFKKIGIGAFLHSAKKF 20 P3 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H146 (IC50=10.9 µM); NCI-H128 (IC50=9.3 µM); NCI-H69 (IC50=9.3 µM) Human red blood cells: hemolysis 0.1%(50 μg/mL); hemolysis 0.2%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 16 and cecropin A-melittin hybrid peptides DRAMP32363 KWKLFKKIGIGKFLHLAKKF 20 P4 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H128 (IC50=1.3 µM); NCI-H69 (IC50=1.9 µM); NCI-H146 (IC50=2.8 µM) Human red blood cells: hemolysis 0.2%(50 μg/mL); hemolysis 0.7%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 17 and cecropin A-melittin hybrid peptides DRAMP32364 KWKLFKKIGIGAFLHLAKKF 20 P5 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H128 (IC50=2.9 µM); NCI-H69 (IC50=2.9 µM); NCI-H146 (IC50=3.2 µM) Human red blood cells: hemolysis 1.5%(50 μg/mL); hemolysis 8%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 18 and cecropin A-melittin hybrid peptides DRAMP32365 KWKLFKKIGIGKFKLAKKF 19 P6 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.7 µM); NCI-H128 (IC50=2 µM); NCI-H146 (IC50=3.1 µM) Human red blood cells: hemolysis 0.2%(50 μg/mL); hemolysis 1.2%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 19 and cecropin A-melittin hybrid peptides DRAMP32366 KWKLFAKIGIGKFLHLAKKF 20 P7 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H128 (IC50=2.4 µM); NCI-H146 (IC50=2.4 µM); NCI-H69 (IC50=3.1 µM) Human red blood cells: hemolysis 0.4%(50 μg/mL); hemolysis 2.4%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 20 and cecropin A-melittin hybrid peptides DRAMP32367 KWKKFLKIGIGKFLHLAKKF 20 P8 Not available Not found Ceropin A-Magainin 2 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H146 (IC50=1.8 µM); NCI-H128 (IC50=2.3 µM); NCI-H69 (IC50=2.6 µM) Human red blood cells: hemolysis 2.4%(50 μg/mL); hemolysis 13.7%(100 μg/mL) Linear Free Amidation L Not available Not available 9352466 J Pept Res. 1997 Oct;50(4):279-85. Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 21 and cecropin A-melittin hybrid peptides DRAMP32368 RQSHFANAQP 10 CPe-III(CPe-III-S) Not available Not found Chickpea (Cicer arietinum L.) Antimicrobial, Anticancer Not found Not found Not found Not available the bioactive peptide combined the DNA binding domain of p53 protein by hydrogen bonds, induced the expression of p53 protein and facilitated its stability so that it inhibited the cell proliferation. Tumor cells: MDA-MB-231 (EC50=1.50 μmol/mL); MCF-7 (EC50=2.38 μmol/mL ) Not available Linear Free Free L Not available p53 protein Not available Antioxidant activity and anti-proliferative effect of a bioactive peptide from chickpea (Cicer arietinum L.) DRAMP32369 WPP 3 BCP-A Not available Not found hydrolysate of blood clam (Tegillarca granosa) muscle Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=1.99 mg/mL ); HeLa (IC50=2.54 mg/mL ); DU145 (IC50=2.80 mg/mL); NCI-H1299 (IC50=3.3 mg/mL ) Not available Linear Free Free L NIH 3T3: Has hardly any cytotoxicity on normal cells. Not available Not available Antioxidant and anticancer peptides from the protein hydrolysate of blood clam (Tegillarca granosa) muscle DRAMP32370 SLPQNIPPLTQTPVVVPPF 19 P19 Not available Not found Synbiotic yoghurt Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (Antiproliferative acitivity (%)=38.55±1.75%,  Peptide concentration 3 mg/mL) Not available Linear Free Free L Not available Not available Not available Antioxidant peptides isolated from synbiotic yoghurt exhibit antiproliferative activities against HT-29 colon cancer cells DRAMP32371 YQEPVLGPVRGPFPIIV 17 P17 Q9TSI0##P02666 Not found Synbiotic yoghurt Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (Antiproliferative acitivity (%)=41.49±2.18%,  Peptide concentration 3 mg/mL) Not available Linear Free Free L Not available Not available Not available Antioxidant peptides isolated from synbiotic yoghurt exhibit antiproliferative activities against HT-29 colon cancer cells DRAMP32372 XXMXIVVKVLKYLX 14 Brevilaterin B Not available Not found Brevibacillus laterosporus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=1.40±0.09 µg/mL); SW1990 (IC50=13.40±0.08 µg/mL); SMMC-7721 (IC50=13.81±0.31 µg/mL); SW480 (IC50=17.15±0.97 µg/mL); EC109 (IC50=2.13±0.23 µg/mL); A498 (IC50=2.33±0.49 µg/mL); DU145 (IC50=2.56±0.23 µg/mL); HeLa (IC50=2.60±0.24 µg/mL); A431 (IC50=2.75±0.07 µg/mL); PANC-1 (IC50=3.11±0.49 µg/mL); KB (IC50=3.14±0.07 µg/mL); HeLa S3 (IC50=3.16±0.45 µg/mL); EC9706 (IC50=3.23±0.16 µg/mL); A-375 (IC50=4.16±0.15 µg/mL); MDA-MB-231 (IC50=4.16±0.27 µg/mL); SK-OV-3 (IC50=4.26±0.25 µg/mL); MCF-7 (IC50=4.94±0.28 µg/mL); A549 (IC50=5.54±0.55 µg/mL); BGC-823 (IC50=5.68±0.25 µg/mL); SGC-7901 (IC50=5.73±0.21 µg/mL); Tca8113 (IC50=5.82±0.25 µg/mL); K562 (IC50=5.86±0.66 µg/mL); PC-3M (IC50=6.17±0.24 µg/mL); A2780 (IC50=7.40±0.36 µg/mL); HCT 116 (IC50=7.67±0.57 µg/mL); Hep-G2 (IC50=9.84±0.39 µg/mL) Not available Linear Free Free X(1)=Hmp=2-hydroxy-3-methylpentanoic acid; X(2)=Aba=2-amino-2-butenoic acid; X(4)=Ornithine; X(14)=valinol L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL; Human Intrahepatic Biliary Epithelial Cells (HIBEpiC): IC50=2.37±0.38 µg/; HEK293: IC50=4.78±0.32 µg/mL; IOSE80: IC50=1.12±0.04 µg/mL; RWPE-1: IC50=1.07±0.34 µg/mL; GES-1: IC50=10.62±0.73 µg/mL; MCF-10A: IC50=1.58±0.33 µg/mL; Not available Not available Brevilaterin B from Brevibacillus laterosporus has selective antitumor activity and induces apoptosis in epidermal cancer DRAMP32373 INKKI 5 INKKI peptide Not available Not found β-Casein Antimicrobial, Anticancer Not found Not found Not found Not available By apoptosis via mitochondrial pathway in a caspase-independent manner Tumor cells: MCF-7 (IC50=3.07 μg/mL); T-47D (IC50=3.26 μg/mL); MDA-MB-231 (IC50=3.53 μg/mL ); MCF-7 (IC50=3.78 µg/mL) Not available Linear Free Free L Fibroblast FN-1 (human): no effect (testing time is 24 h); Endothelial CRL 1730 (human) : no effect (testing time is 24 h) Not available Not available Evaluation of the antitumor and antiproliferative effects of the INKKI peptide on MCF-7 breast adenocarcinoma cells DRAMP32374 GIKCRFCCGCCTPGICGVCCRF 22 Hepcidin TH1-5 Not available Not found Skin Secretion of the African Frog, Kassina senegalensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=20 μg/mL ) Not available Linear Free Free L Not available Not available Not available Hepcidin TH1-5 Induces Apoptosis and Activate Caspase-9 in MCF-7 Cells DRAMP32375 GLFDIVKGIKSLF 13 ND2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=72.00±4.51 µg/mL) Not available Linear Free Free L Vero: IC50=48.67±1.76 µg/mL; THLE-3: IC50=58.83±0.83 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32376 GLFDIVKKIKSLF 13 ND3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=63.00±5.00 µg/mL) Not available Linear Free Free L Vero: IC50=45.17±2.46 µg/mL; THLE-3: IC50=52.83±0.60 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32377 GLFDIVKKLKSLF 13 ND4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=53.17±1.69 µg/mL) Not available Linear Free Free L Vero: IC50=43.83±1.33 µg/mL; THLE-3: IC50=39.17±2.17 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32378 GLFDIWKGIKSLF 13 ND1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=102.33±1.45 µg/mL) Not available Linear Free Free L Vero: IC50=22.67±0.44 µg/mL; THLE-3: IC50=34.33±0.73 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32379 GLFDRVKKRKSLF 13 ND5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>256 µg/mL) Not available Linear Free Free L Vero: IC50>256 µg/mL; THLE-3: IC50>256 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32380 ILGKIVKKLVSDF 13 DN1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=152.17±7.73 µg/mL) Not available Linear Free Free L Vero: IC50>256 µg/mL; THLE-3: IC50>256 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32381 ILGKIWKGIVSDF 13 DN4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=191.67±12.02 µg/mL) Not available Linear Free Free L Vero: IC50>256 µg/mL; THLE-3: IC50>256 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32382 ILGKIWKGLVSDF 13 DN3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>256 µg/mL) Not available Linear Free Free L Vero: IC50>256 µg/mL; THLE-3: IC50>256 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32383 ILGKIWKKLVSDF 13 DN2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>256 µg/mL) Not available Linear Free Free L Vero: IC50=156.33±4.33 µg/mL; THLE-3: IC50=105.33±4.42 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32384 ILGKRWKGRVSDF 13 DN5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>256 µg/mL) Not available Linear Free Free L Vero: IC50>256 µg/mL; THLE-3: IC50>256 µg/mL Not available Not available Hybrid Anticancer Peptides DN1 and DN4 Exert Selective Cytotoxicity Against Hepatocellular Carcinoma Cells by Inducing Both Intrinsic and Extrinsic Apoptotic Pathways DRAMP32385 YALPAG 6 YALPAG Not available Not found Heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=71.2 μM (42.0 mg/mL)) Not available Linear Free Free L Not available Not available Not available Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) DRAMP32386 YALPAR 6 YALPAR Not available Not found Heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=19.0 μM (13.1 mg/mL)) Not available Linear Free Free L Not available Not available Not available Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) DRAMP32387 YALRAH 6 YALRAH Not available Not found Heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=11.1 μM (8.1 mg/mL)) Not available Linear Free Free L Not available Not available Not available Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty) DRAMP32388 VWLSALKFIGKHLAKHQLSKL 21 Lycosin-II Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Lycosin-II Suppresses the Growth of Tumor Cells and Kills them Through Membrane Disruption and Apoptosis Induction Tumor cells: HCT 116 (IC50=70.79 µg/mL ) Not available Linear Free Free L IC50 on PBMCs was = 92.0 ± 39.6 μM Not available Not available Lycosin-II Suppresses the Growth of Tumor Cells and Kills them Through Membrane Disruption and Apoptosis Induction DRAMP32405 KWKVFKKIEKKWKVFKKIEKAGPKWKVFKKIEK 33 CB1a, Cecropin-B1a P01508 Not found Not available Antimicrobial, Anticancer Not found Not found Not found 2IGR Not available "Tumor cells: NCI-H520 (IC50=22.7±0.2 µM); NCI-H661 (IC50=35.9±0.2 µM); CCRF-CEM (IC50=4.4±0.3 µM); AGS (IC50=5.6±0.5 µM); HL-60 (IC50=6.7±1.1 µM)" Human erythrocytes: 18% Hemolysis=200 µM Linear Free Amidation L RPMI-7666: IC50>100 µM; NIH 3T3: IC50>50 µM; WI-38: IC50>100 µM Not available 19428759 Peptides. 2009 May;30(5):839-48. Wu JM, Jan PS, Yu HC, Haung HY, Fang HJ, Chang YI, Cheng JW, Chen HM. Structure and function of a custom anticancer peptide, CB1a DRAMP32444 XPAXXFXPAXXLXXLXXLX 19 Ⅰ Not available Not found Peptaibols Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50=1.98 μM); BGC-823 (IC50=2.11 μM); A549 (IC50=2.30 μM); A2780 (IC50>10 μM); HCT 8 (IC50>10 μM) Not available Linear Acetylation Aminoethanol X(1/4/5/16/17)=Aib=1-amino-isobutyric acid; X(7/13)=Iva=Isovaline; X(10)=AHMA=3-amino-2-hydroxy-3-methylbutanoic acid; X(11/14/19)(β)A=β-Alanine L Not available Not available Not available Not available DRAMP32445 XPAXXFXPAXXLXXLXXLX 19 Ⅰ Not available Not found Peptaibols Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (IC50=1.03 μM); BEL-7402 (IC50=1.94 μM); A549 (IC50=2.08 μM); A2780 (IC50=3.79 μM); HCT 8 (IC50=5.93 μM) Not available Linear Acetylation Aminoethanol X(1/4/5/16/17)=Aib=1-amino-isobutyric acid; X(7/13)=Iva=Isovaline; X(10)=AHMA=3-amino-2-hydroxy-3-methylbutanoic acid; X(11/14/19)(β)A=β-Alanine L Not available Not available Not available Not available DRAMP32446 XPAXXFXPAXXLXXLXXLX 19 Ⅱ Not available Not found Peptaibols Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50=1.98 μM); BGC-823 (IC50=2.11 μM); A549 (IC50=2.30 μM); A2780 (IC50>10 μM); HCT 8 (IC50>10 μM) Not available Linear Acetylation Aminoethanol X(1/4/5/17)=Aib=1-amino-isobutyric acid; X(7/13/16)=Iva=Isovaline; X(10)=AHMA=3-amino-2-hydroxy-3-methylbutanoic acid; X(11/14/19)(β)A=β-Alanine L Not available Not available Not available Not available DRAMP32447 XPAXXFXPAXXLXXLXXLX 19 Ⅱ Not available Not found Peptaibols Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BGC-823 (IC50=1.03 μM); BEL-7402 (IC50=1.94 μM); A549 (IC50=2.08 μM); A2780 (IC50=3.79 μM); HCT 8 (IC50=5.93 μM) Not available Linear Acetylation Aminoethanol X(1/4/5/17)=Aib=1-amino-isobutyric acid; X(7/13/16)=Iva=Isovaline; X(10)=AHMA=3-amino-2-hydroxy-3-methylbutanoic acid; X(11/14/19)(β)A=β-Alanine L Not available Not available Not available Not available DRAMP32448 GAVPCGESCVYLPCLTTVVGCSCQNSVCYHN 31 B5 Not available Not found Hedyotis biflora Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BxPC-3 (IC50=1.03 μM); PANC-1 (IC50=1.08 μM); Capan-2 (IC50=1.21 μM); MOH-1 (IC50=1.32 μM) Not available Cyclic Free Free L Not available Not available Not available Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo DRAMP32449 GAVPCGETCVYLPCITAAIGCSCQNKVCYRD 31 B6 Not available Not found Hedyotis biflora Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Capan-2 (IC50=1.85 μM); PANC-1 (IC50=1.97 μM); MOH-1 (IC50=2.10 μM); BxPC-3 (IC50=2.33 μM) Not available Cyclic Free Free L Not available Not available Not available Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo DRAMP32450 GIPCGESCAFLPCLTSLLGCTCQNKVCYRD 30 B8 Not available Not found Hedyotis biflora Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MOH-1 (IC50=1.88 μM); PANC-1 (IC50=1.95 μM); Capan-2 (IC50=2.14 μM); BxPC-3 (IC50=3.11 μM) Not available Cyclic Free Free L Not available Not available Not available Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo DRAMP32451 GISCAETCVLLPCLSSVIGCTCQNKRCYKN 30 B7 Not available Not found Hedyotis biflora Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MOH-1 (IC50=0.33 μM); PANC-1 (IC50=0.36 μM); Capan-2 (IC50=0.45 μM); BxPC-3 (IC50=0.68 μM) Not available Cyclic Free Free L Not available Not available Not available Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo DRAMP32452 GNPCGESCVYLPCITTVVGCSCQNSVCYHN 30 B9 Not available Not found Hedyotis biflora Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MOH-1 (IC50=1.14 μM); Capan-2 (IC50=1.32 μM); BxPC-3 (IC50=1.54 μM); PANC-1 (IC50=2.01 μM) Not available Cyclic Free Free L Not available Not available Not available Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo DRAMP32453 AIMSSLMKKLAAHIAK 16 HYL-1 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=19.72±0.38 µmol/L); Hep-G2 (IC50=30.78±0.24 µmol/L); HCT 116 (IC50=47.25±0.33 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32454 GAMSSLMKKLAAHIAK 16 HYL-2 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L); A549 (IC50=39.57±0.12 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32455 GIASSLMKKLAAHIAK 16 HYL-3 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L); A549 (IC50=28.97±0.27 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32457 GIMASLMKKLAAHIAK 16 HYL-4 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=10.66±0.25 µmol/L); HCT 116 (IC50=18.50±0.22 µmol/L); A549 (IC50=6.01±0.15 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32459 GIMSALMKKLAAHIAK 16 HYL-5 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=12.75±0.26 µmol/L); A549 (IC50=5.32±0.47 µmol/L); Hep-G2 (IC50=7.57±0.18 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32460 GIMSSAMKKLAAHIAK 16 HYL-6 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50 ＞50 µmol/L); HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32461 GIMSSLAKKLAAHIAK 16 HYL-7 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L); A549 (IC50=28.32±0.28 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32463 GIMSSLMAKLAAHIAK 16 HYL-8 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=15.17±0.34 µmol/L); Hep-G2 (IC50=17.09±0.26 µmol/L); HCT 116 (IC50=19.81±0.20 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32465 GIMSSLMKALAAHIAK 16 HYL-9 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=4.75±0.33 µmol/L); HCT 116 (IC50=7.22±0.21 µmol/L); Hep-G2 (IC50=8.04±0.27 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32466 GIMSSLMKKAAAHIAK 16 HYL-10 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50 ＞50 µmol/L); HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32468 GIMSSLMKKLAAAIAK 16 HYL-11 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=5.18±0.37 µmol/L); Hep-G2 (IC50=7.35±0.34 µmol/L); HCT 116 (IC50=7.99±0.22 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32469 GIMSSLMKKLAAHAAK 16 HYL-12 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50 ＞50 µmol/L); HCT 116 (IC50 ＞50 µmol/L); Hep-G2 (IC50 ＞50 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32470 GIMSSLMKKLAAHIAA 16 HYL-13 Not available Not found AMP Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=11.84±0.17 µmol/L); HCT 116 (IC50=16.80±0.34 µmol/L); Hep-G2 (IC50=16.84±0.28 µmol/L) Not available Linear Free Amidation L Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL Not available Not available Structural modification and antitumor activity of antimicrobial peptide HYL DRAMP32764 GLPVCGETCFGGTCNTPGCSCXTWPVCSRN 30 Varv Hm Not available Not found Viola arvensis (European field pansy) (Field violet) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) Not available Cyclic Free Free X=Glu-methylation L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32765 GLPVCGETCFGGTCNTPGCSCXTWPVCSRN 30 Varv Hm Not available Not found Viola arvensis (European field pansy) (Field violet) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) Not available Cyclic Free Free X=Glu-methylation L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32766 GLPVCGETCFGGTCNTPGCSCXTWPVCSRN 30 Varv He Not available Not found Viola arvensis (European field pansy) (Field violet) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) Not available Cyclic Free Free X=Glu-ethylation L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32767 GLPVCGETCFGGTCNTPGCSCXTWPVCSRN 30 Varv He Not available Not found Viola arvensis (European field pansy) (Field violet) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) Not available Cyclic Free Free X=Glu-ethylation L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32768 GYPICGESCVGGTCNTPGCSCSWPVCTTN 29 vitri B Not available Not found Viola tricolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) HRBCs: HC50=225.90 μM Cyclic Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32769 GLPICGETCVGGTCNTPGCFCTWPVCTRN 29 vitri C Not available Not found Viola tricolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) HRBCs: HC50=11.53 μM Cyclic Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32770 GLPVCGETCFTGSCYTPGCSCNWPVCNRN 29 vitri D Not available Not found Viola tricolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) HRBCs: HC50=4.29 μM Cyclic Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32771 GLPVCGETCVGGTCNTPGCSCSWPVCFRN 29 vitri E Not available Not found Viola tricolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50>10 µg/ml) HRBCs: HC50=27.06 μM Cyclic Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32772 GTLPCGESCVWIPCISSVVGCACKSKVCYKD 31 vitri F Not available Not found Viola tricolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50=5.36 µg/ml) HRBCs: HC50=10.00 μM Cyclic Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP32773 GRKKRRQRRRPQSKRKKNKKGKRK 24 CP-EPS8-NLS Not available Not found Derived from the NLS of EPS8 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: KG-1a (~45%Cellular viability=105 µM) Not available Linear Acetylation Amidation L Not available Not available 29357910 J Exp Clin Cancer Res. 2018 Jan 22;37(1):12. Chen Y, Xie X, Wu A, Wang L, Hu Y, Zhang H, Li Y. A synthetic cell-penetrating peptide derived from nuclear localization signal of EPS8 exerts anticancer activity against acute myeloid leukemia DRAMP32774 YADAIFTNSYRKVLGQLSARKLLQDIMSR 29 MIA-602 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 15 (~40%Inhibition=5 µM) Not available Linear Phenylacetyl 12-aminododecanoyl Amidation L Not available Not available 28130121 Peptides. 2017 Mar;89:60-70 Zarandi M, Cai R, Kovacs M, Popovics P, Szalontay L, Cui T, Sha W, Jaszberenyi M, Varga J, Zhang X, Block NL, Rick FG, Halmos G, Schally AV. Synthesis and structure-activity studies on novel analogs of human growth hormone releasing hormone (GHRH) with enhanced inhibitory activities on tumor growth DRAMP32775 YADAIFTXSYRKVLGQLSARKLLQDIMSR 29 MIA-606 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP (~90%Inhibition=5 µM) Not available Linear Free Free X=N-methyl Ala L Not available Not available 28130121 Peptides. 2017 Mar;89:60-70 Zarandi M, Cai R, Kovacs M, Popovics P, Szalontay L, Cui T, Sha W, Jaszberenyi M, Varga J, Zhang X, Block NL, Rick FG, Halmos G, Schally AV. Synthesis and structure-activity studies on novel analogs of human growth hormone releasing hormone (GHRH) with enhanced inhibitory activities on tumor growth DRAMP32776 YADAIFTAXXHKVLGQLSAHKLLQDIMSR 29 JMR-132 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP (~88%Inhibition=5 µM) Not available Linear Free Free X(9)=homoArg; X(10)=Tyr methyl ether L Not available Not available 28130121 Peptides. 2017 Mar;89:60-70 Zarandi M, Cai R, Kovacs M, Popovics P, Szalontay L, Cui T, Sha W, Jaszberenyi M, Varga J, Zhang X, Block NL, Rick FG, Halmos G, Schally AV. Synthesis and structure-activity studies on novel analogs of human growth hormone releasing hormone (GHRH) with enhanced inhibitory activities on tumor growth DRAMP32777 FLPLLLAGLPSFLCLVFKKC 20 Amurin-2a Not available Not found Rana amurensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=302.1 µM) Horse erythrocytes: 50% Hemolysis=439.0 µM Cyclic Free Free L HMEC-1: IC50=1545 µM Not available 29366784 Biochem Biophys Res Commun. 2018 Mar 18;497(4):943-949. Zhang L, Chen X, Zhang Y, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T. Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues DRAMP32778 FLPKLLAGLPSFLCLVFKKC 20 Amurin-2a [L4K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=41.6 µM) "Horse erythrocytes: 50% Hemolysis=31.0 µM" Cyclic Free Free L HMEC-1: IC50=85.2 µM Not available 29366784 Biochem Biophys Res Commun. 2018 Mar 18;497(4):943-949. Zhang L, Chen X, Zhang Y, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T. Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues DRAMP32779 FLPLLLAGLPKFLCLVFKKC 20 Amurin-2a [S11K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=310.6 µM) "Horse erythrocytes: 50% Hemolysis=29.1 µM" Cyclic Free Free L HMEC-1: IC50=52.1 µM Not available 29366784 Biochem Biophys Res Commun. 2018 Mar 18;497(4):943-949. Zhang L, Chen X, Zhang Y, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T. Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues DRAMP32780 KRWRWRW 7 K(RW)3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (IC50=4.3 µM) Human erythrocytes: 50% Hemolysis=114 µM Linear C8 Free L Human fibroblasts: IC50=32.5 µM Not available 24900420 ACS Comb Sci. 2013 Nov 11;15(11):585-92. Albada HB, Prochnow P, Bobersky S, Langklotz S, Bandow JE, Metzler-Nolte N. Tuning the activity of a short arg-trp antimicrobial Peptide by lipidation of a C- or N-terminal lysine side-chain DRAMP32781 NIlLWG 6 Desotamide B [V2I] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=606.8 µM) Not available Cyclic Free Free l=D-Leu Mix Vero cells: IC50=90.8 µg/ml Not available 29125222 Chem Biodivers. 2018 Jan;15(1). Chen YX, Liu C, Liu N, Wu Y, Zhao QJ, Hu HG, Li X, Zou Y. Total Synthesis and Antibacterial Study of Cyclohexapeptides Desotamide B, Wollamide B and Their Analogs DRAMP32782 NVlLWX 6 Wollamide B [D-Orn6Orn] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=137.6 µM) Not available Cyclic Free Free l=D-Leu; X=Orn Mix Vero cells: IC50=73.2 µg/ml Not available 29125222 Chem Biodivers. 2018 Jan;15(1). Chen YX, Liu C, Liu N, Wu Y, Zhao QJ, Hu HG, Li X, Zou Y. Total Synthesis and Antibacterial Study of Cyclohexapeptides Desotamide B, Wollamide B and Their Analogs DRAMP32783 NGWLLI 6 Desotamide A Not available Not found Streptomyces scopuliridis SCSIO ZJ46 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>100 µM) Not available Cyclic Free Free L Not available Not available 25072108 J Nat Prod. 2014 Aug 22;77(8):1937-41. Song Y, Li Q, Liu X, Chen Y, Zhang Y, Sun A, Zhang W, Zhang J, Ju J. Cyclic Hexapeptides from the Deep South China Sea-Derived Streptomyces scopuliridis SCSIO ZJ46 Active Against Pathogenic Gram-Positive Bacteria DRAMP32784 XGNIlL 6 Desotamide C Not available Not found Streptomyces scopuliridis SCSIO ZJ47 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>100 µM) Not available Cyclic Free Free X=N-formyl-kynurenine; l=D-Leu Mix Not available Not available 25072108 J Nat Prod. 2014 Aug 22;77(8):1937-41. Song Y, Li Q, Liu X, Chen Y, Zhang Y, Sun A, Zhang W, Zhang J, Ju J. Cyclic Hexapeptides from the Deep South China Sea-Derived Streptomyces scopuliridis SCSIO ZJ46 Active Against Pathogenic Gram-Positive Bacteria DRAMP32785 XGNIlL 6 Desotamide C Not available Not found Streptomyces scopuliridis SCSIO ZJ47 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>100 µM) Not available Cyclic Free Free X=N-formyl-kynurenine; l=D-Leu Mix Not available Not available 25072108 J Nat Prod. 2014 Aug 22;77(8):1937-41. Song Y, Li Q, Liu X, Chen Y, Zhang Y, Sun A, Zhang W, Zhang J, Ju J. Cyclic Hexapeptides from the Deep South China Sea-Derived Streptomyces scopuliridis SCSIO ZJ46 Active Against Pathogenic Gram-Positive Bacteria DRAMP32786 XGNIlL 6 Desotamide D Not available Not found Streptomyces scopuliridis SCSIO ZJ48 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>100 µM) Not available Cyclic Free Free X=kynurenine; l=D-Leu Mix Not available Not available 25072108 J Nat Prod. 2014 Aug 22;77(8):1937-41. Song Y, Li Q, Liu X, Chen Y, Zhang Y, Sun A, Zhang W, Zhang J, Ju J. Cyclic Hexapeptides from the Deep South China Sea-Derived Streptomyces scopuliridis SCSIO ZJ46 Active Against Pathogenic Gram-Positive Bacteria DRAMP32787 XGNIlL 6 Desotamide D Not available Not found Streptomyces scopuliridis SCSIO ZJ48 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50>100 µM) Not available Cyclic Free Free X=kynurenine; l=D-Leu Mix Not available Not available 25072108 J Nat Prod. 2014 Aug 22;77(8):1937-41. Song Y, Li Q, Liu X, Chen Y, Zhang Y, Sun A, Zhang W, Zhang J, Ju J. Cyclic Hexapeptides from the Deep South China Sea-Derived Streptomyces scopuliridis SCSIO ZJ46 Active Against Pathogenic Gram-Positive Bacteria DRAMP32788 fxisfSSxFSVix 13 Syn-BNP (1) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC=64 µg/ml) Not available Linear C10 Free f=D-Phe; x=D-Orn; i=D-Ile; s=D-Ser Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32789 fxisfSSxFSViX 13 Syn-BNP (1.HMA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free f=D-Phe; x=D-Orn; i=D-Ile; s=D-Ser; X=Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32790 fxiswSSxWSViX 13 Syn-BNP (1N) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C10 Free f=D-Phe; x=D-Orn; i=D-Ile; s=D-Ser; w=D-Trp; X=Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32791 fxisvSSxVSViX 13 Syn-BNP (1S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C10 Free f=D-Phe; x=D-Dab; i=D-Ile; s=D-Ser; v=D-Val; X=Dab Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32792 kLGvPLKRK 9 Syn-BNP (2) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; v=D-Val Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32793 kSGxKHKKK 9 Syn-BNP (2S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; x=D-Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32794 aLGvPLKRK 9 Syn-BNP (2. Ala1) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free a=D-Ala; x=D-Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32795 kLGvALKRK 9 Syn-BNP (2. Ala5) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; v=D-Val Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32796 kLGvPLARK 9 Syn-BNP (2. Ala7) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; v=D-Val Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32797 kLGvPLKAK 9 Syn-BNP (2. Ala8) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; v=D-Val Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32798 kLGvPLKRA 9 Syn-BNP (2. Ala9) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free k=D-Lys; v=D-Val Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32799 WEXWtIW 7 Syn-BNP (2.81) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free t=D-Thr; X=Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32800 WyTxXxTwxWXY 12 Syn-BNP (3.29) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC=64 µg/ml) Not available Linear C14OH Free y=D-TYR; x(4/6)=D-Orn; w=D-Trp; x(9)=D-Dab; X=Orn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32801 XrIRL 5 Syn-BNP (3.46) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC=64 µg/ml) Not available Linear C14OH Free X=Orn; r=D-Arg Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32802 sRxRtLxTTnGT 12 Syn-BNP (3.85) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC>128 µg/ml) Not available Linear C14OH Free s=D-Ser; x=D-Dab; t=D=Thr; n=D-Asn Mix Not available Not available 28055186 J Am Chem Soc. 2017 Feb 1;139(4):1404-1407. Vila-Farres X, Chu J, Inoyama D, Ternei MA, Lemetre C, Cohen LJ, Cho W, Reddy BV, Zebroski HA, Freundlich JS, Perlin DS, Brady SF. Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters DRAMP32803 GKEFKRIVWLSKTAKKL 17 LL37 (14-21)+Cecropin-P1 (2-9), LC P49913##P14661 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (Not active up to 128 µM) Human erythrocytes: 5%Hemolysis>128 µM Linear Free Amidation L Not available Not available 29282543 Amino Acids. 2018 Apr;50(3-4):453-468. Dong N, Li XR, Xu XY, Lv YF, Li ZY, Shan AS, Wang JL. Characterization of bactericidal efficiency, cell selectivity, and mechanism of short interspecific hybrid peptides DRAMP32804 GKEFKRIVKWPWWPWRR 17 LL37 (14-21)+Indolicidin (5-13), LI P49913##P33046 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (87.5% Killing=128µM) Human erythrocytes: 5%Hemolysis>128 µM Linear Free Amidation L Not available Not available 29282543 Amino Acids. 2018 Apr;50(3-4):453-468. Dong N, Li XR, Xu XY, Lv YF, Li ZY, Shan AS, Wang JL. Characterization of bactericidal efficiency, cell selectivity, and mechanism of short interspecific hybrid peptides DRAMP32805 GKEFKRIVGRIYRLCCR 17 LL37 (14-21)+NP-1 (23-31), LN P49913##Q62716 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (80% Killing=128µM) Human erythrocytes: 5%Hemolysis>128 µM Linear Free Amidation L Not available Not available 29282543 Amino Acids. 2018 Apr;50(3-4):453-468. Dong N, Li XR, Xu XY, Lv YF, Li ZY, Shan AS, Wang JL. Characterization of bactericidal efficiency, cell selectivity, and mechanism of short interspecific hybrid peptides DRAMP32806 KKIGQKIKNFFQKL 14 CRAMP (20-35) P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32807 KKIWQKIKNFFQKL 14 CRAMP (20-35)[G4W] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32808 KRIWQKIKNFFQKL 14 CRAMP (20-35)[K2R][G4W] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32809 KKIWQRIKNFFQKL 14 CRAMP (20-35)[G4W][K6R] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50=50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32810 KKIWQKIRNFFQKL 14 CRAMP (20-35)[G4W][K8R] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32811 KKIWQKIKRFFQKL 14 CRAMP (20-35)[G4W][K8R] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32812 KKIWQKIKNFFRKL 14 CRAMP (20-35)[G4W][Q12R] P51437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (EC50>50µM) Not available Linear Free Free L Not available Not available 30176261 Peptides. 2018 Nov;109:33-38. Winderickx S, De Brucker K, Bird MJ, Windmolders P, Meert E, Cammue BPA, Thevissen K. Structure-activity relationship study of the antimicrobial CRAMP-derived peptide CRAMP20-33 DRAMP32813 FLSLIPKAISAVSALANHF 19 Phylloseptin-PHa [A7K] A0A2I2KHV2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (LD50=33.65 µM) Horse erythrocytes:50% Hemolysis=197.7µM Linear Free Amidation L Not available Not available 30774309 Drug Des Devel Ther. 2019 Jan 23;13:447-458 Liu Y, Du Q, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T, Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities DRAMP32814 FLSLIPKAISAISALANHF 19 Phylloseptin-Pha [A7K, V12I] A0A2I2KHV2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (LD50=36.46 µM) Horse erythrocytes:50% Hemolysis=34.86µM Linear Free Amidation L Not available Not available 30774309 Drug Des Devel Ther. 2019 Jan 23;13:447-458 Liu Y, Du Q, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T, Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities DRAMP32815 FLSLIPKAISAISALINHF 19 Phylloseptin-PHa [A7K, V12I, A16I] A0A2I2KHV2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (LD50=10.85 µM) Horse erythrocytes:50% Hemolysis=9.266µM Linear Free Amidation L Not available Not available 30774309 Drug Des Devel Ther. 2019 Jan 23;13:447-458 Liu Y, Du Q, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T, Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities DRAMP32816 FLSLIPKIISAISALINHF 19 Phylloseptin-PHa [A7K, A8I, V12I, A16I] A0A2I2KHV2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (LD50=9.547 µM) Horse erythrocytes:50% Hemolysis=2.766µM Linear Free Amidation L Not available Not available 30774309 Drug Des Devel Ther. 2019 Jan 23;13:447-458 Liu Y, Du Q, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T, Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities DRAMP32817 FLSLIPKIISAISALIKHF 19 Phylloseptin-PHa [A7K, A8I, V12I, A16I, N17K] A0A2I2KHV2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-251MG (LD50=4.059 µM) Horse erythrocytes:50% Hemolysis=1.074µM Linear Free Amidation L Not available Not available 30774309 Drug Des Devel Ther. 2019 Jan 23;13:447-458 Liu Y, Du Q, Ma C, Xi X, Wang L, Zhou M, Burrows JF, Chen T, Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities DRAMP32818 WFGKLYRGKTKVVKKVKGLLKG 22 Chionodracine [F1W; H4,15,17K; I9K; S11,21K] K4Q515 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SH-SY5Y (0% Killing=64 µM) Human erythrocytes: 5% Hemolysis=3µM; 30% Hemolysis=50µM Linear Free Free L HUVEC: 3.84% Killing=64 µM Not available 30790604 Dev Comp Immunol. 2019 Jul;96:9-17. Buonocore F, Picchietti S, Porcelli F, Della Pelle G, Olivieri C, Poerio E, Bugli F, Menchinelli G, Sanguinetti M, Bresciani A, Gennari N, Taddei AR, Fausto AM, Scapigliati G. Fish-derived antimicrobial peptides: Activity of a chionodracine mutant against bacterial models and human bacterial pathogens DRAMP32819 QLGKKKHRRRPSKKKRHW 18 HEXIM1 (147-164), BR O94992 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (5%Killing=100 µM) Not available Linear Free Free L HaCat: Not active up to 100 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32820 QLGRRRHRRRPSRRRRHW 18 HEXIM1 (147-164)[K4,5,6,13,14,15R], BR-RRR12 O94992 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (25%Killing=100 µM) Not available Linear Free Free L HaCat: Not active up to 100 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32821 AAVALLPAVLLALLAPMPFSTGKRIMLGE 29 FGR (7-22)-X13, FGF-X13 P08620 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OCI-AML3 (Not active up to 100 µM) Not available Linear Free Free L HEK293: Not active up to 100 µM; HFF: Not active up to 100 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32822 AAVALLPAVLLALLAPQLGKKKHRRRPSKKKRHW 34 FGR (7-22)-HEXIM1 (147-164), FGF-BR P08620##O94992 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116-/-p53 (30%Killing=10 µM) Not available Linear Free Free L HEK293: 30%Killing=10 µM; HFF: 20%Killing=10 µM; 90%Killing=50 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32823 LTVSPWYGCGQLGKKKHRRRPSKKKRHW 28 LTV-HEXIM1 (147-164, LTV-BR O94992 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OPM-2 (30%Killing=50 µM) Not available Linear Free Free L CHO-K1: 0%Killing=50 µM; HFF: 10%Killing=50 µM; WI-38: 5%Killing=50 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32824 LTVSPWYGCGQLGRRRHRRRPSRRRRHW 28 LTV-HEXIM1 (147-164)[K4,5,6,13,14,15R], LTV-BR (RRR12) O94992 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (78%Killing=10 µM; 100%Killing=50 µM) Not available Linear Free Free L Not available Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32825 MPFSTGKRIMLGE 13 X13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 100 µM) Not available Linear Free Free L Not available Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32826 LTVSPWYGCGMPFSTGKRIMLGE 23 LTV-X13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OPM-2 (0%Killing=50 µM) Not available Linear Free Free L CHO-K1: 0%Killing=50 µM; HFF: 0%Killing=50 µM; WI-38: 0%Killing=50 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32827 LTVSPWYGCGKLAKLAKKLAKLAK 24 LTV-PAP, LTV-KLA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OPM-2 (78%Killing=10 µM; 100%Killing=50 µM) Not available Linear Free Free L CHO-K1: 100%Killing=50 µM; HFF: 80%Killing=50 µM; WI-38: 55%Killing=50 µM Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32828 AAVALLPAVLLALLAPQLGRRRHRRRPSRRRRHW 34 FGR (7-22)-HEXIM1 (147-164)[K4,5,6,13,14,15R], FGF-BR(RRR12) O94992##P08620 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116-/-p53 (100%Killing=10 µM) Not available Linear Free Free L Not available Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32829 AAVALLPAVLLALLAPQLGKKILAARPSKKKRHW 34 FGR (7-22)-HEXIM1 (147-164)[K6I,H7L][R8,9A], FGF-BR(ILAA) O94992##P08620 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116-/-p53 (65%Killing=10 µM; 100%Killing=50 µM) Not available Linear Free Free L Not available Not available 26734838 Oncotarget. 2016 Feb 2;7(5):5483-94. Neo SH, Lew QJ, Koh SM, Zheng L, Bi X, Chao SH. Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy DRAMP32830 ALFGILKKAFGKILTIFAGLPGVV 24 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=8.6 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32831 GLGDFIKAIAKHLGPLIGILPSKLKVAA 28 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=11.3 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32832 GLKDPLKSVAKHLVK 15 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32833 GLVMLVKKAGLT 12 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32834 IIFGVIKALSG 11 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32835 FLGPTIGKIAKFILKHIVGLGDAALV 26 6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=10.7 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32836 GIVTILKGAVGVILGGL 17 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32837 GLFKIISGIA 10 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32838 GLGMIAHGV 9 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32839 GLWKILKKGA 10 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32840 GLFAILKKLVNLVG 14 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=4.6 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32841 GLFKIISKLAKKA 13 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=36.3 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32842 GLPLFLKKLGSAV 13 13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32843 GLWGVIKALGGHVG 14 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32844 GLLALLGELAEHLGSKI 17 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32845 GTFAIIQ 7 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32846 GDGDIMKGIAGH 12 20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32847 GLPQIISKVVKT 12 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 μM) Not available Linear Free Amidation L Not available Not available 30953170 J Mol Model. 2019 Apr 5;25(5):112. Grisoni F, Neuhaus CS, Hishinuma M, Gabernet G, Hiss JA, Kotera M, Schneider G. De novo design of anticancer peptides by ensemble artificial neural networks DRAMP32848 GIKKWLHSAKKFGKKFVKKIXNS 23 Magainin-2 [G3,18K; F5W; A15K; E19K; M21Nle] P11006 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (EC50=9.1±3 µM(pH=7.4)) Human kidney-derived GM cells: EC50=7.6±2.1 µM(pH=6); EC50=25.6±4.5 µM(pH=7.4) Linear Free Amidation X=Nle L HEK293: EC50=15.7±1.8 µM(pH=7.4) Not available 31161686 Chembiochem. 2019 Aug 16;20(16):2109-2117. Tanishiki N, Yano Y, Matsuzaki K. Endowment of pH responsivity to anticancer peptides by introducing 2,3-diaminopropionic acid residues DRAMP32849 GIKXWLHSAKKFGXKFVKKIXNS 23 Magainin-2 [G3,18K; K4,14Dap; F5W; A15K; E19K; M21Nle] P11006 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (EC50=14.7±0.6 µM(pH=7.4)) Human kidney-derived GM cells: EC50=25.9±0.6 µM(pH=6); EC50=50.3±0.9 µM(pH=7.4) Linear Free Amidation X(4/14)=Dap; X(21)=Nle L HEK293: EC50=27.2±3.1 µM(pH=7.4) Not available 31161686 Chembiochem. 2019 Aug 16;20(16):2109-2117. Tanishiki N, Yano Y, Matsuzaki K. Endowment of pH responsivity to anticancer peptides by introducing 2,3-diaminopropionic acid residues DRAMP32850 GIKXWLHSAXKFGXKFVKXIXNS 23 Magainin-2 [G3,18K; K4,10,14Dap; F5W; A15K; E19Dap; M21Nle] P11006 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (EC50=35.7±0.7 µM(pH=7.4)) Human kidney-derived GM cells: EC50=21.1±0.3 µM(pH=6); EC50=91.6±5.9 µM(pH=7.4) Linear Free Amidation X(4/10/14/19)=Dap; X(21)=Nle L HEK293: EC50>100 µM(pH=7.4) Not available 31161686 Chembiochem. 2019 Aug 16;20(16):2109-2117. Tanishiki N, Yano Y, Matsuzaki K. Endowment of pH responsivity to anticancer peptides by introducing 2,3-diaminopropionic acid residues DRAMP32851 GIKXWLHSAXXFGXKFVXXIXNS 23 Magainin-2 [G3K; K4,10,11,14Dap; F5W; A15K; G18Dap; E19Dap; M21Nle] P11006 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (EC50=55±1.8 µM(pH=7.4)) "Human kidney-derived GM cells: EC50= 19.8±0.3 µM(pH=6); EC50>100 µM(pH=7.4)" Linear Free Amidation X(4/10/11/14/18/19)=Dap; X(21)=Nle L HEK293: EC50>100 µM(pH=7.4) Not available 31161686 Chembiochem. 2019 Aug 16;20(16):2109-2117. Tanishiki N, Yano Y, Matsuzaki K. Endowment of pH responsivity to anticancer peptides by introducing 2,3-diaminopropionic acid residues DRAMP32852 GIXXWLHSAXXFGXXFVXXIXNS 23 Magainin-2 [G3,18Dap; K4,10,11,14Dap; F5W; A15Dap; E19Dap; M21Nle] P11006 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (EC50=61.4±1.7 µM(pH=7.4)) Human kidney-derived GM cells: EC50=7.6±2.1 µM(pH=6); EC50=25.6±4.5 µM(pH=7.4) Linear Free Amidation X(3/4/10/11/14/15/18/19)=Dap; X(21)=Nle L HEK293: EC50=15.7±1.8 µM(pH=7.4) Not available 31161686 Chembiochem. 2019 Aug 16;20(16):2109-2117. Tanishiki N, Yano Y, Matsuzaki K. Endowment of pH responsivity to anticancer peptides by introducing 2,3-diaminopropionic acid residues DRAMP32853 LAANFLPQILCKIARKC 17 B1CTcu5-LIAG E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 30% Hemolysis=200 µM Cyclic Free Amidation L HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity>100 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32854 KIAGLAANFLPQILCKIARKC 21 B1CTcu5K E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 15% Hemolysis=200 µM Cyclic Free Amidation L HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity=74.5±2.44 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32855 WIAGLAANFLPQILCKIARKC 21 B1CTcu5W E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 39.11% Hemolysis=200 µM Linear Free Amidation L HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity>100 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32856 RIAGLAANFLPQILCKIARKC 21 B1CTcu5R E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 17.4% Hemolysis=200 µM Linear Free Amidation L HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity=75.1±1.46 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32857 HIAGLAANFLPQILCKIARKC 21 B1CTcu5H E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 30.4% Hemolysis=200 µg/ml Linear Free Amidation L HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity=90±2.56 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32858 liaGlaanflpqilckiarkc 21 B1CTcu5D E3SYG2##D2K8D1##C3RTH8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (50% Cytotoxicity>100 µg/ml) Human erythrocytes: 40.22% Hemolysis=200 µg/ml Cyclic Free Amidation D HEK293: 50%Cytotoxicity>100 µg/ml; PBMC: 50%Cytotoxicity=71.4±2.3 µg/ml Not available 25997127 PLoS One. 2015 May 21;10(5):e0124210. Abraham P, Sundaram A, R A, V R, George S, Kumar KS. Structure-Activity Relationship and Mode of Action of a Frog Secreted Antibacterial Peptide B1CTcu5 Using Synthetically and Modularly Modified or Deleted (SMMD) Peptides DRAMP32859 AIIKKIIKKIIKKI 14 A-I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=25 µM) Human erythrocytes: 5% Hemolysis=300 µM; Human erythrocytes: 10% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 25% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32860 EIIKKIIKKIIKKI 14 E-I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=23 µM) Human erythrocytes: 5% Hemolysis=300 µM; Human erythrocytes: 7% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 23% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32861 KIIKKIIKKIIKKI 14 K-I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=20 µM) Human erythrocytes: 5% Hemolysis=300 µM; Human erythrocytes: 8% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 40% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32862 VIIKKIIKKIIKKI 14 V-I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=15 µM) Human erythrocytes: 7% Hemolysis=300 µM; Human erythrocytes: 12% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 25% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32863 GIIKKIIKKIIKKA 14 G-A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50>40 µM) Human erythrocytes: 5% Hemolysis=300 µM; Human erythrocytes: 15% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 25% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32864 GIIKKIIKKIIKKE 14 G-E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50>40 µM) Human erythrocytes: 0% Hemolysis=500 µM Linear Free Amidation L Not active up to 40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32865 GIIKKIIKKIIKKK 14 G-K Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50>40 µM) Human erythrocytes: 0% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 10% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32866 GIIKKIIKKIIKKV 14 G-V Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=15 µM) Human erythrocytes: 22% Hemolysis=300 µM; Human erythrocytes: 35% Hemolysis=500 µM Linear Free Amidation L Human chondrocytes-articular cells Hca: 50% Killing=40 µM Not available 27644109 ACS Appl Mater Interfaces. 2016 Oct 12;8(40):26501-26510. Chen C, Yang C, Chen Y, Wang F, Mu Q, Zhang J, Li Z, Pan F, Xu H, Lu JR. Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity DRAMP32867 KLWKKIEKLIKKLLTSIR 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=47±3 µM) Human erythrocytes: 50% Hemolysis=236±13 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32868 YIWARAERVWLWWGKFLSL 19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=56±3 µM) Human erythrocytes: Not active up to 400 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32869 DLFKQLQRLFLGILYCLYKIW 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=47±4 µM) Human erythrocytes：50% Hemolysis=132±16 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32870 AIKKFGPLAKIVAKV 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=95±4 µM) Human erythrocytes: Not active up to 400 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32871 RWNGRIIKGFYNLVKIWKDLKG 22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=42±4 µM) Human erythrocytes：50% Hemolysis=89±6 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32872 KVWKIKKNIRRLLHGIKRGWKG 22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=34±4 µM) Human erythrocytes: Not active up to 400 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32873 GFWARIGKVFAAVKNL 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=101±4 µM) Human erythrocytes: Not active up to 400 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32874 AFLYRLTRQIRPWWRWLYKW 20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=45.5±0.8 µM) Human erythrocytes: 50% Hemolysis=34±5 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32875 RIWGKHSRYIKIVKRLIQ 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=50±10 µM) Human erythrocytes: Not active up to 400 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32876 QIWHKIRKLWQIIKDGF 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=16.1±0.3 µM) Human erythrocytes: 50% Hemolysis=23±5 µM Linear Free Amidation L Not available Not available 29679519 ChemMedChem. 2018 Jul 6;13(13):1300-1302. Grisoni F, Neuhaus CS, Gabernet G, Müller AT, Hiss JA, Schneider G. Designing Anticancer Peptides by Constructive Machine Learning DRAMP32877 RPFTRAQWFAIQHISPRTIAMRAINNYRWR 30 RNase 3 (1-36)[P3,Q4,L18,N19,P20,C23DEL], RN3(5-17P22-36) P12724 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=74.43±1.91 µM) Sheep erythrocytes: 50% Hemolysis=178.33±81.72 µM; Horse erythrocytes: 44±4% Hemolysis=250 µM Linear Free Free L MRC-5: IC50>150 µM Not available 29763807 Eur J Med Chem. 2018 May 25;152:590-599. Pulido D, Prats-Ejarque G, Villalba C, Albacar M, Moussaoui M, Andreu D, Volkmer R, Torrent M, Boix E. Positional scanning library applied to the human eosinophil cationic protein/RNase3 N-terminus reveals novel and potent anti-biofilm peptides DRAMP32878 RPFIRAQWFAIQHISPRTIAMRAINNYRWR 30 RN3(5-17P22-36)[T4I] P12724 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=95.78±6.37 µM) Sheep erythrocytes:50% Hemolysis>150 µM Linear Free Free L MRC-5: IC50>150 µM Not available 29763807 Eur J Med Chem. 2018 May 25;152:590-599. Pulido D, Prats-Ejarque G, Villalba C, Albacar M, Moussaoui M, Andreu D, Volkmer R, Torrent M, Boix E. Positional scanning library applied to the human eosinophil cationic protein/RNase3 N-terminus reveals novel and potent anti-biofilm peptides DRAMP32879 RPFTRAQIFAIQHISPRTIAMRAINNYRWR 30 RN3(5-17P22-36)[W8I] P12724 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=171.55±1.23 µM) Sheep erythrocytes: 50% Hemolysis>150 µM Linear Free Free L MRC-5: IC50>150 µM Not available 29763807 Eur J Med Chem. 2018 May 25;152:590-599. Pulido D, Prats-Ejarque G, Villalba C, Albacar M, Moussaoui M, Andreu D, Volkmer R, Torrent M, Boix E. Positional scanning library applied to the human eosinophil cationic protein/RNase3 N-terminus reveals novel and potent anti-biofilm peptides DRAMP32880 RPFTRAQWFAIIHISPRTIAMRAINNYRWR 30 RN3(5-17P22-36)[Q12I] P12724 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Hep-G2 (IC50=59.64±6.17 µM) Sheep erythrocytes: 50% Hemolysis>100µM Linear Free Free L MRC-5: IC50>100 µM Not available 29763807 Eur J Med Chem. 2018 May 25;152:590-599. Pulido D, Prats-Ejarque G, Villalba C, Albacar M, Moussaoui M, Andreu D, Volkmer R, Torrent M, Boix E. Positional scanning library applied to the human eosinophil cationic protein/RNase3 N-terminus reveals novel and potent anti-biofilm peptides DRAMP32881 MRGENMSEGNRPEGTPHGLRSTPARELPIPAFLEPAR 37 KA081020-065 I3TKW5 Not found Tistrella mobilis (strain KA081020-065) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22458477 J Am Chem Soc. 2012 May 23;134(20):8625-32. Xu Y, Kersten RD, Nam SJ, Lu L, Al-Suwailem AM, Zheng H, Fenical W, Dorrestein PC, Moore BS, Qian PY. Bacterial biosynthesis and maturation of the didemnin anti-cancer agents DRAMP32882 GTTCYCGKTIGIYWFGKYSCPTNRGYTGSCPYFLGICCYPVD 42 APETx4 C0HL40 Not found Anthopleura elegantissima (Green aggregating anemone) (Actinia elegantissima) Antimicrobial, Anticancer Not found Not found Not found Not available APETx4 is able to selectively inhibit the human ether-à-go-go channel (hEag1 or KV10.1), which a cancer-relevant voltage-gated potassium channel that is overexpressed in a majority of human tumors. Tumor cells: MDA-MB-435S (KV10.1 Expression Level: Moderate) Not available Linear Free Free L NIH-3T3: KV10.1 Expression Level (Undetectable); Human epithelial cell line hTERT RPE-1: KV10.1 Expression Level (Moderate) Not available 28902151 Mar Drugs. 2017 Sep 13;15(9):287. Moreels L, Peigneur S, Galan DT, De Pauw E, Béress L, Waelkens E, Pardo LA, Quinton L, Tytgat J. APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KV10.1 DRAMP32883 EGKLSSNDTEGGLCKEFLHPSKVDLPR 27 SOR-C27 Not available Not found Blarina brevicauda Antimicrobial, Anticancer Not found Not found Not found Not available SOR-C13 and SOR-C27, derived from the C-terminus of soricidin, are high-affinity antagonists of human TRPV6 channels that are up-regulated in a number of cancers Tumor cells: HeLa (~95%Inhibition=100 µM) Not available Linear Free Free L Not available Not available 23554944 PLoS One. 2013;8(3):e58866. Bowen CV, DeBay D, Ewart HS, Gallant P, Gormley S, Ilenchuk TT, Iqbal U, Lutes T, Martina M, Mealing G, Merkley N, Sperker S, Moreno MJ, Rice C, Syvitski RT, Stewart JM. In Vivo Detection of Human TRPV6-Rich Tumors with Anti-Cancer Peptides Derived from Soricidin DRAMP32884 KEFLHPSKVDLPR 13 SOR-C13 Not available Not found Blarina brevicauda Antimicrobial, Anticancer Not found Not found Not found Not available SOR-C13 and SOR-C27, derived from the C-terminus of soricidin, are high-affinity antagonists of human TRPV6 channels that are up-regulated in a number of cancers Tumor cells: HeLa (~18%Inhibition=100 µM) Not available Linear Free Free L Not available Not available 23554944 PLoS One. 2013;8(3):e58866. Bowen CV, DeBay D, Ewart HS, Gallant P, Gormley S, Ilenchuk TT, Iqbal U, Lutes T, Martina M, Mealing G, Merkley N, Sperker S, Moreno MJ, Rice C, Syvitski RT, Stewart JM. In Vivo Detection of Human TRPV6-Rich Tumors with Anti-Cancer Peptides Derived from Soricidin DRAMP32885 NEPCDSDGDCCTSSEQCISTGSKYFC 26 CCP-Ts sub peptide (14-39) P0DM29 Not found Tityus serrulatus Antimicrobial, Anticancer Not found Not found Not found Not available As a drug delivery system targeting cancer cell nucleus using CPP-Ts’s nuclear-targeting property. Tumor cells: DU145 (Sub peptide was internalized and directed to the intranuclear region.) Not available Linear Free Free L HUV-EC-C, HFF-1, MCR-5, HEK-293, BHK-21, MDCK: sub peptide was unable to cross the cell membrane Not available 30282983 Sci Rep. 2018 Oct 3;8(1):14739. Oliveira-Mendes BBR, Horta CCR, do Carmo AO, Biscoto GL, Sales-Medina DF, Leal HG, Brandão-Dias PFP, Miranda SEM, Aguiar CJ, Cardoso VN, de Barros ALB, Chávez-Olortégui C, Leite MF, Kalapothakis E. CPP-Ts: a new intracellular calcium channel modulator and a promising tool for drug delivery in cancer cells DRAMP32886 GKWMSFLKHILK 12 HAL-2/6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=23±3 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50=69 μM Linear Free Amidation L HUVEC: IC50=55±9 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32887 gkwmsllkhilk 12 HAL-2/22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=12 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50=54 μM Linear Free Amidation D HUVEC: IC50=22±7 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32888 GKwMSLLKHILK 12 HAL-2/8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15±3 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50=99 μM Linear Free Amidation w=D-Trp Mix HUVEC: IC50=52±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32889 GKWMSLLKHIWK 12 HAL-2/18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=14±2 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50=87 μM Linear Free Amidation L HUVEC: IC50=56±9 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32890 GKWMSLLKHWLK 12 HAL-2/19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16±4 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50=106 μM Linear Free Amidation L HUVEC: IC50=40±1 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32891 GKWMSLLKKILK 12 HAL-2/4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=38±6 µM); HeLa (IC50> 40 µM) Rat erythrocytes: IC50=126 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32892 GKWMSLWKHILK 12 HAL-2/20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=30±5 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50>100 μM Linear Free Amidation L HUVEC: IC50=73±3 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32893 GKWMTLLKHILK 12 HAL-2/13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=13±3 µM); SW480 (IC50> 60 µM) Rat erythrocytes: IC50=86 μM Linear Free Amidation L HUVEC: IC50=60±12 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32894 GKWSKILGHLIR 12 HAL-1/12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=43±14 µM); SW480 (IC50> 100 µM); CCRF-CEM (IC50> 40 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32895 GKWSKILGKLIR 12 HAL-1/20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22±3 µM); CCRF-CEM (IC50> 40 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32896 GMWKKILGHLIR 12 HAL-1/5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=44±5 µM); HeLa (IC50=9±1 µM); CCRF-CEM (IC50> 40 µM) Rat erythrocytes: IC50=93 μM Linear Free Amidation L HUVEC: IC50=49±16 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32897 GMWKKILGKLIR 12 HAL-1/10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=13±2 µM); SW480 (IC50> 60 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=63±13 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32898 GMWSKILGHLIk 12 HAL-1/6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15±1 µM); SW480 (IC50> 100 µM) Rat erythrocytes: IC50=132 μM Linear Free Amidation Mix HUVEC: IC50=≥40 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32899 gmwskilghlir 12 HAL-1/22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15±3 µM); SW480 (IC50> 40 µM) Rat erythrocytes: IC50=52 μM Linear Free Amidation D HUVEC: IC50=42±7 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32900 GMWSkILGHLIR 12 HAL-1/29 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation k=D-Lys Mix HUVEC: IC50> 100 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32901 GMWSKILGHLKR 12 HAL-1/4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50> 100 µM) Rat erythrocytes: IC50>200 μM Linear Free Amidation L HUVEC: IC50=NA μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32902 GMWSKILGKLIR 12 HAL-1/9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CCRF-CEM (IC50=30±10 µM); HeLa (IC50=9±1 µM); SW480 (IC50> 50 µM) Rat erythrocytes: IC50=143 μM Linear Free Amidation L HUVEC: IC50=≥40 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32903 GMWSKILKHLIR 12 HAL-1/18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW480 (IC50=18±2 µM); HeLa (IC50=4±2 µM) Rat erythrocytes: IC50=45 μM Linear Free Amidation L HUVEC: IC50=20±4 μM Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP32904 CVRRFPWWYPFLRRC 15 Tritrp DiSu Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=12.3 µM) RBC: IC50=20.9 µM Cyclic Free Amidation L PBMC: IC50=26.2 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32905 FRVTXRTKXXKG 12 PuroB3-hW Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation X=HTrp=5-hydroxytryptophan L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32906 GALFLGFLGAAGSTMGAWSQPKKKRKV 27 MPG Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=15.8 µM) RBC: IC50 ≥ 65 µM Linear Free Cysteamidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32907 FPVTWKWWKWWKG 13 PuroA-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=10.0 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=23.0 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32908 FRVTWRTKWWKG 12 PuroB3 Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32909 GIGKWLHSAKKFGKAFVGEIMNS 23 MagaininF5W-Lys Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=16.8 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32910 FPVTWRWWRWWRG 13 PuroA-Arg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=12.0 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50=34.3 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32911 FRWWHR 6 Combi-2 Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50 ≥ 65 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32912 GIGRWLHSARRFGRAFVGEIMNS 23 MagaininF5W-Arg Not available Not found porcine cathelicidin peptide Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=16.8 µM) RBC: IC50 ≥ 65 µM Linear Free Amidation L PBMC: IC50 ≥ 65 µM Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of synthetic peptides derived from the host defence peptide tritrpticin DRAMP32913 CHHNLTHAC 9 PTPRJ pep-19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (19 ± 2.82% Inhibition=160 μM); HeLa (4.5 ± 0.1.4% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32914 CHHNLTHAC 9 PTPRJ pep-19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (4 ± 1.4% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32915 CHHNLTHAC 9 PTPRJ pep-19.0 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (19 ± 2.82% Inhibition=160 μM); HeLa (4.5 ± 0.1.4% Inhibition=160 μM) Not available Linear Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32916 CHHNLTHAC 9 PTPRJ pep-19.0 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (4 ± 1.4% Inhibition=160 μM) Not available Linear Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32917 CAHNLTHAC 9 PTPRJ pep-19.2 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (16.5 ± 2.12% Inhibition=160 μM); HeLa (30 ± 2.82% Inhibition=160 μM); HeLa (32.0 ± 4.2% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32918 CHANLTHAC 9 PTPRJ pep-19.3 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (28 ± 5.5% Inhibition=160 μM); HeLa (46 ± 4.2% Inhibition=160 μM); HeLa (51 ± 1.4% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32919 CHHALTHAC 9 PTPRJ pep-19.4 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (48.0 ± 2.82% Inhibition=160 μM); HeLa (62.5 ± 4.9% Inhibition=160 μM); HeLa (66.5 ± 2.12% Inhibition=160 μM) Not available Cyclic Free Free L HUVEC: ~5% Inhibition=160 μM (24 h); ~25% Inhibition=160 μM (48 h); ~35% Inhibition=160 μM (24 h) PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32920 CHHNATHAC 9 PTPRJ pep-19.5 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (19 ± 4.2% Inhibition=160 μM); HeLa (2 ± 1.5% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32921 CHHNLAHAC 9 PTPRJ pep-19.6 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (19 ± 4.2% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32922 CHHNLTAAC 9 PTPRJ pep-19.7 Not available Not found Synthetic (Derived from PTPRJ pep-19) Antimicrobial, Anticancer Not found Not found Not found Not available PTPRJ is a receptor-type protein tyrosine phosphatase whose expression is strongly reduced in the majority of investigated cancer cell lines and tumor specimens.It showed tumor suppressor activity in several models. Tumor cells: HeLa (20 ± 1.4% Inhibition=160 μM); HeLa (4.5 ± 2.13% Inhibition=160 μM) Not available Cyclic Free Free L Not available PTPRJ 23627474 ACS Chem Biol. 2013 Jul 19;8(7):1497-506. Ortuso F, Paduano F, Carotenuto A, Gomez-Monterrey I, Bilotta A, Gaudio E, Sala M, Artese A, Vernieri E, Dattilo V, Iuliano R, Brancaccio D, Bertamino A, Musella S, Alcaro S, Grieco P, Perrotti N, Croce CM, Novellino E, Fusco A, Campiglia P, Trapasso F. Discovery of PTPRJ agonist peptides that effectively inhibit in vitro cancer cell proliferation and tube formation DRAMP32923 KAaK 4 Chol-KAaK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Human erythrocytes: 50% Hemolysis=60 µM Linear Cholesterol Amidation k=D-Lys Mix Not available Not available 22006001 Antimicrob Agents Chemother. 2012 Jan;56(1):1-9. Arnusch CJ, Ulm H, Josten M, Shadkchan Y, Osherov N, Sahl HG, Shai Y. Ultrashort peptide bioconjugates are exclusively antifungal agents and synergize with cyclodextrin and amphotericin B DRAMP32924 XFLGTLVNLAKKIL 14 Temporin-1DRa [Aib1] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=40 µM) Human erythrocytes: 50% Hemolysis=60 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=17 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32925 HXLGTLVNLAKKIL 14 Temporin-1DRa [Aib2] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=55 µM) Human erythrocytes: 50% Hemolysis=100 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=30 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32926 HFXGTLVNLAKKIL 14 Temporin-1DRa [Aib3] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=40 µM) Human erythrocytes: 50% Hemolysis=90 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=20 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32927 HFLXTLVNLAKKIL 14 Temporin-1DRa [Aib4] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=25 µM) Human erythrocytes: 50% Hemolysis=25 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=9 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32928 HFLGXLVNLAKKIL 14 Temporin-1DRa [Aib5] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=40 µM) Human erythrocytes: 50% Hemolysis=40 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=16 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32929 HFLGTXVNLAKKIL 14 Temporin-1DRa [Aib6] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50>200 µM) Human erythrocytes: 50% Hemolysis>200 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50>200 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32930 HFLGTLXNLAKKIL 14 Temporin-1DRa [Aib7] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=22 µM) Human erythrocytes: 50% Hemolysis=22 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=13 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32931 HFLGTLVXLAKKIL 14 Temporin-1DRa [Aib8] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=10 µM) Human erythrocytes: 50% Hemolysis=10 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=6 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32932 HFLGTLVNXAKKIL 14 Temporin-1DRa [Aib9] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=75 µM) Human erythrocytes: 50% Hemolysis=75 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=42 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32933 HFLGTLVNLXKKIL 14 Temporin-1DRa [Aib10] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=10 µM) Human erythrocytes: 50% Hemolysis=10 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=8 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32934 HFLGTLVNLAKKXL 14 Temporin-1DRa [Aib13] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=90 µM) Human erythrocytes: 50% Hemolysis=0 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=55 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Conlon JM, Al-Kharrge R, Ahmed E, Raza H, Galadari S, Condamine E. Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32935 HFLGTLVNLAKKIX 14 Temporin-1DRa [Aib14] Not available Not found Synthetic (Derived from Temporin-1DRa) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=130 µM) Human erythrocytes: 50% Hemolysis=130 µM Linear Free Amidation X=AIB (Aminoisobutyric acid) L Mouse fibroblasts L929: LC50=90 µM Not available 17767978 Peptides. 2007 Oct;28(10):2075-80. Amino Acids. 2013 Feb;44(2):715-23. AS1258:AT1259 Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa DRAMP32936 KYLNFAKWLKGANLAKYANA 20 GW-H1-scr Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AGS (IC50>500 µM) Not available Linear Free Free L NIH 3T3: IC50>500 μM Not available 25380626 Mol Cell Biochem. 2015 Feb;400(1-2):77-86. Pan WR, Chen YL, Hsu HC, Chen WJ. Antimicrobial peptide GW-H1-induced apoptosis of human gastric cancer AGS cell line is enhanced by suppression of autophagy DRAMP32937 ILKKLLSTAAGLLSNL 16 Alyteserin-2a [G3K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=100 μM) Human erythrocytes: 50% Hemolysis=105 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32938 ILGKLLKTAAGLLSNL 16 Alyteserin-2a [S7K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=35 μM) Human erythrocytes: 50% Hemolysis=28 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32939 ILGKLLkTAAGLLSNL 16 Alyteserin-2a [S7k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50>100 μM) Human erythrocytes: 50% Hemolysis=105 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32940 ILGKLLSTAAKLLSNL 16 Alyteserin-2a [G11K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=20 μM) Human erythrocytes: 50% Hemolysis=24 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32941 ILGKLLSTAAkLLSNL 16 Alyteserin-2a [G11k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=28 μM) Human erythrocytes: 50% Hemolysis=42 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32942 ILGKLLSTAAGLLKNL 16 Alyteserin-2a [S14K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=30 μM) Human erythrocytes: 50% Hemolysis=55 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32943 ILGKLLSTAAGLLSKL 16 Alyteserin-2a [N15K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=13 μM); HepG2 (LC50=17 μM); MDA-MB-231 (LC50=18 μM); HT-29 (LC50=32 μM) Human erythrocytes: 50% Hemolysis=50 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32944 ILGKLLSTAAGLLSkL 16 Alyteserin-2a [N15k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (LC50=125 μM); A549 (LC50=75 μM); MDA-MB-231 (LC50=80 μM); HepG2 (LC50=90 μM) Human erythrocytes: 50% Hemolysis=310 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32945 ILGKLLKTAAKLLSNL 16 Alyteserin-2a [S7K, G11K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=20 μM) Human erythrocytes: 50% Hemolysis=38 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32946 ILGKLLkTAAkLLSNL 16 Alyteserin-2a [S7k, G11k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=65 μM) Human erythrocytes: 50% Hemolysis=185 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32947 ILGKLLSTAAKLLSKL 16 Alyteserin-2a [G11K, N15K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (LC50=10 μM); HT-29 (LC50=18 μM); A549 (LC50=6 μM); HepG2 (LC50=8 μM) Human erythrocytes: 50% Hemolysis=16 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32948 ILGKLLSTAAkLLSKL 16 Alyteserin-2a [G11k, N15K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=15 μM); MDA-MB-231 (LC50=20 μM); HepG2 (LC50=26 μM); HT-29 (LC50=28 μM) Human erythrocytes: 50% Hemolysis=195 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32949 ILGKLLSWAAGLLSNL 16 Alyteserin-2a [T8W] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=12 μM) Human erythrocytes: 50% Hemolysis=13 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32950 ILGKLLSTWAGLLSNL 16 Alyteserin-2a [A9W] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=21 μM) Human erythrocytes: 50% Hemolysis=39 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32951 ILGKLLSTAWGLLSNL 16 Alyteserin-2a [A10W] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=7 μM) Human erythrocytes: 50% Hemolysis=11 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32952 ILGKLLSTAWkLLSNL 16 Alyteserin-2a [A10W, G11k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=17 μM) Human erythrocytes: 50% Hemolysis=21 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32953 ILGKLLSTAWGLLSKL 16 Alyteserin-2a [A10W, N15K] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=6 μM) Human erythrocytes: 50% Hemolysis=6 µM Linear Free Amidation L Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32954 ILGKLLSTAWALLSkL 16 Alyteserin-2a [A10W, N15k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=20 μM) Human erythrocytes: 50% Hemolysis=27 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32955 ILGKLLSTAWkLLSkL 16 Alyteserin-2a [A10W, G11k, N15k] Not available Not found Synthetic (Derived from Alyteserin-2a) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=17 μM) Human erythrocytes: 50% Hemolysis=68 µM Linear Free Amidation k=D-Lys Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, AS1258:AT1258Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP32956 KLKLKFKLKQ 10 BPC10L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 84 ± 6.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32957 KKKKKFLLLQ 10 BPC58 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 6 ± 0.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32958 KKKKLFKLLQ 10 BPC60 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 72 ± 5.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32959 KKKLKFKLLQ 10 BPC62 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 6 ± 0.6% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32960 KKLKKFKLLQ 10 BPC64 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 10 ± 2.0% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32961 KLKKKFKLLQ 10 BPC66 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (4 ± 0.11% Growth inhibition=40 μM) Human erythrocytes: 22 ± 4.0% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32962 LKKKKFKLLQ 10 BPC68 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 0 ± 0.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32963 KKKKLFLKLQ 10 BPC70 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (4 ± 0.07% Growth inhibition=40 μM) Human erythrocytes: 19 ± 0.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32964 KKKLKFLKLQ 10 BPC72 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (2 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 7 ± 2.0% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32965 KKLKKFLKLQ 10 BPC74 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (22 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 36 ± 1.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32966 KLKKKFLKLQ 10 BPC76 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (14 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 13 ± 1.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32967 LKKKKFLKLQ 10 BPC78 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (13 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 0 ± 0.4% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32968 KKKLLFKKLQ 10 BPC80 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (9 ± 0.11% Growth inhibition=40 μM) Human erythrocytes: 19 ± 0.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32969 KKLKLFKKLQ 10 BPC82 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (25 ± 0.03% Growth inhibition=40 μM) Human erythrocytes: 36 ± 2.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32970 KLKKLFKKLQ 10 BPC84 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (27 ± 0.11% Growth inhibition=40 μM) Human erythrocytes: 45 ± 3.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32971 LKKKLFKKLQ 10 BPC86 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (8 ± 0.21% Growth inhibition=40 μM) Human erythrocytes: 8 ± 0.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32972 KKKKLFLLKQ 10 BPC100 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (6 ± 0.10% Growth inhibition=40 μM) Human erythrocytes: 1.8 ± 0.8% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32973 KKKLKFLLKQ 10 BPC102 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (23 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 26 ± 3.0% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32974 KKLKKFLLKQ 10 BPC104 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (11 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 15 ± 2.2% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32975 KLKKKFLLKQ 10 BPC106 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (17 ± 0.10% Growth inhibition=40 μM) Human erythrocytes: 0 ± 0.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32976 LKKKKFLLKQ 10 BPC108 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (9 ± 0.09% Growth inhibition=40 μM) Human erythrocytes: 2 ± 0.2% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32977 KKKLLFKLKQ 10 BPC110 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (14 ± 0.15% Growth inhibition=40 μM) Human erythrocytes: 9 ± 0.4% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32978 KKLKLFKLKQ 10 BPC112 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (9 ± 0.06% Growth inhibition=40 μM) Human erythrocytes: 1 ± 0.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32979 KLKKLFKLKQ 10 BPC114 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (17 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 24 ± 1.8% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32980 LKKKLFKLKQ 10 BPC116 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (5 ± 0.24% Growth inhibition=40 μM) Human erythrocytes: 13 ± 0.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32981 KKLLKFKLKQ 10 BPC118 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (19 ± 0.01% Growth inhibition=40 μM) Human erythrocytes: 6 ± 0.6% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32982 LKKLKFKLKQ 10 BPC120 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (12 ± 0.02% Growth inhibition=40 μM) Human erythrocytes: 8 ± 1.6% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32983 KLLKKFKLKQ 10 BPC122 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (7 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 4 ± 1.3% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32984 LKLKKFKLKQ 10 BPC124 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (4 ± 0.07% Growth inhibition=40 μM) Human erythrocytes: 3 ± 0.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32985 LLKKKFKLKQ 10 BPC126 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (8 ± 0.03% Growth inhibition=40 μM) Human erythrocytes: 4 ± 0.6% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32986 KKKLLFLKKQ 10 BPC128 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (22 ± 0.06% Growth inhibition=40 μM) Human erythrocytes: 1 ± 0.3% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32987 KKLKLFLKKQ 10 BPC130 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (15 ± 0.20% Growth inhibition=40 μM) Human erythrocytes: 6 ± 3.0% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32988 KLKKLFLKKQ 10 BPC132 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (18 ± 0.18% Growth inhibition=40 μM) Human erythrocytes: 4 ± 0.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32989 LKKKLFLKKQ 10 BPC134 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (3 ± 0.15% Growth inhibition=40 μM) Human erythrocytes: 2 ± 0.3% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32990 KKLLKFLKKQ 10 BPC136 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (29 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 41 ± 1.8% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32991 KLKLKFLKKQ 10 BPC138 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 5 ± 0.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32992 LKKLKFLKKQ 10 BPC140 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 23 ± 1.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32993 KLLKKFLKKQ 10 BPC142 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 14 ± 1.6% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32994 LKLKKFLKKQ 10 BPC144 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (7 ± 0.17% Growth inhibition=40 μM) Human erythrocytes: 9 ± 1.9% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32995 LLKKKFLKKQ 10 BPC146 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (12 ± 0.19% Growth inhibition=40 μM) Human erythrocytes: 3 ± 0.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32996 KKLLLFKKKQ 10 BPC148 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (19 ± 0.09% Growth inhibition=40 μM) Human erythrocytes: 1 ± 0.2% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32997 KLKLLFKKKQ 10 BPC150 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (11 ± 0.22% Growth inhibition=40 μM) Human erythrocytes: 4 ± 0.2% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32998 LKKLLFKKKQ 10 BPC152 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: 2 ± 0.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP32999 KLLKLFKKKQ 10 BPC154 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (28 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 11 ± 1.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33000 LKLKLFKKKQ 10 BPC156 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (1 ± 0.26% Growth inhibition=40 μM) Human erythrocytes: 3 ± 0.4% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33001 LLKKLFKKKQ 10 BPC158 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (2 ± 0.13% Growth inhibition=40 μM) Human erythrocytes: 9 ± 0.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33002 KLLLKFKKKQ 10 BPC160 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (20 ± 0.26% Growth inhibition=40 μM) Human erythrocytes: 3 ± 0.4% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33003 LKLLKFKKKQ 10 BPC162 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (16 ± 0.31% Growth inhibition=40 μM) Human erythrocytes: 2 ± 0.8% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33004 LLKLKFKKKQ 10 BPC164 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (16 ± 0.15% Growth inhibition=40 μM) Human erythrocytes: 4 ± 0.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33005 LLLKKFKKKQ 10 BPC166 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (5 ± 0.24% Growth inhibition=40 μM) Human erythrocytes: 0 ± 0.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33006 KKLLKFKKLQ 10 BPC88 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (50 ± 0.10% Growth inhibition=40 μM; IC50=31.2 ± 5 μM); HeLa (IC50=22.5 ± 0 μM); A431 (IC50=28.0 ± 3 μM); PANC-1 (IC50=32.5 ± 11 μM); HepG2 (IC50=32.5 ± 4 μM) Human erythrocytes: 33 ± 3.3% Hemolysis=375 µM; IC50=33 ± 3.3 µM Cyclic Free Free L Human non-malignant fibroblasts: IC50=42.0 ± 7.1 µM Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33007 KLKLKFKKLQ 10 BPC90 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (23 ± 0.17% Growth inhibition=40 μM) Human erythrocytes: 30 ± 4.1% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33008 LKKLKFKKLQ 10 BPC92 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (13 ± 0.08% Growth inhibition=40 μM) Human erythrocytes: 7 ± 0.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33009 KLLKKFKKLQ 10 BPC94 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (95 ± 0.01% Growth inhibition=40 μM; IC50=22.0 ± 0 μM); PANC-1 (IC50=18.5 ± 8 μM); HepG2 (IC50=20.5 ± 6 μM); A431 (IC50=21.5 ± 8 μM); HeLa (IC50=23.0 ± 3 μM) Human erythrocytes: 73 ± 1.6% Hemolysis=375 µM; IC50=73 ± 1.6 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33010 LKLKKFKKLQ 10 BPC96 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (59 ± 0.08% Growth inhibition=40 μM; IC50=40.0 ± 7 μM); HeLa (IC50=24.5 ± 0.7 μM); HepG2 (IC50=34.5 ± 2 μM); A431 (IC50=35.0 ± 7 μM); PANC-1 (IC50=51.0 ± 6 μM) Human erythrocytes: 32 ± 7.2% Hemolysis=375 µM; IC50=32 ± 7.2 µM Cyclic Free Free L Human non-malignant fibroblasts: IC50=39.0 ± 9.9 µM Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33011 LLKKKFKKLQ 10 BPC98 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (60 ± 0.07% Growth inhibition=40 μM; IC50=40.7 ± 3 μM); HeLa (IC50=38.5 ± 4 μM); HepG2 (IC50=44.0 ± 3 μM); PANC-1 (IC50=44.5 ± 0.7 μM); A431 (IC50=47.5 ± 4 μM) Human erythrocytes: 36 ± 3.7% Hemolysis=375 µM; IC50=36 ± 3.7 µM Cyclic Free Free L Human non-malignant fibroblasts: IC50=58.5 ± 2.1 µM Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33012 KLLLKFKKLQ 10 BPC184 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: MDA-MB-231 (88 ± 0.01% Growth inhibition=40 μM; IC50=32.2 ± 7 μM); A431 (IC50=24.5 ± 0.7 μM); HeLa (IC50=30.5 ± 12 μM); PANC-1 (IC50=41.5 ± 11 μM); HepG2 (IC50=42.2 ± 2 μM)" Human erythrocytes: 89 ± 5.3% Hemolysis=375 µM; IC50=89 ± 5.3 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33013 KKKLKFKKLQ 10 BPC186 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (22 ± 0.09% Growth inhibition=40 μM) Human erythrocytes: 0 ± 0.4% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33014 LLLKKFKKLQ 10 BPC188 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (14 ± 0.01% Growth inhibition=40 μM) Human erythrocytes: 87 ± 6.5% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33015 LKKKKFKKLQ 10 BPC190 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Not active up to 40 μM) Human erythrocytes: Not active up to 375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33016 LKLLKFKKLQ 10 BPC192 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (20 ± 0.05% Growth inhibition=40 μM) Human erythrocytes: 49 ± 7.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33017 KKLKKFKKLQ 10 BPC194 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (70 ± 0.01% Growth inhibition=40 μM; IC50=32.5 ± 0.5 μM); HeLa (IC50=29.5 ± 2 μM); PANC-1 (IC50=40.0 ± 3 μM); HepG2 (IC50=46.0 ± 3 μM); A431 (IC50=50.0 ± 10 μM) Human erythrocytes: 17 ± 1.7% Hemolysis=375 µM; IC50=17 ± 1.7 µM Cyclic Free Free L Human non-malignant fibroblasts: IC50=56.5 ± 0.7 µM Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33018 LLKLKFKKLQ 10 BPC196 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (18 ± 0.09% Growth inhibition=40 μM) Human erythrocytes: 47 ± 7.2% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33019 KLKKKFKKLQ 10 BPC198 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (56 ± 0.06% Growth inhibition=40 μM; IC50=53.2 ± 13 μM); HeLa (IC50=35.0 ± 1 μM); A431 (IC50=49.5 ± 6 μM); PANC-1 (IC50=57.5 ± 6 μM); HepG2 (IC50>60 μM) Human erythrocytes: 14 ± 1.4% Hemolysis=375 µM; IC50=14 ± 1.4 µM Cyclic Free Free L Human non-malignant fibroblasts: IC50=7.5 ± 0.7 µM Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33020 LLLLKFKKLQ 10 BPC200 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (11 ± 0.27% Growth inhibition=40 μM) Human erythrocytes: 71 ± 11.7% Hemolysis=375 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33021 KKKKKFKKLQ 10 BPC202 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (63 ± 0.02% Growth inhibition=40 μM; IC50=40.5 ± 9 μM); A431 (IC50=35.5 ± 2 μM); PANC-1 (IC50=43.5 ± 0.7 μM); HepG2 (IC50=46.0 ± 8 μM); HeLa (IC50=54.0 ± 6 μM) Human erythrocytes: 2 ± 0.2% Hemolysis=375 µM; IC50=2 ± 0.2 µM Cyclic Free Free L Not available Not available 20708052 Peptides. 2010 Nov;31(11):2017-26 Feliu L, Oliveras G, Cirac AD, Besalú E, Rosés C, Colomer R, Bardají E, Planas M, Puig T. Antimicrobial cyclic decapeptides with anticancer activity DRAMP33022 RIIDLLWRVWRPQKPKFVTVWVR 23 PMAP-23 [R10W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=19 µM); SNU-601 (IC50=28 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33023 RIIDLLWRVRRPWKPKFVTVWVR 23 PMAP-23 [Q13W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=20 µM); SNU-601 (IC50=30 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33024 RIIDLLWRVRRPQWPKFVTVWVR 23 PMAP-23 [K14W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=29 µM); SNU-601 (IC50=39 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33025 RIIDLLWRVRRPWWPKFVTVWVR 23 PMAP-23 [Q13W][K14W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=23 µM); SNU-601 (IC50=37 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33026 RIIDLLWRVWRPWKPKFVTVWVR 23 PMAP-23 [R10W][Q13W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=16 µM); SNU-601 (IC50=21 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33027 RIIDLLWRVWRPWWPKFVTVWVR 23 PMAP-23 [R10W][Q13W][K14W] P49930 Not found Synthetic (Derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SNU-601 (IC50=10 µM); Jurkat (IC50=11 µM) Not available Linear Free Amidation L Not available Not available 12054589 Biochem Biophys Res Commun. 2002 Apr 26;293(1):231-8. Lee DG, Kim PI, Park Y, Woo ER, Choi JS, Choi CH, Hahm KS. Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid DRAMP33028 GKKLKKIGQKIKNFFQKL 18 CRAMP-18[E2K] P51437 Not found Synthetic (Derived from CRAMP-18) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=20 µM); A549 (IC50=25 µM); K562 (IC50=34 µM) Human erythrocytes: Not active up to 100 µM Linear Free Free L Not available Not available 10973820 Biochem Biophys Res Commun. 2000 Sep 7;275(3):904-9. Shin SY, Kang SW, Lee DG, Eom SH, Song WK, Kim JI. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity DRAMP33029 GEKLKKIGKKIKNFFQKL 18 CRAMP-18[Q9K] P51437 Not found Synthetic (Derived from CRAMP-18) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (IC50=66 µM); K562 (IC50=85 µM); A549 (IC50=88 µM) Human erythrocytes: Not active up to 100 µM Linear Free Free L Not available Not available 10973820 Biochem Biophys Res Commun. 2000 Sep 7;275(3):904-9. Shin SY, Kang SW, Lee DG, Eom SH, Song WK, Kim JI. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity DRAMP33030 GEKLKKIGQKIKKFFQKL 18 CRAMP-18[N13K] P51437 Not found Synthetic (Derived from CRAMP-18) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=100 µM); Jurkat (IC50=78 µM); A549 (IC50=93 µM) Human erythrocytes: Not active up to 100 µM Linear Free Free L Not available Not available 10973820 Biochem Biophys Res Commun. 2000 Sep 7;275(3):904-9. Shin SY, Kang SW, Lee DG, Eom SH, Song WK, Kim JI. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity DRAMP33031 GEKLKKIGQKIKNFFKKL 18 CRAMP-18[Q16K] P51437 Not found Synthetic (Derived from CRAMP-18) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>100 µM); Jurkat (IC50>100 µM); K562 (IC50>100 µM) Human erythrocytes: 0.2% Hemolysis=100 µM Linear Free Free L Not available Not available 10973820 Biochem Biophys Res Commun. 2000 Sep 7;275(3):904-9. Shin SY, Kang SW, Lee DG, Eom SH, Song WK, Kim JI. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity DRAMP33032 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33033 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33034 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33035 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33036 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33037 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33038 GLLxRIkTLL 10 Ano-D4,7–4C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33039 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33040 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33041 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33042 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33043 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33044 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33045 GLLxRIkTLL 10 Ano-D4,7–4C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33046 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33047 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33048 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33049 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33050 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33051 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33052 GLLxRIkTLL 10 Ano-D4,7–4C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50>256 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33053 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33054 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33055 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33056 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33057 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33058 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33059 GLLxRIkTLL 10 Ano-D4,7–4C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33060 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33061 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33062 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33063 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33064 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33065 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33066 GLLxRIkTLL 10 Ano-D4,7–4C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=32 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33067 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33068 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33069 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33070 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33071 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33072 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33073 GLLxRIkTLL 10 Ano-D4,7–4C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33074 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33075 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33076 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>256 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33077 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=64 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33078 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33079 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33080 GLLxRIkTLL 10 Ano-D4,7–4C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33081 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33082 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33083 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33084 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33085 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33086 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33087 GLLkRIxTLL 10 Ano-D4,7–7C4 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C4 (D-Lysine with butyrylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33088 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33089 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33090 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33091 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33092 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33093 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33094 GLLkRIxTLL 10 Ano-D4,7–7C6 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis>256 µM Linear Free Amidation x=D-Lys-C6 (D-Lysine with 2-hexanoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33095 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33096 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33097 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33098 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33099 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33100 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33101 GLLkRIxTLL 10 Ano-D4,7–7C8 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=256 µM Linear Free Amidation x=D-Lys-C8 (D-Lysine with octanoylated side group); k=D-Lys Mix HEK293T: IC50=128 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33102 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33103 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33104 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33105 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33106 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33107 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33108 GLLkRIxTLL 10 Ano-D4,7–7C10 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=128 µM Linear Free Amidation x=D-Lys-C10 (D-Lysine with decanoylated side group); k=D-Lys Mix HEK293T: IC50=16 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33109 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33110 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33111 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33112 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33113 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33114 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33115 GLLkRIxTLL 10 Ano-D4,7–7C12 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C12 (D-Lysine with laurylated side group); k=D-Lys Mix HEK293T: IC50=8 µM Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33116 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33117 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33118 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33119 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33120 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33121 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33122 GLLkRIxTLL 10 Ano-D4,7–7C14 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=32 µM Linear Free Amidation x=D-Lys-C14 (D-Lysine with myristoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33123 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33124 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33125 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=128 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33126 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=16 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33127 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=8 µM) Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33128 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33129 GLLkRIxTLL 10 Ano-D4,7–7C16 Not available Not found Synthetic (Derived from Anoplin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mouse erythrocytes: 10% Hemolysis=16 µM Linear Free Amidation x=D-Lys-C16 (D-Lysine with palmitoylated side group); k=D-Lys Mix Not available Not available 31676352 Eur J Pharm Sci. 2020 Jan 1;141:105123. Zhong C, Zhu N, Zhu Y, Liu T, Gou S, Xie J, Yao J, Ni J. Antimicrobial peptides conjugated with fatty acids on the side chain of D-amino acid promises antimicrobial potency against multidrug-resistant bacteria DRAMP33130 RLLRLIRKLII 11 Decoralin [AC1] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11±1 μM); A549 (EC50=21±1 μM); Jurkat (EC50=39±1 μM); 1205Lu (EC50=9±1 μM) Not available Linear Free Amidation L HDMEC: EC50=141±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33131 RLLRLIRKLIL 11 Decoralin [AC2] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=14±1 μM); Jurkat (EC50=25±1 μM); 1205Lu (EC50=7±1 μM); MCF-7 (EC50=9±1 μM) Not available Linear Free Amidation L HDMEC: EC50=125–250 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33132 LLLLLIRKLIK 11 Decoralin [AC3] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11±1 μM); 1205Lu (EC50=16±1 μM); A549 (EC50=22±1 μM); Jurkat (EC50=25±1 μM) Not available Linear Free Amidation L HDMEC: EC50=125–250 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33133 YLLYLIRKLIL 11 Decoralin [AC4] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=13±1 μM); 1205Lu (EC50=14±1 μM); Jurkat (EC50=22±1 μM); A549 (EC50=29±1 μM) Not available Linear Free Amidation L HDMEC: EC50=256±2 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33134 RLLRLIRKLIR 11 Decoralin [AC5] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=14±1 μM); 1205Lu (EC50=16±1 μM); A549 (EC50=27±1 μM); Jurkat (EC50=27±1 μM) Not available Linear Free Amidation L HDMEC: EC50=138±7 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33135 QLLQLIRKLII 11 Decoralin [AC6] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=21±1 μM); MCF-7 (EC50=22±1 μM); A549 (EC50=29±1 μM); Jurkat (EC50=35±1 μM) Not available Linear Free Amidation L HDMEC: EC50=171±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33136 QLLQLIRKLIM 11 Decoralin [AC7] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=24±1 μM); A549 (EC50=33±1 μM); MCF-7 (EC50=33±1 μM); Jurkat (EC50=46±1 μM) Not available Linear Free Amidation L HDMEC: EC50=142±2 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33137 MLLMLIRKLIL 11 Decoralin [AC8] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=16±1 μM); 1205Lu (EC50=31±1 μM); Jurkat (EC50=31±1 μM); A549 (EC50=58±1 μM) Not available Linear Free Amidation L HDMEC: EC50=262±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33138 QLLQLIRKLIR 11 Decoralin [AC9] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=38±1 μM); MCF-7 (EC50=53±1 μM); A549 (EC50=60±1 μM); Jurkat (EC50=75±1 μM) Not available Linear Free Amidation L HDMEC: EC50=260±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33139 QLLQLIRKLIK 11 Decoralin [AC10] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=39±1 μM); MCF-7 (EC50=50-100 μM); A549 (EC50=54±1 μM); Jurkat (EC50=69±1 μM) Not available Linear Free Amidation L HDMEC: EC50~=250 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33140 QLLQLIRKLIY 11 Decoralin [AC11] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=29±1 μM); MCF-7 (EC50=50-100 μM); Jurkat (EC50=58±1 μM); A549 (EC50=61±1 μM) Not available Linear Free Amidation L HDMEC: EC50=349±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33141 LLLQLIRKLIL 11 Decoralin [AT1] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=10±1 μM); 1205Lu (EC50=12±1 μM); A549 (EC50=30±1 μM); Jurkat (EC50=53±1 μM) Not available Linear Free Amidation L HDMEC: EC50=154±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33142 TLLLLIRKLIL 11 Decoralin [AT2] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=16±1 μM); Jurkat (EC50=30±1 μM); MCF-7 (EC50=38±1 μM); A549 (EC50=79±1 μM) Not available Linear Free Amidation L HDMEC: EC50=348±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33143 RLLLLIRKLIL 11 Decoralin [AT3] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=18±1 μM); MCF-7 (EC50=24±1 μM); A549 (EC50=35±1 μM); Jurkat (EC50=40±1 μM) Not available Linear Free Amidation L HDMEC: EC50=160±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33144 LLLLLIRKLIL 11 Decoralin [AT4] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=25±1 μM); 1205Lu (EC50=48±1 μM); Jurkat (EC50=50±1 μM); A549 (EC50>100 μM) Not available Linear Free Amidation L HDMEC: EC50=278±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33145 QLLLLIRKLIL 11 Decoralin [AT5] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (EC50=39±1 μM); 1205Lu (EC50=44±1 μM); MCF-7 (EC50=63±1 μM); A549 (EC50>100 μM) Not available Linear Free Amidation L HDMEC: EC50=271±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33146 QLLLLIRKLIV 11 Decoralin [AT6] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=53±1 μM); MCF-7 (EC50=77±1 μM); A549 (EC50>100 μM); Jurkat (EC50>100 μM) Not available Linear Free Amidation L HDMEC: EC50=339±1 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33147 CLLLLIRKLIL 11 Decoralin [AT7] Not available Not found Synthetic (Derived from Decoralin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: 1205Lu (EC50=76±1 μM); A549 (EC50>100 μM); Jurkat (EC50>100 μM); MCF-7 (EC50>100 μM) Not available Linear Free Amidation L HDMEC: EC50~=500 μM Not available 26119906 Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10370-4. Lin YC, Lim YF, Russo E, Schneider P, Bolliger L, Edenharter A, Altmann KH, Halin C, Hiss JA, Schneider G. Multidimensional Design of Anticancer Peptides DRAMP33148 WKWLKKWIK 9 PL-D 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OVCAR-3 (IC50=51.1 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33149 WKWLKKWIK 9 PL-D 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=24.3 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33150 WRKFWKYLK 9 PL-D 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=47.3 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33151 RLWWWWRRK 9 PL-D 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=87 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33152 KWKWWWRKI 9 PL-D 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=90.4 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33153 RIRRWKFRW 9 PL-D 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=182.5 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33154 RLKRWWKFL 9 PL-D 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=48 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33155 RRWWRWVVW 9 PL-D 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=179.1 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33156 WFKMRWWGR 9 PL-D 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=189.3 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33157 KFKWWRMLI 9 PL-D 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=49 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33158 RWRWWWRVY 9 PL-D 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=171.5 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33159 LKRRWKWWI 9 PL-D 23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=186.7 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33160 RRRIKIRWY 9 PL-D 24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=190.2 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33161 RLWWKIWLK 9 PL-D 25 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=192.8 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33162 KRRWRIWLV 9 PL-D 26 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=195.1 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33163 FFIYVWRRR 9 PL-D 27 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=190.8 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33164 IRMRIRVLL 9 PL-D 28 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=219 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33165 RWWRKIWKW 9 PL-D 29 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=177.3 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33166 RWWIRIRWH 9 PL-D 31 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=181.8 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33167 RRRWWKLMM 9 PL-D 32 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=94 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33168 LRRWIRIRW 9 PL-D 33 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=189.1 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33169 RKFRWWVIR 9 PL-D 34 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=190.2 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33170 WKIVFWWRR 9 PL-D 35 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=186 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33171 RQRRVVIWW 9 PL-D 36 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=197.2 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33172 RRWRVIVKW 9 PL-D 37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=197.2 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33173 RLWRIVVIRVKR 12 PL-D 39 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=138.4 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33174 RLRRIVVIRVFR 12 PL-D 40 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=158.8 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33175 RKWKIKWYW 9 PL-D 43 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=183.8 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33176 YRLRVKWKW 9 PL-D 44 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=191.9 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33177 WKWRVRVTI 9 PL-D 45 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=206 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33178 RTKKWIVWI 9 PL-D 46 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=208.3 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33179 KRKKRFKWW 9 PL-D 49 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=188 µM) Not available Linear Free Free L Not available Not available 23478953 Antimicrob Agents Chemother. 2013 May;57(5):2295-303 Ramón-García S, Mikut R, Ng C, Ruden S, Volkmer R, Reischl M, Hilpert K, Thompson CJ. Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides DRAMP33180 VXLfPFfNQY 10 Tyrocidine A, TrcA Not available Not found Bacillus subtilis; Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=14 µM); HeLa (LC50=21 µM) Human erythrocytes: 50% Hemolysis=4.5 µM Cyclic Free Free X=Orn; f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33181 VKLfPFfNQY 10 Tyrocidine A1, TrcA1 Not available Not found Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=12 µM); HeLa (LC50=15 µM) Human erythrocytes: 50% Hemolysis=4.1 µM Cyclic Free Free f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33182 VXLfPWfNQY 10 Tyrocidine B, TrcB Not available Not found Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=12 µM); HeLa (LC50=17 µM) Human erythrocytes: 50% Hemolysis=2.6 µM Cyclic Free Free X=Orn; f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33183 VKLfPWfNQY 10 Tyrocidine B1, TrcB1 Not available Not found Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=24 µM); HeLa (LC50=28 µM) Human erythrocytes: 50% Hemolysis=8.6 µM Cyclic Free Free f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33184 VXLfPWwNQY 10 Tyrocidine C, TrcC Not available Not found Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=12 µM); HeLa (LC50=13 µM) Human erythrocytes: 50% Hemolysis=3.2 µM Cyclic Free Free X=Orn; f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33185 VKLfPWwNQY 10 Tyrocidine C1, TrcC1 Not available Not found Bacillus aneurinolyticus; Bacillus brevis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=12 µM); HeLa (LC50=16 µM) Human erythrocytes: 50% Hemolysis=5.4 µM Cyclic Free Free f=D-Phe Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP33186 FLPILASLAAKFGPKLFXLVTKKX 24 DC-brevinin-1BYa, peak 1 (cis) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=4 μM ); MDA-MB-231 (LC50=7 μM ) Human erythrocytes: LC50=4 μM Cyclic Free Free X=Allylglycine L Not available Not available 21312033 Eur Biophys J. 2011 Apr;40(4):555-64. Hossain MA, Guilhaudis L, Sonnevend A, Attoub S, van Lierop BJ, Robinson AJ, Wade JD, Conlon JM. Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa DRAMP33187 FLPILASLAAKFGPKLFXLVTKKX 24 DC-brevinin-1BYa, peak 1 (cis) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Human erythrocytes: LC50=4 μM Cyclic Free Free X=Allylglycine L Not available Not available 21312033 Eur Biophys J. 2011 Apr;40(4):555-64. Hossain MA, Guilhaudis L, Sonnevend A, Attoub S, van Lierop BJ, Robinson AJ, Wade JD, Conlon JM. Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa DRAMP33188 FLPILASLAAKFGPKLFXLVTKKX 24 DC-brevinin-1BYa, peak 2 (trans) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=4 μM ); MDA-MB-231 (LC50=7 μM ) Human erythrocytes: LC50=4 μM Cyclic Free Free X=Allylglycine L Not available Not available 21312033 Eur Biophys J. 2011 Apr;40(4):555-64. Hossain MA, Guilhaudis L, Sonnevend A, Attoub S, van Lierop BJ, Robinson AJ, Wade JD, Conlon JM. Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa DRAMP33189 FLPILASLAAKFGPKLFXLVTKKX 24 DC-brevinin-1BYa, peak 2 (trans) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Human erythrocytes: LC50=4 μM Cyclic Free Free X=Allylglycine L Not available Not available 21312033 Eur Biophys J. 2011 Apr;40(4):555-64. Hossain MA, Guilhaudis L, Sonnevend A, Attoub S, van Lierop BJ, Robinson AJ, Wade JD, Conlon JM. Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa DRAMP33190 FLPILASLAAKFGPKLFSLVTKKS 24 [Ser18,Ser24]-brevinin-1BYa Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=10 μM ); MDA-MB-231 (LC50=13 μM ) Human erythrocytes: LC50=75 μM Cyclic Free Free L Not available Not available 21312033 Eur Biophys J. 2011 Apr;40(4):555-64. Hossain MA, Guilhaudis L, Sonnevend A, Attoub S, van Lierop BJ, Robinson AJ, Wade JD, Conlon JM. Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa DRAMP33191 GQSQWRDVCRNFMRR 15 Granulysin (37-51) [R38Q][R40Q] P22749 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (Not active at 20 µM) Not available Linear Free Free L Not available Not available 10903754 J Immunol. 2000 Aug 1;165(3):1486-90. Wang Z, Choice E, Kaspar A, Hanson D, Okada S, Lyu SC, Krensky AM, Clayberger C. Bactericidal and tumoricidal activities of synthetic peptides derived from granulysin DRAMP33192 FLSLIPHIVSGVASLAKHF 19 PLS-S2 Not available Not found Phyllomedusa sauvagii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=22.5 µM) Human erythrocytes: LC50=25 µM Linear Free Amidation L Not available Not available 23967105 PLoS One. 2013 Aug 13;8(8):e70782. Raja Z, André S, Piesse C, Sereno D, Nicolas P, Foulon T, Oury B, Ladram A. Structure, antimicrobial activities and mode of interaction with membranes of novel [corrected] phylloseptins from the painted-belly leaf frog, Phyllomedusa sauvagii DRAMP33193 FLSMIPHIVSGVAALAKHL 19 PLS-S4 Not available Not found Phyllomedusa sauvagii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (IC50=23 µM) Human erythrocytes: LC50=33 µM Linear Free Amidation L Not available Not available 23967105 PLoS One. 2013 Aug 13;8(8):e70782. Raja Z, André S, Piesse C, Sereno D, Nicolas P, Foulon T, Oury B, Ladram A. Structure, antimicrobial activities and mode of interaction with membranes of novel [corrected] phylloseptins from the painted-belly leaf frog, Phyllomedusa sauvagii DRAMP33194 KTCENLADTYKGPCFTTGSCDDHCKNKEHLRSGRCRDDFRCWCTKNC 47 PvD1, Defensin D1 V7BTW4##F8QXP9 Not found Phaseolus vulgaris Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=0.82±0.14 µM) Not available Cyclic Free Free L MCF-10a: 50% Cell death=7 µM Not available 29076508 Nanoscale. 2017 Nov 9;9(43):16887-16899. Figueira TN, Oliveira FD, Almeida I, Mello ÉO, Gomes VM, Castanho MARB, Gaspar D. Challenging metastatic breast cancer with the natural defensin PvD1 DRAMP33195 GFSSIFRGVAKFASKGLGKKLAKLGVKLVACKISKQC 37 Esculentin-2CHa [D20K,D27K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=3 μM ) Human erythrocytes: 50% Hemolysis=11 µM Linear Free Free L Not available Not available 23159562 Peptides. 2013 Jan;39:95-102. Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells DRAMP33196 GFSSIFRGVAKFASKGLGKDLAKLGVDLVASKISKQS 37 Esculentin-2CHa [C31S, C37S] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=26 μM ) Human erythrocytes: 50% Hemolysis>200 µM Linear Free Free L Not available Not available 23159562 Peptides. 2013 Jan;39:95-102. Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells DRAMP33197 RGVAKFASKGLGKDLAKLGVDLVACKISKQC 31 Esculentin-2CHa (7–37) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50>100 μM ) Human erythrocytes: 50% Hemolysis>200 µM Cyclic Free Free L Not available Not available 23159562 Peptides. 2013 Jan;39:95-102. Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells DRAMP33198 KPPPWVPV 8 PsT-1 C0HJF6 Not found Phyllomedusa sauvagii Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: DU145 (~25% Cell death=10 µM); PC-3 (~25% Cell death=10 µM); LNCaP (~50% Cell death=10 µM) Horse erythrocytes: Not active up to 160 µM Linear Free Free L Not available Not available 23518460 ACS Chem Biol. 2013 Apr 19;8(4):778-88. Dutta S, Chen TS, Keating AE. PsT-1: a new tryptophyllin peptide from the skin secretion of Waxy Monkey Leaf Frog, Phyllomedusa sauvagei DRAMP33199 GIPCGESCVYIPCTVTALLGCSCKDKVCYKN 31 Cliotides T12, CT12 C0HKG2 Not found Clitoria ternatea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=0.78 µM ) Not available Cyclic Free Free L Not available Not available 23419988 Oncol Lett. 2013 Feb;5(2):641-644. Sen Z, Zhan XK, Jing J, Yi Z, Wanqi Z. Chemosensitizing activities of cyclotides from Clitoria ternatea in paclitaxel-resistant lung cancer cells DRAMP33200 GSVIKCGESCLLGKCYTPGCTCSRPICKKD 30 Cliotides T19, CT19 Not available Not found Clitoria ternatea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=9.59 µM ) Not available Cyclic Free Free L Not available Not available 23419988 Oncol Lett. 2013 Feb;5(2):641-644. Sen Z, Zhan XK, Jing J, Yi Z, Wanqi Z. Chemosensitizing activities of cyclotides from Clitoria ternatea in paclitaxel-resistant lung cancer cells DRAMP33201 GSAIRCGESCLLGKCYTPGCTCDRPICKKN 30 Cliotides T20, CT20 Not available Not found Clitoria ternatea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>10 µM ) Not available Cyclic Free Free L Not available Not available 23419988 Oncol Lett. 2013 Feb;5(2):641-644. Sen Z, Zhan XK, Jing J, Yi Z, Wanqi Z. Chemosensitizing activities of cyclotides from Clitoria ternatea in paclitaxel-resistant lung cancer cells DRAMP33202 GNPANPLNLKKHHGVFCDVCKALVEGGEKVGDDDLDAWLDVNIGTLCWTMLLPLHHECEEELKKVKKELKKDIENKDSPDKACKDVDLC 89 SPP-1 Q22291 Not found Caenorhabditis elegans Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (Low active up to 10 µM ) Not available Cyclic Free Free L Not available Not available 22519640 Biochem J. 2012 Jul 15;445(2):205-12. Hoeckendorf A, Stanisak M, Leippe M. The saposin-like protein SPP-12 is an antimicrobial polypeptide in the pharyngeal neurons of Caenorhabditis elegans and participates in defence against a natural bacterial pathogen DRAMP33203 GSHGAFCHLCEDLIKDGKEAGDVALDVWLDEEIGSRCKDFGVLASECFKELKVAEHDIWEAIDQEIPEDKTCKEAKLC 78 SPP-12 Q9XVI5 Not found Caenorhabditis elegans Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Jurkat (Low active up to 10 µM ) Not available Cyclic Free Free L Not available Not available 22519640 Biochem J. 2012 Jul 15;445(2):205-12. Hoeckendorf A, Stanisak M, Leippe M. The saposin-like protein SPP-12 is an antimicrobial polypeptide in the pharyngeal neurons of Caenorhabditis elegans and participates in defence against a natural bacterial pathogen DRAMP33204 RRQRRTSKLMKRGGKLAKLAKKLAKLAKLAK 31 DP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available It is possible that the DP1 fusion peptide can be used to facilitate an immune response against tumor antigens by triggering massive apoptosis within tumors Tumor cells: Clinical isolate 22B (LC50<50 μM ); Clinical isolate 4129 (LC50<50 μM ); MCA 205 (LC50<50 μM ) Not available Linear Free Free L Not available Not available 11691780 Cancer Res. 2001 Nov 1;61(21):7709-12. Mai JC, Mi Z, Kim SH, Ng B, Robbins PD. A proapoptotic peptide for the treatment of solid tumors DRAMP33205 KRIIQRILSRNS 12 PTD-1, Protein transduction domain 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11020349 Mol Ther. 2000 Oct;2(4):339-47. Mi Z, Mai J, Lu X, Robbins PD. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo DRAMP33206 KRIHPRLTRSIR 12 PTD-2, Protein transduction domain 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11020349 Mol Ther. 2000 Oct;2(4):339-47. Mi Z, Mai J, Lu X, Robbins PD. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo DRAMP33207 PPRLRKRRQLNM 12 PTD-3, Protein transduction domain 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11020349 Mol Ther. 2000 Oct;2(4):339-47. Mi Z, Mai J, Lu X, Robbins PD. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo DRAMP33208 PIRRRKKLRRLK 12 PTD-4, Protein transduction domain 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11020349 Mol Ther. 2000 Oct;2(4):339-47. Mi Z, Mai J, Lu X, Robbins PD. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo DRAMP33209 MHKRPTTPSRKM 12 PTD-6, Protein transduction domain 6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11020349 Mol Ther. 2000 Oct;2(4):339-47. Mi Z, Mai J, Lu X, Robbins PD. Characterization of a class of cationic peptides able to facilitate efficient protein transduction in vitro and in vivo DRAMP33210 klaklakklaklak 14 D-PAP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LD50>256 µg/ml; 12% Killing=250 µg/ml) Not available Linear Free Free D Not available Not available 33335804 PeerJ. 2020 Nov 30;8:e10176. Ohno MK, Kirikae T, Yoshihara E, Kirikae F, Ishida I. Addition of L-cysteine to the N- or C-terminus of the all-D-enantiomer [D(KLAKLAK)2] increases antimicrobial activities against multidrug-resistant Pseudomonas aeruginosa, Acinetobacter baumannii and Escherichia coli DRAMP33211 Cklaklakklaklak 15 C-D-PAP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LD50>256 µg/ml; 32% Killing=250 µg/ml) Not available Linear Free Free k=D-Lys; l=D-Leu; a=D-Ala Mix Not available Not available 33335804 PeerJ. 2020 Nov 30;8:e10176. Ohno MK, Kirikae T, Yoshihara E, Kirikae F, Ishida I. Addition of L-cysteine to the N- or C-terminus of the all-D-enantiomer [D(KLAKLAK)2] increases antimicrobial activities against multidrug-resistant Pseudomonas aeruginosa, Acinetobacter baumannii and Escherichia coli DRAMP33212 klaklakklaklakC 15 D-PAP-C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LD50=192 µg/ml) Not available Linear Free Free k=D-Lys; l=D-Leu; a=D-Ala Mix Not available Not available 33335804 PeerJ. 2020 Nov 30;8:e10176. Ohno MK, Kirikae T, Yoshihara E, Kirikae F, Ishida I. Addition of L-cysteine to the N- or C-terminus of the all-D-enantiomer [D(KLAKLAK)2] increases antimicrobial activities against multidrug-resistant Pseudomonas aeruginosa, Acinetobacter baumannii and Escherichia coli DRAMP33213 GLWNSIKIAGKKLFVNVLDKIR 22 GL-22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=128.89 μM); NCI-H838 (IC50=25.25 μM); U-251MG (IC50=40.58 μM); H157 (IC50=9.36 μM) Horse erythrocytes: 10% Hemolysis=87.304 µM; 50% Hemolysis=254.11 µM Linear Free Amidation L Human keratinocytes HaCat: IC50=38.90 µM Not available 36009917 Antibiotics (Basel). 2022 Aug 3;11(8):1048. Liu S, Lin Y, Liu J, Chen X, Ma C, Xi X, Zhou M, Chen T, Burrows JF, Wang L. Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb DRAMP33214 XLPICGETCVLGTCYTPGCRCQYPICVR 28 Linear Cyclotide Panitide L1 K9Y490 Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=4.1 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33215 XLPICGETCVLGRCYTPNCRCQYPICVR 28 Linear Cyclotide Panitide L2 K9Y2Z0 Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=6 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33216 XAFCGETCLLGKCYTPGCSCHTGICLK 27 Linear Cyclotide Panitide L3 Not available Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>10 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33217 XAFCGETCLLGTCYTPGCRCTAGICLK 27 Linear Cyclotide Panitide L4 K9Y385 Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>10 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33218 XLPICGETCVLGTCYTPGCSCAYPICAR 28 Linear Cyclotide Panitide L5 Not available Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33219 XLPICGETCVLGTCYTPGCSCAYPICVR 28 Linear Cyclotide Panitide L6 K9Y572 Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=5.7 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33220 XAFCGETCVLGTCYTPGCSCNFGICLK 27 Linear Cyclotide Panitide L7 Not available Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=7.7 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33221 XDCGETCVLGTCYTPGCSCSAYPLCV 26 Linear Cyclotide Panitide L8 Not available Not found Steinchisma laxum (Panicum laxum) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50>10 µM) Not available Cyclic Free Free X=PYA (Pyroglutamic acid) L Not available Not available 23195955 J Biol Chem. 2013 Feb 1;288(5):3370-80 Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of Poaceae family provides new insights into evolution and distribution of cyclotides in plants DRAMP33222 FLGALFHALSHLL 13 PTP-7c P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PANC-1 (IC50>120 μM ); A549 (IC50>160 μM ) Human erythrocytes: 0% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50>120 μM Not available 22526264 Arch Microbiol. 2012 Sep;194(9):769-78. Kharidia R, Tu Z, Chen L, Liang JF. Activity and selectivity of histidine-containing lytic peptides to antibiotic-resistant bacteria DRAMP33223 FLGALWKALSKLL 13 LL-1 P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=9 μM ); PANC-1 (IC50=9 μM ) Human erythrocytes: 41% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50=9 μM Not available 22526264 Arch Microbiol. 2012 Sep;194(9):769-78. Kharidia R, Tu Z, Chen L, Liang JF. Activity and selectivity of histidine-containing lytic peptides to antibiotic-resistant bacteria DRAMP33224 FLGALWHALSKLL 13 LL-1a P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=22 μM ); PANC-1 (IC50=39 μM ) Human erythrocytes: 15% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50=65 μM Not available 22526264 Arch Microbiol. 2012 Sep;194(9):769-78. Kharidia R, Tu Z, Chen L, Liang JF. Activity and selectivity of histidine-containing lytic peptides to antibiotic-resistant bacteria DRAMP33225 FLGALWKALSHLL 13 LL-1b P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=31 μM ); PANC-1 (IC50=54 μM ) Human erythrocytes: 15% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50=49 μM Not available 22526264 Arch Microbiol. 2012 Sep;194(9):769-78. Kharidia R, Tu Z, Chen L, Liang JF. Activity and selectivity of histidine-containing lytic peptides to antibiotic-resistant bacteria DRAMP33226 FLGALWHALSHLL 13 LL-1c P80399 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=59 μM ); PANC-1 (IC50>120 μM ) Human erythrocytes: 0% Hemolysis=30 µM Linear Free Free L MCF-10A: IC50>120 μM Not available 22526264 Arch Microbiol. 2012 Sep;194(9):769-78. Kharidia R, Tu Z, Chen L, Liang JF. Activity and selectivity of histidine-containing lytic peptides to antibiotic-resistant bacteria DRAMP33227 PAWHHAFHWAWRMLKKAA 18 L5a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=19 ± 3 μM(pH=7.4); IC50=10 ± 2 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50=13 ± 2 μM(pH=7.4); IC50=8 ± 1 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33228 PAWRKAFRWAWHMLHHAA 18 L5b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12 ± 2 μM(pH=7.4); IC50=7 ± 2 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50=12 ± 1 μM(pH=7.4); IC50=6 ± 2 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33229 PAWRHAFHWAWHMLHKAA 18 L5c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>80 μM(pH=7.4); IC50=12 ± 2 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50=67 ± 3 μM(pH=7.4); IC50=7 ± 2 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33230 GLFAVIHKVASVIGGL 16 Citropin-a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=56±3 μM(pH=7.4); IC50=44±3 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50=78 ± 2 μM(pH=7.4); IC50=47 ± 3 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33231 GLFAVIKHVASVIGGL 16 Citropin-b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=97 ± 4 μM(pH=7.4); IC50=61±3 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50=76 ± 4 μM(pH=7.4); IC50=41 ± 5 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33232 GLFAVIHHVASVIGGL 16 Citropin-c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=156 ± 7 μM(pH=7.4); IC50=36 ± 2 μM(pH=5.5)) Not available Linear Free Free L CHO: IC50>120 μM(pH=7.4); IC50>120 μM(pH=5.5) Not available 19464332 Peptides. 2009 Aug;30(8):1523-8. Tu Z, Volk M, Shah K, Clerkin K, Liang JF.  Constructing bioactive peptides with pH-dependent activities DRAMP33241 KRKILILIKRK 11 M1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM ) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33242 KRKILILILIL 11 M2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM ) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33243 ILILILILKRK 11 M3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33244 KRKILILIGSG 11 M4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33245 GSGILILIKRK 11 M5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33246 KRKSGSGSKRK 11 M6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33247 KRKRKILILIKRK 13 N1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50=36 µm) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33248 RKRKILILIKRK 12 N2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33249 RKILILIKRK 10 N3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33250 KILILIKRK 9 N4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50=58 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33251 ILILIKRK 8 N5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33252 LILIKRK 7 N6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33253 ILIKRK 6 N7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33254 LIKRK 5 N8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33255 KRKILILIKRKRK 13 C1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50=61 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33256 KRKILILIKRKR 12 C2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33257 KRKILILIKR 10 C3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33258 KRKILILIK 9 C4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33259 KRKILILI 8 C5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33260 KRKILIL 7 C6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33261 KRKILI 6 C7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33262 KRKIL 5 C8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33263 KRKILILILIKRK 13 H1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33264 KRKLILIKRK 10 H2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33265 KRKILIKRK 9 H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33266 KRKLIKRK 8 H4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33267 KRKIKRK 7 H5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33268 KRKKRK 6 H6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33269 KRKGKRK 7 H7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33270 KRKGSGKRK 9 H8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33271 RKRKLILILIKRKR 14 A1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33272 KRKLILKRILIKRK 14 A2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33273 RKLILKRKRILIKR 14 A3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33274 KLILKRKRKRILIK 14 A4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33275 LILKRKRKRKRILI 14 A5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33276 RRRIIIIIRRR 11 S1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33277 KKKIIIIIKKK 11 S2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33278 RRRLLLLLRRR 11 S3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33279 KKKLLLLLKKK 11 S4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33280 RRRVVVVVRRR 11 S5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33281 KKKVVVVVKKK 11 S6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33282 RRRFFFFFRRR 11 S7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33283 KKKFFFFFKKK 11 S8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33284 KKKIIIIIIKKK 12 O1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (LD50>64 µM) Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial β-strand-forming antimicrobial peptides with biocompatible properties DRAMP33285 XGLXGGLXGIX 11 Trichogin GA IV, TG Not available Not found Trichoderma longibrachiatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=2 μM); HeLa (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=4 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33286 XGLXGGLXGIX 11 Trichogin GA IV, TG Not available Not found Trichoderma longibrachiatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=4 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33287 XGLXGGLXGIX 11 Trichogin GA IV, TG Not available Not found Trichoderma longibrachiatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=4 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33288 XGLXGGLXGIX 11 Trichogin GA IV, TG Not available Not found Trichoderma longibrachiatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=13 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=4 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33289 XGLXGGLXGIX 11 Trichogin GA IV, TG Not available Not found Trichoderma longibrachiatum Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=4 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33290 XGLXGGLXGIX 11 [TOAC1] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=2 μM); HeLa (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33291 XGLXGGLXGIX 11 [TOAC1] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33292 XGLXGGLXGIX 11 [TOAC1] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33293 XGLXGGLXGIX 11 [TOAC1] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=13 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33294 XGLXGGLXGIX 11 [TOAC1] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33295 XGLXGKLXGIX 11 [Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=2 μM); T67 (EC50=4 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=2 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33296 XGLXGKLXGIX 11 [Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=2 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33297 XGLXGKLXGIX 11 [Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=2 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33298 XGLXGKLXGIX 11 [TOAC1, Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=2 μM); T67 (EC50=4 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33299 XGLXGKLXGIX 11 [TOAC1, Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33300 XGLXGKLXGIX 11 [TOAC1, Lys6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=5 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33301 XRLXGGLXGIX 11 [Arg2] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=4 μM); T67 (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=8 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33302 XRLXGGLXGIX 11 [Arg2] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (EC50=9 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=8 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33303 XRLXGGLXGIX 11 [TOAC1, Arg2] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=4 μM); T67 (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33304 XRLXGGLXGIX 11 [TOAC1, Arg2] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (EC50=9 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33305 XGLXGGLXRIX 11 [TOAC1, Arg9] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=5 μM); T67 (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=8 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33306 XGLXKKLXGIX 11 [Lys5,6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=10 μM); T67 (EC50=7 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33307 XGLXKKLXGIX 11 [Lys5,6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=10 μM); HeLa (EC50=6 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33308 XGLXKKLXGIX 11 [TOAC1, Lys5,6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=10 μM); T67 (EC50=7 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33309 XGLXKKLXGIX 11 [TOAC1, Lys5,6] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=10 μM); HeLa (EC50=6 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: EC50=15 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33310 XGLXGGLXGIX 11 [TOAC1, Api4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=2 μM); HeLa (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Api; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33311 XGLXGGLXGIX 11 [TOAC1, Api4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Api; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33312 XGLXGGLXGIX 11 [TOAC1, Api4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Api; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33313 XGLXGGLXGIX 11 [TOAC1, Api4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=13 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Api; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33314 XGLXGGLXGIX 11 [TOAC1, Api4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Api; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33315 XGLXGGLXGIX 11 [Api8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=2 μM); HeLa (EC50=8 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4)=Aib; X(8)=Api; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33316 XGLXGGLXGIX 11 [Api8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4)=Aib; X(8)=Api; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33317 XGLXGGLXGIX 11 [Api8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4)=Aib; X(8)=Api; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33318 XGLXGGLXGIX 11 [Api8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=13 μM); HeLa (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4)=Aib; X(8)=Api; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33319 XGLXGGLXGIX 11 [Api8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4)=Aib; X(8)=Api; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33320 XGLLGGLXGIX 11 [Leu4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 20 μM); T67 (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33321 XGLLGGLXGIX 11 [Leu4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 20 μM); T67 (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33322 XGLLGGLXGIX 11 [TOAC1, Leu4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 20 μM); T67 (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33323 XGLLGGLXGIX 11 [TOAC1, Leu4] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 20 μM); T67 (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33324 XGLXGGLLGIX 11 [TOAC1, Leu8] TG Not available Not found Synthetic (Derived from TG) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 20 μM); T67 (Not active up to 20 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1)=TOAC; X(4)=Aib; X(11)=Lol (Amino alcohol leucinol) L Human dermal fibroblasts: Not active up to 20 μM Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP33325 GFKDLLKKAAKALVKTVLF 19 [Lys8] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=8 µM) Human erythrocytes: LC50=11 µM Linear Free Amidation L L929 fibroblast-derived cells: LC50=5 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33326 GFKDLLKGAKKALVKTVLF 19 [Lys10] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50>200 µM) Human erythrocytes: LC50>500 µM Linear Free Amidation L L929 fibroblast-derived cells: LC50>200 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33327 GFKDLLKGAAKALKKTVLF 19 [Lys14] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=200 µM) Human erythrocytes: LC50>500 µM Linear Free Amidation L L929 fibroblast-derived cells: LC50=110 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33328 GFKDLLKGAAKALVKTVKF 19 [Lys18] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=200 µM) Human erythrocytes: LC50>500 µM Linear Free Amidation L L929 fibroblast-derived cells: LC50=55 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33329 GFKDLLKkAAKALVKTVLF 19 [D-Lys8] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=15 µM) Human erythrocytes: LC50=150 µM Linear Free Amidation Mix L929 fibroblast-derived cells: LC50=9 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33330 GFKDLLKGAkKALVKTVLF 19 [D-Lys10] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50>200 µM) Human erythrocytes: LC50>500 µm Linear Free Amidation Mix L929 fibroblast-derived cells: LC50>200 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33331 GFKDLLKGAAKALkKTVLF 19 [D-Lys14] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50>200 µM) Human erythrocytes: LC50>500 µM Linear Free Amidation Mix L929 fibroblast-derived cells: LC50=140 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33332 GFKDLLKGAAKALVKTVkF 19 [D-Lys18] Ascaphin-8 P0CJ32 Not found Synthetic (Derived from Ascaphin-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=140 µM) Human erythrocytes: LC50>500 µM Linear Free Amidation Mix L929 fibroblast-derived cells: LC50=65 µM Not available 18554256 Chem Biol Drug Des. 2008 Jul;72(1):58-64. Conlon JM, Galadari S, Raza H, Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7 DRAMP33355 NGRKACLNPASPIVKKIIEKMLNS 24 Chemokinostatin-1 P09341 Not found Homo sapiens (CXCL1/Gro-α) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33356 NGKKACLNPASPMVQKIIEKIL 22 Chemokinostatin-3 P19876 Not found Homo sapiens (CXCL3/Gro-γ) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33357 NGKEICLDPEAPFLKKVIQKILD 23 Chemokinostatin-5 P42830 Not found Homo sapiens (CXCL5/ENA-78) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33358 NGKQVCLDPEAPFLKKVIQKILDS 24 Chemokinostatin-6 P80162 Not found Homo sapiens (CXCL6/GCP-2) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33359 DGRKICLDPDAPRIKKIVQKKL 22 Chemokinostatin-7 P02775 Not found Homo sapiens (CXCL7/PBP) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33360 DGRELCLDPKENWVQRVVEKFLK 23 Chemokinostatin-8 P10145 Not found Homo sapiens (CXCL8/IL-8) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available CXCR 18307172 J Cell Biochem. 2008 Jul 1;104(4):1356-63. Karagiannis ED, Popel AS. Novel anti-angiogenic peptides derived from ELR-containing CXC chemokines DRAMP33361 KILRGVSKKIMRTFLRR 17 N17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33362 KKIMRTFLRR 10 I10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33363 KKIMRTFLRRISKDILTGKK 20 C20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33364 KKIMRTFLRRISKKILTGKK 20 C20-DK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33365 KILRGVSKKIMRRISKDILTGKK 23 N23b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33366 KILGVSKKIMRRISKDILTGKK 22 N22b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33367 KISKKIMRTFLRRILTGKK 19 NK19a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (21.1 ± 4.0% Cytotoxicity=100 μg/ml) Human erythrocytes: 100% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33368 KILRGVSKKIMRRILTGKK 19 NK19b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33369 RILRGVSRRIMRRILTGRR 19 NK19b-KR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (6.6 ± 7.9% Cytotoxicity=100 μg/ml) Human erythrocytes: <10% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33370 KILRGVSKRILTGKK 15 NK15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33371 KILGVSKRILTGKK 14 NK14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33372 KISKKIMRTFLRR 13 NK13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (6.4 ± 3.0% Cytotoxicity=100 μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33373 ISKRILTGKK 10 NK10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33374 KISKRILTGKK 11 NK11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 100μg/ml) Human erythrocytes: <5% Hemolysis=100 µg/ml Linear Free Amidation L Not available Not available 17389605 J Biol Chem. 2007 May 18;282(20):14719-28. Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens DRAMP33375 CLB 3 CLB Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CAPAN-1 (IC50=129.0 ± 35.5 µM); MCF-7 (IC50=73.7 ± 4.5 µM) Not available Linear Free Amidation L NIH 3T3: IC50=152.5 ± 5.6 µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63 Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP33376 CLBCREKA 8 CLB-CREKA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CAPAN-1 (IC50>200 µM); MCF-7 (IC50>200 µM) Not available Linear Free Amidation L NIH 3T3: IC50>200 µM Not available 24480922 Org Biomol Chem. 2014 Mar 14;12(10):1652-63 Soler M, González-Bártulos M, Soriano-Castell D, Ribas X, Costas M, Tebar F, Massaguer A, Feliu L, Planas M. Identification of BP16 as a non-toxic cell-penetrating peptide with highly efficient drug delivery properties DRAMP33377 KWKKLLKKLLKLLKKLLK 18 KLW Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=0.6 µM); SK-OV-3 (IC50=0.6 µM); SK-MEL-2 (IC50=0.7 µM) Human erythrocytes: 55% Hemolysis=100 µM Linear Free Amidation L NIH 3T3: IC50=1.8 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33378 KWKKLLKKXLKLLKKLLK 18 KLW-L9-Nala Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-OV-3 (IC50=1.7 µM); A549 (IC50=2 µM); SK-MEL-2 (IC50=2.1 µM) Human erythrocytes: 5% Hemolysis=100 µM Linear Free Amidation X=NAla L NIH 3T3: IC50=7.1 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33379 KWKKLLKKLXKLLKKLLK 18 KLW-L10-Nala Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-OV-3 (IC50=0.9 µM); A549 (IC50=1 µM); SK-MEL-2 (IC50=1.3 µM) Human erythrocytes: 23% Hemolysis=100 µM Linear Free Amidation X=NAla L NIH 3T3: IC50=2 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33380 KWKKLLKKLLXLLKKLLK 18 KLW-K11-Nala Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-OV-3 (IC50=0.5 µM); A549 (IC50=0.6 µM); SK-MEL-2 (IC50=0.6 µM) Human erythrocytes: 50% Hemolysis=100 µM Linear Free Amidation X=NAla L NIH 3T3: IC50=1 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33381 KWKKLLKKXLKLXKKLLK 18 KLW-L9,13-Nala Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-OV-3 (IC50=31.9 µM); SK-MEL-2 (IC50=38.7 µM); A549 (IC50=75.5 µM) Human erythrocytes: 0% Hemolysis=100 µM Linear Free Amidation X=NAla L NIH 3T3: IC50>100 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33382 KWKKLLXKLLXLLKKLLK 18 KLW-K7,11-Nala Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-OV-3 (IC50=0.7 µM); A549 (IC50=1 µM); SK-MEL-2 (IC50=1.1 µM) Human erythrocytes: 27% Hemolysis=100 µM Linear Free Amidation X=NAla L NIH 3T3: IC50=2 µM Not available 16142907 Biochemistry. 2005 Sep 13;44(36):12094-106. Song YM, Park Y, Lim SS, Yang ST, Woo ER, Park IS, Lee JS, Kim JI, Hahm KS, Kim Y, Shin SY. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues DRAMP33383 RGDfX 5 Cilengitide, EMD 121974 Not available Not found RGD Fibronectin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: M21 (IC50 (Cilengitide inhibited integrin-mediated binding to vitronectin) =0.4 µM); UCLA-P3 (IC50 (Cilengitide inhibited integrin-mediated binding to vitronectin) =0.4 µM) Not available Cyclic Free Free f=D-Phe Mix Not available Integrins αvβ3, αvβ5 11855984 J Med Chem. 2002 Feb 28;45(5):1045-51 Goodman SL, Hölzemann G, Sulyok GA, Kessler H. Nanomolar small molecule inhibitors for alphav(beta)6, alphav(beta)5, and alphav(beta)3 integrins DRAMP33384 FQNRRMKWKK 10 Pen10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa WT (50% Cytotoxicity= μM ) Not available Linear Free Amidation L Not available Not available 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-32. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: effect of sequence and secondary structure DRAMP33385 WRRRRRRRR 9 WR8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa WT (50% Cytotoxicity=442 ± 66.7 μM ) Human erythrocytes: HD50>128 μM Linear Free Amidation L Not available Not available 23085001 Biochim Biophys Acta. 2013 Feb;1828(2):223-32. Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM. Antimicrobial and cell-penetrating properties of penetratin analogs: effect of sequence and secondary structure DRAMP33386 GFXGXKKXGXFXGXGKKXKKKK 22 AMP 1A analogs1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.9 μM ); RL (IC50=2 μM ); UACC-62 (IC50=2.6 μM ); A498 (IC50=3 μM ); COLO 205 (IC50=5.4 μM ); MCF-7 (IC50=6.2 μM ); A549 (IC50=7.2 μM ); Mia PaCa-2 (IC50=7.3 μM ); CFPAC-1 (IC50>7.5 μM ); DLD-1 (IC50>7.5 μM ); IGROV-1 (IC50>7.5 μM ); PC-3 (IC50>7.5 μM ) Not available Linear Acetylation Amidation X=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33387 GFXGXRXGXFXGXGRXRRRR 20 AMP 1A analogs2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=1.1 μM ); NCI-H69 (IC50=2 μM ); CFPAC-1 (IC50=2.6 μM ); Mia PaCa-2 (IC50=5 μM ); A498 (IC50=5.6 μM ); IGROV-1 (IC50=6 μM ); A549 (IC50=6.4 μM ); DLD-1 (IC50=6.4 μM ); UACC-62 (IC50=6.4 μM ); COLO 205 (IC50=6.6 μM ); MCF-7 (IC50=7 μM ); PC-3 (IC50=7.4 μM ) Not available Linear Acetylation Amidation X=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33388 GFXGXRXGXFXGXGRXRRRR 20 AMP 1A analogs2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=3.7 μM); NCI-H69 (IC50=7.1 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33389 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.7 μM); RL (IC50=2.5 μM); UACC-62 (IC50=3.1 μM); COLO 205 (IC50=3.2 μM); Mia PaCa-2 (IC50=3.6 μM); MCF-7 (IC50=4.6 μM); A498 (IC50=4.7 μM); IGROV-1 (IC50=5.4 μM); CFPAC-1 (IC50=5.9 μM ); DLD-1 (IC50=6.2 μM); A549 (IC50=6.5 μM); PC-3 (IC50=7.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Orn (Ornithine) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33390 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.5 μM); RL (IC50=1.7 μM); UACC-62 (IC50=1.9 μM); A498 (IC50=2.1 μM); IGROV-1 (IC50=2.3 μM); A549 (IC50=2.4 μM); DLD-1 (IC50=2.6 μM); CFPAC-1 (IC50=2.7 μM); MCF-7 (IC50=3 μM); Mia PaCa-2 (IC50=4.4 μM); COLO 205 (IC50=6.4 μM); PC-3 (IC50=6.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Orn (Ornithine) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33391 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Orn (Ornithine) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33392 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.7 μM); RL (IC50=2.5 μM); UACC-62 (IC50=3.1 μM); COLO 205 (IC50=3.2 μM); Mia PaCa-2 (IC50=3.6 μM); MCF-7 (IC50=4.6 μM); A498 (IC50=4.7 μM); IGROV-1 (IC50=5.4 μM); CFPAC-1 (IC50=5.9 μM ); DLD-1 (IC50=6.2 μM); A549 (IC50=6.5 μM); PC-3 (IC50=7.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dab (Diaminobutyric acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33393 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.5 μM); RL (IC50=1.7 μM); UACC-62 (IC50=1.9 μM); A498 (IC50=2.1 μM); IGROV-1 (IC50=2.3 μM); A549 (IC50=2.4 μM); DLD-1 (IC50=2.6 μM); CFPAC-1 (IC50=2.7 μM); MCF-7 (IC50=3 μM); Mia PaCa-2 (IC50=4.4 μM); COLO 205 (IC50=6.4 μM); PC-3 (IC50=6.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dab (Diaminobutyric acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33394 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dab (Diaminobutyric acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33395 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.7 μM); RL (IC50=2.5 μM); UACC-62 (IC50=3.1 μM); COLO 205 (IC50=3.2 μM); Mia PaCa-2 (IC50=3.6 μM); MCF-7 (IC50=4.6 μM); A498 (IC50=4.7 μM); IGROV-1 (IC50=5.4 μM); CFPAC-1 (IC50=5.9 μM ); DLD-1 (IC50=6.2 μM); A549 (IC50=6.5 μM); PC-3 (IC50=7.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dpr (Diaminopropionic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33396 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=1.5 μM); RL (IC50=1.7 μM); UACC-62 (IC50=1.9 μM); A498 (IC50=2.1 μM); IGROV-1 (IC50=2.3 μM); A549 (IC50=2.4 μM); DLD-1 (IC50=2.6 μM); CFPAC-1 (IC50=2.7 μM); MCF-7 (IC50=3 μM); Mia PaCa-2 (IC50=4.4 μM); COLO 205 (IC50=6.4 μM); PC-3 (IC50=6.5 μM) Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dpr (Diaminopropionic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33397 GFXGXXXGXFXGXGXXXXXX 20 AMP 1A analogs5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X(3/5/7/9/11/13/16)=A6c (1-aminocyclohexane carboxylic acid); X(6/15/17/18/19/20)=Dpr (Diaminopropionic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33398 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A498 (IC50>7.5 μM ); A549 (IC50>7.5 μM ); CFPAC-1 (IC50>7.5 μM ); COLO 205 (IC50>7.5 μM ); DLD-1 (IC50>7.5 μM ); IGROV-1 (IC50>7.5 μM ); MCF-7 (IC50>7.5 μM ); Mia PaCa-2 (IC50>7.5 μM ); NCI-H69 (IC50>7.5 μM ); PC-3 (IC50>7.5 μM ); RL (IC50>7.5 μM ); UACC-62 (IC50>7.5 μM ) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33399 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.8 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33400 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33401 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=5.9 μM); RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33402 GFXGXRXGXFXGXGRXRRRR 20 AMP 1A analogs7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=1.1 μM ); NCI-H69 (IC50=2 μM ); CFPAC-1 (IC50=2.6 μM ); Mia PaCa-2 (IC50=5 μM ); A498 (IC50=5.6 μM ); IGROV-1 (IC50=6 μM ); A549 (IC50=6.4 μM ); DLD-1 (IC50=6.4 μM ); UACC-62 (IC50=6.4 μM ); COLO 205 (IC50=6.6 μM ); MCF-7 (IC50=7 μM ); PC-3 (IC50=7.4 μM ) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33403 GFXGXRXGXFXGXGRXRRRR 20 AMP 1A analogs7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=3.7 μM); NCI-H69 (IC50=7.1 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A5c (1-aminocyclopentane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33404 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A498 (IC50>7.5 μM ); A549 (IC50>7.5 μM ); CFPAC-1 (IC50>7.5 μM ); COLO 205 (IC50>7.5 μM ); DLD-1 (IC50>7.5 μM ); IGROV-1 (IC50>7.5 μM ); MCF-7 (IC50>7.5 μM ); Mia PaCa-2 (IC50>7.5 μM ); NCI-H69 (IC50>7.5 μM ); PC-3 (IC50>7.5 μM ); RL (IC50>7.5 μM ); UACC-62 (IC50>7.5 μM ) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Tic (Tetrahydroisoquinolinecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33405 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.8 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Tic (Tetrahydroisoquinolinecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33406 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Tic (Tetrahydroisoquinolinecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33407 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=5.9 μM); RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Tic (Tetrahydroisoquinolinecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33408 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A498 (IC50>7.5 μM ); A549 (IC50>7.5 μM ); CFPAC-1 (IC50>7.5 μM ); COLO 205 (IC50>7.5 μM ); DLD-1 (IC50>7.5 μM ); IGROV-1 (IC50>7.5 μM ); MCF-7 (IC50>7.5 μM ); Mia PaCa-2 (IC50>7.5 μM ); NCI-H69 (IC50>7.5 μM ); PC-3 (IC50>7.5 μM ); RL (IC50>7.5 μM ); UACC-62 (IC50>7.5 μM ) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Oic (Octahydroindolecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33409 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.8 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Oic (Octahydroindolecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33410 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Oic (Octahydroindolecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33411 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=5.9 μM); RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A6c (1-aminocyclohexane carboxylic acid); X(5/9/13/16)=Oic (Octahydroindolecarboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33412 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A498 (IC50>7.5 μM ); A549 (IC50>7.5 μM ); CFPAC-1 (IC50>7.5 μM ); COLO 205 (IC50>7.5 μM ); DLD-1 (IC50>7.5 μM ); IGROV-1 (IC50>7.5 μM ); MCF-7 (IC50>7.5 μM ); Mia PaCa-2 (IC50>7.5 μM ); NCI-H69 (IC50>7.5 μM ); PC-3 (IC50>7.5 μM ); RL (IC50>7.5 μM ); UACC-62 (IC50>7.5 μM ) Not available Linear Acetylation Amidation X(3/7/11)=A5c (1-aminocyclopentane carboxylic acid); X(5/9/13/16)=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33413 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.8 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A5c (1-aminocyclopentane carboxylic acid); X(5/9/13/16)=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33414 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); NCI-H69 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A5c (1-aminocyclopentane carboxylic acid); X(5/9/13/16)=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33415 GFXGXKXGXFXGXGKXKKKK 20 AMP 1A analogs10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=5.9 μM); RL (IC50=6.7 μM); A498 (IC50>7.5 μM); A549 (IC50>7.5 μM); CFPAC-1 (IC50>7.5 μM); COLO 205 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); MCF-7 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM); UACC-62 (IC50>7.5 μM) Not available Linear Acetylation Amidation X(3/7/11)=A5c (1-aminocyclopentane carboxylic acid); X(5/9/13/16)=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33416 KKKKGFXGXKXGXFXGXGKX 20 AMP 1A analogs11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H69 (IC50=2.2 μM); RL (IC50=3.7 μM); A498 (IC50=4.2 μM); UACC-62 (IC50=6.4 μM); COLO 205 (IC50=6.7 μM); A549 (IC50=7.2 μM); MCF-7 (IC50=7.3 μM); CFPAC-1 (IC50>7.5 μM); DLD-1 (IC50>7.5 μM); IGROV-1 (IC50>7.5 μM); Mia PaCa-2 (IC50>7.5 μM); PC-3 (IC50>7.5 μM) Not available Linear Acetylation Amidation X=A6c (1-aminocyclohexane carboxylic acid) L Not available Not available 27387357 Bioorg Med Chem. 2016 Sep 15;24(18):4056-4065. Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids DRAMP33417 KKWWKKWWK 9 peptide 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=31.0 ± 1.0 µM); A20 (IC50=37.3 ± 1.5 µM) Not available Linear Free Amidation L MRC-5: IC50>357 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33418 KKXWKKWWK 9 peptide 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=36.7 ± 9.5 µM); A20 (IC50=51.7 ± 6.5 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=488 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33419 KKXWKKWWK 9 peptide 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=13.0 ± 1.0 µM); IGROV-1 (IC50=13.4 ± 1.6 µM); AT84 (IC50=17.7 ± 3.1 µM); HL-60 (IC50=6.1 ± 1.8 µM); IGROV-1/CDDP (IC50=6.6 ± 2.6 µM); MCF-7 (IC50=6.8 ± 2.8 µM); HL-60/ADR (IC50=7.0 ± 3.7 µM); K562 (IC50=7.2 ± 0.4 µM); K562/Gleevec (IC50=7.9 ± 2.9 µM); MCF-7/mdr (IC50=8.4 ± 2.7 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=488 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33420 KKWXKKWWK 9 peptide 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=24.7 ± 2.3 µM); A20 (IC50=25.7 ± 0.6 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=287 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33421 KKWXKKWWK 9 peptide 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=18.7 ± 1.5 µM); AT84 (IC50=27.3 ± 5.1 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=287 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33422 KKWXKKWWK 9 peptide 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=24.0 ± 1.0 µM); AT84 (IC50=26.3 ± 7.1 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=287 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33423 KKWXKKWWK 9 peptide 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=26.0 ± 1.7 µM); AT84 (IC50=29.3 ± 7.8 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=287 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33424 KKWXKKWWK 9 peptide 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.0 ± 1.0 µM); A20 (IC50=9.3 ± 1.2 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=287 ± 52 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33425 KKWWKKXWK 9 peptide 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=12.3 ± 1.5 µM); AT84 (IC50=25.3 ± 4.2 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=102 ± 7.6 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33426 KKWXKKWXK 9 peptide 6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=12 µM); AT84 (IC50=15.0 ± 1.0 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=80.0 ± 7.0 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33427 KKWXKKWWK 9 peptide 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=24.7 ± 2.3 µM); A20 (IC50=25.7 ± 0.6 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=174 ± 22 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33428 KKWXKKWWK 9 peptide 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=18.7 ± 1.5 µM); AT84 (IC50=27.3 ± 5.1 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=174 ± 22 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33429 KKWXKKWWK 9 peptide 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=24.0 ± 1.0 µM); AT84 (IC50=26.3 ± 7.1 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=174 ± 22 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33430 KKWXKKWWK 9 peptide 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=26.0 ± 1.7 µM); AT84 (IC50=29.3 ± 7.8 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=174 ± 22 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33431 KKWXKKWWK 9 peptide 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.0 ± 1.0 µM); A20 (IC50=9.3 ± 1.2 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=174 ± 22 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33432 KKWXKKWWK 9 peptide 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=24.7 ± 2.3 µM); A20 (IC50=25.7 ± 0.6 µM) Not available Linear Free Amidation X=1-Nal (1-naphthylalanine) L MRC-5: IC50=238 ± 69 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33433 KKWXKKWWK 9 peptide 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=18.7 ± 1.5 µM); AT84 (IC50=27.3 ± 5.1 µM) Not available Linear Free Amidation X=1-Nal (1-naphthylalanine) L MRC-5: IC50=238 ± 69 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33434 KKWXKKWWK 9 peptide 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=24.0 ± 1.0 µM); AT84 (IC50=26.3 ± 7.1 µM) Not available Linear Free Amidation X=1-Nal (1-naphthylalanine) L MRC-5: IC50=238 ± 69 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33435 KKWXKKWWK 9 peptide 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=26.0 ± 1.7 µM); AT84 (IC50=29.3 ± 7.8 µM) Not available Linear Free Amidation X=1-Nal (1-naphthylalanine) L MRC-5: IC50=238 ± 69 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33436 KKWXKKWWK 9 peptide 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.0 ± 1.0 µM); A20 (IC50=9.3 ± 1.2 µM) Not available Linear Free Amidation X=1-Nal (1-naphthylalanine) L MRC-5: IC50=238 ± 69 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33437 KKWXKKWWK 9 peptide 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=24.7 ± 2.3 µM); A20 (IC50=25.7 ± 0.6 µM) Not available Linear Free Amidation X=2-Nal (2-naphthylalanine) L MRC-5: IC50=257 ± 20 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33438 KKWXKKWWK 9 peptide 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=18.7 ± 1.5 µM); AT84 (IC50=27.3 ± 5.1 µM) Not available Linear Free Amidation X=2-Nal (2-naphthylalanine) L MRC-5: IC50=257 ± 20 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33439 KKWXKKWWK 9 peptide 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=24.0 ± 1.0 µM); AT84 (IC50=26.3 ± 7.1 µM) Not available Linear Free Amidation X=2-Nal (2-naphthylalanine) L MRC-5: IC50=257 ± 20 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33440 KKWXKKWWK 9 peptide 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=26.0 ± 1.7 µM); AT84 (IC50=29.3 ± 7.8 µM) Not available Linear Free Amidation X=2-Nal (2-naphthylalanine) L MRC-5: IC50=257 ± 20 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33441 KKWXKKWWK 9 peptide 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.0 ± 1.0 µM); A20 (IC50=9.3 ± 1.2 µM) Not available Linear Free Amidation X=2-Nal (2-naphthylalanine) L MRC-5: IC50=257 ± 20 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33442 KKWXKKWWK 9 peptide 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=24.7 ± 2.3 µM); A20 (IC50=25.7 ± 0.6 µM) Not available Linear Free Amidation X=9-Ath (9-anthracenylalanine) L MRC-5: IC50=40.0 ± 1.7 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33443 KKWXKKWWK 9 peptide 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=18.7 ± 1.5 µM); AT84 (IC50=27.3 ± 5.1 µM) Not available Linear Free Amidation X=9-Ath (9-anthracenylalanine) L MRC-5: IC50=40.0 ± 1.7 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33444 KKWXKKWWK 9 peptide 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=24.0 ± 1.0 µM); AT84 (IC50=26.3 ± 7.1 µM) Not available Linear Free Amidation X=9-Ath (9-anthracenylalanine) L MRC-5: IC50=40.0 ± 1.7 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33445 KKWXKKWWK 9 peptide 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=26.0 ± 1.7 µM); AT84 (IC50=29.3 ± 7.8 µM) Not available Linear Free Amidation X=9-Ath (9-anthracenylalanine) L MRC-5: IC50=40.0 ± 1.7 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33446 KKWXKKWWK 9 peptide 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.0 ± 1.0 µM); A20 (IC50=9.3 ± 1.2 µM) Not available Linear Free Amidation X=9-Ath (9-anthracenylalanine) L MRC-5: IC50=40.0 ± 1.7 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33447 KKXWKKWWK 9 peptide 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=36.7 ± 9.5 µM); A20 (IC50=51.7 ± 6.5 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=151 ± 16 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33448 KKXWKKWWK 9 peptide 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=13.0 ± 1.0 µM); IGROV-1 (IC50=13.4 ± 1.6 µM); AT84 (IC50=17.7 ± 3.1 µM); HL-60 (IC50=6.1 ± 1.8 µM); IGROV-1/CDDP (IC50=6.6 ± 2.6 µM); MCF-7 (IC50=6.8 ± 2.8 µM); HL-60/ADR (IC50=7.0 ± 3.7 µM); K562 (IC50=7.2 ± 0.4 µM); K562/Gleevec (IC50=7.9 ± 2.9 µM); MCF-7/mdr (IC50=8.4 ± 2.7 µM) Not available Linear Free Amidation X=Bip (Biphenylalanine) L MRC-5: IC50=151 ± 16 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33449 kkxwkkwwk 9 peptide 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=11.3 ± 1.2 µM); IGROV-1 (IC50=14.3 ± 5.3 µM); MCF-7 (IC50=4.6 ± 1.1 µM); MCF-7/mdr (IC50=4.9 ± 1.6 µM); HL-60/ADR (IC50=4.9 ± 3.7 µM); HL-60 (IC50=6.1 ± 3.4 µM); IGROV-1/CDDP (IC50=6.6 ± 2.7 µM); K562 (IC50=7.4 ± 0.1 µM); K562/Gleevec (IC50=7.6 ± 1.3 µM); A20 (IC50=8.3 ± 1.5 µM) Not available Linear Free Amidation X=D-Bip (D-Biphenylalanine) D MRC-5: IC50=87.0 ± 15.1 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33450 XXWXXXWWX 9 peptide 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=21.7 ± 2.5 µM); MT-1 (IC50=216 ± 36 µM); AT84 (IC50=23.0 ± 3.6 µM); HT-29 (IC50=248 ± 5 µM); Kelly (IC50=78 ± 7 µM) Not available Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L MRC-5: IC50=97.7 ± 5.1 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33451 XXWXXXWWX 9 peptide 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=14.3 ± 1.2 µM); A20 (IC50=8.3 ± 0.6 µM) Not available Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L MRC-5: IC50=97.7 ± 5.1 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33452 XXWXXXWWX 9 peptide 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=154 ± 29 µM); A20 (IC50=67.7 ± 13.2 µM) Not available Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L MRC-5: IC50=97.7 ± 5.1 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33453 XXWXXXWWX 9 peptide 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=21.7 ± 2.5 µM); MT-1 (IC50=216 ± 36 µM); AT84 (IC50=23.0 ± 3.6 µM); HT-29 (IC50=248 ± 5 µM); Kelly (IC50=78 ± 7 µM) Not available Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L MRC-5: IC50=516 ± 5.2 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33454 XXWXXXWWX 9 peptide 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=14.3 ± 1.2 µM); A20 (IC50=8.3 ± 0.6 µM) Not available Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L MRC-5: IC50=516 ± 5.2 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33455 XXWXXXWWX 9 peptide 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=154 ± 29 µM); A20 (IC50=67.7 ± 13.2 µM) Not available Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L MRC-5: IC50=516 ± 5.2 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33456 RRWXRRWWR 9 peptide 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: IGROV-1 (IC50=11.1 ± 3.4 µM); AT84 (IC50=11.3 ± 2.1 µM); MCF-7 (IC50=5.5 ± 0.9 µM); IGROV-1/CDDP (IC50=5.5 ± 2.2 µM); HL-60/ADR (IC50=6.0 ± 4.5 µM); MCF-7/mdr (IC50=6.6 ± 2.8 µM); A20 (IC50=6.7 ± 1.2 µM); HL-60 (IC50=6.7 ± 3.7 µM); K562 (IC50=7.0 ± 0.8 µM); K562/Gleevec (IC50=7.7 ± 1.6 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=76.0 ± 9.5 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33457 kkWXkkWWk 9 peptide 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: AT84 (IC50=113 ± 10 µM); A20 (IC50=134 ± 13 µM) Not available Linear Free Amidation k=D-Lys; X=Dip (Diphenylalanine) Mix MRC-5: IC50>347 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33458 KWWKKWXK 8 LTX-315 Metabolites 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=13.5 ± 0.9 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=43.9 ± 19.3 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33459 WWKKWXK 7 LTX-315 Metabolites 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=20.3 ± 2.9 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=53.2 ± 21.2 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33460 WKKWXK 6 LTX-315 Metabolites 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A20 (IC50=247 ± 13 µM) Not available Linear Free Amidation X=Dip (Diphenylalanine) L MRC-5: IC50=460 ± 71 µM Not available 26982623 J Med Chem. 2016 Apr 14;59(7):2918-27. Haug BE, Camilio KA, Eliassen LT, Stensen W, Svendsen JS, Berg K, Mortensen B, Serin G, Mirjolet JF, Bichat F, Rekdal Ø. Discovery of a 9-mer Cationic Peptide (LTX-315) as a Potential First in Class Oncolytic Peptide DRAMP33461 GLPVCGETCVGGTCYTPGCTCSWPVCTRN 29 Kalata B1 [N15Y] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=12.3±0.6 μM); K562 (CC50=3.2±0.1 μM); HeLa (CC50=8.1±0.4 μM) Human erythrocytes: 50% Hemolysis=6.9±0.3 µM Cyclic Free Free L HFF-1: CC50=6.7±0.6 µM; PBMCs: CC50=1.0±0.1 µM Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33462 GLPVCGETCVGGTCDTPGCTCSWPVCTRN 29 Kalata B1 [N15D] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 60 µM); K562 (Not active up to 60 µM); MM96L (Not active up to 60 µM) Human erythrocytes: Not active up to 50 µM Cyclic Free Free L HFF-1: Not active up to 60 µM; PBMCs: Not active up to 60 µM Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33463 GLPVCGETCVGGTCNYPGCTCSWPVCTRN 29 Kalata B1 [T16Y] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 60 µM); K562 (Not active up to 60 µM); MM96L (Not active up to 60 µM) Human erythrocytes: Not active up to 50 µM Cyclic Free Free L HFF-1: Not active up to 60 µM; PBMCs: Not active up to 60 µM Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33464 GLPVCGETCVGGTCNSPGCTCSWPVCTRN 29 Kalata B1 [T16S] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (CC50=43.8±0.5 μM) Human erythrocytes: Weak active up to 50 µM Cyclic Free Free L Not available Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33465 GLPVCGETCVGGTCNTPGCTCSYPVCTRN 29 Kalata B1 [W23Y] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 60 µM); K562 (Not active up to 60 µM); MM96L (Not active up to 60 µM) Human erythrocytes: Not active up to 50 µM Cyclic Free Free L HFF-1: Not active up to 60 µM; PBMCs: Not active up to 60 µM Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33466 GLPVCGETCVGGTCNTPGCTCSWWPVCTRN 30 Kalata B1 [W23WW] P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MM96L (CC50=12.2±0.6 μM); HeLa (CC50=9.8±0.5 μM) Human erythrocytes: 50% Hemolysis=14.0±0.7 µM Cyclic Free Free L HFF-1: CC50=9.2±0.7 µM Not available 25099014 Chembiochem. 2014 Sep 5;15(13):1956-65. Troeira Henriques S, Huang YH, Chaousis S, Wang CK, Craik DJ. Anticancer and toxic properties of cyclotides are dependent on phosphatidylethanolamine phospholipid targeting DRAMP33467 KKLIKVWAKGFKKAKKLFKGIG 22 PBP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (21% Cytotoxicity=15 µM) Sheep erythrocytes: 10% Hemolysis=15 µM Linear Free Free L Not available Not available 30637367 Pept Sci (Hoboken). 2018 Jul;110(4):e24074. Shirley DJ, Chrom CL, Richards EA, Carone BR, Caputo GA. Antimicrobial activity of a porphyrin binding peptide DRAMP33468 KKLIKVFAKGWKKAKKLFKGIG 22 PBP-W11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (52% Cytotoxicity=15 µM) Sheep erythrocytes: 0% Hemolysis=15 µM Linear Free Free L Not available Not available 30637367 Pept Sci (Hoboken). 2018 Jul;110(4):e24074. Shirley DJ, Chrom CL, Richards EA, Carone BR, Caputo GA. Antimicrobial activity of a porphyrin binding peptide DRAMP33469 KKLIKVFAKGFKKAKKLWKGIG 22 PBP-W18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (52% Cytotoxicity=15 µM) Sheep erythrocytes: 0% Hemolysis=15 µM Linear Free Free L Not available Not available 30637367 Pept Sci (Hoboken). 2018 Jul;110(4):e24074. Shirley DJ, Chrom CL, Richards EA, Carone BR, Caputo GA. Antimicrobial activity of a porphyrin binding peptide DRAMP33470 XXLIXVWAXGFXXAXXLFXGIG 22 PBP-X Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (8% Cytotoxicity=15 µM) Sheep erythrocytes: 0% Hemolysis=15 µM Linear Free Free X=Diaminopropionic acid L Not available Not available 30637367 Pept Sci (Hoboken). 2018 Jul;110(4):e24074. Shirley DJ, Chrom CL, Richards EA, Carone BR, Caputo GA. Antimicrobial activity of a porphyrin binding peptide DRAMP33471 KKAAKAWAKGAKKAKKLAKGAG 22 PBP-A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (12% Cytotoxicity=15 µM) Sheep erythrocytes: 0% Hemolysis=15 µM Linear Free Free L Not available Not available 30637367 Pept Sci (Hoboken). 2018 Jul;110(4):e24074. Shirley DJ, Chrom CL, Richards EA, Carone BR, Caputo GA. Antimicrobial activity of a porphyrin binding peptide DRAMP33472 WLlXNG 6 Desotamide A Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free X=Allo-Ile Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33473 WLlVNG 6 Desotamide B Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33474 WLvXNG 6 Desotamide E Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free X=Allo-Ile; v=D-Val Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33475 WLxXNG 6 Desotamide F Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free x=D-Allo-Ile; X=Allo-Ile Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33476 WLlXNx 6 Wollamide A Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free X=Allo-Ile; x=D-Orn Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33477 WLlVNx 6 Wollamide B Not available Not found Streptomyces nov. sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=56 µM); NCI-H460 (Not active up to 30 µM); SW620 (Not active up to 30 µM) Not available Cyclic Free Free x=D-Orn Mix Not available Not available 25229313 Org Lett. 2014 Oct 3;16(19):5120-3. Khalil ZG, Salim AA, Lacey E, Blumenthal A, Capon RJ. Wollamides: antimycobacterial cyclic hexapeptides from an Australian soil Streptomyces DRAMP33478 GWKDWFRKAKKVGKTVGGLALNHYL 25 NRC-123 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=16 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation L Zebrafish embryos: >10% Killing=5 µg/ml (4, 28, 52hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33479 GIRKWFKKAAHVGKEVGKVALNACL 25 NRC-124 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=128 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Free L Zebrafish embryos: >10% Killing=5 µg/ml (4, 52hpf embryo); >10% Killing=25 µg/ml (28hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33480 GLKKWFKKAVHVGKKVGKVALNAYL 25 NRC-125 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=16 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation L Zebrafish embryos: >10% Killing=5 µg/ml (4, 28, 52hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33481 GWRKWIKKATHVGKHIGKAALDAYI 25 NRC-126 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=32 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation L Zebrafish embryos: >10% Killing=5 µg/ml (4, 52hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33482 GCKKWFKKAAHVGKNVGKVALNAYL 25 NRC-127 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=32 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation L Zebrafish embryos: >10% Killing=5 µg/ml (4, 28hpf embryo); >10% Killing=25 µg/ml (52hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33483 GIRKWFKKAAHVGKKVGKVALNAYL 25 NRC-128 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death=64 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation L Zebrafish embryos: >10% Killing=5 µg/ml (28, 52hpf embryo); >10% Killing=25 µg/ml (4hpf embryo) Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33484 GrrkrkWLrrIGkGVkIIGGAALDHL 26 NRC-03D Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (50% Cell death>128 µg/ml) Human erythrocytes: 50% Hemolysis>256 µg/ml Linear Free Amidation r=D-Arg; k=D-Lys Mix Zebrafish embryos: No killing Not available 21729875 Dis Model Mech. 2011 Sep;4(5):622-33. Morash MG, Douglas SE, Robotham A, Ridley CM, Gallant JW, Soanes KH. The zebrafish embryo as a tool for screening and characterizing pleurocidin host-defense peptides as anti-cancer agents DRAMP33485 GLVGTLLGHIGKAILG 16 Frenatin 2.1S Not available Not found Sphaenorhynchus lacteus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=80 ± 6 μM ) Human erythrocytes: HC50=167 ± 8 µM Linear Free Amidation L Not available Not available 24704757 Peptides. 2014 Jun;56:132-40. Conlon JM, Mechkarska M, Radosavljevic G, Attoub S, King JD, Lukic ML, McClean S. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae) DRAMP33486 GLVGTLLGHIGKAILG 16 Frenatin 2.1S Not available Not found Sphaenorhynchus lacteus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50>100 μM ) Human erythrocytes: HC50=167 ± 8 µM Linear Free Amidation L Not available Not available 24704757 Peptides. 2014 Jun;56:132-40. Conlon JM, Mechkarska M, Radosavljevic G, Attoub S, King JD, Lukic ML, McClean S. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae) DRAMP33487 GLVGTLLGHIGKAILS 16 Frenatin 2.2S Not available Not found Sphaenorhynchus lacteus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=65 ± 5 μM ) Human erythrocytes: HC50=169 ± 7 µM Linear Free Amidation L Not available Not available 24704757 Peptides. 2014 Jun;56:132-40. Conlon JM, Mechkarska M, Radosavljevic G, Attoub S, King JD, Lukic ML, McClean S. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae) DRAMP33488 GLVGTLLGHIGKAILG 16 Frenatin 2.3S Not available Not found Sphaenorhynchus lacteus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50=80 ± 6 μM ) Human erythrocytes: HC50=404 ± 11 µM Linear Free Free L Not available Not available 24704757 Peptides. 2014 Jun;56:132-40. Conlon JM, Mechkarska M, Radosavljevic G, Attoub S, King JD, Lukic ML, McClean S. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae) DRAMP33489 GLVGTLLGHIGKAILG 16 Frenatin 2.3S Not available Not found Sphaenorhynchus lacteus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (LC50>100 μM ) Human erythrocytes: HC50=404 ± 11 µM Linear Free Free L Not available Not available 24704757 Peptides. 2014 Jun;56:132-40. Conlon JM, Mechkarska M, Radosavljevic G, Attoub S, King JD, Lukic ML, McClean S. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae) DRAMP33490 ELLVDLL 7 Gageostatin A Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=10.8 µg/mL); NCI-H23 (IC50=11.2 µg/mL); HCT 15 (IC50=11.4 µg/mL); ACHN (IC50=11.5 µg/mL); NUGC-3 (IC50=11.8 µg/mL); MDA-MB-231 (IC50=14.9 µg/mL) Not available Linear 3-β-hydroxy-11-methyltridecanoic Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33491 ELLVDLL 7 Gageostatin A Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H23 (IC50=11.7 µg/mL); NUGC-3 (IC50=13.9 µg/mL); MDA-MB-231 (IC50=16.1 µg/mL); HCT 15 (IC50=18.3 µg/mL); ACHN (IC50=18.4 µg/mL); PC-3 (IC50=19.4 µg/mL) Not available Linear 3-β-hydroxy-11-methyltridecanoic Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33492 ELLVDLL 7 Gageostatin A Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NUGC-3 (IC50=10.5 µg/mL); NCI-H23 (IC50=10.9 µg/mL); MDA-MB-231 (IC50=11.2 µg/mL); PC-3 (IC50=11.7 µg/mL); ACHN (IC50=12.3 µg/mL); HCT 15 (IC50=23.2 µg/mL) Not available Linear 3-β-hydroxy-11-methyltridecanoic Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33493 ELLVDLL 7 Gageostatin B Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=10.8 µg/mL); NCI-H23 (IC50=11.2 µg/mL); HCT 15 (IC50=11.4 µg/mL); ACHN (IC50=11.5 µg/mL); NUGC-3 (IC50=11.8 µg/mL); MDA-MB-231 (IC50=14.9 µg/mL) Not available Linear 3-β-hydroxy-9,11-dimethyltridecanoic acids Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33494 ELLVDLL 7 Gageostatin B Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H23 (IC50=11.7 µg/mL); NUGC-3 (IC50=13.9 µg/mL); MDA-MB-231 (IC50=16.1 µg/mL); HCT 15 (IC50=18.3 µg/mL); ACHN (IC50=18.4 µg/mL); PC-3 (IC50=19.4 µg/mL) Not available Linear 3-β-hydroxy-9,11-dimethyltridecanoic acids Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33495 ELLVDLL 7 Gageostatin B Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NUGC-3 (IC50=10.5 µg/mL); NCI-H23 (IC50=10.9 µg/mL); MDA-MB-231 (IC50=11.2 µg/mL); PC-3 (IC50=11.7 µg/mL); ACHN (IC50=12.3 µg/mL); HCT 15 (IC50=23.2 µg/mL) Not available Linear 3-β-hydroxy-9,11-dimethyltridecanoic acids Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33496 ELLVDLL 7 Gageostatin C Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=10.8 µg/mL); NCI-H23 (IC50=11.2 µg/mL); HCT 15 (IC50=11.4 µg/mL); ACHN (IC50=11.5 µg/mL); NUGC-3 (IC50=11.8 µg/mL); MDA-MB-231 (IC50=14.9 µg/mL) Not available Linear (E)-7,9-dimethylundec-2-enoic acid Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33497 ELLVDLL 7 Gageostatin C Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H23 (IC50=11.7 µg/mL); NUGC-3 (IC50=13.9 µg/mL); MDA-MB-231 (IC50=16.1 µg/mL); HCT 15 (IC50=18.3 µg/mL); ACHN (IC50=18.4 µg/mL); PC-3 (IC50=19.4 µg/mL) Not available Linear (E)-7,9-dimethylundec-2-enoic acid Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33498 ELLVDLL 7 Gageostatin C Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NUGC-3 (IC50=10.5 µg/mL); NCI-H23 (IC50=10.9 µg/mL); MDA-MB-231 (IC50=11.2 µg/mL); PC-3 (IC50=11.7 µg/mL); ACHN (IC50=12.3 µg/mL); HCT 15 (IC50=23.2 µg/mL) Not available Linear (E)-7,9-dimethylundec-2-enoic acid Free L Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85 Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP33499 GIMDTIKGAAKDLAGQLLDKLKCKITKC 28 Ranatuerin-2VLb Not available Not found Lithobates vaillanti Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (LC50=30 µM ) Huµan erythrocytes: HC50>200 µM Cyclic Free Free L Not available Not available 19379837 Comp Biochem Physiol C Toxicol Pharmacol. 2009 Aug;150(2):150-4. Conlon JM, Raza H, Coquet L, Jouenne T, Leprince J, Vaudry H, King JD. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae) DRAMP33500 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33501 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33502 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33503 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33504 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33505 VKRFKKFFRKLKKSV 15 B1-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=81.3 ± 6.8 µM; HEK293: IC50=81.3 ± 6.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33506 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33507 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33508 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33509 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33510 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33511 VKRFKKFFRKLKKSV 15 B1-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=77.6 ± 7.3 µM; HEK293: IC50=75.8 ± 6.6 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33512 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33513 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33514 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33515 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33516 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33517 VKRFKKFFRKLKKSV 15 B1-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=70.8 ± 7.1 µM; HEK293: IC50=70.2 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33518 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33519 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33520 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33521 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33522 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33523 VKRFKKFFRKLKKSV 15 B1-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=67.6 ± 6.5 µM; HEK293: IC50=68.1 ± 5.3 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33524 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=22.2±1.3 μM); MCF-7 (IC50=24.6±3.7 μM); K562 (IC50=27.0±2.1 μM); K562/ADM (IC50=45.1±3.7 μM); MCF-7/Taxol (IC50=57.6±6.3 μM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33525 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=10.5 ± 1.3 µM); K562 (IC50=11.0 ± 1.1 µM); K562/ADM (IC50=11.7 ± 0.7 µM); MCF-7 (IC50=9.1 ± 0.7 µM ) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33526 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562/ADM (IC50=10.0 ± 0.8 µM); K562 (IC50=11.5 ± 0.9 µM); MCF-7 (IC50=8.8 ± 0.5 µM ); MCF-7/Taxol (IC50=9.5 ± 1.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33527 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.2 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.4 µM); K562/ADM (IC50=4.9 ± 0.1 µM); K562 (IC50=6.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33528 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=1.9 ± 0.2 µM); MCF-7/Taxol (IC50=2.0 ± 0.3 µM); K562/ADM (IC50=3.4 ± 0.3 µM); K562 (IC50=3.8 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33529 VKRFKKFFRKLKKSV 15 B1-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7/Taxol (IC50=2.0 ± 0.1 µM); MCF-7 (IC50=2.3 ± 0.1 µM); K562 (IC50=3.9 ± 0.2 µM); K562/ADM (IC50=4.2 ± 0.5 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=66.1 ± 5.4 µM; HEK293: IC50=66.4 ± 4.8 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33530 GGVKRFKKFFRKLKKSV 17 B1-GG-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=10.5 ± 0.9 µM); MCF-7/Taxol (IC50=11.5 ± 0.8 µM); K562/ADM (IC50=9.2 ± 1.1 µM); K562 (IC50=9.7 ± 0.7 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=85.1 ± 6.9 µM; HEK293: IC50=72.2 ± 6.9 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33531 GGVKRFKKFFRKLKKSV 17 B1-GG-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.2 ± 1.1 µM); K562/ADM (IC50=10.5 ± 1.3 µM); MCF-7/Taxol (IC50=10.7 ± 1.0 µM); MCF-7 (IC50=9.6 ± 0.4 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=85.1 ± 6.9 µM; HEK293: IC50=72.2 ± 6.9 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33532 GGVKRFKKFFRKLKKSV 17 B1-GG-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.5 ± 0.1 µM); K562 (IC50=3.8 ± 0.2 µM); MCF-7/Taxol (IC50=4.3 ± 0.2 µM); K562/ADM (IC50=4.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=85.1 ± 6.9 µM; HEK293: IC50=72.2 ± 6.9 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33533 GGVKRFKKFFRKLKKSV 17 B1-GG-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.7 ± 0.3 µM); MCF-7/Taxol (IC50=3.2 ± 0.2 µM); K562/ADM (IC50=3.4 ± 0.1 µM); K562 (IC50=3.4 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=85.1 ± 6.9 µM; HEK293: IC50=72.2 ± 6.9 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33534 GGVKRFKKFFRKLKKSV 17 B1-GG-C10 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.1 µM); K562/ADM (IC50=3.3 ± 0.3 µM); K562 (IC50=3.4 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)8CO, Decanoic acid Amidation L GES-1: IC50=85.1 ± 6.9 µM; HEK293: IC50=72.2 ± 6.9 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33535 GGVKRFKKFFRKLKKSV 17 B1-GG-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=10.5 ± 0.9 µM); MCF-7/Taxol (IC50=11.5 ± 0.8 µM); K562/ADM (IC50=9.2 ± 1.1 µM); K562 (IC50=9.7 ± 0.7 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=83.2 ± 7.8 µM; HEK293: IC50=68.7 ± 5.7 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33536 GGVKRFKKFFRKLKKSV 17 B1-GG-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.2 ± 1.1 µM); K562/ADM (IC50=10.5 ± 1.3 µM); MCF-7/Taxol (IC50=10.7 ± 1.0 µM); MCF-7 (IC50=9.6 ± 0.4 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=83.2 ± 7.8 µM; HEK293: IC50=68.7 ± 5.7 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33537 GGVKRFKKFFRKLKKSV 17 B1-GG-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.5 ± 0.1 µM); K562 (IC50=3.8 ± 0.2 µM); MCF-7/Taxol (IC50=4.3 ± 0.2 µM); K562/ADM (IC50=4.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=83.2 ± 7.8 µM; HEK293: IC50=68.7 ± 5.7 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33538 GGVKRFKKFFRKLKKSV 17 B1-GG-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.7 ± 0.3 µM); MCF-7/Taxol (IC50=3.2 ± 0.2 µM); K562/ADM (IC50=3.4 ± 0.1 µM); K562 (IC50=3.4 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=83.2 ± 7.8 µM; HEK293: IC50=68.7 ± 5.7 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33539 GGVKRFKKFFRKLKKSV 17 B1-GG-C12 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.1 µM); K562/ADM (IC50=3.3 ± 0.3 µM); K562 (IC50=3.4 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)10CO, Dodecanoic acid Amidation L GES-1: IC50=83.2 ± 7.8 µM; HEK293: IC50=68.7 ± 5.7 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33540 GGVKRFKKFFRKLKKSV 17 B1-GG-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=10.5 ± 0.9 µM); MCF-7/Taxol (IC50=11.5 ± 0.8 µM); K562/ADM (IC50=9.2 ± 1.1 µM); K562 (IC50=9.7 ± 0.7 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=74.1 ± 6.5 µM; HEK293: IC50=67.1 ± 4.2 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33541 GGVKRFKKFFRKLKKSV 17 B1-GG-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.2 ± 1.1 µM); K562/ADM (IC50=10.5 ± 1.3 µM); MCF-7/Taxol (IC50=10.7 ± 1.0 µM); MCF-7 (IC50=9.6 ± 0.4 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=74.1 ± 6.5 µM; HEK293: IC50=67.1 ± 4.2 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33542 GGVKRFKKFFRKLKKSV 17 B1-GG-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.5 ± 0.1 µM); K562 (IC50=3.8 ± 0.2 µM); MCF-7/Taxol (IC50=4.3 ± 0.2 µM); K562/ADM (IC50=4.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=74.1 ± 6.5 µM; HEK293: IC50=67.1 ± 4.2 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33543 GGVKRFKKFFRKLKKSV 17 B1-GG-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.7 ± 0.3 µM); MCF-7/Taxol (IC50=3.2 ± 0.2 µM); K562/ADM (IC50=3.4 ± 0.1 µM); K562 (IC50=3.4 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=74.1 ± 6.5 µM; HEK293: IC50=67.1 ± 4.2 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33544 GGVKRFKKFFRKLKKSV 17 B1-GG-C14 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.1 µM); K562/ADM (IC50=3.3 ± 0.3 µM); K562 (IC50=3.4 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)12CO, Myristic acid Amidation L GES-1: IC50=74.1 ± 6.5 µM; HEK293: IC50=67.1 ± 4.2 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33545 GGVKRFKKFFRKLKKSV 17 B1-GG-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=10.5 ± 0.9 µM); MCF-7/Taxol (IC50=11.5 ± 0.8 µM); K562/ADM (IC50=9.2 ± 1.1 µM); K562 (IC50=9.7 ± 0.7 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=69.2 ± 4.4 µM; HEK293: IC50=65.9 ± 5.4 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33546 GGVKRFKKFFRKLKKSV 17 B1-GG-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.2 ± 1.1 µM); K562/ADM (IC50=10.5 ± 1.3 µM); MCF-7/Taxol (IC50=10.7 ± 1.0 µM); MCF-7 (IC50=9.6 ± 0.4 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=69.2 ± 4.4 µM; HEK293: IC50=65.9 ± 5.4 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33547 GGVKRFKKFFRKLKKSV 17 B1-GG-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.5 ± 0.1 µM); K562 (IC50=3.8 ± 0.2 µM); MCF-7/Taxol (IC50=4.3 ± 0.2 µM); K562/ADM (IC50=4.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=69.2 ± 4.4 µM; HEK293: IC50=65.9 ± 5.4 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33548 GGVKRFKKFFRKLKKSV 17 B1-GG-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.7 ± 0.3 µM); MCF-7/Taxol (IC50=3.2 ± 0.2 µM); K562/ADM (IC50=3.4 ± 0.1 µM); K562 (IC50=3.4 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=69.2 ± 4.4 µM; HEK293: IC50=65.9 ± 5.4 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33549 GGVKRFKKFFRKLKKSV 17 B1-GG-C16 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.1 µM); K562/ADM (IC50=3.3 ± 0.3 µM); K562 (IC50=3.4 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)14CO, Palmitic acid Amidation L GES-1: IC50=69.2 ± 4.4 µM; HEK293: IC50=65.9 ± 5.4 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33550 GGVKRFKKFFRKLKKSV 17 B1-GG-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=10.5 ± 0.9 µM); MCF-7/Taxol (IC50=11.5 ± 0.8 µM); K562/ADM (IC50=9.2 ± 1.1 µM); K562 (IC50=9.7 ± 0.7 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=67.6 ± 5.4 µM; HEK293: IC50=63.3 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33551 GGVKRFKKFFRKLKKSV 17 B1-GG-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=10.2 ± 1.1 µM); K562/ADM (IC50=10.5 ± 1.3 µM); MCF-7/Taxol (IC50=10.7 ± 1.0 µM); MCF-7 (IC50=9.6 ± 0.4 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=67.6 ± 5.4 µM; HEK293: IC50=63.3 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33552 GGVKRFKKFFRKLKKSV 17 B1-GG-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=3.5 ± 0.1 µM); K562 (IC50=3.8 ± 0.2 µM); MCF-7/Taxol (IC50=4.3 ± 0.2 µM); K562/ADM (IC50=4.6 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=67.6 ± 5.4 µM; HEK293: IC50=63.3 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33553 GGVKRFKKFFRKLKKSV 17 B1-GG-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.7 ± 0.3 µM); MCF-7/Taxol (IC50=3.2 ± 0.2 µM); K562/ADM (IC50=3.4 ± 0.1 µM); K562 (IC50=3.4 ± 0.3 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=67.6 ± 5.4 µM; HEK293: IC50=63.3 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33554 GGVKRFKKFFRKLKKSV 17 B1-GG-C18 B6D434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=2.5 ± 0.2 µM); MCF-7/Taxol (IC50=3.2 ± 0.1 µM); K562/ADM (IC50=3.3 ± 0.3 µM); K562 (IC50=3.4 ± 0.1 µM) "Human erythrocytes: <20% Hemolysis =160 µM" Linear CH3(CH2)16CO, Octadecanoic acid Amidation L GES-1: IC50=67.6 ± 5.4 µM; HEK293: IC50=63.3 ± 5.0 µM Not available 26083110 Org Biomol Chem. 2015 Jul 28;13(28):7673-80. Deng X, Qiu Q, Ma K, Wang X, Huang W, Qian H. Aliphatic acid-conjugated antimicrobial peptides--potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP33555 inlkalaalakkil 14 Inverso Mastoparan P01514 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=10 µM); U-373MG (LD50=45.92 μM) Not available Linear Free Amidation D Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33556 LIKKALAALAKLNI 14 Retro Mastoparan Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50=95.46 μM) Not available Linear Free Amidation L Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33557 likkalaalaklni 14 Retro-inverso Mastoparan Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50=80.40 μM) Not available Linear Free Amidation D Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33558 INLKKLAKLXKKIL 14 Mitoparan, Mastoparan [A5,8K;A10Aib] P01514 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50=9.44 μM) Not available Linear Free Amidation X=AIB (Aminoisobutyric acid) L Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33559 inlkklaklXkkil 14 Inverso Mitoparan Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50=13.95 μM) Not available Linear Free Amidation X=AIB (Aminoisobutyric acid) Mix Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33560 LIKKXLKALKKLNI 14 Retro Mitoparan Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50>100 μM) Not available Linear Free Amidation X=AIB (Aminoisobutyric acid) L Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33561 likkXlkalkklni 14 Retro-inverso Mitoparan Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-373MG (LD50=67.15 μM) Not available Linear Free Amidation X=AIB (Aminoisobutyric acid) Mix Not available Not available 22148546 Bioconjug Chem. 2012 Jan 18;23(1):47-56. Jones S, Howl J. Enantiomer-specific bioactivities of peptidomimetic analogues of mastoparan and mitoparan: characterization of inverso mastoparan as a highly efficient cell penetrating peptide DRAMP33562 GNNKPVYRPQPRPPHPRL 18 Apidaecin-1B [R4K, I8R] P35581 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (30% Cytotoxicity=10 µM); MDA-MB-231 (Not active up to 10 µM) Not available Linear Free Free L Not available Not available 31209863 Biotechnol Bioeng. 2019 Oct;116(10):2439-2450. Lai PK, Tresnak DT, Hackel BJ. Identification and elucidation of proline-rich antimicrobial peptides with enhanced potency and delivery DRAMP33563 VDKGSYRPRPTPPKPIYNRN 20 Pyrrhocoricin [L7R, R14K] P37362 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A431 (<10% Cytotoxicity=10 µM); MDA-MB-231 (Not active up to 10 µM) Not available Linear Free Free L Not available Not available 31209863 Biotechnol Bioeng. 2019 Oct;116(10):2439-2450. Lai PK, Tresnak DT, Hackel BJ. Identification and elucidation of proline-rich antimicrobial peptides with enhanced potency and delivery DRAMP33564 VDKPPYLPRPRPPRXIYNX 19 Oncocin Onc72 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 600 µg/ml); HepG2 (Not active up to 600 µg/ml); SH-SY5Y (Not active up to 600 µg/ml) Not available Linear Free Amidation X=Orn L HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33565 VRKPPYLPRPRWPRXIYNX 19 Oncocin Onc72 analog a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SH-SY5Y (<5% Cytotoxicity=600 µg/ml); HeLa (25% Cytotoxicity=600 µg/ml); HepG2 (Not active up to 600 µg/ml) Not available Linear Free Amidation X=Orn L HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33566 VXKPPYLPRPRWPRXIYNX 19 Oncocin Onc72 analog b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SH-SY5Y (10% Cytotoxicity=600 µg/ml); HeLa (20-25% Cytotoxicity=600 µg/ml); HepG2 (Not active up to 600 µg/ml) Not available Linear Free Amidation X=Orn L HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33567 VrKPPYLPRPRWPRXIYNX 19 Oncocin Onc72 analog c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (<5% Cytotoxicity=600 µg/ml); HeLa (20-25% Cytotoxicity=600 µg/ml); SH-SY5Y (Not active up to 600 µg/ml) Not available Linear Free Amidation r=D-Arg; X=Orn Mix HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33568 VDKPPYLPRPRPxRxXYNX 19 Oncocin Onc110 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SH-SY5Y (<5% Cytotoxicity=600 µg/ml); HeLa (20-25% Cytotoxicity=600 µg/ml); HepG2 (Not active up to 600 µg/ml) Not available Linear Free Amidation x=trans-4-hydroxyproline; X(16)=tert-Leu; X(19)=Orn Mix HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33569 VRKPPYLPRPRWxRxjYNX 19 Oncocin Onc110 analog a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (<10% Cytotoxicity=600 µg/ml); HeLa (10-20% Cytotoxicity=600 µg/ml); SH-SY5Y (Not active up to 600 µg/ml) Not available Linear Free Amidation x=trans-4-hydroxyproline; X(16)=tert-Leu; X(19)=Orn Mix HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33570 VXKPPYLPRPRWxRxjYNX 19 Oncocin Onc110 analog b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (<5% Cytotoxicity=600 µg/ml); SH-SY5Y (10% Cytotoxicity=600 µg/ml); HeLa (10-20% Cytotoxicity=600 µg/ml) Not available Linear Free Amidation x=trans-4-hydroxyproline; X(16)=tert-Leu; X(2/19)=Orn Mix HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33571 VrKPPYLPRPRWxRxjYNX 19 Oncocin Onc110 analog c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (10-20% Cytotoxicity=600 µg/ml); SH-SY5Y (5% Cytotoxicity=600 µg/ml); HepG2 (Not active up to 600 µg/ml) Not available Linear Free Amidation r=D-Arg; x=trans-4-hydroxyproline; X(16)=tert-Leu; X(19)=Orn Mix HEK293: Not active up to 600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33572 VRKPPYLPRPRWPRrIYNr 19 Oncocin Onc112 analog a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (<5% Cytotoxicity=600 µg/ml); SH-SY5Y (10% Cytotoxicity=600 µg/ml); HeLa (50-60% Cytotoxicity=600 µg/ml) Not available Linear Free Amidation r=D-Arg Mix HEK293: 50-60% Cytotoxicity=600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33573 VXKPPYLPRPRWPRrIYNr 19 Oncocin Onc112 analog b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SH-SY5Y (<10% Cytotoxicity=600 µg/ml); HepG2 (10% Cytotoxicity=600 µg/ml); HeLa (40% Cytotoxicity=601 µg/ml) Not available Linear Free Amidation r=D-Arg; X=Orn Mix HEK293: 50-60% Cytotoxicity=600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33574 VrKPPYLPRPRWPRrIYNr 19 Oncocin Onc112 analog c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (<10% Cytotoxicity=600 µg/ml); SH-SY5Y (10% Cytotoxicity=600 µg/ml); HeLa (50-60% Cytotoxicity=600 µg/ml) Not available Linear Free Amidation r=D-Arg Mix HEK293: 50-60% Cytotoxicity=600 µg/ml Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP33575 KIVPAMICAVTKKC 14 C14C3lexin, Ranalexin (7-20) C14 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=12 µg/ml); LNCaP C4-2 (IC50=16 µg/ml); HepG2 (IC50=18 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)12CO, Myristic acid Free L CHO-K1: IC50=17 µg/ml; PBMC: IC50=15 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33576 KIVPAMICAVTKKC 14 C14C3lexin, Ranalexin (7-20) C14 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=13 µg/ml); MEC-7 (IC50=13 µg/ml); HepG2 (IC50=15 µg/ml); HeLa (IC50=22 µg/ml) Not available Cyclic CH3(CH2)12CO, Myristic acid Free L CHO-K1: IC50=17 µg/ml; PBMC: IC50=15 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33577 KIVPAMICAVTKKC 14 C14C3lexin, Ranalexin (7-20) C14 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=10 µg/ml); LNCaP C4-2 (IC50=15 µg/ml); HepG2 (IC50=19 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)12CO, Myristic acid Free L CHO-K1: IC50=17 µg/ml; PBMC: IC50=15 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33578 KIVPAMICAVTKKC 14 C14C3lexin, Ranalexin (7-20) C14 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=17 µg/ml); LNCaP C4-2 (IC50=20 µg/ml); HeLa (IC50=30 µg/ml); HepG2 (IC50=32 µg/ml) Not available Cyclic CH3(CH2)12CO, Myristic acid Free L CHO-K1: IC50=17 µg/ml; PBMC: IC50=15 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33579 KIVPAMICAVTKKC 14 C14C3lexin, Ranalexin (7-20) C14 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=35 µg/ml); MEC-7 (IC50=35 µg/ml); HeLa (IC50=36 µg/ml); HepG2 (IC50=48 µg/ml) Not available Cyclic CH3(CH2)12CO, Myristic acid Free L CHO-K1: IC50=17 µg/ml; PBMC: IC50=15 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33580 KIVPAMICAVTKKC 14 C13C3lexin, Ranalexin (7-20) C13 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=12 µg/ml); LNCaP C4-2 (IC50=16 µg/ml); HepG2 (IC50=18 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)11CO, Tridecanoic acid Free L CHO-K1: IC50=16 µg/ml; PBMC: IC50=16 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33581 KIVPAMICAVTKKC 14 C13C3lexin, Ranalexin (7-20) C13 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=13 µg/ml); MEC-7 (IC50=13 µg/ml); HepG2 (IC50=15 µg/ml); HeLa (IC50=22 µg/ml) Not available Cyclic CH3(CH2)11CO, Tridecanoic acid Free L CHO-K1: IC50=16 µg/ml; PBMC: IC50=16 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33582 KIVPAMICAVTKKC 14 C13C3lexin, Ranalexin (7-20) C13 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=10 µg/ml); LNCaP C4-2 (IC50=15 µg/ml); HepG2 (IC50=19 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)11CO, Tridecanoic acid Free L CHO-K1: IC50=16 µg/ml; PBMC: IC50=16 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33583 KIVPAMICAVTKKC 14 C13C3lexin, Ranalexin (7-20) C13 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=17 µg/ml); LNCaP C4-2 (IC50=20 µg/ml); HeLa (IC50=30 µg/ml); HepG2 (IC50=32 µg/ml) Not available Cyclic CH3(CH2)11CO, Tridecanoic acid Free L CHO-K1: IC50=16 µg/ml; PBMC: IC50=16 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33584 KIVPAMICAVTKKC 14 C13C3lexin, Ranalexin (7-20) C13 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=35 µg/ml); MEC-7 (IC50=35 µg/ml); HeLa (IC50=36 µg/ml); HepG2 (IC50=48 µg/ml) Not available Cyclic CH3(CH2)11CO, Tridecanoic acid Free L CHO-K1: IC50=16 µg/ml; PBMC: IC50=16 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33585 KIVPAMICAVTKKC 14 C12C3lexin, Ranalexin (7-20) C12 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=12 µg/ml); LNCaP C4-2 (IC50=16 µg/ml); HepG2 (IC50=18 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)10CO, Dodecanoic acid Free L CHO-K1: IC50=23 µg/ml; PBMC: IC50=20 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33586 KIVPAMICAVTKKC 14 C12C3lexin, Ranalexin (7-20) C12 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=13 µg/ml); MEC-7 (IC50=13 µg/ml); HepG2 (IC50=15 µg/ml); HeLa (IC50=22 µg/ml) Not available Cyclic CH3(CH2)10CO, Dodecanoic acid Free L CHO-K1: IC50=23 µg/ml; PBMC: IC50=20 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33587 KIVPAMICAVTKKC 14 C12C3lexin, Ranalexin (7-20) C12 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=10 µg/ml); LNCaP C4-2 (IC50=15 µg/ml); HepG2 (IC50=19 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)10CO, Dodecanoic acid Free L CHO-K1: IC50=23 µg/ml; PBMC: IC50=20 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33588 KIVPAMICAVTKKC 14 C12C3lexin, Ranalexin (7-20) C12 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=17 µg/ml); LNCaP C4-2 (IC50=20 µg/ml); HeLa (IC50=30 µg/ml); HepG2 (IC50=32 µg/ml) Not available Cyclic CH3(CH2)10CO, Dodecanoic acid Free L CHO-K1: IC50=23 µg/ml; PBMC: IC50=20 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33589 KIVPAMICAVTKKC 14 C12C3lexin, Ranalexin (7-20) C12 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=35 µg/ml); MEC-7 (IC50=35 µg/ml); HeLa (IC50=36 µg/ml); HepG2 (IC50=48 µg/ml) Not available Cyclic CH3(CH2)10CO, Dodecanoic acid Free L CHO-K1: IC50=23 µg/ml; PBMC: IC50=20 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33590 KIVPAMICAVTKKC 14 C11C3lexin, Ranalexin (7-20) C11 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=12 µg/ml); LNCaP C4-2 (IC50=16 µg/ml); HepG2 (IC50=18 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)9CO, Undecanoic acid Free L CHO-K1: IC50=25 µg/ml; PBMC: IC50=22 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33591 KIVPAMICAVTKKC 14 C11C3lexin, Ranalexin (7-20) C11 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=13 µg/ml); MEC-7 (IC50=13 µg/ml); HepG2 (IC50=15 µg/ml); HeLa (IC50=22 µg/ml) Not available Cyclic CH3(CH2)9CO, Undecanoic acid Free L CHO-K1: IC50=25 µg/ml; PBMC: IC50=22 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33592 KIVPAMICAVTKKC 14 C11C3lexin, Ranalexin (7-20) C11 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=10 µg/ml); LNCaP C4-2 (IC50=15 µg/ml); HepG2 (IC50=19 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)9CO, Undecanoic acid Free L CHO-K1: IC50=25 µg/ml; PBMC: IC50=22 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33593 KIVPAMICAVTKKC 14 C11C3lexin, Ranalexin (7-20) C11 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=17 µg/ml); LNCaP C4-2 (IC50=20 µg/ml); HeLa (IC50=30 µg/ml); HepG2 (IC50=32 µg/ml) Not available Cyclic CH3(CH2)9CO, Undecanoic acid Free L CHO-K1: IC50=25 µg/ml; PBMC: IC50=22 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33594 KIVPAMICAVTKKC 14 C11C3lexin, Ranalexin (7-20) C11 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=35 µg/ml); MEC-7 (IC50=35 µg/ml); HeLa (IC50=36 µg/ml); HepG2 (IC50=48 µg/ml) Not available Cyclic CH3(CH2)9CO, Undecanoic acid Free L CHO-K1: IC50=25 µg/ml; PBMC: IC50=22 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33595 KIVPAMICAVTKKC 14 C10C3lexin, Ranalexin (7-20) C10 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=12 µg/ml); LNCaP C4-2 (IC50=16 µg/ml); HepG2 (IC50=18 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)8CO, Decanoic acid Free L CHO-K1: IC50=40 µg/ml; PBMC: IC50=108.1 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33596 KIVPAMICAVTKKC 14 C10C3lexin, Ranalexin (7-20) C10 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=13 µg/ml); MEC-7 (IC50=13 µg/ml); HepG2 (IC50=15 µg/ml); HeLa (IC50=22 µg/ml) Not available Cyclic CH3(CH2)8CO, Decanoic acid Free L CHO-K1: IC50=40 µg/ml; PBMC: IC50=108.1 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33597 KIVPAMICAVTKKC 14 C10C3lexin, Ranalexin (7-20) C10 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=10 µg/ml); LNCaP C4-2 (IC50=15 µg/ml); HepG2 (IC50=19 µg/ml); HeLa (IC50=30 µg/ml) Not available Cyclic CH3(CH2)8CO, Decanoic acid Free L CHO-K1: IC50=40 µg/ml; PBMC: IC50=108.1 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33598 KIVPAMICAVTKKC 14 C10C3lexin, Ranalexin (7-20) C10 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MEC-7 (IC50=17 µg/ml); LNCaP C4-2 (IC50=20 µg/ml); HeLa (IC50=30 µg/ml); HepG2 (IC50=32 µg/ml) Not available Cyclic CH3(CH2)8CO, Decanoic acid Free L CHO-K1: IC50=40 µg/ml; PBMC: IC50=108.1 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33599 KIVPAMICAVTKKC 14 C10C3lexin, Ranalexin (7-20) C10 P39084 Not found Synthetic (Derived from Ranalexin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: LNCaP C4-2 (IC50=35 µg/ml); MEC-7 (IC50=35 µg/ml); HeLa (IC50=36 µg/ml); HepG2 (IC50=48 µg/ml) Not available Cyclic CH3(CH2)8CO, Decanoic acid Free L CHO-K1: IC50=40 µg/ml; PBMC: IC50=108.1 µg/ml Not available 29649587 Int J Antimicrob Agents. 2018 Jul;52(1):52-62. Domhan C, Uhl P, Meinhardt A, Zimmermann S, Kleist C, Lindner T, Leotta K, Mier W, Wink M. A novel tool against multiresistant bacterial pathogens: lipopeptide modification of the natural antimicrobial peptide ranalexin for enhanced antimicrobial activity and improved pharmacokinetics DRAMP33600 GLLKKLLKKLLKKL 14 G(LLKK)3L-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (>80% Killing=50 µM); HeLa (70% Killing=50 µM) Human erythrocytes: HC50=30 µM Linear Free Amidation L Human keratinocytes HaCat: >90% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33601 GXXKKXXKKXXKKX 14 G(ZZKK)3Z-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (>80% Killing=50 µM); HeLa (60% Killing=50 µM) Human erythrocytes: HC50=30 µM Linear Free Amidation X=Norleucine L Human keratinocytes HaCat: 30% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33602 GVVKKVVKKVVKKV 14 G(VVKK)3V-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (<10% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: Not active up to 250 µM Linear Free Amidation L Human keratinocytes HaCat: <30% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33603 GIIXXIIXXIIXXI 14 G(IIOO)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50>250 µM Linear Free Amidation X=Orn L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33604 GIIXXIIXXIIXXI 14 G(IIOO)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50>250 µM Linear Free Amidation X=Orn L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33605 GIIXXIIXXIIXXI 14 G(IIOO)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50>250 µM Linear Free Amidation X=Orn L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33606 GIIXXIIXXIIXXI 14 G(II66)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33607 GIIXXIIXXIIXXI 14 G(II66)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33608 GIIXXIIXXIIXXI 14 G(II66)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dab ((S)-2,4-diaminobutyric acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33609 GIIXXIIXXIIXXI 14 G(II55)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33610 GIIXXIIXXIIXXI 14 G(II55)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33611 GIIXXIIXXIIXXI 14 G(II55)3I-NH2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=50 µM); HL-60 (>80% Killing=50 µM) Human erythrocytes: HC50=200 µM Linear Free Amidation X=Dap ((S)-2,3-diaminopropionic acid) L Human keratinocytes HaCat: <5% Killing=40 µM Not available Not available Amino acid side chains affect the bioactivity of designed short peptide amphiphiles DRAMP33612 AEEASKKAEEASKKAEEASKKAEEASKKAEEASKKXK 37 AAS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=2.38±0.9 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33613 VEEVSKKVEEVSKKVEEVSKKVEEVSKKVEEVSKKXK 37 VVS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=74.5±6.8 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33614 FEEFSKKFEEFSKKFEEFSKKFEEFSKKFEEFSKKXK 37 FFS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33615 YEEYSKKYEEYSKKYEEYSKKYEEYSKKYEEYSKKXK 37 YYS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=19.8±1.6 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33616 LEELSKKLEELSKKLEELSKKLEELSKKLEELSKKXK 37 LLS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=4.04±0.4 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33617 IEEISKKIEEISKKIEEISKKIEEISKKIEEISKKXK 37 IIS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=88.8±28 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33618 IEEIYKKIEEIYKKIEEIYKKIEEIYKKIEEIYKKXK 37 IIY Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33619 IEEIWKKIEEIWKKIEEIWKKIEEIWKKIEEIWKKXK 37 IIW Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33620 IEEIHKKIEEIHKKIEEIHKKIEEIHKKIEEIHKKXK 37 IIH Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33621 IEEIQKKIEEIQKKIEEIQKKIEEIQKKIEEIQKKXK 37 IIQ Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33622 IEEIKKKIEEIKKKIEEIKKKIEEIKKKIEEIKKKXK 37 IIK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50=4.54±0.6 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33623 IEEIEKKIEEIEKKIEEIEKKIEEIEKKIEEIEKKXK 37 IIE Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Huh-7 (CC50>100 µM ) Not available Linear Acetylation CH3(CH2)14CONH2, Hexadecanamide X= β-Ala L Not available Not available 30192544 J Med Chem. 2018 Oct 11;61(19):8734-8745. Wang C, Zhao L, Xia S, Zhang T, Cao R, Liang G, Li Y, Meng G, Wang W, Shi W, Zhong W, Jiang S, Liu K. De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery DRAMP33624 FLWIKLGKLAGAVLKLILGLKKVV 24 Helical1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=4.4 ± 1.3 µM ); A549 (EC50=8.3 ± 2.0 µM) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33625 GLWAIAVKAGKVILKLIVFIWIRV 24 Helical2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM ); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33626 GLLDIAGGNAETLAGHAV 18 Helical3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM ); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33627 GLFDVIGSQAGGAAPHFLG 19 Helical4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33628 KWVKKVHNWLRRWIKVFEALFG 22 AmphiArc1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=18.4 ± 0.7 µM); MCF-7 (EC50=7.0 ± 0.5 µM) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33629 KIFKKFKTIIKKVWRIFGRF 20 AmphiArc2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=5.7 ± 0.7 µM); A549 (EC50=9.3 ± 1.5 µM) Human erythrocytes: HC50=16 ± 2 µM Linear Free Amidation L HDMEC: EC50=3.3 ± 0.2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33630 AFRHSVKEELNYIRRRLERFPNRL 24 AmphiArc3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM ); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33631 RIENGLRKRLQSIYRHLEE 19 AmphiArc4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM ); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33632 KWVRIWIKVLRGLFVWVWFF 20 Gradient1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33633 AWLKRIKKFLKALFWVWVW 19 Gradient2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=19.0 ± 1.8 µM); A549 (EC50>50 µM) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33634 KVVDNFENILII 12 Gradient3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33635 RVNAAIPNIIV 11 Gradient4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>50 µM); MCF-7 (EC50>50 µM ) Not available Linear Free Amidation L Not available Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33636 RVFKKFHPIYHRVWRLWGHL 20 AmphiArc2 Off1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=27.4 ± 0.5 µM); A549 (EC50=49 ± 2 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=56 ± 7 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33637 HIIKKIRTWYRKAWHVLGKV 20 AmphiArc2 Off2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=10 ± 2 µM); A549 (EC50=17.0 ± 0.6 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=32 ± 3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33638 KLYKKFRHILKKVWHYVGKI 20 AmphiArc2 Off3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=10 ± 1 µM); A549 (EC50=14 ± 3 µM) Human erythrocytes: HC50=29 ± 3 µM Linear Free Free L HDMEC: EC50=10 ± 3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33639 KYIRHLKTWFKKVFKLIGEV 20 AmphiArc2 Off4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11 ± 2 µM); A549 (EC50=15.0 ± 0.1 µM) Human erythrocytes: HC50=20 ± 3 µM Linear Free Free L HDMEC: EC50=7.1 ± 0.1 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33640 KIFKKFKDFLKKIFQYLGKV 20 AmphiArc2 Off5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=12.4 ± 0.4 µM); A549 (EC50=17.4 ± 0.1 µM) Human erythrocytes: HC50=15 ± 2 µM Linear Free Free L HDMEC: EC50=10.1 ± 0.2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33641 HIFKKVKTYWKKLFRILGRF 20 AmphiArc2 Off6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=12 ± 3 µM); A549 (EC50=18 ± 2 µM) Human erythrocytes: HC50=16 ± 2 µM Linear Free Free L HDMEC: EC50=5.0 ± 0.7 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33642 RLIKRLKTFVRKTWKWVGHF 20 AmphiArc2 Off7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=39 ± 3 µM); A549 (EC50=52 ± 2 µM) Human erythrocytes: HC50=95 ± 7 µM Linear Free Free L HDMEC: EC50=12 ± 3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33643 RFLKHFKTVYKRYWKVLGRL 20 AmphiArc2 Off8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11.9 ± 0.1 µM); A549 (EC50=17 ± 4 µM) Human erythrocytes: HC50=144 ± 4 µM Linear Free Free L HDMEC: EC50=14.3 ± 0.2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33644 KLIHRLKTVFKKVWHFLGHL 20 AmphiArc2 Off9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=18.9 ± 0.2 µM); A549 (EC50=22 ± 4 µM) Human erythrocytes: HC50=41 ± 3 µM Linear Free Free L HDMEC: EC50=22 ± 3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33645 HRIRQLKTTIKKFWEIWPKI 20 AmphiArc2 Off10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=56 ± 5 µM); A549 (EC50=83 ± 11 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=58.1 ± 0.3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33646 QVFKKFRPFYRRPWELFGKL 20 AmphiArc2 Off2.1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=91 ± 2 µM); A549 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=173 ± 1 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33647 QIIKKIRTWYRKAWHVLGKV 20 AmphiArc2 Off2.2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11.6 ± 0.8 µM); A549 (EC50=20 ± 1 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=42 ± 7 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33648 TLYKKFRHFLKKPWHVVGKI 20 AmphiArc2 Off2.3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=65 ± 3 µM); A549 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=167 ± 13 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33649 HYIRHLKTWFHKPFKLIGKV 20 AmphiArc2 Off2.4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 µM); MCF-7 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=169 ± 28 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33650 KIFKKFKDWFKKAFHVLGKV 20 AmphiArc2 Off2.5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=10.4 ± 0.8 µM); A549 (EC50=14.8 ± 0.7 µM) Human erythrocytes: HC50>100 µM Linear Free Free L HDMEC: EC50=22 ± 1 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33651 QIFKKVKTWYKKAFQILGRL 20 AmphiArc2 Off2.6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=12.4 ± 0.1 µM); MCF-7 (EC50=9.3 ± 0.2 µM) Human erythrocytes: HC50>100 µM Linear Free Free L HDMEC: EC50=21 ± 2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33652 RLIKRIKTWYRKAWKVVGKF 20 AmphiArc2 Off2.7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11.2 ± 0.7 µM); A549 (EC50=15 ± 1 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=23 ± 5 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33653 RFLKHLHTYYERAWHVIGHL 20 AmphiArc2 Off2.8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 µM); MCF-7 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=2 ± 2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33654 HLIHRLHTYWHKPWHYLGKL 20 AmphiArc2 Off2.9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50>100 µM); MCF-7 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=135 ± 2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33655 QRIRQLHTWIKKAWHIWPKI 20 AmphiArc2 Off2.10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=28.6 ± 0.1 µM); A549 (EC50=40 ± 2 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=39.7 ± 0.3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33656 QVVKKIRTWYHKAWHVLGKV 20 AmphiArc2 Off2.2.1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=76 ± 15 µM); A549 (EC50>100 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=96 ± 7 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33657 QLIHKIRTWYRKAWHVLGKV 20 AmphiArc2 Off2.2.2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=13 ± 1 µM); A549 (EC50=20 ± 2 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=28 ± 3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33658 HLLKKWRTWLRKAWHIVGKV 20 AmphiArc2 Off2.2.3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=7 ± 1 µM); A549 (EC50=9 ± 1 µM) Human erythrocytes: HC50=59 ± 6 µM Linear Free Free L HDMEC: EC50=6.1 ± 0.5 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33659 QVLKKVRTWYRKAFHVIGKV 20 AmphiArc2 Off2.2.4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=68 ± 5 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50>100 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33660 QLLKKVRTWYRKAWHLYGKV 20 AmphiArc2 Off2.2.5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=16 ± 2 µM); A549 (EC50=29.3 ± 0.9 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=27.2 ± 0.5 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33661 QLIKKLRTWYRKAWHVLGKL 20 AmphiArc2 Off2.2.6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=10.6 ± 0.8 µM); MCF-7 (EC50=6.5 ± 0.2 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=9 ± 1 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33662 QIIKKVRTWIKKAWHLIGKI 20 AmphiArc2 Off2.2.7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (EC50=12 ± 2 µM); MCF-7 (EC50=8 ± 1 µM) Human erythrocytes: HC50>100 µM Linear Free Free L HDMEC: EC50=17 ± 1 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33663 QYLRRVRTWLRRAWHILGKV 20 AmphiArc2 Off2.2.8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=11.0 ± 0.2 µM); A549 (EC50=16.5 ± 0.2 µM) Human erythrocytes: HC50=21 ± 1 µM Linear Free Free L HDMEC: EC50=10.3 ± 0.3 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33664 QLLKKIRTWYRKAWHVYGKV 20 AmphiArc2 Off2.2.9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=13 ± 1 µM); A549 (EC50=28 ± 3 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=21 ± 2 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33665 QIYKKYRTWYRKAWKVLGKV 20 AmphiArc2 Off2.2.10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (EC50=16.9 ± 0.8 µM); A549 (EC50=36 ± 7 µM) Human erythrocytes: HC50>200 µM Linear Free Free L HDMEC: EC50=71 ± 12 µM Not available 31375699 Sci Rep. 2019 Aug 2;9(1):11282. Gabernet G, Gautschi D, Müller AT, Neuhaus CS, Armbrecht L, Dittrich PS, Hiss JA, Schneider G. In silico design and optimization of selective membranolytic anticancer peptides DRAMP33666 CXGRCLLIIKLAKLAKKLAKLAK 23 CDAK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available AMPs containing CisoDGRC selectively kill CD13-/αvβ3+ breast cancer cells by inducing apoptosis and inhibiting proliferation. Furthermore, the vivo experiments showed that AMPs containing CisoDGRC could significantly inhibited CD13-/αvβ3+ tumor progression and angiogenesis. Tumor cells: MCF-7 (IC50=190 µg/ml); MDA-MB-231 (IC50=212 µg/ml) Not available Cyclic Free Free X=iso-Asp L HUVEC: IC50=861 µg/ml; HFF: IC50=912 µg/ml CD13-/αvβ3+ tumor cells 23326440 PLoS One. 2013;8(1):e53491. Hou L, Zhao X, Wang P, Ning Q, Meng M, Liu C. Antitumor Activity of Antimicrobial Peptides Containing CisoDGRC in CD13 Negative Breast Cancer Cells DRAMP33667 RFRLPFRRIHPPPFVRIHPPPFYRRFL 27 ChBac3.4-1-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (IC50=4.5 ± 1.6 μM); K562 (IC50=8.4 ± 1.1 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50=12.1 ± 0.8 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33668 RFRLPFRRIHPPPFVRIHPPPFYRRFL 27 ChBac3.4-1-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=16.5 ± 1.3 μM); U-937 (IC50=9.8 ± 0.5 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50=12.1 ± 0.8 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33669 RFRLPFRRIHPPPFVRIHPPPFYRRFL 27 ChBac3.4-1-COOH P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (IC50=4.5 ± 1.6 μM); K562 (IC50=8.4 ± 1.1 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Free L Human PBMC: IC50=33.7 ± 3.2 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33670 RFRLPFRRIHPPPFVRIHPPPFYRRFL 27 ChBac3.4-1-COOH P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=16.5 ± 1.3 μM); U-937 (IC50=9.8 ± 0.5 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Free L Human PBMC: IC50=33.7 ± 3.2 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33671 RFRRFRLPFRRIHPPPFVRIHPPPFYRRFL 30 RFR-ChBac3.4-1-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=20.0 ± 3.4 μM); U-937 (IC50=3.2 ± 0.4 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50=18.3 ± 4.1 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33672 RFRLPFRRPWPIRIHPPPFYPWPFRRFL 28 ChBac3.4-2-COOH P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=13.7 ± 2.3 μM); U-937 (IC50=4.1 ± 0.3 μM) Human erythrocytes: 25 ± 2% Hemolysis=64 µM Linear Free Free L Human PBMC: IC50=20.2 ± 4.5 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33673 RFRLPFRRPPIRIPPPFYPPFRRFL 25 ChBac3.4 (H-) P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (IC50=11.5 ± 0.5 μM); K562 (IC50=25.0 ± 3.5 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50=34.7 ± 7.3 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33674 RIHPPPFYPPFRRFL 15 ChBac3.4 (12-26) P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (IC50=17.0 ± 1.1 μM); K562 (IC50=39.4 ± 2.3 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50=43.3 ± 7.7 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33675 RFRLPFRRPPIRIHPPPFY 19 ChBac3.4 (1-19)-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=28.0 ± 6.5 μM); U-937 (IC50>64 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50>64 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33676 RFRLPFRRPPIRIH 14 ChBac3.4 (1-14)-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=33.6 ± 4.1 μM); U-937 (IC50>64 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50>64 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33677 RFRRFRLPFRRPPIRIH 17 RFR-ChBac3.4 (1-14)-NH2 P85170 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=39.4 ± 6.6 μM); U-937 (IC50>64 μM) Human erythrocytes: <5% Hemolysis=64 µM Linear Free Amidation L Human PBMC: IC50>64 µM Not available 33194795 Front Cell Infect Microbiol. 2020 Oct 19;10:552905. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs DRAMP33678 FTILKKLKSFIK 12 Modifed Coco1 I0YNC0 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM ) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33679 KLVKKLLKKYITF 13 Modifed Coco2 I0Z3W2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50=200 μM ) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33680 LARFVLRILKYGFK 14 Modifed Coco3 I0YQ90 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50=12.5 μM); CaCo-2 (CC50=25 μM) Human erythrocytes: 10% Hemolysis=9.38 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33681 IPLLRKGKKIIWW 13 Modifed Opero1 A0A0L7KPW9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33682 GLKKVIKLLRPLL 13 Modifed Opero2 A0A0L7L9V8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50=50 μM) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33683 ILKPKLWKLTVVARKIIK 18 Modifed Opero3 A0A0L7LPN7 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50=200 μM) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33684 IVIKSLGKFLKNVGGFAG 18 Modifed Pyro1 O58222 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM) Human erythrocytes: <10% Hemolysis=50 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33685 FKLVWKLLKKLALKL 15 Modifed Aper1 Q9Y8Y1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: CaCo-2 (CC50=12.5 μM); A549 (CC50=25 μM) Human erythrocytes: 10% Hemolysis=5.96 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33686 ITKWLLNAIKKGFKL 15 Modifed Thermo1 B6YW36 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM) Human erythrocytes: 10% Hemolysis=21.9 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33687 IHKLVKLWLNLGKKF 15 Modifed Thermo2 B6YTI2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM) Human erythrocytes: 10% Hemolysis=39.3 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33688 LFSIIWKLNRKLIKA 15 Modifed Thermo3 B6YWQ6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (CC50>200 μM); CaCo-2 (CC50>200 μM) Human erythrocytes: 10% Hemolysis=37.3 µM Linear Free Free L Not available Not available 33063186 Amino Acids. 2020 Oct;52(10):1403-1412 Duque-Salazar G, Mendez-Otalvaro E, Ceballos-Arroyo AM, Orduz S. Design of antimicrobial and cytolytic peptides by computational analysis of bacterial, algal, and invertebrate proteomes DRAMP33689 KKK 3 L1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.9 ± 1.1 μg/mL) Human erythrocytes:HC50=90.0 ± 6.5 µg/ml Linear CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=5.2 ± 0.6 µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP33690 CKKKKC 6 C2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=17.9 ± 2.1 μg/mL) Human erythrocytes:HC50=30.6 ± 1.1 µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=26.9 ± 1.9 µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP33691 KRKK 4 L4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=3.0 ± 0.6 μg/mL) Human erythrocytes:HC50=79.8 ± 9.0 µg/ml Linear CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=4.3 ± 0.9 µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP33692 CKRKKC 6 C4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=27.5 ± 3.4 μg/mL) Human erythrocytes:HC50=122.4 ± 16.5 µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=33.8 ± 3.1 µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP33693 CRRKKC 6 C7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=20.9 ± 2.1 μg/mL) Human erythrocytes:HC50=92.0 ± 9.6 µg/ml Cyclic CH3(CH2)14CO, Palmitic acid Amidation L HaCat: IC50=21.3 ± 8.2 µg/ml Not available 33003569 Int J Mol Sci. 2020 Sep 29;21(19):7208. Neubauer D, Jaśkiewicz M, Sikorska E, Bauer SBM, Kapusta M, Narajczyk M, Kamysz W. Effect of Disulfide Cyclization of Ultrashort Cationic Lipopeptides on Antimicrobial Activity and Cytotoxicity DRAMP33694 FPVTWRWWKWWKGKFPVTWRWWKWWKG 27 Di-PuroA P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=32 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33695 RRRRWRWWRWWRR 13 TRPs R8 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50>250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33696 RKRWWRWWKWWKR 13 TRPs P1 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=32 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33697 RKrWWrWwkWWkR 13 TRPs dP1 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=125 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation r=D-Arg; w=D-Trp Mix NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33698 RWWKWW 6 TRPs R6 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50>250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33699 RWWKWWK 7 TRPs R7 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50>250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33700 WRWWKWW 7 TRPs W7 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33701 WrWwkWW 7 TRPs dW7 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=125 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation r=D-Arg; w=D-Trp Mix NIH 3T3: IC50>250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33702 WRWWKWWK 8 TRPs W8 P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50>250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33703 WWRWWKWW 8 TRPs WW P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=250 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation L NIH 3T3: IC50>250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33704 WWrWwkWW 8 TRPs dWW P33432 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Dual mechanism, with the disruption of the membrane integrity possibly being the main cause of cell death, but only after peptide translocation and binding to intracellular targets. Tumor cells: HeLa (IC50=125 μg/mL) Sheep erythrocytes: No hemolysis up tp 500 µg/ml Linear Free Amidation r=D-Arg; w=D-Trp Mix NIH 3T3: IC50=250 µg/ml Not available 33207639 Int J Mol Sci. 2020 Nov 16;21(22):8624. Shagaghi N, Clayton AHA, Aguilar MI, Lee TH, Palombo EA, Bhave M. Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells DRAMP33705 AFALIAGALYRIFHRR 16 LHH1 Q036I7 Not found Lactobacillus casei HZ1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C666-1 (IC50=18.27 μM ); MGC-803 (IC50=31.55 μM ); HCT 116 (IC50=40.83 μM ) Goat erythrocytes: HC50=187.2 µM Linear Free Free L Not available Not available 33175275 AMB Express. 2020 Nov 11;10(1):204. He JF, Jin DX, Luo XG, Zhang TC. LHH1, a novel antimicrobial peptide with anti-cancer cell activity identified from Lactobacillus casei HZ1 DRAMP33706 GARELRRLERELRRLEGGGGGGGKLAALKFKLLWLKLAC 39 cHLH-p53R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available (1) The positively charged peptide targets the negative surface of cancer cells via electrostatic attractions; (2) The peptide inserts into cell membranes and enters inside cells very efficaciously; (3) Once inside cells, the peptide induces toxicity through fusion and/or disruption of intracellular organelles; (4) The cell membrane is disrupted and the cells die. Tumor cells: MDA-MB-231 (CC50=15.9 ± 2.3 μM); MCF-7 (CC50=16.0 ± 0.5 μM); MM96L (CC50=5.4 ± 0.3 μM ); MDA-MB-435S (CC50=5.7 ± 0.4 μM ); K562 (CC50=8.2 ± 0.4 μM) Human erythrocytes: 50% Hemolysis>64 µM Cyclic CAA, Chloroacetic acid Free L HFF-1: CC50=11.9 ± 1.0 µM; MCF-10A: CC50=8.0 ± 0.8 µM; Human PBMC: CC50=48.9 ± 5.3 µM Not available 31390185 ACS Chem Biol. 2019 Sep 20;14(9):2071-2087. Philippe GJ, Gaspar D, Sheng C, Huang YH, Benfield AH, Condon ND, Weidmann J, Lawrence N, Löwer A, Castanho MARB, Craik DJ, Troeira Henriques S. Cell Membrane Composition Drives Selectivity and Toxicity of Designed Cyclic Helix-Loop-Helix Peptides with Cell Penetrating and Tumor Suppressor Properties DRAMP33707 GARELRRLERELRRLEKGGGGGGKLAALKFKLLWLKLAC 39 [G17K]cHLH-p53R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available (1) The positively charged peptide targets the negative surface of cancer cells via electrostatic attractions; (2) The peptide inserts into cell membranes and enters inside cells very efficaciously; (3) Once inside cells, the peptide induces toxicity through fusion and/or disruption of intracellular organelles; (4) The cell membrane is disrupted and the cells die. Tumor cells: MM96L (CC50=5.3 ± 0.5 μM ); MDA-MB-435S (CC50=7.1 ± 0.6 μM ) Human erythrocytes: 50% Hemolysis>64 µM Cyclic CAA, Chloroacetic acid Free L HFF-1: CC50=8.8 ± 1.2 µM; MCF-10A: CC50=25.7 ± 3.2 µM; Human PBMC: CC50=42.8 ± 7.0 µM Not available 31390185 ACS Chem Biol. 2019 Sep 20;14(9):2071-2087. Philippe GJ, Gaspar D, Sheng C, Huang YH, Benfield AH, Condon ND, Weidmann J, Lawrence N, Löwer A, Castanho MARB, Craik DJ, Troeira Henriques S. Cell Membrane Composition Drives Selectivity and Toxicity of Designed Cyclic Helix-Loop-Helix Peptides with Cell Penetrating and Tumor Suppressor Properties DRAMP33708 GARELRRLERELRRLEKGGGGGGKLAALTFEHYWAQLTSC 40 cHLH-pDI1-R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available (1) The positively charged peptide targets the negative surface of cancer cells via electrostatic attractions; (2) The peptide inserts into cell membranes and enters inside cells very efficaciously; (3) Once inside cells, the peptide induces toxicity through fusion and/or disruption of intracellular organelles; (4) The cell membrane is disrupted and the cells die. Tumor cells: K562 (CC50>64 μM); MCF-7 (CC50>64 μM); MDA-MB-435S (CC50>64 μM); MM96L (CC50>64 μM) Human erythrocytes: 50% Hemolysis>64 µM Cyclic CAA, Chloroacetic acid Free L HFF-1: CC50>64 µM; MCF-10A: CC50>64 µM; Human PBMC: CC50>64 µM Not available 31390185 ACS Chem Biol. 2019 Sep 20;14(9):2071-2087. Philippe GJ, Gaspar D, Sheng C, Huang YH, Benfield AH, Condon ND, Weidmann J, Lawrence N, Löwer A, Castanho MARB, Craik DJ, Troeira Henriques S. Cell Membrane Composition Drives Selectivity and Toxicity of Designed Cyclic Helix-Loop-Helix Peptides with Cell Penetrating and Tumor Suppressor Properties DRAMP33709 GARELRRLERELRRLEGGGGGGGKLAALKAKLLWLKLAC 39 [F30A]cHLH-p53-R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available (1) The positively charged peptide targets the negative surface of cancer cells via electrostatic attractions; (2) The peptide inserts into cell membranes and enters inside cells very efficaciously; (3) Once inside cells, the peptide induces toxicity through fusion and/or disruption of intracellular organelles; (4) The cell membrane is disrupted and the cells die. Tumor cells: K562 (CC50=36.7 ± 1.9 μM); MDA-MB-435S (CC50>32 μM); MCF-7 (CC50>64 μM); MDA-MB-231 (CC50>64 μM); MM96L (CC50>64 μM) Human erythrocytes: 50% Hemolysis>64 µM Cyclic CAA, Chloroacetic acid Free L HFF-1: CC50>64 µM; MCF-10A: CC50>64 µM; Human PBMC: CC50>64 µM Not available 31390185 ACS Chem Biol. 2019 Sep 20;14(9):2071-2087. Philippe GJ, Gaspar D, Sheng C, Huang YH, Benfield AH, Condon ND, Weidmann J, Lawrence N, Löwer A, Castanho MARB, Craik DJ, Troeira Henriques S. Cell Membrane Composition Drives Selectivity and Toxicity of Designed Cyclic Helix-Loop-Helix Peptides with Cell Penetrating and Tumor Suppressor Properties DRAMP33710 GLAKVMREVLGYERNSYKKFFLR 23 Ixosin [H3A] Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (8% Killing=16 µM) Not available Linear Free Amidation L HEK-293: Not active up to 16 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33711 KVMREVLGYERNSYKKFFLR 20 Ixosin (4-23) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (19% Killing=128 µM) Not available Linear Free Amidation L HEK-293: Not active up to 128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33712 GLHKVMRKVLGYLRNVYK 18 Ixosin [E8K,E13L,S16V], Ixosin-pch Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (24% Killing=1 µM) Not available Linear Free Amidation L HEK-293: 14% Killing=1 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33713 GLAKVMRKVLGYLRNVYK 18 Ixosin [H3A,E8K,E13L,S16V], Ixosin-pch-H3A Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (28% Killing=2-4 µM) Not available Linear Free Amidation L HEK-293: 23% Killing=2-4 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33714 KVMRKVLGYLRNVYK 15 Ixosin (4-18)[E8K,E13L,S16V], Ixosin-pch4–18 Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (19% Killing=2 µM) Not available Linear Free Amidation L HEK-293: 15% Killing=2 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33715 GLHKVMREVLGY 12 Ixosin (1-12) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (27% Killing=128 µM) Not available Linear Free Amidation L HEK-293: 3% Killing>128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33716 YERNSYKKFFLR 12 Ixosin (12-23) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (28% Killing=128 µM) Not available Linear Free Amidation L HEK-293: 10% Killing>128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33717 GLHKVMREVLGYERNSYK 18 Ixosin (1-18) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (13% Killing=128 µM) Not available Linear Free Amidation L HEK-293: 6% Killing>128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33718 KVMREVLGYERNSYK 15 Ixosin (4-18) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (3% Killing=128 µM) Not available Linear Free Amidation L HEK-293: 14% Killing>128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33719 REVLGYERNSYK 12 Ixosin (7-18) Q2LKX9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (15% Killing=128 µM) Not available Linear Free Amidation L HEK-293: 18% Killing>128 µM Not available 27622949 Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Libardo MD, Gorbatyuk VY, Angeles-Boza AM. Central Role of the Copper-Binding Motif in the Complex Mechanism of Action of Ixosin: Enhancing Oxidative Damage and Promoting Synergy with Ixosin B DRAMP33720 LKRIVQRIKDFLR 13 LL-37 (17-29) [F17L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=33.7 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=56.9 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33721 FKRIVQRILDFLR 13 LL-37 (17-29) [K25L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=3.9 μg/ml) Human erythrocytes: HC50=450 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=20.1 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33722 FXRIVQRILDFLR 13 LL-37 (17-29) [18SA-K] [K25L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=10.7 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation X=Sialic acid-Lys L DLF lung fibroblasts: IC50=24.3 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33723 FKRIVQRIRDFLR 13 LL-37 (17-29) [K25R] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=56 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33724 FKRIVQRIRDFLR 13 LL-37 (17-29) [K25R] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.5 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33725 FKRIVQRIRDFLR 13 LL-37 (17-29) [K25R]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=56 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=54.1 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33726 FKRIVQRIRDFLR 13 LL-37 (17-29) [K25R]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.5 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=54.1 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33727 FKRIVQKIKDFLR 13 LL-37 (17-29) [R23K] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=145.1 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33728 FKRIVQLIKDFLR 13 LL-37 (17-29) [R23L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=18.9 μg/ml) Human erythrocytes: HC50=114 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=23.5 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33729 FKRIVQLIKDFLR 13 LL-37 (17-29) [R23L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.9 μg/ml) Human erythrocytes: HC50=114 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=23.5 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33730 FKRIVQLIKDFLR 13 LL-37 (17-29) [R23L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=18.9 μg/ml) Human erythrocytes: HC50=227 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=22.5 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33731 FKRIVQLIKDFLR 13 LL-37 (17-29) [R23L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=13.9 μg/ml) Human erythrocytes: HC50=227 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=22.5 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33732 FKRIVQRIKDLLR 13 LL-37 (17-29) [F27L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=75 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33733 FKRIVQRIKDLLR 13 LL-37 (17-29) [F27L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=45.5 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33734 FKRIVQRIKDLLR 13 LL-37 (17-29) [F27L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=75 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33735 FKRIVQRIKDLLR 13 LL-37 (17-29) [F27L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=45.5 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: Not active up to 200 µg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33736 FKRIVQIIKKFLR 13 LL-37 (17-29) [R23I,D26K] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=20 μg/ml) Human erythrocytes: HC50=361 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=27 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33737 FKRIVQIIKKFLR 13 LL-37 (17-29) [R23I,D26K] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.9 μg/ml) Human erythrocytes: HC50=361 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=27 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33738 FKRIVQIIKKFLR 13 LL-37 (17-29) [R23I,D26K]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=20 μg/ml) Human erythrocytes: HC50=292 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=15.7 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33739 FKRIVQIIKKFLR 13 LL-37 (17-29) [R23I,D26K]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.9 μg/ml) Human erythrocytes: HC50=292 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=15.7 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33740 FKRIVQLLKKLLR 13 LL-37 (17-29) [R23L,I24L,D26K,F27L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.8 μg/ml) Human erythrocytes: HC50=411 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=23.7 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33741 FKRIVQLLKKLLR 13 LL-37 (17-29) [R23L,I24L,D26K,F27L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=9.8 μg/ml) Human erythrocytes: HC50=411 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=23.7 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33742 FKRIVQLLKKLLR 13 LL-37 (17-29) [R23L,I24L,D26K,F27L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=12.8 μg/ml) Human erythrocytes: HC50=185 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=17.3 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33743 FKRIVQLLKKLLR 13 LL-37 (17-29) [R23L,I24L,D26K,F27L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=9.8 μg/ml) Human erythrocytes: HC50=185 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=17.3 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33744 FKRILQRIKDFLR 13 LL-37 (17-29) [V21L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=19.2 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=76.8 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33745 FKRILQRIKDFLR 13 LL-37 (17-29) [V21L] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=29.2 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Free Amidation L DLF lung fibroblasts: IC50=76.8 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33746 FKRILQRIKDFLR 13 LL-37 (17-29) [V21L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=19.2 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=160.9 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33747 FKRILQRIKDFLR 13 LL-37 (17-29) [V21L]-Ac P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=29.2 μg/ml) Human erythrocytes: Not active up to 500 µg/ml Linear Acetylation Amidation L DLF lung fibroblasts: IC50=160.9 μg/ml Not available 32567085 J Pept Sci. 2020 Jul;26(7):e3254. Tzitzilis A, Boura-Theodorou A, Michail V, Papadopoulos S, Krikorian D, Lekka ME, Koukkou AI, Sakarellos-Daitsiotis M, Panou-Pomonis E. Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents DRAMP33748 GXFKKTFHKVSHAVKSGIHAGQRGCSALGF 30 CEN1 HC-Br D8WN02 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (50% Killing=100 mg/L) Not available Linear Free Free X=Br-Trp L Not available Not available 23237525 AMB Express. 2012 Dec 13;2(1):67. Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis DRAMP33749 GWFKKTFHKVSHAVKSGIHA 20 CEN1 HC (1–20) D8WN02 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (Weak active up to 125 mg/L) Not available Linear Free Free L Not available Not available 23237525 AMB Express. 2012 Dec 13;2(1):67. Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis DRAMP33750 GWFKKTFHKVSHAVKSGIHAGQRGSSALGF 30 CEN1 HC (Ser) D8WN02 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: THP-1 (Weak active up to 125 mg/L) Not available Linear Free Free L Not available Not available 23237525 AMB Express. 2012 Dec 13;2(1):67. Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis DRAMP33752 IKLXKEXKKXLKKVLKGXIKGXIAVAKMV 29 H-57, Hymenochirin-1B [P5K,D9K; S4,T7,N10-GlcNAc; A18,A22 S5] W8PRC4 Not found Synthetic (Derived from Hymenochirin-1B) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=1.10±0.31 μM); HCT 116 (IC50=1.65±0.28 μM); HepG2 (IC50=2.71±0.05 μM) Not available Linear Free Free X(4)=Ser-GlcNAc; X(7)=Thr-GlcNAc; X(10)=Asn-GlcNAc; X(18/22)=(S)-N-Fmoc-2-(4′-pentenyl)alanine L Not available Not available 30789695 ACS Chem Biol. 2019 Mar 15;14(3):516-525. Li Y, Zhang Y, Wu M, Chang Q, Hu H, Zhao X. Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy DRAMP33753 IKLXKKXKKXLKKVLKGXIKGXIAVAKMV 29 H-58, Hymenochirin-1B [P5K,E6K,D9K; S4,T7,N10-GlcNAc; A18,22 S5] W8PRC4 Not found Synthetic (Derived from Hymenochirin-1B) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=0.62±0.12 μM); HCT 116 (IC50=1.29±0.08 μM); HepG2 (IC50=2.13±0.07 μM) Not available Linear Free Free X(4)=Ser-GlcNAc; X(7)=Thr-GlcNAc; X(10)=Asn-GlcNAc; X(18/22)=(S)-N-Fmoc-2-(4′-pentenyl)alanine L Not available Not available 30789695 ACS Chem Biol. 2019 Mar 15;14(3):516-525. Li Y, Zhang Y, Wu M, Chang Q, Hu H, Zhao X. Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy DRAMP33754 ALWMTLLKKVLKAAAKAALNAVLVGA 26 Dermaseptin S4 (1-26)a P80280 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW620 (42.19±24.29% Cytotoxicity=256 µg/ml) Human erythrocytes: 74.2±5.82% Hemolysis=256 µg/ml Linear Free Amidation L Not available Not available 33774792 Environ Sci Pollut Res Int. 2021 Aug;28(30):40908-40916. Belaid A, Braiek A, Alibi S, Hassen W, Beltifa A, Nefzi A, Mansour HB. Evaluating the effect of dermaseptin S4 and its derivatives on multidrug-resistant bacterial strains and on the colon cancer cell line SW620 DRAMP33755 ALWMTLLKKVLKAAAKAALNAVLV 24 Dermaseptin S4 (1-24)a P80280 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW620 (71.48±4.81% Cytotoxicity=256 µg/ml) Human erythrocytes: 57.1±6.34% Hemolysis=256 µg/ml Linear Free Amidation L Not available Not available 33774792 Environ Sci Pollut Res Int. 2021 Aug;28(30):40908-40916. Belaid A, Braiek A, Alibi S, Hassen W, Beltifa A, Nefzi A, Mansour HB. Evaluating the effect of dermaseptin S4 and its derivatives on multidrug-resistant bacterial strains and on the colon cancer cell line SW620 DRAMP33756 ALWMTLLKKVLKAAAKAALNAV 22 Dermaseptin S4 (1-22)a P80280 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW620 (66.21±20.07% Cytotoxicity=256 µg/ml) Human erythrocytes: 80±1.12% Hemolysis=256 µg/ml Linear Free Amidation L Not available Not available 33774792 Environ Sci Pollut Res Int. 2021 Aug;28(30):40908-40916. Belaid A, Braiek A, Alibi S, Hassen W, Beltifa A, Nefzi A, Mansour HB. Evaluating the effect of dermaseptin S4 and its derivatives on multidrug-resistant bacterial strains and on the colon cancer cell line SW620 DRAMP33757 WMTLLKKVLKAAAKAALNAVLVGANA 26 Dermaseptin S4 (3-28)a P80280 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW620 (54.02±3.37% Cytotoxicity=256 µg/ml) Human erythrocytes: 68.5±7.58% Hemolysis=256 µg/ml Linear Free Amidation L Not available Not available 33774792 Environ Sci Pollut Res Int. 2021 Aug;28(30):40908-40916. Belaid A, Braiek A, Alibi S, Hassen W, Beltifa A, Nefzi A, Mansour HB. Evaluating the effect of dermaseptin S4 and its derivatives on multidrug-resistant bacterial strains and on the colon cancer cell line SW620 DRAMP33758 LKKVLKAAAKAALNAVLVGANA 22 Dermaseptin S4 (7-28) P80280 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SW620 (35.72±18.49% Cytotoxicity=256 µg/ml) Human erythrocytes: 35.4±6.28% Hemolysis=256 µg/ml Linear Free Amidation L Not available Not available 33774792 Environ Sci Pollut Res Int. 2021 Aug;28(30):40908-40916. Belaid A, Braiek A, Alibi S, Hassen W, Beltifa A, Nefzi A, Mansour HB. Evaluating the effect of dermaseptin S4 and its derivatives on multidrug-resistant bacterial strains and on the colon cancer cell line SW620 DRAMP33759 GLRKRLRKFFNKIKEK 16 sC18 [R10F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (<20% Killing=40 µM); HeLa (Not active up to 40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: <20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33760 GLRKRLRKFRNKIKFK 16 sC18 [E15F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (Not active up to 40 µM); MCF-7 (Not active up to 40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: <10% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33761 GLRKRLRKFRNKIKEF 16 sC18 [K16F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (<10% Killing=40 µM); MCF-7 (<20% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: Not active up to 40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33762 GLEKRKRKFFNKIKFK 16 sC18 [R10F,E15F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (60% Killing=40 µM); HeLa (75% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: 20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33763 GLRKRLRKFFNKIKEF 16 sC18 [R10F,K16F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (>50% Killing=40 µM); HeLa (40% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: <5% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33764 GLRKRLRKFRNKIKFF 16 sC18 [E15F,K16F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (40% Killing=40 µM); HeLa (80% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: Not active up to 40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33765 GLRKRLRKFFNKIKFF 16 sC18 [E15F,E15F,K16F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (80% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: 40% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33766 GLRKRLRKFRNKIKK 15 sC18 [E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (<10% Killing=40 µM); MCF-7 (35% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: <10% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33767 GLRKRLRKFFNKIKF 15 sC18 [R10F,E15Del,K16F] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (<10% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation L HEK293: 20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33768 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 4-F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=4-F-Phe L HEK293: <10% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33769 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 4-F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=4-F-Phe L HEK293: <10% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33770 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 4-F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=4-F-Phe L HEK293: <10% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33771 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 2F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=2-F-Phe L HEK293: 20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33772 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 2F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=2-F-Phe L HEK293: 20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33773 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 2F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=2-F-Phe L HEK293: 20% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33774 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 5F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=5-F-Phe L HEK293: <25% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33775 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 5F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=5-F-Phe L HEK293: <25% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33776 GLRKRLRKFXNKIKX 15 sC18 [R10,K16 5F-Phe,E15Del] P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (>80% Killing=40 µM); MCF-7 (>90% Killing=40 µM) "Human erythrocytes: <10% Hemolysis =40 µM" Linear Free Amidation X=5-F-Phe L HEK293: <25% Killing=40 µM Not available 33313751 Biochem J. 2021 Jan 15;478(1):63-78. Drexelius M, Reinhardt A, Grabeck J, Cronenberg T, Nitsche F, Huesgen PF, Maier B, Neundorf I. Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity DRAMP33777 PWIPLTPL 8 Phakellistatin 15 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (IC50=8.5 μM) Not available Cyclic Free Free L Not available Not available 20345147 J Nat Prod. 2010 Apr 23;73(4):650-5. Zhang HJ, Yi YH, Yang GJ, Hu MY, Cao GD, Yang F, Lin HW. Proline-containing cyclopeptides from the marine sponge Phakellia fusca DRAMP33778 PFDSRAVTY 9 Phakellistatin 16 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: BEL-7402 (IC50=14.3 μM); P388 (IC50=5.4 μM) Not available Cyclic Free Free L Not available Not available 20345147 J Nat Prod. 2010 Apr 23;73(4):650-5. Zhang HJ, Yi YH, Yang GJ, Hu MY, Cao GD, Yang F, Lin HW. Proline-containing cyclopeptides from the marine sponge Phakellia fusca DRAMP33779 PWVPLIPI 8 Phakellistatin 17 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (Not active up to 100 µg/ml) Not available Cyclic Free Free L Not available Not available 20345147 J Nat Prod. 2010 Apr 23;73(4):650-5. Zhang HJ, Yi YH, Yang GJ, Hu MY, Cao GD, Yang F, Lin HW. Proline-containing cyclopeptides from the marine sponge Phakellia fusca DRAMP33780 PYPIFPI 7 Phakellistatin 18 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=3.9 μM ); K562 (IC50=33 μM); SNU-638 (IC50=37 μM); A549 (IC50=6.7 μM ); SK-HEP-1 (IC50=7.7 μM); MDA-MB-231 (IC50=9.1 μM); P388 (Not active up to 100 µg/ml) Not available Cyclic Free Free L Not available Not available 20345147 J Nat Prod. 2010 Apr 23;73(4):650-5. Zhang HJ, Yi YH, Yang GJ, Hu MY, Cao GD, Yang F, Lin HW. Proline-containing cyclopeptides from the marine sponge Phakellia fusca DRAMP33781 IPWFPLTP 8 Phakellistatin 19 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=0.44 µM); HT-29 (IC50=0.462 µM); MDA-MB-231 (IC50=0.515 µM) Not available Cyclic Free Free L Not available Not available 24252114 J Med Chem. 2013 Dec 12;56(23):9780-8. Pelay-Gimeno M, Meli A, Tulla-Puche J, Albericio F. Rescuing biological activity from synthetic phakellistatin 19 DRAMP33782 PFNAXAI 7 Phakellistatin 20 Not available Not found Stylissa flabelliformis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=11 µM); HCT 116 (IC50=12 µM); MDA-MB-231 (IC50=12 µM); SNU-638 (IC50=12 µM); SK-HEP-1 (IC50=13 µM); A549 (IC50=15 µM) Not available Cyclic Free Free X=Methionine sulfone L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33783 PPXFELPPYI 10 Phakellistatin 21 Not available Not found Stylissa flabelliformis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-HEP-1 (IC50=0.041 µM); HCT 116 (IC50=0.14 µM); SNU-638 (IC50=0.16 µM); K562 (IC50=0.17 µM); A549 (IC50=0.19 µM); MDA-MB-231 (IC50=0.4 µM) Not available Cyclic Free Free X=Methionine sulfone L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33784 PPXFELPPYI 10 Phakellistatin 21 Not available Not found Stylissa flabelliformis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SNU-638 (IC50=0.01 µM); HCT 116 (IC50=0.011 µM); SK-HEP-1 (IC50=0.014 µM); K562 (IC50=0.021 µM); A549 (IC50=0.023 µM); MDA-MB-231 (IC50=0.35 µM) Not available Cyclic Free Free X=Methionine sulfone L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33785 PPXFELPPYI 10 Phakellistatin 22 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SK-HEP-1 (IC50=0.041 µM); HCT 116 (IC50=0.14 µM); SNU-638 (IC50=0.16 µM); K562 (IC50=0.17 µM); A549 (IC50=0.19 µM); MDA-MB-231 (IC50=0.4 µM) Not available Cyclic Free Free X=Methionine sulfone L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33786 PPXFELPPYI 10 Phakellistatin 22 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SNU-638 (IC50=0.01 µM); HCT 116 (IC50=0.011 µM); SK-HEP-1 (IC50=0.014 µM); K562 (IC50=0.021 µM); A549 (IC50=0.023 µM); MDA-MB-231 (IC50=0.35 µM) Not available Cyclic Free Free X=Methionine sulfone L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33787 IxPYPFP 7 Phakellistatin 2 Not available Not found Stylotella aurantium Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50=0.66 µM); HCT 116 (IC50=0.71 µM); SK-HEP-1 (IC50=0.77 µM); MDA-MB-231 (IC50=1.3 µM); SNU-638 (IC50=1.6 µM); A2780 (IC50=28.27 µg/ml (DMSO); IC50=2.72 µg/ml (MeOH)); K562 (IC50=3.2 µM) Not available Cyclic Free Free x=D-Allo-Ile Mix Not available Not available 12444643 J Org Chem. 2002 Nov 29;67(24):8593-601. Tabudravu JN, Jaspars M, Morris LA, Kettenes-Van Den Bosch JJ, Smith N. Two distinct conformers of the cyclic heptapeptide phakellistatin 2 isolated from the fijian marine sponge stylotellaaurantium DRAMP33788 PtPfiFS 7 Phakellistatin 4 Not available Not found Phakellia costata Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (IC50=10 µM); SNU-638 (IC50=24 µM); K562 (IC50=30 µM); HCT 116 (IC50=4.5 µM); SK-HEP-1 (IC50=7.2 µM); A549 (IC50=7.4 µM) Not available Cyclic Free Free t=D-Thr; f=D-Phe; i=D-Ile Mix Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33789 lPPYvPPXfv 10 Phakellistatin 9 Not available Not found Phakellia costata Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=1 µM); K562 (IC50=1.1 µM); A549 (IC50=1.4 µM); SK-HEP-1 (IC50=12 µM); SNU-638 (IC50=2.2 µM); MDA-MB-231 (IC50=8.6 µM) Not available Cyclic Free Free X=Allo-Ile Mix Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33790 QPFPfifp 8 Phakellistatin 11 Not available Not found Phakellia sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=0.2 µg/ml); HCT 116 (IC50=1.6 µM); SK-HEP-1 (IC50=1.7 µM); A549 (IC50=2.8 µM); MDA-MB-231 (IC50=3.2 µM); K562 (IC50=5.6 µM); SNU-638 (IC50=6.9 µM) Not available Cyclic Free Free f=D-Phe; i=D-Ile Mix Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33791 IFVLPPYIPP 10 Phakellistatin 8 Not available Not found Phakellia fusca Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 (IC50=0.1 µM); K562 (IC50=0.29 µM); A549 (IC50=0.54 µM); SNU-638 (IC50=1.7 µM); SK-HEP-1 (IC50=2.3 µM); MDA-MB-231 (IC50=2.5 µM) Not available Cyclic Free Free L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33792 ANPRYPYT 8 Cyclonellin Not available Not found Axinella carteri Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A549 (IC50>50 µM); HCT 116 (IC50>50 µM); K562 (IC50>50 µM); MDA-MB-231 (IC50>50 µM); SK-HEP-1 (IC50>50 µM); SNU-638 (IC50>50 µM) Not available Cyclic Free Free L Not available Not available 29893558 J Nat Prod. 2018 Jun 22;81(6):1426-1434. Kwon OS, Kim CK, Byun WS, Oh J, Lee YJ, Lee HS, Sim CJ, Oh DC, Lee SK, Oh KB, Shin J. Cyclopeptides from the Sponge Stylissa flabelliformis DRAMP33793 IPYVPLTP 8 Phakellistatin 10 Not available Not found Phakellia sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=2.1 µg/ml) Not available Cyclic Free Free L Not available Not available 7673945 J Nat Prod. 1995 Jun;58(6):961-5 ettit GR, Tan R, Ichihara Y, Williams MD, Doubek DL, Tackett LP, Schmidt JM, Cerny RL, Boyd MR, Hooper JN. Antineoplastic agents, 325. Isolation and structure of the human cancer cell growth inhibitory cyclic octapeptides phakellistatin 10 and 11 from Phakellia sp DRAMP33794 AIPFNAM 7 Phakellistatin 5 Not available Not found Phakellia costada Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: DU145 (GI50=0.14-0.74 μg/mL); KM20L2 (GI50=0.14-0.74 μg/mL); NCI-H460 (GI50=0.14-0.74 μg/mL); OVCAR-3 (GI50=0.14-0.74 μg/mL); P388 (GI50=0.14-0.74 μg/mL); SF295 (GI50=0.14-0.74 μg/mL); SK-MEL-5 (GI50=0.14-0.74 μg/mL) Not available Cyclic Free Free L Not available Not available 10650072 J Nat Prod. 2000 Jan;63(1):22-8. Pettit GR, Toki BE, Xu JP, Brune DC. Synthesis of the marine sponge cycloheptapeptide phakellistatin 5(1) DRAMP33795 PIPIFPY 7 Phakellistatin 1 Not available Not found Phakellia costata; Stylotella aurantium Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=7.5 μg/mL) Not available Cyclic Free Free L Not available Not available 28335479 Mar Drugs. 2017 Mar 18;15(3):78. Meli A, Tedesco C, Della Sala G, Schettini R, Albericio F, De Riccardis F, Izzo I. Phakellistatins: An Underwater Unsolved Puzzle DRAMP33796 PFGPTIX 7 Phakellistatin 3 Not available Not found Phakellia carteri Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=0.33 μg/mL) Not available Cyclic Free Free X=Photo-Trp L Not available Not available 28335479 Mar Drugs. 2017 Mar 18;15(3):78. Meli A, Tedesco C, Della Sala G, Schettini R, Albericio F, De Riccardis F, Izzo I. Phakellistatins: An Underwater Unsolved Puzzle DRAMP33797 PFPWLPI 7 Phakellistatin 6 Not available Not found Phakellia costata Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=0.18 μg/mL) Not available Cyclic Free Free L Not available Not available 28335479 Mar Drugs. 2017 Mar 18;15(3):78. Meli A, Tedesco C, Della Sala G, Schettini R, Albericio F, De Riccardis F, Izzo I. Phakellistatins: An Underwater Unsolved Puzzle DRAMP33798 PPIFALPPYI 10 Phakellistatin 7 Not available Not found Phakellia costata Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=3.2 μg/mL) Not available Cyclic Free Free L Not available Not available 28335479 Mar Drugs. 2017 Mar 18;15(3):78. Meli A, Tedesco C, Della Sala G, Schettini R, Albericio F, De Riccardis F, Izzo I. Phakellistatins: An Underwater Unsolved Puzzle DRAMP33799 PPIFTLPPYI 10 Phakellistatin 12 Not available Not found Phakellia sp. Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=2.8 μg/mL) Not available Cyclic Free Free L Not available Not available 12639558 Bioorg Med Chem Lett. 2003 Feb 24;13(4):685-8. Pettit GR, Tan R. Antineoplastic agents 390. Isolation and structure of phakellistatin 12 from a Chuuk archipelago marine sponge DRAMP33800 AIPFXAX 7 Phakellistatin 14 Not available Not found Phakellia sp Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: P388 (ED50=0.0042 μg/mL) Not available Cyclic Free Free X(5)=β-OMe-Asp; X(7)=Met(SO) L Not available Not available 15679318 J Nat Prod. 2005 Jan;68(1):60-3. Pettit GR, Tan R. Isolation and structure of phakellistatin 14 from the Western Pacific marine sponge Phakellia sp DRAMP33801 XP 2 Diketopiperazine (preWP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=21.1 μM); A2780 (IC50=82.8 μM); A2780-cisR (IC50=85.9 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33802 XP 2 Diketopiperazine (preWP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2780 (IC50=100 μM); K562 (IC50=40.4 μM); A2780-cisR (IC50=87.8 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33803 XG 2 Diketopiperazine (preWG) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=16.7 μM); A2780 (IC50=82.4 μM); A2780-cisR (IC50=85.2 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33804 XL 2 Diketopiperazine (preWL) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=30.1 μM); A2780-cisR (IC50=75 μM); A2780 (IC50=92.6 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33805 XW 2 Diketopiperazine (preWW) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=29.8 μM); A2780-cisR (IC50=80.8 μM); A2780 (IC50=89.7 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33806 XY 2 Diketopiperazine (preWY) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=31.6 μM); A2780-cisR (IC50=83.3 μM); A2780 (IC50=89.8 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33807 XF 2 Diketopiperazine (preWF) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=70.4 μM); A2780-cisR (IC50=81.6 μM); A2780 (IC50=87 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33808 Xp 2 Diketopiperazine (preWp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2780 (IC50=106 μM); K562 (IC50=34.7 μM); A2780-cisR (IC50=92 μM) Not available Cyclic Free Free X=Prenylated-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33809 Xp 2 Diketopiperazine (preWp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=30.9 μM); A2780-cisR (IC50=85.6 μM); A2780 (IC50=93.1 μM) Not available Cyclic Free Free X=Prenylated-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33810 XP 2 Diketopiperazine (prewP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=21.1 μM); A2780 (IC50=82.8 μM); A2780-cisR (IC50=85.9 μM) Not available Cyclic Free Free x=Prenylated-D-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33811 XP 2 Diketopiperazine (prewP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2780 (IC50=100 μM); K562 (IC50=40.4 μM); A2780-cisR (IC50=87.8 μM) Not available Cyclic Free Free x=Prenylated-D-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33812 Xp 2 Diketopiperazine (prewp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: A2780 (IC50=106 μM); K562 (IC50=34.7 μM); A2780-cisR (IC50=92 μM) Not available Cyclic Free Free x=Prenylated-D-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33813 Xp 2 Diketopiperazine (prewp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=30.9 μM); A2780-cisR (IC50=85.6 μM); A2780 (IC50=93.1 μM) Not available Cyclic Free Free x=Prenylated-D-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33814 XA 2 Diketopiperazine (preWA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=35.2 μM); A2780-cisR (IC50=82.2 μM); A2780 (IC50=89.8 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33815 Xa 2 Diketopiperazine (preWa) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=34.5 μM); A2780-cisR (IC50=77 μM); A2780 (IC50=77.2 μM) Not available Cyclic Free Free X=Prenylated-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33816 xa 2 Diketopiperazine (prewa) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=34.7 μM); A2780-cisR (IC50=81.1 μM); A2780 (IC50=85 μM) Not available Cyclic Free Free x=Prenylated-D-Trp D Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33817 xA 2 Diketopiperazine (prewA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=35.3 μM); A2780-cisR (IC50=84.3 μM); A2780 (IC50=86.2 μM) Not available Cyclic Free Free x=Prenylated-D-Trp Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33818 XH 2 Diketopiperazine (preWH) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (IC50=32.2 μM); A2780-cisR (IC50=91.7 μM); A2780 (IC50=91.8 μM) Not available Cyclic Free Free X=Prenylated-Trp L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9. Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM. Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP33819 GL 2 Diketopiperazine (GL) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (12.58±1.23% Inhibition=10 µM ; 28.64 ± 1.51% Inhibition=100 µM ); MCF-7 (19.50 ± 1.34% Inhibition=10 µM; 27.49 ± 2.68% Inhibition=100 µM); HT-29 (21.55 ± 1.93% Inhibition=10 µM; 17.25 ± 1.66% Inhibition=100 µM) Not available Cyclic Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP33820 GV 2 Diketopiperazine (GV) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (12.58 ± 1.23% Inhibition=10 µM ; 23.46 ± 2.04% Inhibition=100 µM); HT-29 (6.87 ± 0.67% Inhibition=10 µM; 23.90 ± 2.25% Inhibition=100 µM); MCF-7 (7.00 ± 0.56% Inhibition=10 µM; 21.19 ± 2.04% Inhibition=100 µM) Not available Cyclic Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP33821 Gv 2 Diketopiperazine (Gv) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (14.29 ± 1.40% Inhibition=10 µM; 16.78 ± 1.65% Inhibition=100 µM); HeLa (19.61 ± 0.82% Inhibition=10 µM ; 20.55 ± 2.03% Inhibition=100 µM); MCF-7 (19.78 ± 1.86% Inhibition=10 µM; 21.94 ± 2.17% Inhibition=100 µM) Not available Cyclic Free Free Mix Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP33822 GC 2 Diketopiperazine (GC) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (30.56 ± 0.03% Inhibition=10 µM; 51.29 ± 0.01% Inhibition=100 µM); MCF-7 (36.49 ± 0.02% Inhibition=10 µM; 56.08 ± 0.01% Inhibition=100 µM); HeLa (43.92 ± 0.02% Inhibition=10 µM ; 57.79 ± 0.02% Inhibition=100 µM) Not available Cyclic Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP33823 YC 2 Diketopiperazine (YC) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (32.41 ± 0.03% Inhibition=10 µM; 52.27 ± 0.02% Inhibition=100 µM); MCF-7 (35.15 ± 0.01% Inhibition=10 µM; 56.08 ± 0.01% Inhibition=100 µM); HeLa (54.61 ± 0.02% Inhibition=10 µM ; 57.79 ± 0.02% Inhibition=100 µM) Not available Cyclic Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP33824 VWKPPYLPRPRPPRrIYNr 19 Oncocin Onc112 [D2W], Onc245 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (40% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 32% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33825 VDRPPYLPRPRPPRrIYNr 19 Oncocin Onc112 [K3R], Onc246 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33826 VDKKPYLPRPRPPRrIYNr 19 Oncocin Onc112 [P4K], Onc247 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (50% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33827 VDKFPYLPRPRPPRrIYNr 19 Oncocin Onc112 [P4F], Onc248 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (39% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 48% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33828 VDKYPYLPRPRPPRrIYNr 19 Oncocin Onc112 [P4Y], Onc249 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (30% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 45% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33829 VDKPFYLPRPRPPRrIYNr 19 Oncocin Onc112 [P5F], Onc250 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (34% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33830 VDKPYYLPRPRPPRrIYNr 19 Oncocin Onc112 [P5Y], Onc251 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (35% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 45% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33831 VDKPHYLPRPRPPRrIYNr 19 Oncocin Onc112 [P5H], Onc252 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (34% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 46% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33832 VDKPRYLPRPRPPRrIYNr 19 Oncocin Onc112 [P5R], Onc253 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (40% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33833 VDKPPWLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6W], Onc254 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (34% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 55% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33834 VDKPPFLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6F], Onc255 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (44% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 45% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33835 VDKPPHLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6H], Onc256 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 56% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33836 VDKPPXLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6Dit], Onc257 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (58% Killing=600 µg/ml) Not available Linear Free Amidation X=3,5‐Diiodotyrosine Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33837 VDKPPXLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6Dit], Onc257 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (54% Killing=600 µg/ml) Not available Linear Free Amidation X=3,5‐Diiodotyrosine Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33838 VDKPPXLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6Nty], Onc258 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (58% Killing=600 µg/ml) Not available Linear Free Amidation X=3‐Nitrotyrosine Mix HEK293: 45% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33839 VDKPPXLPRPRPPRrIYNr 19 Oncocin Onc112 [Y6Nty], Onc258 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (54% Killing=600 µg/ml) Not available Linear Free Amidation X=3‐Nitrotyrosine Mix HEK293: 45% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33840 VDKPPYXPRPRPPRrIYNr 19 Oncocin Onc112 [L7Nle], Onc259 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation X=nor-Leu Mix HEK293: 60% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33841 VDKPPYXPRPRPPRrIYNr 19 Oncocin Onc112 [L7Nle], Onc259 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (43% Killing=600 µg/ml) Not available Linear Free Amidation X=nor-Leu Mix HEK293: 60% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33842 VDKPPYXPRPRPPRrIYNr 19 Oncocin Onc112 [L7Tle], Onc260 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation X=tert‐Leu Mix HEK293: 52% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33843 VDKPPYXPRPRPPRrIYNr 19 Oncocin Onc112 [L7Tle], Onc260 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (43% Killing=600 µg/ml) Not available Linear Free Amidation X=tert‐Leu Mix HEK293: 52% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33844 VDKPPYRPRPRPPRrIYNr 19 Oncocin Onc112 [L7R], Onc261 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (42% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33845 VDKPPYMPRPRPPRrIYNr 19 Oncocin Onc112 [L7M], Onc262 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 50% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33846 VDKPPYFPRPRPPRrIYNr 19 Oncocin Onc112 [L7F], Onc263 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (32% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 38% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33847 VDKPPYLPRWRPPRrIYNr 19 Oncocin Onc112 [P10W], Onc264 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 43% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33848 VDKPPYLPRPWPPRrIYNr 19 Oncocin Onc112 [R11W], Onc265 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (44% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 43% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33849 VDKPPYLPRPHPPRrIYNr 19 Oncocin Onc112 [R11H], Onc266 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 50% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33850 VDKPPYLPRPKPPRrIYNr 19 Oncocin Onc112 [R11K], Onc267 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (58% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 59% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33851 VDKPPYLPRPFPPRrIYNr 19 Oncocin Onc112 [R11F], Onc268 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (50% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 38% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33852 VDKPPYLPRPXPPRrIYNr 19 Oncocin Onc112 [R11Har], Onc269 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (43% Killing=600 µg/ml) Not available Linear Free Amidation X=Homoarginine Mix HEK293: 41% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33853 VDKPPYLPRPRPPRrIXNr 19 Oncocin Onc112 [Y17Dit], Onc270 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation X=3,5‐Diiodotyrosine Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33854 VDKPPYLPRPRPPRrIXNr 19 Oncocin Onc112 [Y17Dit], Onc270 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation X=3,5‐Diiodotyrosine Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33855 VDKPPYLPRPRPPRrIXNr 19 Oncocin Onc112 [Y17Nty], Onc271 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation X=3‐Nitrotyrosine Mix HEK293: 34% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33856 VDKPPYLPRPRPPRrIXNr 19 Oncocin Onc112 [Y17Nty], Onc271 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation X=3‐Nitrotyrosine Mix HEK293: 34% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33857 VDKPPYLPRPRWPRrIYNr 19 Oncocin Onc112 [P12W], Onc272 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 38% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33858 VDKPPYLPRPRWERrIYNr 19 Oncocin Onc112 [P12W, P13E], Onc273 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (46% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 38% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33859 VDKPPYLPRPRWRRrIYNr 19 Oncocin Onc112 [P12W, P13R], Onc274 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (43% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33860 VDKPPYLPRPRWWRrIYNr 19 Oncocin Onc112 [P12W, P13W], Onc275 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (64% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 57% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33861 VDKPPYLPRPRWKRrIYNr 19 Oncocin Onc112 [P12W, P13K], Onc276 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (48% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 48% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33862 VDKPPYLPRPRWHRrIYNr 19 Oncocin Onc112 [P12W, P13H], Onc277 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (51% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 50% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33863 VDKPPYLPRPRWIRrIYNr 19 Oncocin Onc112 [P12W, P13I], Onc278 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (56% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33864 VDKPPYLPRPRWFRrIYNr 19 Oncocin Onc112 [P12W, P13F], Onc279 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (61% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 48% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33865 VDKPPYLPRPRWLRrIYNr 19 Oncocin Onc112 [P12W, P13L], Onc280 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (50% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 44% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33866 VDKPPYLPRPRWARrIYNr 19 Oncocin Onc112 [P12W, P13A], Onc281 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (48% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 46% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33867 VDKPPYLPRPRWNRrIYNr 19 Oncocin Onc112 [P12W, P13N], Onc282 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (54% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33868 VDKPPYLPRPRWVRrIYNr 19 Oncocin Onc112 [P12W, P13V], Onc283 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (25% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 28% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33869 VDKPPYLPRPRWGRrIYNr 19 Oncocin Onc112 [P12W, P13G], Onc284 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (27% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 28% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33870 VDKPPYLPRPRWSRrIYNr 19 Oncocin Onc112 [P12W, P13S], Onc285 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (38% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 34% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33871 VDKPPYLPRPRWQRrIYNr 19 Oncocin Onc112 [P12W, P13Q], Onc286 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (41% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 36% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33872 VDKPPYLPRPRWYRrIYNr 19 Oncocin Onc112 [P12W, P13Y], Onc287 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (30% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33873 VDKPPYLPRPRWDRrIYNr 19 Oncocin Onc112 [P12W, P13D], Onc288 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (28% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 28% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33874 VDKPPYLPRPRWTRrIYNr 19 Oncocin Onc112 [P12W, P13T], Onc289 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (22% Killing=600 µg/ml) Not available Linear Free Amidation Mix HEK293: 38% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33875 VDKPPYLPRPRWXRrIYNr 19 Oncocin Onc112 [P12W, P13O], Onc290 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (34% Killing=600 µg/ml) Not available Linear Free Amidation X=Orn Mix HEK293: 42% Killing=600 µg/ml Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP33876 VLPILLLVL 9 Cyclopeptide GG-8-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=12.22 μM); SMMC-7721 (IC50=6.38 μM ) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33877 VLPILLLVA 9 Cyclopeptide GG-8-6 [L9A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=38.64 μM); SMMC-7721 (IC50=38.92 μM ) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33878 VLPILLLAL 9 Cyclopeptide GG-8-6 [V8A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=40.46 μM); SMMC-7721 (IC50=47.37 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33879 VLPILLAVL 9 Cyclopeptide GG-8-6 [L7A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=31.84 μM); SMMC-7721 (IC50=47.37 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33880 VLPILALVL 9 Cyclopeptide GG-8-6 [L6A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SMMC-7721 (IC50=42.81 μM); HepG2 (IC50>100 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33881 VLPIALLVL 9 Cyclopeptide GG-8-6 [L5A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SMMC-7721 (IC50=29.8 μM); HepG2 (IC50>100 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33882 VLPALLLVL 9 Cyclopeptide GG-8-6 [I4A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SMMC-7721 (IC50=36.08 μM); HepG2 (IC50=55.61 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33883 VAPILLLVL 9 Cyclopeptide GG-8-6 [L2A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=39.37 μM); SMMC-7721 (IC50=48.48 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33884 ALPILLLVL 9 Cyclopeptide GG-8-6 [V1A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SMMC-7721 (IC50=29.94 μM); HepG2 (IC50=29.95 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33885 VLPILLLV 8 Cyclopeptide GG-8-6 (1-8) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=51.72 μM); SMMC-7721 (IC50=73.93 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33886 VLPILLL 7 Cyclopeptide GG-8-6 (1-7) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100 μM); SMMC-7721 (IC50>100 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33887 VLPILL 6 Cyclopeptide GG-8-6 (1-6) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100 μM); SMMC-7721 (IC50>100 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33888 VLPIL 5 Cyclopeptide GG-8-6 (1-5) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50>100 μM); SMMC-7721 (IC50>100 μM) Not available Cyclic Free Free L Not available Not available 29310863 Bioorg Med Chem. 2018 Feb 1;26(3):609-622. Chen JT, Ma R, Sun SC, Zhu XF, Xu XL, Mu Q. Synthesis and biological evaluation of cyclopeptide GG-8-6 and its analogues as anti-hepatocellular carcinoma agents DRAMP33889 EQWAREIGAQLRRMADDLNA 20 Puma-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Bc1-xL dependent) (EC50=1.006 ± 0.337 μM); OCI-Ly1 (Bcl-2 dependent) (EC50=1.967 ± 0.48 μM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33890 RPEIWYAQGLKRFGDEFNAYYAR 23 XXA1-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OCI-Ly1 (Bcl-2 dependent) (EC50=228 ± 56 nM); MDA-MB-231 (Bc1-xL dependent) (EC50=50 ± 16 nM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33891 RPEIWYAQWLKRFGDQFNAYYAR 23 XXA4-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33892 RPEIWIAQGLKRFGDEFNAYYAR 23 XXA1_Y2dI-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33893 RPEIWYAQELKRFGDEFNAYYAR 23 XXA1_G2gE-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Bc1-xL dependent) (EC50=12 ± 4 nM); OCI-Ly1 (Bcl-2 dependent) (EC50=37 ± 9 nM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33894 RPEIWYAQGLRRFGDEFNAYYAR 23 XXA1_K3bR-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33895 RPEIWYAQGLKRIGDEFNAYYAR 23 XXA1_F3dI-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33896 RPEIWYAQGLKRFGDEFNAYKAR 23 XXA1_Y4eK-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Bc1-xL dependent) (EC50=82 ± 27 nM); OCI-Ly1 (Bcl-2 dependent) (EC50=911 ± 222 nM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33897 IWYAQGLKRFGDEFNAYK 18 Y4eK_18-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: OCI-Ly1 (Bcl-2 dependent) (EC50=3.325 ± 0.812 μM); MDA-MB-231 (Bc1-xL dependent) (EC50=847 ± 284 nM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33898 RPEIWYAQGLKRFGDEFNAYK 21 Y4eK_21-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MDA-MB-231 (Bc1-xL dependent) (EC50=159 ± 53 nM); OCI-Ly1 (Bcl-2 dependent) (EC50=3.435 ± 0.839 μM) Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33899 LRPEIRYAQELRRIGDEFNE 20 BimEL-I146Y Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33900 LWAAIRIAQELRRIGDEFNE 20 Bim-WAA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33901 LRPEIRIARELRRIGDEFNE 20 BimEL-Q148R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33902 LRPEIRIAQELRRMGDEFNE 20 BimEL-I153M Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33903 LRPEIRYARELRRIGDEFNE 20 BimEL-I146Y-Q148R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33904 LRPEIRYAQELRRMGDEFNE 20 BimEL I146Y-I153M Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33905 PQMVILQLLRFIFRLVWRRH 20 BimEL-CTS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33906 PQMVELQLLRFIFRLVWRRH 20 BimEL-I181E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33907 PQMVILQLERFIFRLVWRRH 20 BimEL-L185E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33908 PQMVILQLLRFEFRLVWRRH 20 BimEL-I188E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33909 PQMVILQLLRFIFRLEWRRH 20 BimEL-V192E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33910 PQMVILQLLAFIFALVWRRH 20 BimEL-CST-2A (R186A-R190A) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 30860026 Elife. 2019 Mar 12;8:e37689. Liu Q, Osterlund EJ, Chi X, Pogmore J, Leber B, Andrews DW. Bim escapes displacement by BH3-mimetic anti-cancer drugs by double-bolt locking both Bcl-XL and Bcl-2 DRAMP33911 IWIAQELRRIGDEFNA 16 Bim SM-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937 (18% Killing= 50 μM); HL-60 (23% Killing= 50 μM); K562 (25% Killing= 50 μM) Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33912 IWIAQELRRIGDEF 14 Bim SM-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33913 IAQELRRIGDEFNA 14 Bim SM-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33914 WIAQELRRIGDEFN 14 Bim SM-4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33915 IAQELRRIGDEF 12 Bim SM-5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (21% Killing= 50 μM); K562 (26% Killing= 50 μM); U-937 (40% Killing= 50 μM) Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33916 IAQELRRIGDEF 12 Bim SM-5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (20% Killing= 50 μM); HL-60 (23% Killing= 50 μM); U-937 (45% Killing= 50 μM) Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33917 IAQELRRIGDEF 12 Bim SM-5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33918 IAQELRRIGDEF 12 Bim SM-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (21% Killing= 50 μM); K562 (26% Killing= 50 μM); U-937 (40% Killing= 50 μM) Not available Linear Pal, CH3(CH2)14CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33919 IAQELRRIGDEF 12 Bim SM-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (20% Killing= 50 μM); HL-60 (23% Killing= 50 μM); U-937 (45% Killing= 50 μM) Not available Linear Pal, CH3(CH2)14CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33920 IAQELRRIGDEF 12 Bim SM-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Pal, CH3(CH2)14CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33921 IAQELRRIGDEF 12 Bim SM-7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HL-60 (21% Killing= 50 μM); K562 (26% Killing= 50 μM); U-937 (40% Killing= 50 μM) Not available Linear mPEG, CH3(OCH2CH2)4OCH2CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33922 IAQELRRIGDEF 12 Bim SM-7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: K562 (20% Killing= 50 μM); HL-60 (23% Killing= 50 μM); U-937 (45% Killing= 50 μM) Not available Linear mPEG, CH3(OCH2CH2)4OCH2CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33923 IAQELRRIGDEF 12 Bim SM-7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear mPEG, CH3(OCH2CH2)4OCH2CO Amidation L Not available Bcl-2 Not available Discovery of novel inhibitors of anti-apoptotic Bcl-2proteins derived from Bim BH3 domain DRAMP33924 EIWIAQELRRRGDSFNAYYAR 21 Bim BH3 (I155R, E158S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33925 EIWIAQELRRRGDXFNAYYAR 21 p-Bim BH3 (I155R, E158S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Phosphorylated-Ser L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33926 EIWIAQELRRRGDAFNAYYAR 21 Bim BH3 (I155R, E158A) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33927 EIWIAQELRSRGDSFNAYYAR 21 Bim BH3 (R154S, I155R, E158S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33928 EIWIAQELRSRGDXFNAYYAR 21 p-Bim BH3 (R154S, I155R, E158S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Phosphorylated-Ser L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33929 EIWIAQELRRIGDSFNAYYAR 21 Bim BH3 (E158S) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-2/Bcl-xL 26136077 Cell Death Dis. 2015 Jul 2;6(7):e1804. Kim JS, Ku B, Woo TG, Oh AY, Jung YS, Soh YM, Yeom JH, Lee K, Park BJ, Oh BH, Ha NC. Conversion of cell-survival activity of Akt into apoptotic death of cancer cells by two mutations on the BIM BH3 domain DRAMP33930 LWAAQRYGRELRRMSDEFEGSFKGL 25 Bad-BH3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Bcl-xL 25451027 J Mol Biol. 2015 Mar 27;427(6 Pt B):1241-1253. Dutta S, Ryan J, Chen TS, Kougentakis C, Letai A, Keating AE. Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL DRAMP33931 RPEIWMTQGLRRLGDEINAYYAR 23 MS1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33932 RPEIWLTQSLQRLGDEINAYYAR 23 MS2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33933 RPEIWLTQHLQRLGDEINAYYAR 23 MS3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33934 RPEIWMGQGLRRLGDEINAYYAR 23 A12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33935 RPEIWLGQSLQRLGDEINAYYAR 23 B3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33936 RPEIWLGQHLQRLGDEINAYYAR 23 G9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33937 AELPPEFAAQLRKIGDKVYC 20 NoxaA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33938 RPEIWIAQELRRIGDEFNAYYAR 23 Bim Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33939 RPEIWITQELRRIGDEFNAYYAR 23 Bim-A2eT Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33940 RPEIWMTQELRRIGDEFNAYYAR 23 Bim-A2eT-I2dM Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33941 RPEIWITQGLRRIGDEFNAYYAR 23 Bim-A2eT-E2gG Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33942 RPEIWITQELRRLGDEFNAYYAR 23 Bim-A2eT-I3dL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33943 RPEIWITQELRRIGDEINAYYAR 23 Bim-A2eT-F4aI Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5/6-Fluorescein amidite Amidation L Not available Mcl-1 25052212 ACS Chem Biol. 2014 Sep 19;9(9):1962-8. Foight GW, Ryan JA, Gullá SV, Letai A, Keating AE. Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells DRAMP33944 RPEIWLAQYLRRLGDQINAYYAR 23 Bim-FD1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bfl-1 23363053 ACS Chem Biol. 2013 Apr 19;8(4):778-88. Dutta S, Chen TS, Keating AE. Peptide ligands for pro-survival protein Bfl-1 from computationally guided library screening DRAMP33945 RPEIWMAQVLRRFGDLLNAYYAR 23 Bim-FD2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Bfl-1 23363053 ACS Chem Biol. 2013 Apr 19;8(4):778-88. Dutta S, Chen TS, Keating AE. Peptide ligands for pro-survival protein Bfl-1 from computationally guided library screening DRAMP33946 RPEIWIAQELRRAGDVLNAYYAR 23 Bim-FA1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bfl-1 23363053 ACS Chem Biol. 2013 Apr 19;8(4):778-88. Dutta S, Chen TS, Keating AE. Peptide ligands for pro-survival protein Bfl-1 from computationally guided library screening DRAMP33947 RPEIWIAQGLRRIGDTWNAYYAR 23 Bim-FW1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Bfl-1 23363053 ACS Chem Biol. 2013 Apr 19;8(4):778-88. Dutta S, Chen TS, Keating AE. Peptide ligands for pro-survival protein Bfl-1 from computationally guided library screening DRAMP33948 MRPEIWIAQELRRIGDEVNAYYARRVZ 27 LIB2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33949 MRPEIWIAQELRRIGDENNAYYARRVZ 27 LIB3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33950 MRPEIWIAQELRRFGDEFNAYYARRVZ 27 LIB4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33951 MRPEIWIAQELRRFGDEVNAYYARRVZ 27 LIB5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33952 MRPEIWIAQELRRFGDENNAYYARRVZ 27 LIB6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33953 MRPEIWIAQELRRDGDEFNAYYARRVZ 27 LIB7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33954 MRPEIWIAQELRRDGDEVNAYYARRVZ 27 LIB8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33955 MRPEIWIAQELRRDGDENNAYYARRVZ 27 LIB9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33956 MRPEIWIAQELRRNGDEFNAYYARRVZ 27 LIB10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33957 MRPEIWIAQELRRNGDEVNAYYARRVZ 27 LIB11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33958 MRPEIWIAQELRRNGDENNAYYARRVZ 27 LIB12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33959 MRPEIWIAQELRRAGDEFNAYYARRVZ 27 LIB13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33960 MRPEIWIAQELRRAGDEVNAYYARRVZ 27 LIB14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33961 MRPEIWIAQELRRAGDENNAYYARRVZ 27 LIB15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33962 MRPEIWIAQELDRIGDEFNAYYARRVZ 27 LIB16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33963 MRPEIWIAQELDRIGDEVNAYYARRVZ 27 LIB17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33964 MRPEIWIAQELDRIGDENNAYYARRVZ 27 LIB18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33965 MRPEIWIAQELDRFGDEFNAYYARRVZ 27 LIB19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33966 MRPEIWIAQELDRFGDEVNAYYARRVZ 27 LIB20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33967 MRPEIWIAQELDRFGDENNAYYARRVZ 27 LIB21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33968 MRPEIWIAQELDRDGDEFNAYYARRVZ 27 LIB22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33969 MRPEIWIAQELDRDGDEVNAYYARRVZ 27 LIB23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33970 MRPEIWIAQELDRDGDENNAYYARRVZ 27 LIB24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33971 MRPEIWIAQELDRNGDEFNAYYARRVZ 27 LIB25 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33972 MRPEIWIAQELDRNGDEVNAYYARRVZ 27 LIB26 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33973 MRPEIWIAQELDRNGDENNAYYARRVZ 27 LIB27 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33974 MRPEIWIAQELDRAGDEFNAYYARRVZ 27 LIB28 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33975 MRPEIWIAQELDRAGDEVNAYYARRVZ 27 LIB29 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33976 MRPEIWIAQELDRAGDENNAYYARRVZ 27 LIB30 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33977 MRPEIWIAQEIRRIGDEFNAYYARRVZ 27 LIB31 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33978 MRPEIWIAQEIRRIGDEVNAYYARRVZ 27 LIB32 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33979 MRPEIWIAQEIRRIGDENNAYYARRVZ 27 LIB33 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33980 MRPEIWIAQEIRRFGDEFNAYYARRVZ 27 LIB34 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33981 MRPEIWIAQEIRRFGDEVNAYYARRVZ 27 LIB35 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33982 MRPEIWIAQEIRRFGDENNAYYARRVZ 27 LIB36 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33983 MRPEIWIAQEIRRDGDEFNAYYARRVZ 27 LIB37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33984 MRPEIWIAQEIRRDGDEVNAYYARRVZ 27 LIB38 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33985 MRPEIWIAQEIRRDGDENNAYYARRVZ 27 LIB39 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33986 MRPEIWIAQEIRRNGDEFNAYYARRVZ 27 LIB40 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33987 MRPEIWIAQEIRRNGDEVNAYYARRVZ 27 LIB41 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33988 MRPEIWIAQEIRRNGDENNAYYARRVZ 27 LIB42 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33989 MRPEIWIAQEIRRAGDEFNAYYARRVZ 27 LIB43 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33990 MRPEIWIAQEIRRAGDEVNAYYARRVZ 27 LIB44 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33991 MRPEIWIAQEIRRAGDENNAYYARRVZ 27 LIB45 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33992 MRPEIWIAQEIDRIGDEFNAYYARRVZ 27 LIB46 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33993 MRPEIWIAQEIDRIGDEVNAYYARRVZ 27 LIB47 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33994 MRPEIWIAQEIDRIGDENNAYYARRVZ 27 LIB48 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33995 MRPEIWIAQEIDRFGDEFNAYYARRVZ 27 LIB49 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33996 MRPEIWIAQEIDRFGDEVNAYYARRVZ 27 LIB50 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33997 MRPEIWIAQEIDRFGDENNAYYARRVZ 27 LIB51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33998 MRPEIWIAQEIDRDGDEFNAYYARRVZ 27 LIB52 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP33999 MRPEIWIAQEIDRDGDEVNAYYARRVZ 27 LIB53 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34000 MRPEIWIAQEIDRDGDENNAYYARRVZ 27 LIB54 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34001 MRPEIWIAQEIDRNGDEFNAYYARRVZ 27 LIB55 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34002 MRPEIWIAQEIDRNGDEVNAYYARRVZ 27 LIB56 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34003 MRPEIWIAQEIDRNGDENNAYYARRVZ 27 LIB57 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34004 MRPEIWIAQEIDRAGDEFNAYYARRVZ 27 LIB58 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34005 MRPEIWIAQEIDRAGDEVNAYYARRVZ 27 LIB59 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34006 MRPEIWIAQEIDRAGDENNAYYARRVZ 27 LIB60 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34007 MRPEIWIAQEFRRIGDEFNAYYARRVZ 27 LIB61 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34008 MRPEIWIAQEFRRIGDEVNAYYARRVZ 27 LIB62 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34009 MRPEIWIAQEFRRIGDENNAYYARRVZ 27 LIB63 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34010 MRPEIWIAQEFRRFGDEFNAYYARRVZ 27 LIB64 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34011 MRPEIWIAQEFRRFGDEVNAYYARRVZ 27 LIB65 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34012 MRPEIWIAQEFRRFGDENNAYYARRVZ 27 LIB66 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34013 MRPEIWIAQEFRRDGDEFNAYYARRVZ 27 LIB67 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34014 MRPEIWIAQEFRRDGDEVNAYYARRVZ 27 LIB68 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34015 MRPEIWIAQEFRRDGDENNAYYARRVZ 27 LIB69 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34016 MRPEIWIAQEFRRNGDEFNAYYARRVZ 27 LIB70 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34017 MRPEIWIAQEFRRNGDEVNAYYARRVZ 27 LIB71 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34018 MRPEIWIAQEFRRNGDENNAYYARRVZ 27 LIB72 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34019 MRPEIWIAQEFRRAGDEFNAYYARRVZ 27 LIB73 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34020 MRPEIWIAQEFRRAGDEVNAYYARRVZ 27 LIB74 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34021 MRPEIWIAQEFRRAGDENNAYYARRVZ 27 LIB75 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34022 MRPEIWIAQEFDRIGDEFNAYYARRVZ 27 LIB76 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34023 MRPEIWIAQEFDRIGDEVNAYYARRVZ 27 LIB77 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34024 MRPEIWIAQEFDRIGDENNAYYARRVZ 27 LIB78 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34025 MRPEIWIAQEFDRFGDEFNAYYARRVZ 27 LIB79 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34026 MRPEIWIAQEFDRFGDEVNAYYARRVZ 27 LIB80 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34027 MRPEIWIAQEFDRFGDENNAYYARRVZ 27 LIB81 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34028 MRPEIWIAQEFDRDGDEFNAYYARRVZ 27 LIB82 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34029 MRPEIWIAQEFDRDGDEVNAYYARRVZ 27 LIB83 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34030 MRPEIWIAQEFDRDGDENNAYYARRVZ 27 LIB84 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34031 MRPEIWIAQEFDRNGDEFNAYYARRVZ 27 LIB85 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34032 MRPEIWIAQEFDRNGDEVNAYYARRVZ 27 LIB86 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34033 MRPEIWIAQEFDRNGDENNAYYARRVZ 27 LIB87 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34034 MRPEIWIAQEFDRAGDEFNAYYARRVZ 27 LIB88 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34035 MRPEIWIAQEFDRAGDEVNAYYARRVZ 27 LIB89 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34036 MRPEIWIAQEFDRAGDENNAYYARRVZ 27 LIB90 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34037 MRPEIWIAQEARRIGDEFNAYYARRVZ 27 LIB91 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34038 MRPEIWIAQEARRIGDEVNAYYARRVZ 27 LIB92 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34039 MRPEIWIAQEARRIGDENNAYYARRVZ 27 LIB93 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34040 MRPEIWIAQEARRFGDEFNAYYARRVZ 27 LIB94 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34041 MRPEIWIAQEARRFGDEVNAYYARRVZ 27 LIB95 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34042 MRPEIWIAQEARRFGDENNAYYARRVZ 27 LIB96 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34043 MRPEIWIAQEARRDGDEFNAYYARRVZ 27 LIB97 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34044 MRPEIWIAQEARRDGDEVNAYYARRVZ 27 LIB98 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34045 MRPEIWIAQEARRDGDENNAYYARRVZ 27 LIB99 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34046 MRPEIWIAQEARRNGDEFNAYYARRVZ 27 LIB100 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34047 MRPEIWIAQEARRNGDEVNAYYARRVZ 27 LIB101 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34048 MRPEIWIAQEARRNGDENNAYYARRVZ 27 LIB102 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34049 MRPEIWIAQEARRAGDEFNAYYARRVZ 27 LIB103 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34050 MRPEIWIAQEARRAGDEVNAYYARRVZ 27 LIB104 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34051 MRPEIWIAQEARRAGDENNAYYARRVZ 27 LIB105 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34052 MRPEIWIAQEADRIGDEFNAYYARRVZ 27 LIB106 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34053 MRPEIWIAQEADRIGDEVNAYYARRVZ 27 LIB107 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34054 MRPEIWIAQEADRIGDENNAYYARRVZ 27 LIB108 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34055 MRPEIWIAQEADRFGDEFNAYYARRVZ 27 LIB109 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34056 MRPEIWIAQEADRFGDEVNAYYARRVZ 27 LIB110 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34057 MRPEIWIAQEADRFGDENNAYYARRVZ 27 LIB111 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34058 MRPEIWIAQEADRDGDEFNAYYARRVZ 27 LIB112 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34059 MRPEIWIAQEADRDGDEVNAYYARRVZ 27 LIB113 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34060 MRPEIWIAQEADRDGDENNAYYARRVZ 27 LIB114 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34061 MRPEIWIAQEADRNGDEFNAYYARRVZ 27 LIB115 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34062 MRPEIWIAQEADRNGDEVNAYYARRVZ 27 LIB116 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34063 MRPEIWIAQEADRNGDENNAYYARRVZ 27 LIB117 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34064 MRPEIWIAQEADRAGDEFNAYYARRVZ 27 LIB118 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34065 MRPEIWIAQEADRAGDEVNAYYARRVZ 27 LIB119 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34066 MRPEIWIAQEADRAGDENNAYYARRVZ 27 LIB120 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34067 MRPEIWAAQELRRIGDEFNAYYARRVZ 27 LIB121 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34068 MRPEIWAAQELRRIGDEVNAYYARRVZ 27 LIB122 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34069 MRPEIWAAQELRRIGDENNAYYARRVZ 27 LIB123 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34070 MRPEIWAAQELRRFGDEFNAYYARRVZ 27 LIB124 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34071 MRPEIWAAQELRRFGDEVNAYYARRVZ 27 LIB125 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34072 MRPEIWAAQELRRFGDENNAYYARRVZ 27 LIB126 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34073 MRPEIWAAQELRRDGDEFNAYYARRVZ 27 LIB127 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34074 MRPEIWAAQELRRDGDEVNAYYARRVZ 27 LIB128 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34075 MRPEIWAAQELRRDGDENNAYYARRVZ 27 LIB129 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34076 MRPEIWAAQELRRNGDEFNAYYARRVZ 27 LIB130 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34077 MRPEIWAAQELRRNGDEVNAYYARRVZ 27 LIB131 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34078 MRPEIWAAQELRRNGDENNAYYARRVZ 27 LIB132 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34079 MRPEIWAAQELRRAGDEFNAYYARRVZ 27 LIB133 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34080 MRPEIWAAQELRRAGDEVNAYYARRVZ 27 LIB134 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34081 MRPEIWAAQELRRAGDENNAYYARRVZ 27 LIB135 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34082 MRPEIWAAQELDRIGDEFNAYYARRVZ 27 LIB136 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34083 MRPEIWAAQELDRIGDEVNAYYARRVZ 27 LIB137 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34084 MRPEIWAAQELDRIGDENNAYYARRVZ 27 LIB138 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34085 MRPEIWAAQELDRFGDEFNAYYARRVZ 27 LIB139 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34086 MRPEIWAAQELDRFGDEVNAYYARRVZ 27 LIB140 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34087 MRPEIWAAQELDRFGDENNAYYARRVZ 27 LIB141 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34088 MRPEIWAAQELDRDGDEFNAYYARRVZ 27 LIB142 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34089 MRPEIWAAQELDRDGDEVNAYYARRVZ 27 LIB143 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34090 MRPEIWAAQELDRDGDENNAYYARRVZ 27 LIB144 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34091 MRPEIWAAQELDRNGDEFNAYYARRVZ 27 LIB145 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34092 MRPEIWAAQELDRNGDEVNAYYARRVZ 27 LIB146 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34093 MRPEIWAAQELDRNGDENNAYYARRVZ 27 LIB147 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34094 MRPEIWAAQELDRAGDEFNAYYARRVZ 27 LIB148 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34095 MRPEIWAAQELDRAGDEVNAYYARRVZ 27 LIB149 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34096 MRPEIWAAQELDRAGDENNAYYARRVZ 27 LIB150 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34097 MRPEIWAAQEIRRIGDEFNAYYARRVZ 27 LIB151 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34098 MRPEIWAAQEIRRIGDEVNAYYARRVZ 27 LIB152 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34099 MRPEIWAAQEIRRIGDENNAYYARRVZ 27 LIB153 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34100 MRPEIWAAQEIRRFGDEFNAYYARRVZ 27 LIB154 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34101 MRPEIWAAQEIRRFGDEVNAYYARRVZ 27 LIB155 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34102 MRPEIWAAQEIRRFGDENNAYYARRVZ 27 LIB156 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34103 MRPEIWAAQEIRRDGDEFNAYYARRVZ 27 LIB157 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34104 MRPEIWAAQEIRRDGDEVNAYYARRVZ 27 LIB158 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34105 MRPEIWAAQEIRRDGDENNAYYARRVZ 27 LIB159 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34106 MRPEIWAAQEIRRNGDEFNAYYARRVZ 27 LIB160 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34107 MRPEIWAAQEIRRNGDEVNAYYARRVZ 27 LIB161 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34108 MRPEIWAAQEIRRNGDENNAYYARRVZ 27 LIB162 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34109 MRPEIWAAQEIRRAGDEFNAYYARRVZ 27 LIB163 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34110 MRPEIWAAQEIRRAGDEVNAYYARRVZ 27 LIB164 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34111 MRPEIWAAQEIRRAGDENNAYYARRVZ 27 LIB165 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34112 MRPEIWAAQEIDRIGDEFNAYYARRVZ 27 LIB166 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34113 MRPEIWAAQEIDRIGDEVNAYYARRVZ 27 LIB167 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34114 MRPEIWAAQEIDRIGDENNAYYARRVZ 27 LIB168 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34115 MRPEIWAAQEIDRFGDEFNAYYARRVZ 27 LIB169 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34116 MRPEIWAAQEIDRFGDEVNAYYARRVZ 27 LIB170 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34117 MRPEIWAAQEIDRFGDENNAYYARRVZ 27 LIB171 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34118 MRPEIWAAQEIDRDGDEFNAYYARRVZ 27 LIB172 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34119 MRPEIWAAQEIDRDGDEVNAYYARRVZ 27 LIB173 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34120 MRPEIWAAQEIDRDGDENNAYYARRVZ 27 LIB174 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34121 MRPEIWAAQEIDRNGDEFNAYYARRVZ 27 LIB175 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34122 MRPEIWAAQEIDRNGDEVNAYYARRVZ 27 LIB176 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34123 MRPEIWAAQEIDRNGDENNAYYARRVZ 27 LIB177 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34124 MRPEIWAAQEIDRAGDEFNAYYARRVZ 27 LIB178 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34125 MRPEIWAAQEIDRAGDEVNAYYARRVZ 27 LIB179 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34126 MRPEIWAAQEIDRAGDENNAYYARRVZ 27 LIB180 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34127 MRPEIWAAQEFRRIGDEFNAYYARRVZ 27 LIB181 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34128 MRPEIWAAQEFRRIGDEVNAYYARRVZ 27 LIB182 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34129 MRPEIWAAQEFRRIGDENNAYYARRVZ 27 LIB183 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34130 MRPEIWAAQEFRRFGDEFNAYYARRVZ 27 LIB184 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34131 MRPEIWAAQEFRRFGDEVNAYYARRVZ 27 LIB185 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34132 MRPEIWAAQEFRRFGDENNAYYARRVZ 27 LIB186 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34133 MRPEIWAAQEFRRDGDEFNAYYARRVZ 27 LIB187 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34134 MRPEIWAAQEFRRDGDEVNAYYARRVZ 27 LIB188 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34135 MRPEIWAAQEFRRDGDENNAYYARRVZ 27 LIB189 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34136 MRPEIWAAQEFRRNGDEFNAYYARRVZ 27 LIB190 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34137 MRPEIWAAQEFRRNGDEVNAYYARRVZ 27 LIB191 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34138 MRPEIWAAQEFRRNGDENNAYYARRVZ 27 LIB192 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34139 MRPEIWAAQEFRRAGDEFNAYYARRVZ 27 LIB193 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34140 MRPEIWAAQEFRRAGDEVNAYYARRVZ 27 LIB194 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34141 MRPEIWAAQEFRRAGDENNAYYARRVZ 27 LIB195 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34142 MRPEIWAAQEFDRIGDEFNAYYARRVZ 27 LIB196 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34143 MRPEIWAAQEFDRIGDEVNAYYARRVZ 27 LIB197 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34144 MRPEIWAAQEFDRIGDENNAYYARRVZ 27 LIB198 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34145 MRPEIWAAQEFDRFGDEFNAYYARRVZ 27 LIB199 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34146 MRPEIWAAQEFDRFGDEVNAYYARRVZ 27 LIB200 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34147 MRPEIWAAQEFDRFGDENNAYYARRVZ 27 LIB201 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34148 MRPEIWAAQEFDRDGDEFNAYYARRVZ 27 LIB202 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34149 MRPEIWAAQEFDRDGDEVNAYYARRVZ 27 LIB203 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34150 MRPEIWAAQEFDRDGDENNAYYARRVZ 27 LIB204 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34151 MRPEIWAAQEFDRNGDEFNAYYARRVZ 27 LIB205 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34152 MRPEIWAAQEFDRNGDEVNAYYARRVZ 27 LIB206 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34153 MRPEIWAAQEFDRNGDENNAYYARRVZ 27 LIB207 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34154 MRPEIWAAQEFDRAGDEFNAYYARRVZ 27 LIB208 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34155 MRPEIWAAQEFDRAGDEVNAYYARRVZ 27 LIB209 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34156 MRPEIWAAQEFDRAGDENNAYYARRVZ 27 LIB210 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34157 MRPEIWAAQEARRIGDEFNAYYARRVZ 27 LIB211 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34158 MRPEIWAAQEARRIGDEVNAYYARRVZ 27 LIB212 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34159 MRPEIWAAQEARRIGDENNAYYARRVZ 27 LIB213 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34160 MRPEIWAAQEARRFGDEFNAYYARRVZ 27 LIB214 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34161 MRPEIWAAQEARRFGDEVNAYYARRVZ 27 LIB215 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34162 MRPEIWAAQEARRFGDENNAYYARRVZ 27 LIB216 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34163 MRPEIWAAQEARRDGDEFNAYYARRVZ 27 LIB217 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34164 MRPEIWAAQEARRDGDEVNAYYARRVZ 27 LIB218 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34165 MRPEIWAAQEARRDGDENNAYYARRVZ 27 LIB219 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34166 MRPEIWAAQEARRNGDEFNAYYARRVZ 27 LIB220 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34167 MRPEIWAAQEARRNGDEVNAYYARRVZ 27 LIB221 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34168 MRPEIWAAQEARRNGDENNAYYARRVZ 27 LIB222 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34169 MRPEIWAAQEARRAGDEFNAYYARRVZ 27 LIB223 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34170 MRPEIWAAQEARRAGDEVNAYYARRVZ 27 LIB224 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34171 MRPEIWAAQEARRAGDENNAYYARRVZ 27 LIB225 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34172 MRPEIWAAQEADRIGDEFNAYYARRVZ 27 LIB226 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34173 MRPEIWAAQEADRIGDEVNAYYARRVZ 27 LIB227 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34174 MRPEIWAAQEADRIGDENNAYYARRVZ 27 LIB228 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34175 MRPEIWAAQEADRFGDEFNAYYARRVZ 27 LIB229 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34176 MRPEIWAAQEADRFGDEVNAYYARRVZ 27 LIB230 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34177 MRPEIWAAQEADRFGDENNAYYARRVZ 27 LIB231 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34178 MRPEIWAAQEADRDGDEFNAYYARRVZ 27 LIB232 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34179 MRPEIWAAQEADRDGDEVNAYYARRVZ 27 LIB233 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34180 MRPEIWAAQEADRDGDENNAYYARRVZ 27 LIB234 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34181 MRPEIWAAQEADRNGDEFNAYYARRVZ 27 LIB235 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34182 MRPEIWAAQEADRNGDEVNAYYARRVZ 27 LIB236 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34183 MRPEIWAAQEADRNGDENNAYYARRVZ 27 LIB237 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34184 MRPEIWAAQEADRAGDEFNAYYARRVZ 27 LIB238 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34185 MRPEIWAAQEADRAGDEVNAYYARRVZ 27 LIB239 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34186 MRPEIWAAQEADRAGDENNAYYARRVZ 27 LIB240 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34187 MRPEIWFAQELRRIGDEFNAYYARRVZ 27 LIB241 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34188 MRPEIWFAQELRRIGDEVNAYYARRVZ 27 LIB242 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34189 MRPEIWFAQELRRIGDENNAYYARRVZ 27 LIB243 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34190 MRPEIWFAQELRRFGDEFNAYYARRVZ 27 LIB244 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34191 MRPEIWFAQELRRFGDEVNAYYARRVZ 27 LIB245 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34192 MRPEIWFAQELRRFGDENNAYYARRVZ 27 LIB246 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34193 MRPEIWFAQELRRDGDEFNAYYARRVZ 27 LIB247 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34194 MRPEIWFAQELRRDGDEVNAYYARRVZ 27 LIB248 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34195 MRPEIWFAQELRRDGDENNAYYARRVZ 27 LIB249 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34196 MRPEIWFAQELRRNGDEFNAYYARRVZ 27 LIB250 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34197 MRPEIWFAQELRRNGDEVNAYYARRVZ 27 LIB251 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34198 MRPEIWFAQELRRNGDENNAYYARRVZ 27 LIB252 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34199 MRPEIWFAQELRRAGDEFNAYYARRVZ 27 LIB253 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34200 MRPEIWFAQELRRAGDEVNAYYARRVZ 27 LIB254 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34201 MRPEIWFAQELRRAGDENNAYYARRVZ 27 LIB255 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34202 MRPEIWFAQELDRIGDEFNAYYARRVZ 27 LIB256 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34203 MRPEIWFAQELDRIGDEVNAYYARRVZ 27 LIB257 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34204 MRPEIWFAQELDRIGDENNAYYARRVZ 27 LIB258 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34205 MRPEIWFAQELDRFGDEFNAYYARRVZ 27 LIB259 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34206 MRPEIWFAQELDRFGDEVNAYYARRVZ 27 LIB260 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34207 MRPEIWFAQELDRFGDENNAYYARRVZ 27 LIB261 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34208 MRPEIWFAQELDRDGDEFNAYYARRVZ 27 LIB262 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34209 MRPEIWFAQELDRDGDEVNAYYARRVZ 27 LIB263 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34210 MRPEIWFAQELDRDGDENNAYYARRVZ 27 LIB264 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34211 MRPEIWFAQELDRNGDEFNAYYARRVZ 27 LIB265 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34212 MRPEIWFAQELDRNGDEVNAYYARRVZ 27 LIB266 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34213 MRPEIWFAQELDRNGDENNAYYARRVZ 27 LIB267 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34214 MRPEIWFAQELDRAGDEFNAYYARRVZ 27 LIB268 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34215 MRPEIWFAQELDRAGDEVNAYYARRVZ 27 LIB269 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34216 MRPEIWFAQELDRAGDENNAYYARRVZ 27 LIB270 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34217 MRPEIWFAQEIRRIGDEFNAYYARRVZ 27 LIB271 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34218 MRPEIWFAQEIRRIGDEVNAYYARRVZ 27 LIB272 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34219 MRPEIWFAQEIRRIGDENNAYYARRVZ 27 LIB273 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34220 MRPEIWFAQEIRRFGDEFNAYYARRVZ 27 LIB274 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34221 MRPEIWFAQEIRRFGDEVNAYYARRVZ 27 LIB275 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34222 MRPEIWFAQEIRRFGDENNAYYARRVZ 27 LIB276 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34223 MRPEIWFAQEIRRDGDEFNAYYARRVZ 27 LIB277 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34224 MRPEIWFAQEIRRDGDEVNAYYARRVZ 27 LIB278 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34225 MRPEIWFAQEIRRDGDENNAYYARRVZ 27 LIB279 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34226 MRPEIWFAQEIRRNGDEFNAYYARRVZ 27 LIB280 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34227 MRPEIWFAQEIRRNGDEVNAYYARRVZ 27 LIB281 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34228 MRPEIWFAQEIRRNGDENNAYYARRVZ 27 LIB282 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34229 MRPEIWFAQEIRRAGDEFNAYYARRVZ 27 LIB283 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34230 MRPEIWFAQEIRRAGDEVNAYYARRVZ 27 LIB284 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34231 MRPEIWFAQEIRRAGDENNAYYARRVZ 27 LIB285 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34232 MRPEIWFAQEIDRIGDEFNAYYARRVZ 27 LIB286 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34233 MRPEIWFAQEIDRIGDEVNAYYARRVZ 27 LIB287 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34234 MRPEIWFAQEIDRIGDENNAYYARRVZ 27 LIB288 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34235 MRPEIWFAQEIDRFGDEFNAYYARRVZ 27 LIB289 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34236 MRPEIWFAQEIDRFGDEVNAYYARRVZ 27 LIB290 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34237 MRPEIWFAQEIDRFGDENNAYYARRVZ 27 LIB291 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34238 MRPEIWFAQEIDRDGDEFNAYYARRVZ 27 LIB292 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34239 MRPEIWFAQEIDRDGDEVNAYYARRVZ 27 LIB293 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34240 MRPEIWFAQEIDRDGDENNAYYARRVZ 27 LIB294 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34241 MRPEIWFAQEIDRNGDEFNAYYARRVZ 27 LIB295 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34242 MRPEIWFAQEIDRNGDEVNAYYARRVZ 27 LIB296 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34243 MRPEIWFAQEIDRNGDENNAYYARRVZ 27 LIB297 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34244 MRPEIWFAQEIDRAGDEFNAYYARRVZ 27 LIB298 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34245 MRPEIWFAQEIDRAGDEVNAYYARRVZ 27 LIB299 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34246 MRPEIWFAQEIDRAGDENNAYYARRVZ 27 LIB300 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34247 MRPEIWFAQEFRRIGDEFNAYYARRVZ 27 LIB301 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34248 MRPEIWFAQEFRRIGDEVNAYYARRVZ 27 LIB302 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34249 MRPEIWFAQEFRRIGDENNAYYARRVZ 27 LIB303 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34250 MRPEIWFAQEFRRFGDEFNAYYARRVZ 27 LIB304 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34251 MRPEIWFAQEFRRFGDEVNAYYARRVZ 27 LIB305 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34252 MRPEIWFAQEFRRFGDENNAYYARRVZ 27 LIB306 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34253 MRPEIWFAQEFRRDGDEFNAYYARRVZ 27 LIB307 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34254 MRPEIWFAQEFRRDGDEVNAYYARRVZ 27 LIB308 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34255 MRPEIWFAQEFRRDGDENNAYYARRVZ 27 LIB309 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34256 MRPEIWFAQEFRRNGDEFNAYYARRVZ 27 LIB310 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34257 MRPEIWFAQEFRRNGDEVNAYYARRVZ 27 LIB311 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34258 MRPEIWFAQEFRRNGDENNAYYARRVZ 27 LIB312 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34259 MRPEIWFAQEFRRAGDEFNAYYARRVZ 27 LIB313 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34260 MRPEIWFAQEFRRAGDEVNAYYARRVZ 27 LIB314 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34261 MRPEIWFAQEFRRAGDENNAYYARRVZ 27 LIB315 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34262 MRPEIWFAQEFDRIGDEFNAYYARRVZ 27 LIB316 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34263 MRPEIWFAQEFDRIGDEVNAYYARRVZ 27 LIB317 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34264 MRPEIWFAQEFDRIGDENNAYYARRVZ 27 LIB318 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34265 MRPEIWFAQEFDRFGDEFNAYYARRVZ 27 LIB319 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34266 MRPEIWFAQEFDRFGDEVNAYYARRVZ 27 LIB320 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34267 MRPEIWFAQEFDRFGDENNAYYARRVZ 27 LIB321 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34268 MRPEIWFAQEFDRDGDEFNAYYARRVZ 27 LIB322 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34269 MRPEIWFAQEFDRDGDEVNAYYARRVZ 27 LIB323 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34270 MRPEIWFAQEFDRDGDENNAYYARRVZ 27 LIB324 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34271 MRPEIWFAQEFDRNGDEFNAYYARRVZ 27 LIB325 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34272 MRPEIWFAQEFDRNGDEVNAYYARRVZ 27 LIB326 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34273 MRPEIWFAQEFDRNGDENNAYYARRVZ 27 LIB327 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34274 MRPEIWFAQEFDRAGDEFNAYYARRVZ 27 LIB328 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34275 MRPEIWFAQEFDRAGDEVNAYYARRVZ 27 LIB329 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34276 MRPEIWFAQEFDRAGDENNAYYARRVZ 27 LIB330 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34277 MRPEIWFAQEARRIGDEFNAYYARRVZ 27 LIB331 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34278 MRPEIWFAQEARRIGDEVNAYYARRVZ 27 LIB332 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34279 MRPEIWFAQEARRIGDENNAYYARRVZ 27 LIB333 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34280 MRPEIWFAQEARRFGDEFNAYYARRVZ 27 LIB334 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34281 MRPEIWFAQEARRFGDEVNAYYARRVZ 27 LIB335 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34282 MRPEIWFAQEARRFGDENNAYYARRVZ 27 LIB336 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34283 MRPEIWFAQEARRDGDEFNAYYARRVZ 27 LIB337 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34284 MRPEIWFAQEARRDGDEVNAYYARRVZ 27 LIB338 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34285 MRPEIWFAQEARRDGDENNAYYARRVZ 27 LIB339 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34286 MRPEIWFAQEARRNGDEFNAYYARRVZ 27 LIB340 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34287 MRPEIWFAQEARRNGDEVNAYYARRVZ 27 LIB341 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34288 MRPEIWFAQEARRNGDENNAYYARRVZ 27 LIB342 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34289 MRPEIWFAQEARRAGDEFNAYYARRVZ 27 LIB343 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34290 MRPEIWFAQEARRAGDEVNAYYARRVZ 27 LIB344 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34291 MRPEIWFAQEARRAGDENNAYYARRVZ 27 LIB345 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34292 MRPEIWFAQEADRIGDEFNAYYARRVZ 27 LIB346 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34293 MRPEIWFAQEADRIGDEVNAYYARRVZ 27 LIB347 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34294 MRPEIWFAQEADRIGDENNAYYARRVZ 27 LIB348 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34295 MRPEIWFAQEADRFGDEFNAYYARRVZ 27 LIB349 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34296 MRPEIWFAQEADRFGDEVNAYYARRVZ 27 LIB350 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34297 MRPEIWFAQEADRFGDENNAYYARRVZ 27 LIB351 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34298 MRPEIWFAQEADRDGDEFNAYYARRVZ 27 LIB352 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34299 MRPEIWFAQEADRDGDEVNAYYARRVZ 27 LIB353 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34300 MRPEIWFAQEADRDGDENNAYYARRVZ 27 LIB354 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34301 MRPEIWFAQEADRNGDEFNAYYARRVZ 27 LIB355 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34302 MRPEIWFAQEADRNGDEVNAYYARRVZ 27 LIB356 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34303 MRPEIWFAQEADRNGDENNAYYARRVZ 27 LIB357 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34304 MRPEIWFAQEADRAGDEFNAYYARRVZ 27 LIB358 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34305 MRPEIWFAQEADRAGDEVNAYYARRVZ 27 LIB359 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mcl-1/Bcl-xL 20363230 J Mol Biol. 2010 May 21;398(5):747-62. Dutta S, Gullá S, Chen TS, Fire E, Grant RA, Keating AE. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-Xl DRAMP34306 LKlLKkLlkKLLkLL 15 Amphipathic-1d, 5D-K6L9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 35759644 J Med Chem. 2022 Jul 14;65(13):9050-9062 Ben Hur D, Kapach G, Wani NA, Kiper E, Ashkenazi M, Smollan G, Keller N, Efrati O, Shai Y. Antimicrobial Peptides against Multidrug-Resistant Pseudomonas aeruginosa Biofilm from Cystic Fibrosis Patients DRAMP34307 GYPICGESCVGGICNIPGCSCSWPVCTTN 29 Vitri B Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 20580652 Peptides. 2010 Aug;31(8):1434-40. Tang J, Wang CK, Pan X, Yan H, Zeng G, Xu W, He W, Daly NL, Craik DJ, Tan N. Isolation and characterization of cytotoxic cyclotides from Viola tricolor DRAMP34308 rlylriGrr 9 Defensin-derived D-Peptide A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 19154767 Peptides. 2009 Apr;30(4):660-8. Iwasaki T, Ishibashi J, Tanaka H, Sato M, Asaoka A, Taylor D, Yamakawa M. Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface DRAMP34309 rlrlriGrr 9 Defensin-derived D-Peptide B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 19154767 Peptides. 2009 Apr;30(4):660-8. Iwasaki T, Ishibashi J, Tanaka H, Sato M, Asaoka A, Taylor D, Yamakawa M. Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface DRAMP34310 alylairrr 9 Defensin-derived D-Peptide C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 19154767 Peptides. 2009 Apr;30(4):660-8. Iwasaki T, Ishibashi J, Tanaka H, Sato M, Asaoka A, Taylor D, Yamakawa M. Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface DRAMP34311 rlllriGrr 9 Defensin-derived D-Peptide D Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 19154767 Peptides. 2009 Apr;30(4):660-8. Iwasaki T, Ishibashi J, Tanaka H, Sato M, Asaoka A, Taylor D, Yamakawa M. Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface DRAMP34312 KLWKKWKKWLK 11 K6L2W3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30447380 Int J Antimicrob Agents. 2019 Jun;53(6):868-872. Baker KR, Jana B, Hansen AM, Vissing KJ, Nielsen HM, Franzyk H, Guardabassi L. Repurposing azithromycin and rifampicin against Gram-negative pathogens by combination with peptide potentiators DRAMP34313 GmwskilGhlir 12 Halictine-1/22, HAL-1/22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available Not available The antifungal effect of peptides from hymenoptera venom and their analogs DRAMP34314 GMWSKILGHLIK 12 Halictine-1/6, HAL-1/6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP34315 Gkwmsllkhilk 12 Halictine-2/22, HAL-2/22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP34316 fPFfNQYVXL 10 Tyrocidine A, TA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 4M6E Not available Not available Not available Linear Free Free Mix Not available Not available 29140694 J Med Chem. 2017 Dec 14;60(23):9565-9574. Cameron AJ, Edwards PJB, Harjes E, Sarojini V. Tyrocidine A Analogues Bearing the Planar d-Phe-2-Abz Turn Motif: How Conformation Impacts Bioactivity DRAMP34317 FKRiVQRiKDFlRNLV 16 D LL-37 (17-32) P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 16637646 J Am Chem Soc. 2006 May 3;128(17):5776-85. Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region DRAMP34318 vnwkkilGkiikvvk 15 Lasioglossin LL-III-D C0HK44 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available Not available The antifungal effect of peptides from hymenoptera venom and their analogs DRAMP34319 vnwkkllGkllkvvk 15 Lasioglossin LL-III/25 C0HK44 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 22100226 Peptides. 2012 Jan;33(1):18-26. Slaninová J, Mlsová V, Kroupová H, Alán L, Tůmová T, Monincová L, Borovičková L, Fučík V, Ceřovský V. Toxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells DRAMP34320 GfGmalkllkkvl 13 Macropin 1-D Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 24616110 J Pept Sci. 2014 Jun;20(6):375-84. Monincová L, Veverka V, Slaninová J, Buděšínský M, Fučík V, Bednárová L, Straka J, Ceřovský V. Structure-activity study of macropin, a novel antimicrobial peptide from the venom of solitary bee Macropis fulvipes (Hymenoptera: Melittidae) DRAMP34321 RRQRRTSKLMKRGGKLAKLAKKLAKLAK 28 DP1 peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11691780 Cancer Res. 2001 Nov 1;61(21):7709-12. Mai JC, Mi Z, Kim SH, Ng B, Robbins PD. A proapoptotic peptide for the treatment of solid tumors DRAMP34322 ILGKLLSTAWGLLSkL 16 Alyteserin-2a [A10W][N15k] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 22965637 Amino Acids. 2013 Feb;44(2):715-23. Conlon JM, Mechkarska M, Prajeep M, Arafat K, Zaric M, Lukic ML, Attoub S. Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent DRAMP34323 GFSSIFRGVAKFASKGLGKDLAKLGVDLVA 30 Esculentin-2CHa (1-30) D3UA61 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23159562 Peptides. 2013 Jan;39:95-102. Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells DRAMP34324 KFASKGLGKDLAKLGVDLVACKISKQC 27 Esculentin-2CHa (11-37) D3UA61 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23159562 Peptides. 2013 Jan;39:95-102. Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells DRAMP34325 gwgsffkkaahvgkhvgkaalthyl 25 D-Pleurocidin P81941 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Calu-3 (IC50=41.9 ± 1.8 μg/ml); HeLa (IC50=47.1 ± 2.1 μg/ml); A549 (IC50=79.3 ± 7.2 μg/ml) Not available Linear Free Amidation D HEK293: IC50=61.4 ± 3.9 µg/ml Not available 33247193 Commun Biol. 2020 Nov 27;3(1):697. Manzo G, Hind CK, Ferguson PM, Amison RT, Hodgson-Casson AC, Ciazynska KA, Weller BJ, Clarke M, Lam C, Man RCH, Shaughnessy BGO, Clifford M, Bui TT, Drake AF, Atkinson RA, Lam JKW, Pitchford SC, Page CP, Phoenix DA, Lorenz CD, Sutton JM, Mason AJ. A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy DRAMP34326 GlpvcGetcvGGtcntpGctcswpvctrn 29 D Kalata-B1 P56254 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2JUE Not available Not available Not available Linear Free Free Mix Not available Not available 21928440 Chembiochem. 2011 Nov 4;12(16):2456-62. Sando L, Henriques ST, Foley F, Simonsen SM, Daly NL, Hall KN, Gustafson KR, Aguilar MI, Craik DJ. A A Synthetic peptide mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptor DRAMP34327 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPLPFP 35 Bactenecin-7 (1-35), Bac-7 (1-35) P19661 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33036159 Int J Mol Sci. 2020 Oct 6;21(19):7367. Sola R, Mardirossian M, Beckert B, Sanghez De Luna L, Prickett D, Tossi A, Wilson DN, Scocchi M. Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens DRAMP34328 RRIRPRPPRLPRPRPRPLPFPRP 23 Bactenecin-7 (1-23) P19661 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35578204 BMC Biol. 2022 May 16;20(1):114. Koch P, Schmitt S, Heynisch A, Gumpinger A, Wüthrich I, Gysin M, Shcherbakov D, Hobbie SN, Panke S, Held M. Optimization of the antimicrobial peptide Bac7 by deep mutational scanning DRAMP34329 WaxVlL 6 Baceridin Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 24692199 Chembiochem. 2014 May 5;15(7):1021-9. Niggemann J, Bozko P, Bruns N, Wodtke A, Gieseler MT, Thomas K, Jahns C, Nimtz M, Reupke I, Brüser T, Auling G, Malek N, Kalesse M. Baceridin, a cyclic hexapeptide from an epiphytic bacillus strain, inhibits the proteasome DRAMP34330 RAGLQFPVGRLLRRLLR 17 Buforin-2 (5-13)[17-20]2 P55897 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23776609 PLoS One. 2013 Jun 11;8(6):e66084. Lim KJ, Sung BH, Shin JR, Lee YW, Kim DJ, Yang KS, Kim SC. A cancer specific cell-penetrating peptide, BR2, for the efficient delivery of an scFv into cancer cells DRAMP34331 ILPIRSLIKKLL 12 Temporin-1RNa Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23632907 World J Microbiol Biotechnol. 2013 Oct;29(10):1941-9. Li A, Zhang Y, Wang C, Wu G, Wang Z. Purification, molecular cloning, and antimicrobial activity of peptides from the skin secretion of the black-spotted frog, Rana nigromaculata DRAMP34332 FLPLKKLRFGLL 12 Temporin-1RNb Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23632907 World J Microbiol Biotechnol. 2013 Oct;29(10):1941-9. Li A, Zhang Y, Wang C, Wu G, Wang Z. Purification, molecular cloning, and antimicrobial activity of peptides from the skin secretion of the black-spotted frog, Rana nigromaculata DRAMP34333 MRKWFHNVLSSGQLLADKWPAWDYNWK 27 Pep27 [E4W][R19W][R22W][R26W] Q9S4I9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 16004618 Cancer Cell Int. 2005 Jul 11;5:21. Lee DG, Hahm KS, Park Y, Kim HY, Lee W, Lim SC, Seo YK, Choi CH. Functional and structural characteristics of anticancer peptide Pep27 analogues DRAMP34334 fPFfNQYVKL 10 Tyrocidine A1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP34335 fPWfNQYVXL 10 Tyrocidine B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 27328781 Biochimie. 2016 Nov;130:122-131. Rautenbach M, Troskie AM, Vosloo JA, Dathe ME. Antifungal membranolytic activity of the tyrocidines against filamentous plant fungi DRAMP34336 fPWfNQYVKL 10 Tyrocidine B1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP34337 fPWwNQYVXL 10 Tyrocidine C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 30301848 J Med Chem. 2017 Dec 14;60(23):9565-9574. Cameron AJ, Edwards PJB, Harjes E, Sarojini V. The Multifaceted Antibacterial Mechanisms of the Pioneering Peptide Antibiotics Tyrocidine and Gramicidin S DRAMP34338 fPWwNQYVKL 10 Tyrocidine C1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 17462586 Biochim Biophys Acta. 2007 Jun;1768(6):1488-97 Rautenbach M, Vlok NM, Stander M, Hoppe HC. Inhibition of malaria parasite blood stages by tyrocidines, membrane-active cyclic peptide antibiotics from Bacillus brevis DRAMP34339 YPLPFIP 7 Stylisin 1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19182416 Chem Pharm Bull (Tokyo). 2009 Feb;57(2):214-7. Dahiya R, Kumar A, Gupta R. Synthesis, cytotoxic and antimicrobial screening of a proline-rich cyclopolypeptide DRAMP34340 KWXWKXVKXAK 11 VA1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 23876294 Biochim Biophys Acta. 2013 Nov;1830(11):5193-203 Maurya IK, Thota CK, Sharma J, Tupe SG, Chaudhary P, Singh MK, Thakur IS, Deshpande M, Prasad R, Chauhan VS. Mechanism of action of novel Synthetic peptide dodecapeptides against Candida albicans DRAMP34341 KAXWKXVKXAK 11 VA2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 23876294 Biochim Biophys Acta. 2013 Nov;1830(11):5193-203 Maurya IK, Thota CK, Sharma J, Tupe SG, Chaudhary P, Singh MK, Thakur IS, Deshpande M, Prasad R, Chauhan VS. Mechanism of action of novel Synthetic peptide dodecapeptides against Candida albicans DRAMP34342 KWXWKXAKXAK 11 VA3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 23876294 Biochim Biophys Acta. 2013 Nov;1830(11):5193-203 Maurya IK, Thota CK, Sharma J, Tupe SG, Chaudhary P, Singh MK, Thakur IS, Deshpande M, Prasad R, Chauhan VS. Mechanism of action of novel Synthetic peptide dodecapeptides against Candida albicans DRAMP34343 QSHLSMCSVCCNCCKNYKGCGFCCRF 26 Om-hep1 (65-90), Hepcidin (65-90) G9B8P3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22051539 Comp Biochem Physiol B Biochem Mol Biol. 2012 Feb;161(2):140-7. Cai L, Cai JJ, Liu HP, Fan DQ, Peng H, Wang KJ. Recombinant medaka (Oryzias melastigmus) pro-hepcidin: Multifunctional characterization DRAMP34344 MGSSHHHHHHSSGLVPRGSHMIPVNGVTELEEAASNDTPVAARHEMSMQSWMMPNHIREKRQSHLSMCSVCCNCCKNYKGCGFCCRF 87 Recombinant Pro-Omhep1, Recombinant Hepcidin G4VXJ6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22051539 Comp Biochem Physiol B Biochem Mol Biol. 2012 Feb;161(2):140-7. Cai L, Cai JJ, Liu HP, Fan DQ, Peng H, Wang KJ. Recombinant medaka (Oryzias melastigmus) pro-hepcidin: Multifunctional characterization DRAMP34345 RPPQFTRAQWFAIQHISLNPPRSTIAMRAINNYRWRSKNQNTFLR 45 Eosinophil cationic protein (1-45) [C23,37S], RNase 3 (1-45) [C23,37S] P12724 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34346 yf 2 Cyclo(D-Tyr-D-Phe), Diketopiperazine (yf) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 30528685 Bioorg Med Chem. 2019 Jun 15;27(12):2323-2331 Simon G, Bérubé C, Voyer N, Grenier D. Anti-biofilm and anti-adherence properties of novel cyclic dipeptides against oral pathogens DRAMP34347 pF 2 Cyclo(D-Pro-L-Phe), Diketopiperazine (pF) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 31243345 J Antibiot (Tokyo). 2019 Oct;72(10):744-751. Betancur LA, Forero AM, Romero-Otero A, Sepúlveda LY, Moreno-Sarmiento NC, Castellanos L, Ramos FA. Cyclic tetrapeptides from the marine strain Streptomyces sp PNM-161a with activity against rice and yam phytopathogens DRAMP34348 PF 2 Cyclo(Pro-Phe), Diketopiperazine (PF) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25821788 Biomed Res Int. 2015;2015:197608. Vázquez-Rivera D, González O, Guzmán-Rodríguez J, Díaz-Pérez AL, Ochoa-Zarzosa A, López-Bucio J, Meza-Carmen V, Campos-García J. Cytotoxicity of cyclodipeptides from Pseudomonas aeruginosa PAO1 leads to apoptosis in human cancer cell lines DRAMP34349 VXVXXVXVXTVX 12 Ohmyungsamycin B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24266328 J Org Chem. 2013 Dec 20;78(24):12321-9. Um S, Choi TJ, Kim H, Kim BY, Kim SH, Lee SK, Oh KB, Shin J, Oh DC. Ohmyungsamycins A and B: cytotoxic and antimicrobial cyclic peptides produced by Streptomyces sp from a volcanic island DRAMP34350 LV 2 Cyclo(Leu-Val), Diketopiperazine (LV) Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30270742 Nat Prod Res. 2020 May;34(10):1461-1464 Lin WX, Xie CL, Zhou M, Xia ML, Zhou TT, Chen HF, Yang XW, Yang Q. Chemical constituents from the deep sea-derived Streptomyces xiamenensis MCCC 1A01570 and their effects on RXRα transcriptional regulation DRAMP34351 pf 2 Cyclo(D-Pro-D-Phe), Diketopiperazine (pf) Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 29439550 J Immunol Res. 2018 May 7;2018:4353580. Wang S, Huang S, Ye Q, Zeng X, Yu H, Qi D, Qiao S. Cytotoxic and Antimicrobial Compounds from the Marine-Derived Fungus, Penicillium Species DRAMP34352 AXEGSnXX 8 Phomafungin Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-Me-C16 Free Mix Not available Not available 19112025 Bioorg Med Chem. 2009 Feb 1;17(3):1361-9. Herath K, Harris G, Jayasuriya H, Zink D, Smith S, Vicente F, Bills G, Collado J, González A, Jiang B, Kahn JN, Galuska S, Giacobbe R, Abruzzo G, Hickey E, Liberator P, Xu D, Roemer T, Singh SB. Isolation, structure and biological activity of phomafungin, a cyclic lipodepsipeptide from a widespread tropical Phoma sp DRAMP34353 DKPKKKPPPPAGPPPPPPPPPGPPPPGP 28 Sus scrofa Uncharacterized protein (208-235), SP-E F1SQ50 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30046246 Infect Drug Resist. 2018 Jul 17;11:969-979. Ciociola T, Giovati L, Giovannelli A, Conti S, Castagnola M, Vitali A. The activity of a mammalian proline-rich peptide against Gram-negative bacteria, including drug-resistant strains, relies on a nonmembranolytic mode of action DRAMP34354 KPKGMTSSQWFKIQHMQPSPQASNSAMKNINKHTKRSKDLNTFLH 45 Ribonuclease 7 (1-45) [C23,37S] Q9H1E1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34355 WP 2 Cyclo(Trp-Pro), Diketopiperazine (WP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22409377 J Agric Food Chem. 2012 Apr 4;60(13):3424-31. Li XJ, Zhang Q, Zhang AL, Gao JM. Metabolites from Aspergillus fumigatus, an endophytic fungus associated with Melia azedarach, and their antifungal, antifeedant, and toxic activities DRAMP34356 WY 2 Cyclo(Trp-Tyr), Diketopiperazine (WY) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32806659 Molecules. 2020 Aug 12;25(16):3676. Liu R, Zhang H, Wu W, Li H, An Z, Zhou F. C7-Prenylation of Tryptophan-Containing Cyclic Dipeptides by 7-Dimethylallyl Tryptophan Synthase Significantly Increases the Anticancer and Antimicrobial Activities DRAMP34357 WL 2 Cyclo(Trp-Leu), Diketopiperazine (WL) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32806659 Molecules. 2020 Aug 12;25(16):3676. Liu R, Zhang H, Wu W, Li H, An Z, Zhou F. C7-Prenylation of Tryptophan-Containing Cyclic Dipeptides by 7-Dimethylallyl Tryptophan Synthase Significantly Increases the Anticancer and Antimicrobial Activities DRAMP34358 WF 2 Cyclo(Trp-Phe), Diketopiperazine (WF) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32806659 Molecules. 2020 Aug 12;25(16):3676. Liu R, Zhang H, Wu W, Li H, An Z, Zhou F. C7-Prenylation of Tryptophan-Containing Cyclic Dipeptides by 7-Dimethylallyl Tryptophan Synthase Significantly Increases the Anticancer and Antimicrobial Activities DRAMP34359 NGVQPKYRWWRWWRRWW 17 Leucrocin I RT2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30031283 Environ Toxicol Pharmacol. 2018 Sep;62:164-176. Maijaroen S, Jangpromma N, Daduang J, Klaynongsruang S. KT2 and RT2 modified antimicrobial peptides derived from Crocodylus siamensis Leucrocin I show activity against human colon cancer HCT-116 cells DRAMP34360 KESRAKKFQRQHMDSDSSPSSSSTYSNQMMRRRNMTQGRSKPVNTFVH 48 Ribonuclease pancreatic (1-48)[C26,40S] P07998 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34361 KPPQFTWAQWFETQHINMTSQQSTNAMQVINNYQRRSKNQNTFLL 45 Non-secretory ribonuclease (1-45)[C23,37S] P10153 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34362 QDGMYQRFLRQHVHPEETGGSDRYSNLMMQRRKMTLYHSKRFNTFIH 47 Ribonuclease 4 (1-47)[C25,39S] P34096 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34363 QDNSRYTHFLTQHYDAKPQGRDDRYSESIMRRRGLTSPSKDINTFIH 47 Angiogenin (1-47)[C26,39S], Ribonuclease A A1 (1-47)[C26,39S] W0UV28##P03950 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34364 WPKRLTKAHWFEIQHIQPSPLQSNRAMSGINNYTQHSKHQNTFLH 45 Ribonuclease K6 (1-45)[C23,37S] Q93091 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34365 KPKDMTSSQWFKTQHVQPSPQASNSAMSIINKYTERSKDLNTFLH 45 Ribonuclease 8 (1-45)[C23,37S] Q8TDE3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31540052 Int J Mol Sci. 2019 Sep 14;20(18):4558. Salazar VA, Arranz-Trullén J, Prats-Ejarque G, Torrent M, Andreu D, Pulido D, Boix E. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides DRAMP34366 RAGLQFPVGRVHRLLRK 17 Buforin-2 (5-21), sh-Buforin P55897 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 25891844 Biochimie. 2015 Jun;113:143-55. Libardo MD, Paul TJ, Prabhakar R, Angeles-Boza AM. Hybrid peptide ATCUN-sh-Buforin: Influence of the ATCUN charge and stereochemistry on antimicrobial activity DRAMP34367 VIHRAGLQFPVGRVHRLLRK 20 VIH-Buforin-2 (5-21), VIH-sh-Buforin P55897 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 25891844 Biochimie. 2015 Jun;113:143-55. Libardo MD, Paul TJ, Prabhakar R, Angeles-Boza AM. Hybrid peptide ATCUN-sh-Buforin: Influence of the ATCUN charge and stereochemistry on antimicrobial activity DRAMP34368 RCpGRTRQIGTIFpGRIKCRSW 22 Act Beta-defensin 2 (18-40)[C12I,G14p,P15G,C-del] P46160 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free Mix Not available Not available 25791057 Biophys Chem. 2015 Apr;199:25-33. Krishnakumari V, Nagaraj R. N-terminal fatty acylation of peptides spanning the cationic C-terminal segment of bovine ?-defensin-2 results in salt-resistant antibacterial activity DRAMP34369 GG 2 Neocryptolepine 9(GG) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear DiMIQ Free L Not available Not available 22574992 J Med Chem. 2012 Jun 14;55(11):5077-87. Sidoryk K, Switalska M, Wietrzyk J, Jaromin A, Piętka-Ottlik M, Cmoch P, Zagrodzka J, Szczepek W, Kaczmarek L, Peczyńska-Czoch W. Synthesis and biological evaluation of new amino acid and dipeptide derivatives of neocryptolepine as anticancer agents DRAMP34370 GP 2 Neocryptolepine 9(GP) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear DiMIQ Free L Not available Not available 22574992 J Med Chem. 2012 Jun 14;55(11):5077-87. Sidoryk K, Switalska M, Wietrzyk J, Jaromin A, Piętka-Ottlik M, Cmoch P, Zagrodzka J, Szczepek W, Kaczmarek L, Peczyńska-Czoch W. Synthesis and biological evaluation of new amino acid and dipeptide derivatives of neocryptolepine as anticancer agents DRAMP34371 KWKVFKKIEKMGRNIRNGIVKAGPKWKVFKKIEK 34 Cecropin B (1-24)+(1-10) P01508 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 11004545 Srisailam S, Arunkumar AI, Wang W, Yu C, Chen HM. Srisailam S, Arunkumar AI, Wang W, Yu C, Chen HM. Conformational study of a custom antibacterial peptide cecropin B1: implications of the lytic activity DRAMP34372 CVLIGQRCDNDRGPRCCSGQGNCVPLPFLGGVCAV 35 Ep-AMP1 Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found 2MFS Not available Not available Not available Linear Free Free L Not available Not available 25821084 Chembiochem. 2015 May 4;16(7):1068-77. Aboye TL, Strömstedt AA, Gunasekera S, Bruhn JG, El-Seedi H, Rosengren KJ, Göransson U. A Cactus-Derived Toxin-Like Cystine Knot Peptide with Selective Antimicrobial Activity DRAMP34373 KGK 3 C16OH-KGK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-C16 Amidation L Not available Not available 27486068 Peptides. 2016 Oct;84:58-67. Domalaon R, Findlay B, Ogunsina M, Arthur G, Schweizer F. Ultrashort cationic lipopeptides and lipopeptoids: Evaluation and mechanistic insights against epithelial cancer cells DRAMP34374 kQrWlWlW 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 11473322 Nature. 2001 Jul 26;412(6845):452-5. doi: 10.1038/35086601. Erratum in: Nature 2001 Nov 15;414(6861):329. Fernandez-Lopez S, Kim HS, Choi EC, Delgado M, Granja JR, Khasanov A, Kraehenbuehl K, Long G, Weinberger DA, Wilcoxen KM, Ghadiri MR. Antibacterial agents based on the cyclic D,L-alpha-peptide architecture DRAMP34375 ILPIIGKILSTIFGK 15 Temporin-1CEe F1AEM7 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 21303203 Zoolog Sci. 2011 Feb;28(2):112-7. Zhao J, Sun Y, Li Z, Su Q. Molecular cloning of novel antimicrobial peptide genes from the skin of the Chinese brown frog, Rana chensinensis DRAMP34376 GLLSVFKGVLKTAGKNVAKNVAGSLLDQLKCKISGGC 37 Brevinin-2CE F1AEM2##F1AEM1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24474334 Curr Microbiol. 2014 Jun;68(6):685-92 Zhang Y, Liu Y, Sun Y, Liu Q, Wang X, Li Z, Hao J. In vitro synergistic activities of antimicrobial peptide brevinin-2CE with five kinds of antibiotics against multidrug-resistant clinical isolates DRAMP34377 LLCIALRKK 9 Coprisin (22-30)[H23L] A9XFZ7 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22297233 J Microbiol Biotechnol. 2012 Jan;22(1):156-8. Kim IW, Kim SJ, Kwon YN, Yun EY, Ahn MY, Kang DC, Hwang JS. Effects of the Synthetic peptide coprisin analog peptide, CopA3 in pathogenic microorganisms and mammalian cancer cells DRAMP34378 YPFX 4 Cyclic peptide-1 Streptomyces sp. YIM67005 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24304298 Nat Prod Res. 2014;28(5):318-23 Zhou H, Yang Y, Yang X, Li W, Xiong Z, Zhao L, Xu L, Ding Z. A new cyclic tetrapeptide from an endophytic Streptomyces sp YIM67005 DRAMP34379 RRRRWWWW 8 [R4W4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36442155 J Med Chem. 2022 Dec 8;65(23):15819-15839. Mohammed EHM, Lohan S, Ghaffari T, Gupta S, Tiwari RK, Parang K. Membrane-Active Cyclic Amphiphilic Peptides: Broad-Spectrum Antibacterial Activity Alone and in Combination with Antibiotics DRAMP34380 CNGRCGGKLAKLAKKLAKLAK 21 CK21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25990455 Tumour Biol. 2015 Sep;36(10):8167-75. hang Z, Hou L, Feng L, Huang S, Luo M, Shao S, Zhang X, Gu S, Zhao X. An antimicrobial peptide containing NGR motif has potent antitumor activity against CD13 DRAMP34381 LRLKSIVSYAKKVL 14 Mastoparan-S Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25869360 Biochemistry (Mosc). 2015 Apr;80(4):433-40. Zare-Zardini H, Taheri-Kafrani A, Ordooei M, Ebrahimi L, Tolueinia B, Soleimanizadeh M. Identification and biochemical characterization of a new antibacterial and antifungal peptide derived from the insect Sphodromantis viridis DRAMP34382 KGIRGYKGGYCKGAFKQTCKCY 22 OsDef2 (16-37) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34866278 J Pept Sci. 2022 May;28(5):e3383. Mbuayama KR, Taute H, Strӧmstedt AA, Bester MJ, Gaspar ARM. Antifungal activity and mode of action of Synthetic peptide peptides derived from the tick OsDef2 defensin DRAMP34383 KGIRGYKGGYKGAFKQTKY 19 OsDef2 (16-37)[C26,34,36Del] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available Not available Antifungal activity and mode of action of Synthetic peptide peptides derived from the tick OsDef2 defensin DRAMP34384 ELLVDLL,ELLVDLL 15 Gageostatin A - Gageostatin B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-Me-C13,3-OH-DiMe-C13 Free Mix Not available Not available 24492520 Mar Drugs. 2014 Jan 31;12(2):871-85. Tareq FS, Lee MA, Lee HS, Lee JS, Lee YJ, Shin HJ. Gageostatins A-C, antimicrobial linear lipopeptides from a marine Bacillus subtilis DRAMP34385 KWKSFLKTFKSAKKTVLHTAAKAISS 26 Peptide P [L21A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: NCI-H1299 (IC50=15.6 μmol/L); A-375 (IC50=59.8 μmol/L); B16 (IC50=63.5 μmol/L); HeLa (IC50=64.7 μmol/L); MCF-7 (IC50=70.8 μmol/L); A549 (IC50=71 μmol/L); RD (IC50>83.6 μmol/L); SW1116 (IC50>83.6 μmol/L) Not available Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP34386 KWKSFLKTFKSAKKTVLHTAAKAISS 26 Peptide P [L21A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 21252288 Mol Cancer Ther. 2011 Mar;10(3):416-26. Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework DRAMP34387 GLPLCGETCVGGTCNTPGCSCGWPVCVRN 29 Cyclotide Vigno 5 Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 26751970 Fitoterapia. 2016 Mar;109:162-8 Esmaeili MA, Abagheri-Mahabadi N, Hashempour H, Farhadpour M, Gruber CW, Ghassempour A. Viola plant cyclotide vigno 5 induces mitochondria-mediated apoptosis via cytochrome C release and caspases activation in cervical cancer cells DRAMP34388 DEDDD 5 XLAsp-P1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 26952034 Arch Microbiol. 2016 Jul;198(5):473-82. Li S, Hao L, Bao W, Zhang P, Su D, Cheng Y, Nie L, Wang G, Hou F, Yang Y. A novel short anionic antibacterial peptide isolated from the skin of Xenopus laevis with broad antibacterial activity and inhibitory activity against breast cancer cell DRAMP34389 HTASDAAAAAALTAANAAAAAAASMA 26 Pa-MAP, Antifreeze peptide analogue Q03659##P04002 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27161201 Biopolymers. 2017 Mar;108(2). Vilas Boas LC, de Lima LM, Migliolo L, Mendes GD, de Jesus MG, Franco OL, Silva PA. Linear Antimicrobial Peptides With Activity Against Herpes Simplex Virus 1 and Aichi Virus DRAMP34390 GIGAVLKVLTTGLPALKSWIKRKRQQ 26 Melittin [I17K] P01501 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27011349 Colloids Surf B Biointerfaces. 2016 Jul 1;143:194-205. Wu X, Singh AK, Wu X, Lyu Y, Bhunia AK, Narsimhan G. Characterization of antimicrobial activity against Listeria and cytotoxicity of native melittin and its mutant variants DRAMP34391 IIGAVLKVLTTGLPALISWIKRKRQQ 26 Melittin [G1I] P01501 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27011349 Colloids Surf B Biointerfaces. 2016 Jul 1;143:194-205. Wu X, Singh AK, Wu X, Lyu Y, Bhunia AK, Narsimhan G. Characterization of antimicrobial activity against Listeria and cytotoxicity of native melittin and its mutant variants DRAMP34392 GWWRRTVDKVRNAGRKVAGFASKACGALGH 30 EeCentrocin 1 Chain A A0A144LUY5 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32403086 EBioMedicine. 2020 May;55:102775. Ma L, Ye X, Sun P, Xu P, Wang L, Liu Z, Huang X, Bai Z, Zhou C. Antimicrobial and antibiofilm activity of the EeCentrocin 1 derived peptide EC1-17KV via membrane disruption DRAMP34393 PMLRVRLASHLRKLRKRLLR 20 rApoE (133-150) P02649 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27028511 FEBS J. 2016 Jun;283(11):2115-31. Pane K, Sgambati V, Zanfardino A, Smaldone G, Cafaro V, Angrisano T, Pedone E, Di Gaetano S, Capasso D, Haney EF, Izzo V, Varcamonti M, Notomista E, Hancock RE, Di Donato A, Pizzo E. A new cryptic cationic antimicrobial peptide (AMP) from human apolipoprotein E with anti-bacterial activity and immunomodulatory effects on human cells DRAMP34394 LRVRLASHLRKLRKRLLR 18 ApoE (133-150) P02649 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27028511 FEBS J. 2016 Jun;283(11):2115-31. Pane K, Sgambati V, Zanfardino A, Smaldone G, Cafaro V, Angrisano T, Pedone E, Di Gaetano S, Capasso D, Haney EF, Izzo V, Varcamonti M, Notomista E, Hancock RE, Di Donato A, Pizzo E. A new cryptic cationic antimicrobial peptide (AMP) from human apolipoprotein E with anti-bacterial activity and immunomodulatory effects on human cells DRAMP34395 MPRRRRSSSRPVRRRRRPRVSRRRRRRGGRRR 32 Protamine P69015 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25192319 Mol Pharm. 2014 Oct 6;11(10):3492-502. Rapsch K, Bier FF, von Nickisch-Rosenegk M. Rational design of artificial ?-strand-forming antimicrobial peptides with biocompatible properties DRAMP34396 GMWSKIKETAMAAAKEAAKAAGKTISDMIKQ 31 Dermaseptin PD-1 A0A0X8XRJ2 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 27187467 Toxins (Basel). 2016 May 12;8(5):144. Shi D, Hou X, Wang L, Gao Y, Wu D, Xi X, Zhou M, Kwok HF, Duan J, Chen T, Shaw C. Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor DRAMP34397 GMWSKIKNAGKAAAKAAAKAAGKAALDAVSEAI 33 Dermaseptin PD-2 A0A0X8XQY5 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 27187467 Toxins (Basel). 2016 May 12;8(5):144. Shi D, Hou X, Wang L, Gao Y, Wu D, Xi X, Zhou M, Kwok HF, Duan J, Chen T, Shaw C. Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor DRAMP34398 RGSALTHLP 9 RP9 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27129462 Protein J. 2016 Jun;35(3):202-11. Theansungnoen T, Maijaroen S, Jangpromma N, Yaraksa N, Daduang S, Temsiripong T, Daduang J, Klaynongsruang S. Cationic Antimicrobial Peptides Derived from Crocodylus siamensis Leukocyte Extract, Revealing Anticancer Activity and Apoptotic Induction on Human Cervical Cancer Cells DRAMP34399 KKKFPWWWPFKKKC,KKKFPWWWPFKKKC 29 di-PST13-RK-C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 18815734 Biotechnol Lett. 2009 Feb;31(2):233-7. Yang ST, Kim JI, Shin SY. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity DRAMP34400 KKKFPWWWPFKKK,KKKFPWWWPFKKKK 28 di-PST13-RK-K Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 18815734 Biotechnol Lett. 2009 Feb;31(2):233-7. Yang ST, Kim JI, Shin SY. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity DRAMP34401 FLPAALAGIGGILGKLF 17 Temporin-SHd D4YWD0 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23116712 Biochimie. 2013 Feb;95(2):388-99. Abbassi F, Raja Z, Oury B, Gazanion E, Piesse C, Sereno D, Nicolas P, Foulon T, Ladram A. Antibacterial and leishmanicidal activities of temporin-SHd, a 17-residue long membrane-damaging peptide DRAMP34402 ffflsrif 8 Temporin-D-SHf D4YWD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34403 firslfff 8 Temporin-RI-SHf Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34404 FIRSLFFF 8 Temporin-Retro-SHf Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34405 FFFLRRIF 8 Temporin-SHf [S5R] D4YWD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34406 XFFLSRIF 8 Temporin-SHf [F1TERT BU PHE] D4YWD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34407 FXFLRRIF 8 Temporin-SHf [F2TERT BU PHE; S5R] D4YWD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26181487 ACS Chem Biol. 2015 Oct 16;10(10):2257-66. André S, Washington SK, Darby E, Vega MM, Filip AD, Ash NS, Muzikar KA, Piesse C, Foulon T, O'Leary DJ, Ladram A. Structure-Activity Relationship-based Optimization of Small Temporin-SHf Analogs with Potent Antibacterial Activity DRAMP34408 ACVNQCPDAIDRFIVKDKGCHGVEKKYYKQVYVACMNGQHLYCRTEWGGPCQL 53 Laterosporulin 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 6LWZ Not available Not available Not available Linear Free Free L Not available Not available 28422156 Sci Rep. 2017 Apr 19;7:46541. Baindara P, Gautam A, Raghava GPS, Korpole S. Anticancer properties of a defensin like class IId bacteriocin Laterosporulin10 DRAMP34409 KRFKKFFKKVKKSV,KKRLKKIFKKPMVIGVTIPF 35 Crotalicidin (1-14) + Crotalicidin (15-35) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 26465972 J Med Chem. 2015 Nov 12;58(21):8553-63. Falcao CB, Pérez-Peinado C, de la Torre BG, Mayol X, Zamora-Carreras H, Jiménez MÁ, Rádis-Baptista G, Andreu D. Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity DRAMP34410 KWRRWIRWL 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30447380 Int J Antimicrob Agents. 2019 Jun;53(6):868-872. Baker KR, Jana B, Hansen AM, Vissing KJ, Nielsen HM, Franzyk H, Guardabassi L. Repurposing azithromycin and rifampicin against Gram-negative pathogens by combination with peptide potentiators DRAMP34411 IKIPSFFrNILKKVGKEAVSLIAGALKQS 29 Pseudhymenochirin-1Pb [R8r] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 26606380 J Nat Prod. 2015 Dec 24;78(12):3041-8 Manzo G, Scorciapino MA, Srinivasan D, Attoub S, Mangoni ML, Rinaldi AC, Casu M, Flatt PR, Conlon JM. Conformational Analysis of the Host-Defense Peptides Pseudhymenochirin-1Pb and -2Pa and Design of Analogues with Insulin-Releasing Activities and Reduced Toxicities DRAMP34412 GSPE 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25988520 Mar Drugs. 2015 May 15;13(5):3029-45. Chakraborty S, Tai DF, Lin YC, Chiou TW. Antitumor and antimicrobial activity of some cyclic tetrapeptides and tripeptides derived from marine bacteria DRAMP34413 GYPFV 5 Longicalycinin A cyclic analogue 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.66 ± 0.0007 μg/mL); HT-29 (IC50=10.45 ± 0.0042 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108902. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP34414 fkklkklfsklwnwk 15 D-HPRP-A1, HPRP-A2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SGC-7901 (IC50=10.42±0.30 μM ); B16 (IC50=19.16±0.38 μM ); PC-3 (IC50=21.38±0.56 μM ); BGC-823 (IC50=8.65 ±0.38 μM ) Not available Linear Acetylation Amidation D Not available Not available 31686873 Infect Drug Resist. 2019 Oct 15;12:3227-3239. Zhu J, Huang Y, Chen M, Hu C, Chen Y. Functional Synergy Of Antimicrobial Peptides And Chlorhexidine Acetate Against Gram-Negative/Gram-Positive Bacteria And A Fungus In Vitro And In Vivo DRAMP34415 fkklkklfsklwnwk 15 D-HPRP-A1, HPRP-A2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation D Not available Not available 31686873 Infect Drug Resist. 2019 Oct 15;12:3227-3239. Zhu J, Huang Y, Chen M, Hu C, Chen Y. Functional Synergy Of Antimicrobial Peptides And Chlorhexidine Acetate Against Gram-Negative/Gram-Positive Bacteria And A Fungus In Vitro And In Vivo DRAMP34416 ADMDFTGIAESIIKKIKETNAKPPA 25 TistH Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 27267248 Toxicon. 2016 Sep 1;119:362-70. Machado RJ, Estrela AB, Nascimento AK, Melo MM, Torres-Rêgo M, Lima EO, Rocha HA, Carvalho E, Silva-Junior AA, Fernandes-Pedrosa MF. Characterization of TistH, a multifunctional peptide from the scorpion Tityus stigmurus: Structure, cytotoxicity and antimicrobial activity DRAMP34417 GrkkrrqrrrGGwmwvtnlrtd 22 TAT-RasGAP317-326 P20936##L0HA15 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 33852935 J Glob Antimicrob Resist. 2021 Jun;25:227-231. Heinonen T, Hargraves S, Georgieva M, Widmann C, Jacquier N. The antimicrobial peptide TAT-RasGAP 317-326 inhibits the formation and expansion of bacterial biofilms in vitro DRAMP34418 KWKSFLKTFKSAKkTVLHTALKAISS 26 V13K [K14k] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=15.6 ± 4.1μM ); MIA PaCa-2 (IC50=17.9 ± 2.3μM); Bxpc-3 (IC50=20.0 ± 0.8μM); HPAC (IC50=7.2 ± 5.2μM) MHC (minimal hemolytic concentration) =125μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34419 KWKSFLKTFKsAKkTVLHTALKAISS 26 V13K [S11s, K14k] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: Bxpc-3 (IC50=22.4 ± 2.3μM); HPAC (IC50=25.5 ± 0.5 μM); HeLa (IC50=30.6 ± 0.5μM ); MIA PaCa-2 (IC50=41.3 ± 2.6μM)" MHC (minimal hemolytic concentration) =125μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34420 KWKSFLKTFKSAKktVLHTALKAISS 26 V13K [K14k, T15t] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HPAC (IC50=22.5 ± 0.5μM); Bxpc-3 (IC50=24.1 ± 5.5μM); HeLa (IC50=31.6 ± 2.1μM); MIA PaCa-2 (IC50=47.1 ± 5.3μM) MHC (minimal hemolytic concentration) =250μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34421 KWKSFLKTFKsAKktVLHTALKAISS 26 V13K [S11s, K14k, T15t] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=41.1 ± 0.5μM); Bxpc-3 (IC50=45.5 ± 5.6μM); HPAC (IC50=54.2 ± 1.2μM); MIA PaCa-2 (IC50=56.8 ± 3.3μM) MHC (minimal hemolytic concentration) =250μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34422 KWKSFLKTFKSaKKTVLHTALKAISS 26 V13K [A12a] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: HPAC (IC50=15.5 ± 1.7μM); HeLa (IC50=28.8 ± 0.8 μM); MIA PaCa-2 (IC50=29.9 ± 4.8μM); Bxpc-3 (IC50=45.1 ± 1.0μM)" MHC (minimal hemolytic concentration) =125μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34423 KWKSFLKTfKSaKKTVLHTALKAISS 26 V13K [F9f, A12a] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available "Tumor cells: Bxpc-3 (IC50=125.0 ± 3.7μM); MIA PaCa-2 (IC50=38.8 ± 2.9 μM); HPAC (IC50=42.4 ± 3.0μM); HeLa (IC50=59.8 ± 0.5μM)" MHC (minimal hemolytic concentration) =250μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34424 KWKSFLKTFKSaKKTvLHTALKAISS 26 V13K [A12a, V16v] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Bxpc-3 (IC50=125.0 ± 5.9μM); HPAC (IC50=41.4 ± 1.4μM); MIA PaCa-2 (IC50=46.2 ± 3.0μM); HeLa (IC50=60.1 ± 1.2μM) MHC (minimal hemolytic concentration) >500μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34425 KWKSFLKTfKSaKKTvLHTALKAISS 26 V13K [F9f, A12a, V16v] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: Bxpc-3 (IC50=125.0 ± 1.8μM); HeLa (IC50=125.0 ± 3.4μM); MIA PaCa-2 (IC50=57.9 ± 2.8μM); HPAC (IC50=95.6 ± 1.8μM) MHC (minimal hemolytic concentration) >500μM Linear Acetylation Amidation Mix Not available Not available 29280948 Int J Mol Sci. 2017 Dec 27;19(1):67. Sun S, Zhao G, Huang Y, Cai M, Yan Q, Wang H, Chen Y. Enantiomeric Effect of d-Amino Acid Substitution on the Mechanism of Action of ?-Helical Membrane-Active Peptides DRAMP34426 XRWRWRW 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24900420 ACS Comb Sci. 2013 Nov 11;15(11):585-92. Albada HB, Prochnow P, Bobersky S, Langklotz S, Bandow JE, Metzler-Nolte N. Tuning the activity of a short arg-trp antimicrobial Peptide by lipidation of a C- or N-terminal lysine side-chain DRAMP34427 XGX 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C20 Amidation L Not available Not available 27486068 Peptides. 2016 Oct;84:58-67. Domalaon R, Findlay B, Ogunsina M, Arthur G, Schweizer F. Ultrashort cationic lipopeptides and lipopeptoids: Evaluation and mechanistic insights against epithelial cancer cells DRAMP34428 LIXFXPx 7 Cordyheptapeptide A linear Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Boc OMe Mix Not available Not available 28554994 Molecules. 2017 May 27;22(6):682. Kumar S, Dahiya R, Khokra SL, Mourya R, Chennupati SV, Maharaj S. Total Synthesis and Pharmacological Investigation of Cordyheptapeptide A DRAMP34429 XFXILxP 7 Cordyheptapeptide A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 28554994 Molecules. 2017 May 27;22(6):682. Kumar S, Dahiya R, Khokra SL, Mourya R, Chennupati SV, Maharaj S. Total Synthesis and Pharmacological Investigation of Cordyheptapeptide A DRAMP34430 XFXVLxP 7 Cordyheptapeptide D Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22642609 J Nat Prod. 2012 Jun 22;75(6):1215-9. Chen Z, Song Y, Chen Y, Huang H, Zhang W, Ju J. Cyclic heptapeptides, cordyheptapeptides C-E, from the marine-derived fungus Acremonium persicinum SCSIO 115 and their cytotoxic activities DRAMP34431 XFXXLxP 7 Cordyheptapeptide E Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22642609 J Nat Prod. 2012 Jun 22;75(6):1215-9. Chen Z, Song Y, Chen Y, Huang H, Zhang W, Ju J. Cyclic heptapeptides, cordyheptapeptides C-E, from the marine-derived fungus Acremonium persicinum SCSIO 115 and their cytotoxic activities DRAMP34432 XAaQyI 6 Fusaripeptide A Not available Not found Fusarium  Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: L5178Y (IC50=5.71μM); PC12 (IC50=9.55μM) Not available Linear 3-OH-4-Me-C15 Free X=Allo-Thr Mix Not available Not available 28446036 J Asian Nat Prod Res. 2018 Jan;20(1):75-85. Ibrahim SRM, Abdallah HM, Elkhayat ES, Al Musayeib NM, Asfour HZ, Zayed MF, Mohamed GA. Fusaripeptide A: new antifungal and anti-malarial cyclodepsipeptide from the endophytic fungus Fusarium sp DRAMP34433 GLGKAQCAALWLQCASGGTIGXGGGAVACQNYRQFCR 37 Sublancin 168 A0A1J5X031##P68578##P68577 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2MIJ Not available Not available Not available Linear Free Free L Not available Not available 29854837 J Immunol Res. 2018 May 7;2018:4353580 Wang S, Huang S, Ye Q, Zeng X, Yu H, Qi D, Qiao S. Prevention of Cyclophosphamide-Induced Immunosuppression in Mice with the Antimicrobial Peptide Sublancin DRAMP34434 CKILSKTIKCRIPCGRRKEY 20 PTN (42-61) C3Z937 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30096337 Dev Comp Immunol. 2018 Dec;89:31-43. Gao Z, Qu B, Yao L, Ma Z, Cui P, Zhang S. Identification and Characterization of Novel Antimicrobial Peptide from Hippocampus comes by In Silico and Experimental Studies DRAMP34435 KRCKNKMEGDDVAVSGRGARKAAKK 25 PTNr1 (42-66) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30096337 Dev Comp Immunol. 2018 Dec;89:31-43. Gao Z, Qu B, Yao L, Ma Z, Cui P, Zhang S. Identification and Characterization of Novel Antimicrobial Peptide from Hippocampus comes by In Silico and Experimental Studies DRAMP34436 EEEEEEEEEEKKRLKKIFKKPMVIGVTIPF 30 E10-Ctn[15-34] U5KJM4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30042491 Sci Rep. 2018 Jul 24;8(1):11127. Júnior NGO, Cardoso MH, Cândido ES, van den Broek D, de Lange N, Velikova N, Kleijn JM, Wells JM, Rezende TMB, Franco OL, de Vries R. An acidic model pro-peptide affects the secondary structure, membrane interactions and antimicrobial activity of a crotalicidin fragment DRAMP34437 ALWKSLLKNVGKAAGKAALNAVTDMVNQ 28 Dermaseptin DRS-DU-1 A0A345FZ90 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: PC-3 (IC50=3.21μM); H157 (IC50=8.43μM) Not available Linear Free Amidation L Not available Not available 30258724 PeerJ. 2018 Sep 19;6:e5635. Zhu H, Ding X, Li W, Lu T, Ma C, Xi X, Wang L, Zhou M, Burden R, Chen T.  Discovery of two skin-derived dermaseptins and design of a TAT-fusion analogue with broad-spectrum antimicrobial activity and low cytotoxicity on healthy cells DRAMP34438 GRKKRRQRRRGALWKSLLKNVGKA 24 TAT(48-57)-G-Dermaseptin DRS-DU-1 (1-13), DP-2 P04610 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H157 (IC50=21.6μM); PC-3 (IC50=6.75μM) Not available Linear Free Amidation L Not available Not available 30258724 PeerJ. 2018 Sep 19;6:e5635. Zhu H, Ding X, Li W, Lu T, Ma C, Xi X, Wang L, Zhou M, Burden R, Chen T.  Discovery of two skin-derived dermaseptins and design of a TAT-fusion analogue with broad-spectrum antimicrobial activity and low cytotoxicity on healthy cells DRAMP34439 AAAARRRR 8 [A4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34440 YYYYRRRR 8 [Y4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34441 FFFFRRRR 8 [F4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34442 FFFFRRRR 8 [F4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34443 IIIIRRRR 8 [I4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34444 LLLLRRRR 8 [L4R4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents DRAMP34445 LYPFA 5 Longicalycinin A cyclic analogue 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=8.76 ± 0.0035 μg/mL); HT-29 (IC50=12.33 ± 0 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108902. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP34446 GLRKRLRKFRNK 12 CAP7 (1-12), sC18* P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30389988 Sci Rep. 2018 Nov 2;8(1):16279. Horn M, Neundorf I. Design of a novel cell-permeable chimeric peptide to promote wound healing DRAMP34447 KCVRQNNKRVCK 12 Cathelicidin (135-146), Tylotoin W0FJD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30389988 Sci Rep. 2018 Nov 2;8(1):16279. Horn M, Neundorf I. Design of a novel cell-permeable chimeric peptide to promote wound healing DRAMP34448 KCVRQNNKRVCKGLRKRLRKFRNK 24 Cathelicidin (135-146)-CAP7 (1-12), Tylotoin-sC18* W0FJD1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30389988 Sci Rep. 2018 Nov 2;8(1):16279. Horn M, Neundorf I. Design of a novel cell-permeable chimeric peptide to promote wound healing DRAMP34449 GLRKRLRKFRNKIKEK,GLRKRLRKFRNKIKEK 33 [CAP7 (1-16)]2, (sC18)2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 23209513 Beilstein J Org Chem. 2012;8:1788-97. Hoyer J, Schatzschneider U, Schulz-Siegmund M, Neundorf I. Dimerization of a cell-penetrating peptide leads to enhanced cellular uptake and drug delivery DRAMP34450 GLLEALAELLEGLRKRLRKFRNKIKEK 27 Hemagglutinin (347-367)[E4G,E7A]-CAP7 (1-16); N-E5L-sC18 P25230 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 27713223 Pharmaceuticals (Basel). 2009 Sep 25;2(2):49-65. Neundorf I, Rennert R, Hoyer J, Schramm F, Löbner K, Kitanovic I, Wölfl S. Fusion of a Short HA2-Derived Peptide Sequence to Cell-Penetrating Peptides Improves Cytosolic Uptake, but Enhances Cytotoxic Activity DRAMP34451 GLLEALAELLEGRKKRRQRRRPPQ 24 Hemagglutinin (347-367)[E4G,E7A]-Tat (48-60); N-E5L-Tat (48-60) D2DUQ8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 27713223 Pharmaceuticals (Basel). 2009 Sep 25;2(2):49-65. Neundorf I, Rennert R, Hoyer J, Schramm F, Löbner K, Kitanovic I, Wölfl S. Fusion of a Short HA2-Derived Peptide Sequence to Cell-Penetrating Peptides Improves Cytosolic Uptake, but Enhances Cytotoxic Activity DRAMP34452 GLLEALAELLEKFHTFPQTAIGVGAP,KKRKAPKKKRKFA 40 Hemagglutinin (347-367)[E4G,E7A]-Calcitonin(18-32) - k7; N-E5L-hCT(18-32)-k7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 27713223 Pharmaceuticals (Basel). 2009 Sep 25;2(2):49-65. Neundorf I, Rennert R, Hoyer J, Schramm F, Löbner K, Kitanovic I, Wölfl S. Fusion of a Short HA2-Derived Peptide Sequence to Cell-Penetrating Peptides Improves Cytosolic Uptake, but Enhances Cytotoxic Activity DRAMP34453 ALWKTMLKKLGTVALHAGKAALGAVADTISQ 31 Dermaseptin-PS1, Dermaseptin cDNA A0A284T6N8 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30461197 J Cell Mol Med. 2019 Feb;23(2):1300-1312. Long Q, Li L, Wang H, Li M, Wang L, Zhou M, Su Q, Chen T, Wu Y. Novel peptide dermaseptin-PS1 exhibits anticancer activity via induction of intrinsic apoptosis signalling DRAMP34454 PKILNKILGKILRLAAAFK 19 PKIL+L39e (4-18)[P6I,K10I], PaDBS1R1 Q8ZTX6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30463701 Biochim Biophys Acta Biomembr. 2019 Jan;1861(1):178-190. Irazazabal LN, Porto WF, Fensterseifer ICM, Alves ESF, Matos CO, Menezes ACS, Felício MR, Gonçalves S, Santos NC, Ribeiro SM, Humblot V, Lião LM, Ladram A, Franco OL. Fast and potent bactericidal membrane lytic activity of PaDBS1R1, a novel cationic antimicrobial peptide DRAMP34455 LVPFIGRTLGGLLARF 16 RTemp_4.3_210 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30578771 Biochim Biophys Acta Biomembr. 2019 Mar 1;1861(3):651-659. Rončević T, Krce L, Gerdol M, Pacor S, Benincasa M, Guida F, Aviani I, Čikeš-Čulić V, Pallavicini A, Maravić A, Tossi A. Membrane-active antimicrobial peptide identified in Rana arvalis by targeted DNA sequencing DRAMP34456 LLGAALSALSSVIPSVISWFQK 22 RArv_10.1_19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30578771 Biochim Biophys Acta Biomembr. 2019 Mar 1;1861(3):651-659. Rončević T, Krce L, Gerdol M, Pacor S, Benincasa M, Guida F, Aviani I, Čikeš-Čulić V, Pallavicini A, Maravić A, Tossi A. Membrane-active antimicrobial peptide identified in Rana arvalis by targeted DNA sequencing DRAMP34457 rGDFV 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 1718779 FEBS Lett. 1991 Oct 7;291(1):50-4. Aumailley M, Gurrath M, Müller G, Calvete J, Timpl R, Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 DRAMP34458 SKWQHQQDSCRKQLQGVNLTPCEKHIMEKIQGRGDDDDDDDDD 43 Lunasin Not available Not found Glycine max Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 10331812 Nat Biotechnol. 1999 May;17(5):495-500. Galvez AF, de Lumen BO. A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells. DRAMP34459 CGESCVWIPCISSAIGCSCKSKVCYRNGIP 30 Cycloviolacin O2 Not available Not found Viola odorata Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 10600388 J Mol Biol. 1999 Dec 17;294(5):1327-36. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. DRAMP34460 TvXXX,XvXXX 11 Actinomycin Z1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 10757717 J Nat Prod. 2000 Mar;63(3):352-6. Lackner H, Bahner I, Shigematsu N, Pannell LK, Mauger AB. Structures of five components of the actinomycin Z complex from Streptomyces fradiae, two of which contain 4-chlorothreonine DRAMP34461 RQIKIWFQNRRMKWK 15 pAntp (43-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34462 CHTNGGYCVRAICPPSARRPGSCFPEKNPCCKYM 34 mBD-2 Not available Not found Mus musculus Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 10922379 J Biol Chem. 2000 Oct 27;275(43):33314-20. Jia HP, Wowk SA, Schutte BC, Lee SK, Vivado A, Tack BF, Bevins CL, McCray PB Jr. A novel murine beta -defensin expressed in tongue, esophagus, and trachea. DRAMP34463 FDIVKKVVGTIAGL 14 K7 P82391 Not found Litoria aurea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 10951191 Eur J Biochem. 2000 Sep;267(17):5330-41. Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. DRAMP34464 MDAQTRRRERRAEKQAQWKAANGC 24 LAMBDA N (1-22) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Conjugation with fluorescein by C-terminal Gly Cys amide L Not available Not available 11084031 J Biol Chem. 2001 Feb 23;276(8):5836-40. Futaki S, Suzuki T, Ohashi W, Yagami T, Tanaka S, Ueda K, Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. DRAMP34465 RKKRRQRR 8 Tat (49-56) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34466 TSPLNIHNGQKL 12 HN-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Not available fluorescein/ FITC/texas red Amidation L Not available Not available 11118031 Cancer Res. 2000 Dec 1;60(23):6551-6. Hong FD, Clayman GL. Isolation of a peptide for targeted drug delivery into human head and neck solid tumors. DRAMP34467 CELDENNTPMC 11 FSEC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34468 XXPXxX 6 Apratoxin A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 11389621 J Am Chem Soc. 2001 Jun 13;123(23):5418-23. Luesch H, Yoshida WY, Moore RE, Paul VJ, Corbett TH. Total structure determination of apratoxin A, a potent novel cytotoxin from the marine cyanobacterium Lyngbya majuscula DRAMP34469 IFSPIPL 7 Stylopeptide 1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 11473416 J Nat Prod. 2001 Jul;64(7):883-91. Pettit GR, Lippert JW 3rd, Taylor SR, Tan R, Williams MD. Synthesis of phakellistatin 11: a micronesia (Chuuk) marine sponge cyclooctapeptide DRAMP34470 GIGVLLSAGKAALKGLAKVLAEKYAN 26 maximin4 Not available Not found Bombina maxima Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 11835991 Peptides. 2002 Mar;23(3):427-35. Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. DRAMP34471 AKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKK 34 F3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 12032302 Proc Natl Acad Sci U S A. 2002 May 28;99(11):7444-9. Porkka K, Laakkonen P, Hoffman JA, Bernasconi M, Ruoslahti E. A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo. DRAMP34472 ALWKTLLKKVLKAPKKKRKV 20 S4(13)-PV Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34473 VQRKRQKLMP 10 NF-kB Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 12204694 Chem Biol. 2002 Aug;9(8):943-8. Ragin AD, Morgan RA, Chmielewski J. Cellular import mediated by nuclear localization signal Peptide sequences. DRAMP34474 LXIGxP 6 Tasiamide Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 2-OH-ME-C5 OMe Mix Not available Not available 12350160 J Nat Prod. 2002 Sep;65(9):1336-9. Williams PG, Yoshida WY, Moore RE, Paul VJ. Tasiamide, a cytotoxic peptide from the marine cyanobacterium Symploca sp DRAMP34475 GRKKRRQRRRPP 12 Tat (48-59) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Free L Not available Not available 12411431 J Biol Chem. 2003 Jan 3;278(1):585-90. Richard JP, Melikov K, Vives E, Ramos C, Verbeure B, Gait MJ, Chernomordik LV, Lebleu B. Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. DRAMP34476 RGGRLSYSRRRFSTSTGR 18 SynB1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NBD and TAMRA Free L Not available Not available 12783857 J Biol Chem. 2003 Aug 15;278(33):31192-201. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. DRAMP34477 RHIKIWFQNRRMKWKK 16 PDX -1-PTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Free L Not available Not available 12829640 Diabetes. 2003 Jul;52(7):1732-7. Noguchi H, Kaneto H, Weir GC, Bonner-Weir S. PDX-1 protein containing its own antennapedia-like protein transduction domain can transduce pancreatic duct and islet cells. DRAMP34478 KLLKKPLKLKL 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 14514057 Biotechnol Lett. 2003 Aug;25(16):1305-10. Park Y, Lee DG, Hahm KS. Antibiotic activity of Leu-Lys rich model peptides DRAMP34479 XFXFLPX 7 Scytalidamide A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 14604342 J Org Chem. 2003 Nov 14;68(23):8767-73. Tan LT, Cheng XC, Jensen PR, Fenical W. Scytalidamides A and B, new cytotoxic cyclic heptapeptides from a marine fungus of the genus Scytalidium DRAMP34480 MFTLKKSLLLLFFLGTISSSLCEQERDSDDEDQGEVTEQVVKRLVRGCWTKSYPPKPCFVRG 62 Peptide leucine arginine Q90WP7##P82110 Not found Lithobates pipiens Antimicrobial, Anticancer Not found Not found Not found 2M3N Not available Not available Not available Free Free L Not available Not available 14636071 Biochemistry. 2003 Dec 2;42(47):14023-35. Mangoni ML, Papo N, Mignogna G, Andreu D, Shai Y, Barra D, Simmaco M. Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity. DRAMP34481 VRLPPP 6 PolyP 1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34482 VCIIIIC 7 Microcionamide A Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free PEA L Not available Not available 15176844 J Org Chem. 2004 Jun 11;69(12):4170-6. Davis RA, Mangalindan GC, Bojo ZP, Antemano RR, Rodriguez NO, Concepcion GP, Samson SC, de Guzman D, Cruz LJ, Tasdemir D, Harper MK, Feng X, Carter GT, Ireland CM. Microcionamides A and B, bioactive peptides from the philippine sponge Clathria (Thalysias) abietina DRAMP34483 CGNKRTRGC 9 Lyp-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 15197262 Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9381-6. Laakkonen P, Akerman ME, Biliran H, Yang M, Ferrer F, Karpanen T, Hoffman RM, Ruoslahti E. Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells. DRAMP34484 GLFDIVKKVVGTIAGL 16 Aurein-2.4 P82391 Not found Litoria aurea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 15203252 Peptides. 2004 Jun;25(6):1035-54. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. DRAMP34485 HHPHG 5 HHPHG Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15313924 Cancer Res. 2004 Aug 15;64(16):5812-7 Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities. DRAMP34486 HHPHGHHPHGHHPHG 15 (HHPHG)3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Acetylation L Not available Not available 15313924 Cancer Res. 2004 Aug 15;64(16):5812-7 Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities. DRAMP34487 HF 2 Cyclo(His-Phe) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15324483 J Pharm Pharmacol. 2004 Sep;56(9):1143-53. McCleland K, Milne PJ, Lucieto FR, Frost C, Brauns SC, Van De Venter M, Du Plessis J, Dyason K. An investigation into the biological activity of the selected histidine-containing diketopiperazines cyclo(His-Phe) and cyclo(His-Tyr) DRAMP34488 GPFYVI 6 Dianthin C Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15387653 J Nat Prod. 2004 Sep;67(9):1522-7 Hsieh PW, Chang FR, Wu CC, Wu KY, Li CM, Chen SL, Wu YC. New cytotoxic cyclic peptides and dianthramide from Dianthus superbus DRAMP34489 AAWIPPG 7 Cherimolacyclopeptide C Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15387664 J Nat Prod. 2004 Sep;67(9):1577-9. Wélé A, Zhang Y, Ndoye I, Brouard JP, Pousset JL, Bodo B. A cytotoxic cyclic heptapeptide from the seeds of Annona cherimola DRAMP34490 RKKRRRESRKKRRRES 16 DPV3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34491 AXQNMEILEXTPLTXVX 17 Dermaseptin-PH Not available Not found Anabaena laxa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15875779 In Vivo. 2005 May-Jun;19(3):577-82. Gbankoto A, Vigo J, Dramane K, Banaigs B, Aina E, Salmon JM. Cytotoxic effect of Laxaphycins A and B on human lymphoblastic cells (CCRF-CEM) using digitised videomicrofluorometry. DRAMP34492 RQIKIWFQNRRMKWKKTYADFIASGRTGRRNAI 33 pAntp–PKI Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 15937518 Br J Pharmacol. 2005 Aug;145(8):1093-102. Jones SW, Christison R, Bundell K, Voyce CJ, Brockbank SM, Newham P, Lindsay MA. Characterisation of cell-penetrating peptide-mediated peptide delivery. DRAMP34493 fXXXXXNfPPR 11 Koshikamide A2 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear MeOAc Free Mix Not available Not available 16041137 Biosci Biotechnol Biochem. 2005 Jul;69(7):1318-22. Araki T, Matsunaga S, Fusetani N. Koshikamide A2, a cytotoxic linear undecapeptide isolated from a marine sponge of Theonella sp DRAMP34494 YTAIAWVKAFIRKLRK 16 YTA2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 16376307 Biochem Pharmacol. 2006 Feb 14;71(4):416-25. Lindgren M, Rosenthal-Aizman K, Saar K, Eiríksdóttir E, Jiang Y, Sassian M, Ostlund P, Hällbrink M, Langel U. Overcoming methotrexate resistance in breast cancer tumour cells by the use of a new cell-penetrating peptide. DRAMP34495 GIPCGESCVWIPCISSAIGCSCXSXVCYRN 30 [Lys(Ac)]2cyO2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50=2.3(2.0-2.5)μM) Not available Linear Free Free X=Lys(Ac)2 L Not available Not available 16389447 Cell Mol Life Sci. 2006 Jan;63(2):235-45. Herrmann A, Svangård E, Claeson P, Gullbo J, Bohlin L, Göransson U. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2 DRAMP34496 GIPCGESCVWIPCISSAIGCSCKSKVCYXN 30 [Arg(CHD)]cyO2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50=0.95(0.82-1.1)μM) Not available Free Free X=ARG(CHD) L Not available Not available 16389447 Cell Mol Life Sci. 2006 Jan;63(2):235-45. Herrmann A, Svangård E, Claeson P, Gullbo J, Bohlin L, Göransson U. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2 DRAMP34497 KSGIACFL 8 TRAIL51-58 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34498 VNADIKATTVFGGKYVSLTTP 21 Inv1, rMce1a (1-21) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34499 FKRIVQRIKDFLX 13 Synthetic Ll-37 Not available Not found Homo sapiens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 16637646 J Am Chem Soc. 2006 May 3;128(17):5776-85. Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. DRAMP34500 XXVXXV 6 Aurilide C Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 16643028 J Nat Prod. 2006 Apr;69(4):572-5. Han B, Gross H, Goeger DE, Mooberry SL, Gerwick WH. Aurilides B and C, cancer cell toxins from a Papua New Guinea collection of the marine cyanobacterium Lyngbya majuscula DRAMP34501 NQL 3 N-Octanoyl Fellutamide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C8 Free L Not available Not available 16697191 Bioorg Med Chem Lett. 2006 Jul 15;16(14):3855-8. Schneekloth JS Jr, Sanders JL, Hines J, Crews CM. Neurotrophic peptide aldehydes: solid phase synthesis of fellutamide B and a simplified analog DRAMP34502 YRXG 4 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Not available DRAMP34503 HG 2 Cyclo(His-Gly) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 16797105 Peptides. 2006 Nov;27(11):2706-14. Lucietto FR, Milne PJ, Kilian G, Frost CL, Van De Venter M. The biological activity of the histidine-containing diketopiperazines cyclo(His-Ala) and cyclo(His-Gly) DRAMP34504 MLLLTRRRST 10 BagP Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation or Conjugation with TMR Free L Not available Not available 16808988 Peptides. 2006 Nov;27(11):2661-9. Niarchos DK, Perez SA, Papamichail M. Characterization of a novel cell penetrating peptide derived from Bag-1 protein. DRAMP34505 VRRFKWWWKFLRR 13 Tritrpticin [P5,9K] P51524 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=24μM) Not available Linear Free Amidation L Not available Not available 17059217 Biochemistry. 2006 Oct 31;45(43):13007-17. Zhu WL, Lan H, Park Y, Yang ST, Kim JI, Park IS, You HJ, Lee JS, Park YS, Kim Y, Hahm KS, Shin SY. Effects of Pro --> peptoid residue substitution on cell selectivity and mechanism of antibacterial action of tritrpticin-amide antimicrobial peptide DRAMP34506 CTTHWGFTLC 10 cyclic decapeptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 17121909 Mol Cancer Ther. 2006 Nov;5(11):2624-33. Cai W, Rao J, Gambhir SS, Chen X. How molecular imaging is speeding up antiangiogenic drug development DRAMP34507 YLKNYRIATFKNWPF 15 msurvivin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 17142738 J Immunol. 2006 Dec 15;177(12):8410-21. Charalambous A, Oks M, Nchinda G, Yamazaki S, Steinman RM. Dendritic cell targeting of survivin protein in a xenogeneic form elicits strong CD4 DRAMP34508 GPFHFYQFLFPPV 13 435B peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Free L Not available Not available 17268054 Biol Pharm Bull. 2007 Feb;30(2):218-23. Kamada H, Okamoto T, Kawamura M, Shibata H, Abe Y, Ohkawa A, Nomura T, Sato M, Mukai Y, Sugita T, Imai S, Nagano K, Tsutsumi Y, Nakagawa S, Mayumi T, Tsunoda S. Creation of novel cell-penetrating peptides for intracellular drug delivery using systematic phage display technology originated from Tat transduction domain. DRAMP34509 AAXGVL 6 Emericellamide B Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 17323993 J Nat Prod. 2007 Apr;70(4):515-20. Oh DC, Kauffman CA, Jensen PR, Fenical W. Induced production of emericellamides A and B from the marine-derived fungus Emericella sp in competing co-culture DRAMP34510 LIRLWSHLIHIWFQNRRLKWKKK 23 EB-1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 17463227 FASEB J. 2007 Sep;21(11):2664-71. Lundberg P, El-Andaloussi S, Sütlü T, Johansson H, Langel U. Delivery of short interfering RNA using endosomolytic cell-penetrating peptides. DRAMP34511 MVTVLFRRLRIRRACGPPRVRV 22 M918 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 17622242 Mol Ther. 2007 Oct;15(10):1820-6. El-Andaloussi S, Johansson HJ, Holm T, Langel U. A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids. DRAMP34512 MVTVLFRRLRIRRACGPPRVRV 22 M918 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 17622242 Mol Ther. 2007 Oct;15(10):1820-6. El-Andaloussi S, Johansson HJ, Holm T, Langel U. A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids. DRAMP34513 vrlpppvrlpppvrlppp 18 D form of Sweat Arrow Protein (SAP) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free D Not available Not available 17635150 Biochem Soc Trans. 2007 Aug;35(Pt 4):794-6. Pujals S, Sabidó E, Tarragó T, Giralt E. all-D proline-rich cell-penetrating peptides: a preliminary in vivo internalization study. DRAMP34514 CNSCWSDK 8 TRAIL227–234[R1C] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34515 GlXGVY 6 1962A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 17944538 J Nat Prod. 2007 Nov;70(11):1696-9. Huang H, She Z, Lin Y, Vrijmoed LL, Lin W. Cyclic peptides from an endophytic fungus obtained from a mangrove leaf (Kandelia candel) DRAMP34516 MVRRFLVTLRIRRACGPPRVRV 22 ARF(1-22) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p14ARF protein. DRAMP34517 GYVPLWP 7 Segetalin E Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18087804 Arch Pharm Res. 2007 Nov;30(11):1380-6. Dahiya R, Kaur K. Synthetic peptide and biological studies on natural cyclic heptapeptide: segetalin E DRAMP34518 LLPFPYPTPF 10 Stylopeptide 2 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18197605 J Nat Prod. 2008 Mar;71(3):453-6 Brennan MR, Costello CE, Maleknia SD, Pettit GR, Erickson KL. Stylopeptide 2, a proline-rich cyclodecapeptide from the sponge Stylotella sp DRAMP34519 AFPGLSF 7 Segetalin D Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18323244 Acta Pol Pharm. 2007 Nov-Dec;64(6):509-16 Dahiya R. Synthesis of a phenylalanine-rich peptide as potential anthelmintic and cytotoxic agent DRAMP34520 XxXxXxXx 8 Bassianolide Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=MeLeu; x=D-HIV, 2-d-hydroxyisovaleric acid Mix Not available Not available 18375793 BCC1067. Microbiology (Reading). 2008 Apr;154(Pt 4):995-1006. Jirakkakul J, Punya J, Pongpattanakitshote S, Paungmoung P, Vorapreeda N, Tachaleat A, Klomnara C, Tanticharoen M, Cheevadhanarak S. Identification of the nonribosomal peptide synthetase gene responsible for bassianolide synthesis in wood-decaying fungus Xylaria sp BCC1067 DRAMP34521 VG 2 Cyclo(Val-Gly), Diketopiperazine (VG) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP34522 KLKNFAKGVAQSLLNKASCKLSGQC 25 Brevinin 2R P40841##P85095 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18494941 J Cell Mol Med. 2008 Jun;12(3):1005-22. Ghavami S, Asoodeh A, Klonisch T, Halayko AJ, Kadkhoda K, Kroczak TJ, Gibson SB, Booy EP, Naderi-Manesh H, Los M. Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway DRAMP34523 TPFVXV 6 Mollamide B Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18543965 J Nat Prod. 2008 Jun;71(6):941-5. Donia MS, Wang B, Dunbar DC, Desai PV, Patny A, Avery M, Hamann MT. Mollamides B and C, Cyclic hexapeptides from the indonesian tunicate Didemnum molle. DRAMP34524 vTVvpXxxxvFXV 13 Kahalalide F Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5-ME-C6 Free Mix Not available Not available 18672864 J Med Chem. 2008 Aug 28;51(16):4920-31. Jiménez JC, López-Macià A, Gracia C, Varón S, Carrascal M, Caba JM, Royo M, Francesch AM, Cuevas C, Giralt E, Albericio F. Structure-activity relationship of kahalalide F Synthetic peptide analogues DRAMP34525 AAPFLECQGRQGTCHFFAN 19 Tetrastatin-3 Not available Not found Homo sapiens (α4 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34526 MAFLKKSLFLVLFLALVPLSICEEKKSEEENEEKQEDDQSEEKRGLVTSLIKGAGKLLGGLFGSVTGGQS 70 Dermaseptin-like PBN2 Q800R4 Not found Phyllomedusa bicolor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18929530 Biochim Biophys Acta. 2009 Aug;1788(8):1537-50. Nicolas P, El Amri C. The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides. DRAMP34527 KSCCKNTTGRNIYNTCRFAGGSRERCAKLSGCKIISASTCPSDYPK 46 Viscotoxin B2 Not available Not found Viscum album Antimicrobial, Anticancer Not found Not found Not found 1ORL Not available Not available Not available Free Free L Not available Not available 18957441 Nucleic Acids Res. 2009 Jan;37(Database issue):D933-7 Wang G, Li X, Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. DRAMP34528 GSGKKGGKKHCQKY 14 (42-38)-(9-1) Crot Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 18983137 J Med Chem. 2008 Nov 27;51(22):7041-4. Rádis-Baptista G, de la Torre BG, Andreu D. A novel cell-penetrating peptide sequence derived by structural minimization of a snake toxin exhibits preferential nucleolar localization. DRAMP34529 XXPXXV 6 Hantupeptin A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19093843 J Nat Prod. 2009 Jan;72(1):29-32. Tripathi A, Puddick J, Prinsep MR, Lee PP, Tan LT. Hantupeptin A, a cytotoxic cyclic depsipeptide from a Singapore collection of Lyngbya majuscula DRAMP34530 AFXGVL 6 Arenamide B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19117399 J Nat Prod. 2009 Mar 27;72(3):396-402. Asolkar RN, Freel KC, Jensen PR, Fenical W, Kondratyuk TP, Park EJ, Pezzuto JM. Arenamides A-C, cytotoxic NFkappaB inhibitors from the marine actinomycete Salinispora arenicola DRAMP34531 CGETCTLGTCYTAGCSCSWPVCTRNGVPI 29 P58451 Not found Antimicrobial, Anticancer Not found Not found Not found 3E4H Not available Not available Not available Free Free L Not available Not available 19211551 J Biol Chem. 2009 Apr 17;284(16):10672-83. Wang CK, Hu SH, Martin JL, Sjögren T, Hajdu J, Bohlin L, Claeson P, Göransson U, Rosengren KJ, Tang J, Tan NH, Craik DJ. Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold. DRAMP34532 xVXvxVXvxVXv 12 Bacillistatin 2 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x(1/9)=2R-hydroxy-3S-methyl-valeryl-R-valine; x(5)=2R-hydroxy-4-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34533 xVXvxVXvxVXv 12 Bacillistatin 2 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x(1/9)=2R-hydroxy-3S-methyl-valeryl-R-valine; x(5)=2R-hydroxy-4-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34534 xVXvxVXvxVXv 12 Bacillistatin 2 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x(1/9)=2R-hydroxy-3S-methyl-valeryl-R-valine; x(5)=2R-hydroxy-4-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34535 xVXvxVXvxVXv 12 Bacillistatin 1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free x=2R-hydroxy-3S-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34536 xVXvxVXvxVXv 12 Bacillistatin 1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free x=2R-hydroxy-3S-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34537 xVXvxVXvxVXv 12 Bacillistatin 1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free x=2R-hydroxy-3S-methyl-valeryl-R-valine; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34538 crkkrrqrrr 10 cTat Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Insulin Free D Not available Not available 19228019 Mol Pharm. 2009 Mar-Apr;6(2):492-503. Patel LN, Wang J, Kim KJ, Borok Z, Crandall ED, Shen WC. Conjugation with cationic cell-penetrating peptide increases pulmonary absorption of insulin. DRAMP34539 PVVXY 5 Cotteslosin A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19245260 J Nat Prod. 2009 Apr;72(4):666-70 Fremlin LJ, Piggott AM, Lacey E, Capon RJ. Cottoquinazoline A and cotteslosins A and B, metabolites from an Australian marine-derived strain of Aspergillus versicolor DRAMP34540 MFTLKKSLLLLFFLGTINLSLCEEERDADEEERRDDPEERAVEVEKRFVDLKKIANIINSIFGK 64 Temporin-1CEa B8QP36 Not found Rana chensinensis Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 19341344 Zoolog Sci. 2009 Mar;26(3):220-6. Shang D, Yu F, Li J, Zheng J, Zhang L, Li Y. Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis. DRAMP34541 FXX 3 Stereocalpin A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19354233 Org Lett. 2009 May 7;11(9):1963-6. Ghosh AK, Xu CX. A convergent synthesis of the proposed structure of antitumor depsipeptide stereocalpin A DRAMP34542 WEAALAEALAEALAEHLAEALAEALEALAA 30 GALA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19388672 Bioconjug Chem. 2009 May 20;20(5):953-9. Kobayashi S, Nakase I, Kawabata N, Yu HH, Pujals S, Imanishi M, Giralt E, Futaki S. Cytosolic targeting of macromolecules using a pH-dependent fusogenic peptide in combination with cationic liposomes. DRAMP34543 HARIKPTFRRLKWKYKGKFW 20 Anti-lipopolysaccharide factor (32-51)[Y2A], L-2 P07086 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23401744 J Amino Acids. 2013;2013:251398.  Fernández Massó JR, Oliva Argüelles B, Tejeda Y, Astrada S, Garay H, Reyes O, Delgado-Roche L, Bollati-Fogolín M, Vallespí MG.  The Antitumor Peptide CIGB-552 Increases COMMD1 and Inhibits Growth of Human Lung Cancer Cells DRAMP34544 CLGENVPCDKDRPNCCSRYECLEPTGYGWWYASYYCYKKRS 41 Brachyin Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 25329070 PLoS One. 2014 Oct 20;9(10):e110221. Zhong Y, Song B, Mo G, Yuan M, Li H, Wang P, Yuan M, Lu Q. A novel neurotoxin from venom of the spider, Brachypelma albopilosum DRAMP34545 ALWKEVLKNAGKAALNEINNLV 22 Dermaseptin-PH Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 29064402 Molecules. 2017 Oct 24;22(10):1805. Huang L, Chen D, Wang L, Lin C, Ma C, Xi X, Chen T, Shaw C, Zhou M. Dermaseptin-PH: A Novel Peptide with Antimicrobial and Anticancer Activities from the Skin Secretion of the South American Orange-Legged Leaf Frog, Pithecopus (Phyllomedusa) hypochondrialis. DRAMP34546 HARIKpTFRRlKWKYKGKFW 20 Anti-lipopolysaccharide factor (32-51)[Y2A,P6p,L11l], CIGB-552 P07086 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free Mix Not available Not available 29601540 Molecules. 2018 Mar 30;23(4):801. Astrada S, Fernández Massó JR, Vallespí MG, Bollati-Fogolín M Cell Penetrating Capacity and Internalization Mechanisms Used by the Synthetic peptide Peptide CIGB-552 and Its Relationship with Tumor Cell Line Sensitivity DRAMP34547 WKLLSKAQEKFGKNKSR,RYGTXIYQXRLWAFSK 34 CH9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 30048118 Bioconjug Chem. 2018 Sep 19;29(9):3060-3071 Ptaszyńska N, Gucwa K, Łęgowska A, Dębowski D, Gitlin-Domagalska A, Lica J, Heldt M, Martynow D, Olszewski M, Milewski S, Ng TB, Rolka K. Antimicrobial Activity of Chimera Peptides Composed of Human Neutrophil Peptide 1 (HNP-1) Truncated Analogues and Bovine Lactoferrampin DRAMP34548 IETFLKQLRSAANKIVGL 18 Citrus-amp1 A0A067DL46 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30192822 PLoS One. 2018 Sep 7;13(9):e0203451. Inui Kishi RN, Stach-Machado D, Singulani JL, Dos Santos CT, Fusco-Almeida AM, Cilli EM, Freitas-Astúa J, Picchi SC, Machado MA. Evaluation of cytotoxicity features of antimicrobial peptides with potential to control bacterial diseases of citrus DRAMP34549 GFWSSVWDGAKNVGTAIIKNAKVCVYAVCVSHK 33 Nicomicin-1 A0A3G2WH77 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found 6HN9 Not available Not available Not available Linear Free Free L Not available Not available 30360541 Mar Drugs. 2018 Oct 23;16(11):401. Panteleev PV, Tsarev AV, Bolosov IA, Paramonov AS, Marggraf MB, Sychev SV, Shenkarev ZO, Ovchinnikova TV.  Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain DRAMP34550 GFWSSVWDGAKNVGTAI 17 Nicomicin-1 (1-17) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360541 Mar Drugs. 2018 Oct 23;16(11):401. Panteleev PV, Tsarev AV, Bolosov IA, Paramonov AS, Marggraf MB, Sychev SV, Shenkarev ZO, Ovchinnikova TV. Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain DRAMP34551 GLFSKKGGKGGKSWIKGVFKGIKGIGKEVGGDVIRTGIEIAACKIKGEC 49 Esculentin-1GN A0A3G6VAR4 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30427189 J Med Chem. 2018 Dec 13;61(23):10709-10723. Zeng B, Chai J, Deng Z, Ye T, Chen W, Li D, Chen X, Chen M, Xu X. Functional Characterization of a Novel Lipopolysaccharide-Binding Antimicrobial and Anti-Inflammatory Peptide in Vitro and in Vivo DRAMP34552 TRGRWGRFKRRAGRFIRRNRWQIISTGLKLIG 32 Cathelicidin Ps-CATH4 A0A2R4A6C7 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30452933 Dev Comp Immunol. 2019 Mar;92:179-192.  Shi N, Cai S, Gao J, Qiao X, Yang H, Wang Y, Yu H. Roles of polymorphic cathelicidins in innate immunity of soft-shell turtle, Pelodiscus sinensis DRAMP34553 FLSLLPHIASGIASLVSKF 19 Phylloseptin-PBa2, Phylloseptin-PBu A0A2K4P1U8 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30612735  Biochem Biophys Res Commun. 2019 Feb 12;509(3):664-673.  Wu Y, Wang L, Zhou M, Chen T, Shaw C. Phylloseptin-PBa1, -PBa2, -PBa3: Three novel antimicrobial peptides from the skin secretion of Burmeister's leaf frog (Phyllomedusa burmeisteri) DRAMP34554 FLSLIPHIASGIASLVKNF 19 Phylloseptin-PBa1, Phylloseptin-PBu A0A5B7LGG0 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30612735 Biochem Biophys Res Commun. 2019 Feb 12;509(3):664-673. Wu Y, Wang L, Zhou M, Chen T, Shaw C. Phylloseptin-PBa1, -PBa2, -PBa3: Three novel antimicrobial peptides from the skin secretion of Burmeister's leaf frog (Phyllomedusa burmeisteri) DRAMP34555 RWCRRYRVRVRGVLVYAYVCW 21 Arenicin-1 [V4R; Y5,7R; A6Y; R16,18Y; Y17A; R19V] Q5SC60 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP34556 RWRPPIRRPPIRPPFYP 17 Bac5 (1-17)[F2W] P19660 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033 Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E Coli, K Pneumoniae, and A Baumannii DRAMP34557 CVRRFPWWWPFLRRC 15 C-Tritrpticin-C P51524 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32126228 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183228. Arias M, Haney EF, Hilchie AL, Corcoran JA, Hyndman ME, Hancock REW, Vogel HJ. Selective anticancer activity of Synthetic peptide peptides derived from the host defence peptide tritrpticin DRAMP34560 XvXXX,TvXXX 11 Actinomycin Z5 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 10757717 J Nat Prod. 2000 Mar;63(3):352-6. Lackner H, Bahner I, Shigematsu N, Pannell LK, Mauger AB. Structures of five components of the actinomycin Z complex from Streptomyces fradiae, two of which contain 4-chlorothreonine DRAMP34561 RQIKIWFQNRRMKW 14 pAntp (43-56) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34562 RQIKIWFQNRRMK 13 pAntp (43-55) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34563 RQIKIWFQNRRM 12 pAntp (43-54) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34564 RQIKIWFQNRR 11 pAntp (43-53) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34565 RQIKIWFQNR 10 pAntp (43-52) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34566 RQIKIWFQN 9 pAntp (43-51) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34567 RQIKIWFQ 8 pAntp (43-50) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34568 RQIKIW 6 pAntp (43-48) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34569 QIKIWFQNRRMKWKK 15 pAntp (44-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34570 IKIWFQNRRMKWKK 14 pAntp (45-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34571 IWFQNRRMKWKK 12 pAntp (47-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34572 WFQNRRMKWKK 11 pAntp (48-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34573 QNRRMKWKK 9 pAntp (50-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34574 NRRMKWKK 8 pAntp (51-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34575 RMKWKK 6 pAntp (53-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34576 AQIKIWFQNRRMKWKK 16 Ala43 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34577 RAIKIWFQNRRMKWKK 16 Ala44 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34578 RQAKIWFQNRRMKWKK 16 Ala45 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34579 RQIAIWFQNRRMKWKK 16 Ala46 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34580 RQIKAWFQNRRMKWKK 16 Ala47 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34581 RQIKIAFQNRRMKWKK 16 Ala48 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34582 RQIKIWAQNRRMKWKK 16 Ala49 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34583 RQIKIWFANRRMKWKK 16 Ala50 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34584 RQIKIWFQARRMKWKK 16 Ala51 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34585 RQIKIWFQNARMKWKK 16 Ala52 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34586 RQIKIWFQNRAMKWKK 16 Ala53 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34587 RQIKIWFQNRRAKWKK 16 Ala54 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34588 RQIKIWFQNRRMAWKK 16 Ala55 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34589 RQIKIWFQNRRMKAKK 16 Ala56 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34590 RQIKIWFQNRRMKWAK 16 Ala57 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34591 RQIKIWFQNRRMKWKA 16 Ala58 substitution mutant of pAntp (43-58) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-beta-Alanine) Amidation L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34592 CRQIKIWFPNRRMKWKKC 18 Reduced linear penetratin Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation (Labeled with Biotinyl-Ahx) Unknown L Not available Not available 10784032 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin. DRAMP34593 PSSSSSSRIGDP 12 PreS2 3S Mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear EGFP Free L Not available Not available 10822301 J Pept Res. 2000 Feb;55(2):163-72. Fischer PM, Zhelev NZ, Wang S, Melville JE, Fåhraeus R, Lane DP. Novel cell permeable motif derived from the PreS2-domain of hepatitis-B virus surface antigens. DRAMP34594 RKKRRQR 7 Tat (49-55) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34595 KKRRQRRR 8 Tat (50-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34596 KRRQRRR 7 Tat (51-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34597 rkkrrqrrr 9 D-Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free D Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34598 rrrqrrkkr 9 D-Tat (57-49) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free D Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34599 AKKRRQRRR 9 Ala49 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34600 RAKRRQRRR 9 Ala50 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34601 RKARRQRRR 9 Ala51 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34602 RKKARQRRR 9 Ala52 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34603 RKKRAQRRR 9 Ala53 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34604 RKKRRARRR 9 Ala54 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34605 RKKRRQARR 9 Ala55 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34606 RKKRRQRAR 9 Ala56 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34607 RKKRRQRRA 9 Ala57 substitution mutant of Tat (49-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34608 RRRRRR 6 R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free L Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34609 rrrrr 5 D-R5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free D Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34610 rrrrrrr 7 D-R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free D Not available Not available 11087855 Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13003-8 Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. DRAMP34611 CQNHHAKHGKVC 12 FSEN Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34612 KCGHKHQCAVHN 12 scFSEN Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34613 LVPLPKIKNSTFT 13 sFlt2-13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34614 MEPECNLNCTD 11 scFSEC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34615 NITVTLKKFPL 11 Flt2-11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34616 RPFVEMYSEIPE 12 Flt1-12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34617 SPNITVTLKKFPL 13 Flt2-13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34618 STNITVTLKKFPL 13 Flt2-13T Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 11311231 FEBS Lett. 2001 Apr 13;494(3):150-6. Tan DC, Kini RM, Jois SD, Lim DK, Xin L, Ge R. A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor DRAMP34619 akvkdepqrrsarlsakpappkpepkpkkapakk 34 D form of F3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein with 6-aminohexanoic acid (Ahx) spacer Free D Not available Not available 12032302 Proc Natl Acad Sci U S A. 2002 May 28;99(11):7444-9. Porkka K, Laakkonen P, Hoffman JA, Bernasconi M, Ruoslahti E. A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo. DRAMP34620 PKKKRKVALWKTLLKKVLKA 20 PV-S4(13) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34621 VKRKKKPALWKTLLKKVLKA 20 PV reverse-S4(13) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34622 RQARRNRRRALWKTLLKKVLKA 22 RR-S4(13) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34623 RQARRNRRRC 10 Rev ARM Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34624 GRKKRRQRRRPPQC 14 Tat ARM Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 12119035 iochemistry. 2002 Jul 23;41(29):9208-14. Hariton-Gazal E, Feder R, Mor A, Graessmann A, Brack-Werner R, Jans D, Gilon C, Loyter A. Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals. DRAMP34625 SKKKKTKV 8 TFIIE BETA Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 12204694 Chem Biol. 2002 Aug;9(8):943-8. Ragin AD, Morgan RA, Chmielewski J. Cellular import mediated by nuclear localization signal Peptide sequences. DRAMP34626 GKKKKRKREKL 11 TCF1-ALPHA Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 12204694 Chem Biol. 2002 Aug;9(8):943-8. Ragin AD, Morgan RA, Chmielewski J. Cellular import mediated by nuclear localization signal Peptide sequences. DRAMP34627 ERKKRRRE 8 HATF3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 12204694 Chem Biol. 2002 Aug;9(8):943-8. Ragin AD, Morgan RA, Chmielewski J. Cellular import mediated by nuclear localization signal Peptide sequences. DRAMP34628 FKKFRKF 7 C.e SDC3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 12204694 Chem Biol. 2002 Aug;9(8):943-8. Ragin AD, Morgan RA, Chmielewski J. Cellular import mediated by nuclear localization signal Peptide sequences. DRAMP34629 rggrlsysrrrfststgr 18 D-SynB1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NBD Free D Not available Not available 12783857 J Biol Chem. 2003 Aug 15;278(33):31192-201. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. DRAMP34630 RRLSYSRRRF 10 SynB3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NBD and TAMRA Free L Not available Not available 12783857 J Biol Chem. 2003 Aug 15;278(33):31192-201. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. DRAMP34631 rrlsysrrrf 10 D-SynB3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NBD Free D Not available Not available 12783857 J Biol Chem. 2003 Aug 15;278(33):31192-201. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. DRAMP34632 RGGRLAYLRRRWAVLGR 17 SynB5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NBD and TAMRA Free L Not available Not available 12783857 J Biol Chem. 2003 Aug 15;278(33):31192-201. Drin G, Cottin S, Blanc E, Rees AR, Temsamani J. Studies on the internalization mechanism of cationic cell-penetrating peptides. DRAMP34633 KPLLKKLLKKL 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 14514057 Biotechnol Lett. 2003 Aug;25(16):1305-10. Park Y, Lee DG, Hahm KS. Antibiotic activity of Leu-Lys rich model peptides DRAMP34634 KWKKLLKKPLKLKL 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 14514057 Biotechnol Lett. 2003 Aug;25(16):1305-10. Park Y, Lee DG, Hahm KS. Antibiotic activity of Leu-Lys rich model peptides DRAMP34635 KWKLKPLLKKLLKKL 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 14514057 Biotechnol Lett. 2003 Aug;25(16):1305-10. Park Y, Lee DG, Hahm KS. Antibiotic activity of Leu-Lys rich model peptides DRAMP34636 XFXFLXX 7 Scytalidamide B Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 14604342 J Org Chem. 2003 Nov 14;68(23):8767-73. Tan LT, Cheng XC, Jensen PR, Fenical W. Scytalidamides A and B, new cytotoxic cyclic heptapeptides from a marine fungus of the genus Scytalidium DRAMP34637 VRLPPPVRLPPP 12 PolyP 2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34638 VRLPPPVRLPPPVRLPPP 18 PolyP 3 (SAP) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34639 VHLPPP 6 PolyP 4 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34640 VHLPPPVHLPPP 12 PolyP 5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34641 VHLPPPVHLPPPVHLPPP 18 PolyP 6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34642 VKLPPP 6 PolyP 7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34643 VKLPPPVKLPPP 12 PolyP 8 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34644 VKLPPPVKLPPPVKLPPP 18 PolyP 9 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 15054781 Angew Chem Int Ed Engl. 2004 Mar 26;43(14):1811-4. Fernández-Carneado J, Kogan MJ, Castel S, Giralt E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34645 MAFLKKSLFLVLFLGLVSLSICEKEKRQNEEDEDENEAANHEEGSEEKRGLFDIVKKVVGAFGSLGKRNDLE 72 Aurein 2.5 Q5K0E4 Not found Litoria aurea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15203252 Peptides. 2004 Jun;25(6):1035-54. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34646 MAFLKKSLFLVLFLGLVSLSICEKEKRQNEEDEDENEAANHEEGSEEKRGLFDIVKKVVGALGSLGKRNDLE 72 Aurein 2.2 Q5K0E6 Not found Litoria aurea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15203252 Peptides. 2004 Jun;25(6):1035-54. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34647 MAFLKKSLFLVLFLGLVSLSICEKEKRQNGEDEDENEAANHEEGSEEKRGLFDIVKKVVGAIGSLGKRNDVE 72 Aurein 2.3 Q5K0E5 Not found Litoria aurea Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15203252 Peptides. 2004 Jun;25(6):1035-54. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of gamma-zein. DRAMP34648 GLLSVLGSVAKHVLGHVVGVIAEHL 25 Caerin 1.1 Modification Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 15203252 Peptides. 2004 Jun;25(6):1035-54. Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance DRAMP34649 HHPHGHHPHG 10 (HHPHG)2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Acetylation L Not available Not available 15313924 Cancer Res. 2004 Aug 15;64(16):5812-7 Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities. DRAMP34650 HY 2 Cyclo(His-Tyr) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15324483 J Pharm Pharmacol. 2004 Sep;56(9):1143-53. McCleland K, Milne PJ, Lucieto FR, Frost C, Brauns SC, Van De Venter M, Du Plessis J, Dyason K. An investigation into the biological activity of the selected histidine-containing diketopiperazines cyclo(His-Phe) and cyclo(His-Tyr) DRAMP34651 GSLPPIF 7 Dianthin D Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15387653 J Nat Prod. 2004 Sep;67(9):1522-7 Hsieh PW, Chang FR, Wu CC, Wu KY, Li CM, Chen SL, Wu YC. New cytotoxic cyclic peptides and dianthramide from Dianthus superbus DRAMP34652 GPISFV 6 Dianthin E Not available Not found Plantae Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 15387653 J Nat Prod. 2004 Sep;67(9):1522-7 Hsieh PW, Chang FR, Wu CC, Wu KY, Li CM, Chen SL, Wu YC. New cytotoxic cyclic peptides and dianthramide from Dianthus superbus DRAMP34653 GRPRESGKKRKRKRLKP 17 DPV6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34654 GKRKKKGKLGKKRPRSR 17 DPV7b Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34655 RKKRRRESRRARRSPRHL 18 DPV3/10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34656 SRRARRSPRESGKKRKRKR 19 DPV10/6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34657 VKRGLKLRHVRPRVTRMDV 19 DPV1047 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34658 SRRARRSPRHLGSG 14 DPV10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34659 LRRERQSRLRRERQSR 16 DPV15 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34660 GAYDLRRRERQSRLRRRERQSR 22 DPV15b Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cys addition Free L Not available Not available 15859953 Biochem J. 2005 Sep 1;390(Pt 2):407-18. De Coupade C, Fittipaldi A, Chagnas V, Michel M, Carlier S, Tasciotti E, Darmon A, Ravel D, Kearsey J, Giacca M, Cailler F. Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules. DRAMP34661 XXEXXXFLIILG 12 Laxaphycin A Not available Not found Anabaena laxa Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 15875779 In Vivo. 2005 May-Jun;19(3):577-82. Gbankoto A, Vigo J, Dramane K, Banaigs B, Aina E, Salmon JM. Cytotoxic effect of Laxaphycins A and B on human lymphoblastic cells (CCRF-CEM) using digitised videomicrofluorometry. DRAMP34662 GRKKRRQRRRPPQTYADFIASGRTGRRNAI 30 Tat-PKI Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 15937518 Br J Pharmacol. 2005 Aug;145(8):1093-102. Jones SW, Christison R, Bundell K, Voyce CJ, Brockbank SM, Newham P, Lindsay MA. Characterisation of cell-penetrating peptide-mediated peptide delivery. DRAMP34663 AGYLLGKINLKALAALAKKILTYADFIASGRTGRRNAI 38 Transportan-PKI Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 15937518 Br J Pharmacol. 2005 Aug;145(8):1093-102. Jones SW, Christison R, Bundell K, Voyce CJ, Brockbank SM, Newham P, Lindsay MA. Characterisation of cell-penetrating peptide-mediated peptide delivery. DRAMP34664 RRRRRRRRRRRTYADFIASGRTGRRNAI 28 R11-PKI Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 15937518 Br J Pharmacol. 2005 Aug;145(8):1093-102. Jones SW, Christison R, Bundell K, Voyce CJ, Brockbank SM, Newham P, Lindsay MA. Characterisation of cell-penetrating peptide-mediated peptide delivery. DRAMP34665 IAWVKAFIRKLRKGPLG 17 YTA4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 16376307 Biochem Pharmacol. 2006 Feb 14;71(4):416-25. Lindgren M, Rosenthal-Aizman K, Saar K, Eiríksdóttir E, Jiang Y, Sassian M, Ostlund P, Hällbrink M, Langel U. Overcoming methotrexate resistance in breast cancer tumour cells by the use of a new cell-penetrating peptide. DRAMP34666 GIPCGXSCVWIPCISSAIGCSCKSKVCYRN 30 [Glu(Me)]cyO2 P58434 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2KNN Not available Tumor cells: U-937/GTB (IC50=36(32-40)μM) Not available Linear Free Free X=Glu(Me) L Not available Not available 16389447 Cell Mol Life Sci. 2006 Jan;63(2):235-45. Herrmann A, Svangård E, Claeson P, Gullbo J, Bohlin L, Göransson U. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2 DRAMP34667 GIPCGESCVWIPCISSAIGCSCXSXVCYXN 30 ([Lys(Ac)]2[Arg(CHD)])cyO2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U-937/GTB (IC50=5.1(4.8-5.5)μM) Not available Free Free X(24)=Lys(Ac)2; X(28)=ARG(CHD) L Not available Not available 16389447 Cell Mol Life Sci. 2006 Jan;63(2):235-45. Herrmann A, Svangård E, Claeson P, Gullbo J, Bohlin L, Göransson U. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2 DRAMP34668 GIACFLKE 8 TRAIL53-60 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34669 CWQVKWQL 8 TRAIL77-84 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34670 NTKNDKQM 8 TRAIL198–206 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34671 SARNSCWS 8 TRAIL225-232 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34672 RNSCWSKD 8 TRAIL227–234 P50591 Not found TRAIL (Tumor necrosis factor-related apoptosis-inducing ligand) Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 16427631 FEBS Lett. 2006 Feb 6;580(3):885-9. Okochi M, Nakanishi M, Kato R, Kobayashi T, Honda H. High-throughput screening of cell death inducible short peptides from TNF-related apoptosis-inducing ligand sequence DRAMP34673 GKYVSLTTPKNPTKRRITPKDV 22 Inv2, rMce1a (13-34) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34674 TKRRITPKDVIDVRSVTTEINT 22 Inv3, rMce1a (25-46) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34675 RSVTTEINTLFQTLTSIAEKVDP 23 Inv4, rMce1a (38-60) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34676 VNADIKATTVFGGKYVSLTTPKNPTKRRITPKDVIDVRSVTTEINTLFQTLTSIAEKVDP 60 Inv5, rMce1a (1-60) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34677 AEKVDPVKLNLTLSAAAEALTGLGDK 26 Inv6, rMce1a (56-80) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34678 GLGDKFGESIVNANTVLDDLNSRMPQSRHDIQQL 34 Inv7, rMce1a (76-109) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34679 GDVYADAAPDLFDFLDSSVTTARTINA 27 Inv8, rMce1a (113-139) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34680 ARTINAQQAELDSALLAAAGFGNTTADVFDRG 32 Inv9, rMce1a (134-166) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34681 ADVFDRGGPYLQRGVADLVPTATLLDTYSP 30 Inv10, rMce1a (159-188) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34682 LDTYSPELFCTIRNFYDADRPDRGAAA 27 Inv11, rMce1a (189-209) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34683 TKRRITPDDVIDVRSVTTEINT 22 Inv3.3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34684 TKRRITPKKVIDVRSVTTEINT 22 Inv3.4 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34685 TKRRITPKDVIDVRSVTTKINT 22 Inv3.5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34686 TKRRITPKDVIDV 13 Inv3.6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34687 TKRRITPKDVIDVESVTTEINT 22 Inv3.7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34688 TARRITPKDVIDVRSVTTEINT 22 Inv3.8 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34689 TKAARITPKDVIDVRSVTTEINT 23 Inv3.9 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34690 HHHHHHTKRRITPKDVIDVRSVTTEINT 28 Inv3.10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free (peptide coated FITC labelled microspheres) Free L Not available Not available 16620748 Anal Biochem. 2006 Jun 1;353(1):7-14. Lu S, Tager LA, Chitale S, Riley LW. A cell-penetrating peptide derived from mammalian cell uptake protein of Mycobacterium tuberculosis. DRAMP34691 YSX 3 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity. DRAMP34692 YSXG 4 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity. DRAMP34693 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HBL (0.8% inhibition at 1μM, 1.4% inhibition at 10μM, 2.4% inhibition at 100μM, 18.3% inhibition at 1000μM); HEp-2 (1% inhibition at 1μM, 10.1% inhibition at 10μM, 16.8% inhibition at 100μM, 36.1% inhibition at 1000μM); SW620 (12.2% inhibition at 1μM, 15.5% inhibition at 10μM, 24.7% inhibition at 100μM, 29% inhibition at 1000μM); MCF-7 (22.8% inhibition at 1000μM); CaCo-2 (3% inhibition at 1μM, 8.4% inhibition at 10μM, 18.5% inhibition at 100μM, 10.6% inhibition at 1000μM); HT-29 (3.3% inhibition at 1μM, 11% inhibition at 10μM, 7.9% inhibition at 100μM, 23.7% inhibition at 1000μM); HeLa (4.9% inhibition at 1μM, 10.2% inhibition at 10μM, 13.3% inhibition at 100μM, 28% inhibition at 1000μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity. DRAMP34694 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HEp-2 (13.7% inhibition at 1μM, 25.8% inhibition at 10μM, 34.7% inhibition at 100μM, 44.5% inhibition at 1000μM); HT-29 (16.2% inhibition at 1μM, 6.6% inhibition at 10μM, 5.1% inhibition at 100μM, 14.5% inhibition at 1000μM); CaCo-2 (17.7% inhibition at 1μM, 10.9% inhibition at 10μM, 12.1% inhibition at 100μM, 8.1% inhibition at 1000μM); HBL (2.4% inhibition at 1μM, 4.5% inhibition at 10μM, 11.4% inhibition at 100μM, 23.2% inhibition at 1000μM); SW620 (26.4% inhibition at 1μM, 13.1% inhibition at 10μM, 14.6% inhibition at 100μM, 38.4% inhibition at 1000μM); HeLa (8.5% inhibition at 1μM, 9.5% inhibition at 10μM, 15.4% inhibition at 100μM, 24.1% inhibition at 1000μM); MCF-7 (9.6% inhibition at 100μM, 29.9% inhibition at 100μM) Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity. DRAMP34695 YXGFM 5 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Cα -dialkylated glycine (Aaa2,2 ) L Not available Not available 16722632 Cancer Res. 2004 Aug 15;64(16):5812-7. Doñate F, Juarez JC, Guan X, Shipulina NV, Plunkett ML, Tel-Tsur Z, Shaw DE, Morgan WT, Mazar AP. Tumor-cell-targeted methionine-enkephalin analogues containing unnatural amino acids: design, synthesis, and in vitro antitumor activity. DRAMP34696 CDSDSDITWDQLWDLMK 17 E-selectin-binding peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 17121909 Mol Cancer Ther. 2006 Nov;5(11):2624-33. Cai W, Rao J, Gambhir SS, Chen X. How molecular imaging is speeding up antiangiogenic drug development DRAMP34697 FLKDHRISTFKNWPF 15 hsurvivin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 17142738 J Immunol. 2006 Dec 15;177(12):8410-21. Charalambous A, Oks M, Nchinda G, Yamazaki S, Steinman RM. Dendritic cell targeting of survivin protein in a xenogeneic form elicits strong CD4 DRAMP34698 RGdFV 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 1718779 FEBS Lett. 1991 Oct 7;291(1):50-4. Aumailley M, Gurrath M, Müller G, Calvete J, Timpl R, Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 DRAMP34699 RGDfV 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 1718779 FEBS Lett. 1991 Oct 7;291(1):50-4. Aumailley M, Gurrath M, Müller G, Calvete J, Timpl R, Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 DRAMP34700 RGDFv 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 1718779 FEBS Lett. 1991 Oct 7;291(1):50-4. Aumailley M, Gurrath M, Müller G, Calvete J, Timpl R, Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 DRAMP34701 GRGDS 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 1718779 FEBS Lett. 1991 Oct 7;291(1):50-4. Aumailley M, Gurrath M, Müller G, Calvete J, Timpl R, Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 DRAMP34702 GSPWGLQHHPPRT 13 439A peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Free L Not available Not available 17268054 Biol Pharm Bull. 2007 Feb;30(2):218-23. Kamada H, Okamoto T, Kawamura M, Shibata H, Abe Y, Ohkawa A, Nomura T, Sato M, Mukai Y, Sugita T, Imai S, Nagano K, Tsutsumi Y, Nakagawa S, Mayumi T, Tsunoda S. Creation of novel cell-penetrating peptides for intracellular drug delivery using systematic phage display technology originated from Tat transduction domain. DRAMP34703 RCSCWSDK 8 TRAIL227–234[N2C] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34704 RKSCWSKD 8 TRAIL227–234[N2K] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34705 RNDCWSKD 8 TRAIL227–234[S3D] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34706 RNLCWSKD 8 TRAIL227–234[S3L] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34707 RNNCWSKD 8 TRAIL227–234[S3N] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34708 RNSCRSKD 8 TRAIL227–234[W5R] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34709 RNSCWSKN 8 TRAIL227–234[D8N] Not available Not found TRAIL227–234 Antimicrobial, Anticancer Not found Not found Not found Not available Induce cell death Not available Not available Linear Free Free L Not available Not available 17822671 Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Kaga C, Okochi M, Nakanishi M, Hayashi H, Kato R, Honda H. Screening of a novel octamer peptide, CNSCWSKD, that induces caspase-dependent cell death DRAMP34710 FVTRGCPRRLVARLIRVMVPRR 22 ARF(1-22) scr Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p14ARF protein. DRAMP34711 VRRFLVTLRIRRA 13 ARF(2-14) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p15ARF protein. DRAMP34712 RVRILARFLRTRV 13 ARF(2-14) scr Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p16ARF protein. DRAMP34713 RVRVFVVHIPRLT 13 ARF(19-31) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p17ARF protein. DRAMP34714 VIRVHFRLPVRTV 13 ARF(19-31) scr Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p18ARF protein. DRAMP34715 MVRRFLVTLRIRRACGPPRVRVFVVHIPRLTGEWAAP 37 ARF(1-37) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p19ARF protein. DRAMP34716 FRVPLRIRPCVVAPRLVMVRHTFGRIARWVAGPLETR 37 ARF(1-37) scr Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear fluorescein Amidation L Not available Not available 17984975 Mol Ther. 2008 Jan;16(1):115-23. Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel U. Characterization of a novel cytotoxic cell-penetrating peptide derived from p20ARF protein. DRAMP34717 FC 2 Cyclo(Phe-Cys) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 18436344 Peptides. 2008 Aug;29(8):1305-11. van der Merwe E, Huang D, Peterson D, Kilian G, Milne PJ, Van de Venter M, Frost C. The synthesis and anticancer activity of selected diketopiperazines DRAMP34718 ASWSACSVSCGGGARQRTR 19 Fibulostatin-6.2 Not available Not found Homo sapiens (Fibulin-6) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34719 ATPFIECSGARGTCHYFAN 19 Hexastatin-1 Not available Not found Homo sapiens (α6 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34720 FCNINNVCNFASRNDYSYW 19 Pentastatin-2 Not available Not found Homo sapiens (α5 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34721 GPWAPCSASCGGGSQSRS 18 Papilostatin-1 Not available Not found Homo sapiens (Papilin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34722 GPWEDCSVSCGGGEQLRSR 19 Scospondistatin Not available Not found Homo sapiens (SCO-spondin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34723 GPWEPCSVTCSKGTRTRRR 19 Properdistatin Not available Not found Homo sapiens (Properdin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available CD36 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34724 GPWERCTAQCGGGIQARRR 19 Semastatin-5A.1 Not available Not found Homo sapiens (Sema 5A) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34725 GPWGDCSRTCGGGVQFSSR 19 Adamtsostatin-4 Not available Not found Homo sapiens (ADAMTS-4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34726 GPWGPCSGSCGPGRRLRRR 19 Cartilostatin-2 Not available Not found Homo sapiens (CILP-2) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34727 LPRFSTMPFIYCNINEVCHY 20 Hexastatin-3 Not available Not found Homo sapiens (α6 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34728 LPVFSTLPFAYCNIHQVCH 19 Tetrastatin-1 Not available Not found Homo sapiens (α4 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34729 LRRFSTMPFMFCNINNVCNF 20 Pentastatin-1 Not available Not found Homo sapiens (α5 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available αvβ3, αvβ1 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34730 QPWGTCSESCGKGTQTRAR 19 Fibulostatin-6.3 Not available Not found Homo sapiens (Fibulin-6) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34731 QPWSQCSATCGDGVRERRR 19 Thrombostatin con-1 Not available Not found Homo sapiens (TSRC-1) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34732 SAPFIECHGRGTCNYYANS 19 Pentastatin-3 Not available Not found Homo sapiens (α5 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34733 SAWRACSVTCGKGIQKRSR 19 Fibulostatin-6.1 Not available Not found Homo sapiens (Fibulin-6) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34734 SEWSDCSVTCGKGMRTRQR 19 Spondinstatin-1 Not available Not found Homo sapiens (F-spondin ) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34735 SKWSECSRTCGGGVKFQER 19 Adamtsostatin-18 Not available Not found Homo sapiens (ADAMTS-18) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34736 SPWSKCSAACGQTGVQTRTR 20 Cartilostatin-1 Not available Not found Homo sapiens (CILP-1) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34737 SPWSPCSGNCSTGKQQRTR 19 Thrombostatin con-3 Not available Not found Homo sapiens (TSRC-3) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34738 SPWSPCSTSCGLGVSTR 17 Wispostatin-1 Not available Not found Homo sapiens (WISP-1) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34739 SPWSQCSVRCGRGQRSRQVR 20 Adamtsostatin-like-4 Not available Not found Homo sapiens (TSRC1) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34740 SPWSQCTASCGGGVQTR 17 Adamtsostatin-16 Not available Not found Homo sapiens (ADAMTS-16) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34741 SPWTKCSATCGGGHYMRTR 19 Semastatin-5A.2 Not available Not found Homo sapiens (Sema 5A) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34742 SQWSPCSRTCGGGVSFRER 19 Papilostatin-2 Not available Not found Homo sapiens (Papilin) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34743 TAWGPCSTTCGLGMATRV 18 Wispostatin-2 Not available Not found Homo sapiens (WISP-2) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34744 TEWSACNVRCGRGWQKRSR 19 Netrinstatin-5D Not available Not found Homo sapiens (UNC-5D) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34745 TEWSACSKTCGMGISTRV 18 Connectostatin Not available Not found Homo sapiens (CTGF) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34746 TEWSVCNSRCGRGYQKRTR 19 Netrinstatin-5C Not available Not found Homo sapiens (UNC-5C) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34747 TEWTACSKSCGMGFSTRV 18 Nephroblastostatin Not available Not found Homo sapiens (NOVH) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34748 TKWTPCSRTCGMGISNRV 18 Wispostatin-3 Not available Not found Homo sapiens (WISP-3) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34749 TLPFAYCNIHQVCHYAQRNDRSYWL 25 Tetrastatin-2 Not available Not found Homo sapiens (α4 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available αvβ3 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34750 TQWTSCSKTCNSGTQSRHR 19 Complestatin-C6 Not available Not found Homo sapiens (Complement comp. C6) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34751 TSWSPCSASCGGGHYQRTR 19 Semastatin-5B Not available Not found Homo sapiens (Sema 5B) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34752 TSWSQCSKTCGTGISTRV 18 Cyrostatin Not available Not found Homo sapiens (CYR61) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34753 WTRCSSSCGRGVSVRSR 17 Thrombostatin con-6 Not available Not found Homo sapiens (TSRC-6) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34754 YCNINEVCHYARRNDKSYWL 20 Hexastatin-2 Not available Not found Homo sapiens (α6 CIV) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 18780781 Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13775-80. Karagiannis ED, Popel AS. A systematic methodology for proteome-wide identification of peptides inhibiting the proliferation and migration of endothelial cells DRAMP34755 KKKFPWWWPFKKKKKKFPWWWPFKKKK 27 di-PST13-RK-K Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 18815734 Biotechnol Lett. 2009 Feb;31(2):233-7. Yang ST, Kim JI, Shin SY. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity. DRAMP34756 GSGKKGGKKICQKY 14 D form of (1-9)-(38-42) Crot Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 18983137 J Med Chem. 2008 Nov 27;51(22):7041-4. Rádis-Baptista G, de la Torre BG, Andreu D. A novel cell-penetrating peptide sequence derived by structural minimization of a snake toxin exhibits preferential nucleolar localization. DRAMP34757 xVXvxVXvxVXv 12 Valinomycin Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x=R-Hiv; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34758 xVXvxVXvxVXv 12 Valinomycin Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x=R-Hiv; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34759 xVXvxVXvxVXv 12 Valinomycin Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x=R-Hiv; X=S-lactic acid-S-Val Mix Not available Not available 19226154 J Nat Prod. 2009 Mar 27;72(3):366-71. Pettit GR, Knight JC, Herald DL, Pettit RK, Hogan F, Mukku VJ, Hamblin JS, Dodson MJ, Chapuis JC. Antineoplastic agents 570 Isolation and structure elucidation of bacillistatins 1 and 2 from a marine Bacillus silvestris DRAMP34760 XTXPX 5 Desacetylmicrocolin B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear DiMe-C8 Free L Not available Not available 19431099  Planta Med. 2009 Oct;75(13):1427-30. Meickle T, Matthew S, Ross C, Luesch H, Paul V. Bioassay-guided isolation and identification of desacetylmicrocolin B from Lyngbya cf polychroa DRAMP34761 FFSLLPSLIGGLVSAIK 17 Imcroporin Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 19451300 Antimicrob Agents Chemother. 2009 Aug;53(8):3472-7. Zhao Z, Ma Y, Dai C, Zhao R, Li S, Wu Y, Cao Z, Li W.  Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates. DRAMP34762 YTMNPRKLFDY 11 KV11 Not available Not found Kringle 5 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available cSrc ERK 19515999 Invest Ophthalmol Vis Sci. 2009 Nov;50(11):5384-95.  Zhao H, Jin H, Li Q, Gu Q, Zheng Z, Wu H, Ye S, Sun X, Xu X, Ho PC. Inhibition of pathologic retinal neovascularization by a small peptide derived from human apolipoprotein(a) DRAMP34763 FPVPLPI 7 Rolloamide A Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19583251 J Nat Prod. 2009 Jul;72(7):1253-7.  Williams DE, Yu K, Behrisch HW, Van Soest R, Andersen RJ.  Rolloamides A and B, cytotoxic cyclic heptapeptides isolated from the Caribbean marine sponge Eurypon laughlini DRAMP34764 TRQARRNRRRRWRERQRGC 19 HIV-1 Rev (34-50) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-76. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34765 RRRRNRTRRNRRRVRGC 17 FHV coat (35-49) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-77. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34766 KMTRAQRRAAARRNRWTARGC 21 BMV Gag (7-25) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-78. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34767 TRRQRTRRARRNRGC 15 HTLV-II Rex (4-16) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-79. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34768 RIKAERKRMRNRIAASKSRKRKLERIARGC 30 Human cJun (252-279) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-80. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34769 KRRIRRERNKMAAAKSRNRRRELTDTGC 28 Human cFos (139-164) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Conjugation with Alexa 488 at glycyl cysteine sequence L Not available Not available 19707187 Mol Ther. 2009 Nov;17(11):1868-81. Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, Takeuchi T, Futaki S. Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. DRAMP34770 GGGARKKAAKAARKKAAKAARKKAAKAARKKAAKA 35 POD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free GFP L Not available Not available 19733192 Vision Res. 2010 Mar 31;50(7):686-97.  Johnson LN, Cashman SM, Read SP, Kumar-Singh R Cell penetrating peptide POD mediates delivery of recombinant proteins to retina, cornea and skin. DRAMP34771 ATPFVPP 7 Euryjanicin B Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19743810 J Nat Prod. 2009 Sep;72(9):1555-62. Vera B, Vicente J, Rodríguez AD. Isolation and structural elucidation of euryjanicins B-D, proline-containing cycloheptapeptides from the Caribbean marine sponge Prosuberites laughlini DRAMP34772 LFPXSXP 7 Euryjanicin C Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19743810 J Nat Prod. 2009 Sep;72(9):1555-63. Vera B, Vicente J, Rodríguez AD. Isolation and structural elucidation of euryjanicins B-D, proline-containing cycloheptapeptides from the Caribbean marine sponge Prosuberites laughlini DRAMP34773 FPXFSPX 7 Euryjanicin D Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19743810 J Nat Prod. 2009 Sep;72(9):1555-64. Vera B, Vicente J, Rodríguez AD. Isolation and structural elucidation of euryjanicins B-D, proline-containing cycloheptapeptides from the Caribbean marine sponge Prosuberites laughlini DRAMP34774 WPISFVP 7 Euryjanicin A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19743810 J Nat Prod. 2009 Sep;72(9):1555-65. Vera B, Vicente J, Rodríguez AD. Isolation and structural elucidation of euryjanicins B-D, proline-containing cycloheptapeptides from the Caribbean marine sponge Prosuberites laughlini DRAMP34775 IIILPPXP 8 Dominicin Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 19743810 J Nat Prod. 2009 Sep;72(9):1555-66. Vera B, Vicente J, Rodríguez AD. Isolation and structural elucidation of euryjanicins B-D, proline-containing cycloheptapeptides from the Caribbean marine sponge Prosuberites laughlini DRAMP34776 AXXlXX 6 Bisebromoamide Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear PivOH Free Mix Not available Not available 19803465  Org Lett. 2009 Nov 5;11(21):5062-5. Teruya T, Sasaki H, Fukazawa H, Suenaga K. Bisebromoamide, a potent cytotoxic peptide from the marine cyanobacterium Lyngbya sp: isolation, stereostructure, and biological activity DRAMP34777 XsfATX 6 Sclerotide B Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 19827766 Org Lett. 2009 Nov 19;11(22):5262-5.  Zheng J, Zhu H, Hong K, Wang Y, Liu P, Wang X, Peng X, Zhu W. Novel cyclic hexapeptides from marine-derived fungus, Aspergillus sclerotiorum PT06-1 DRAMP34778 KCFQWQRNMRKVRGPPVSC 19 M1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36108. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34779 KCFQWQRNMRKVRGPPVSSIKR 22 M2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36109. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34780 KCFQWQRNMRKVR 13 M3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36110. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34781 QWQRNMRKVRGPPVSCIKR 19 M5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36111. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34782 QWQRNMRKVR 10 M6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36112. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34783 KCFMWQEMLNKAGVPKLRCARK 22 rLF Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 19858187 J Biol Chem. 2009 Dec 25;284(52):36099-36113. Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. DRAMP34784 KLWMRWYSPTTRRYG 15 No.14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-51.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34785 RTLVNEYKNTLKFSK 15 No.63 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-52.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34786 IPSRWKDQFWKRWHY 15 No.143 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-53.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34787 GYGNCRHFKQKPRRD 15 No. 440 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-54.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34788 KNAWKHSSCHHRHQI 15 No. 2028 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-55.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34789 RVREWWYTITLKQES 15 No. 2175 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-56.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34790 QQHLLIAINGYPRYN 15 No. 2510 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-57.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34791 WKCRRQCFRVLHHWN 15 JF06 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein Free L Not available Not available 19956900 Int J Mol Med. 2010 Jan;25(1):41-58.  Kamide K, Nakakubo H, Uno S, Fukamizu A. Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. DRAMP34792 AAQYVXX 7 Cordycommunin Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 20028029 J Nat Prod. 2010 Jan;73(1):75-8.  Haritakun R, Sappan M, Suvannakad R, Tasanathai K, Isaka M. An antimycobacterial cyclodepsipeptide from the entomopathogenic fungus Ophiocordyceps communis BCC 16475 DRAMP34793 DDDDDNDKIPDDRDN 15 TSP-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 20056600 J Biol Chem. 2010 Mar 19;285(12):8733-42.  Colombo G, Margosio B, Ragona L, Neves M, Bonifacio S, Annis DS, Stravalaci M, Tomaselli S, Giavazzi R, Rusnati M, Presta M, Zetta L, Mosher DF, Ribatti D, Gobbi M, Taraboletti G. Non-peptidic thrombospondin-1 mimics as fibroblast growth factor-2 inhibitors: an integrated strategy for the development of new antiangiogenic compounds DRAMP34794 KWFETWFTEWPKKRK 15 Pep-3 Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Cysteamide L Not available Not available 20188697 Biochim Biophys Acta. 2010 Dec;1798(12):2274-85. Kurzawa L, Pellerano M, Morris MC.  PEP and CADY-mediated delivery of fluorescent peptides and proteins into living cells. DRAMP34795 GLWWRLWWRLRSWFRLWFRA 20 CADY2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Cysteamide L Not available Not available 20188697 Biochim Biophys Acta. 2010 Dec;1798(12):2274-86. Kurzawa L, Pellerano M, Morris MC.  PEP and CADY-mediated delivery of fluorescent peptides and proteins into living cells. DRAMP34796 ECKFTVKPYLKRFQVYYKGRMWCP 24 SALF Not available Not found Penaeus monodon Antimicrobial, Anticancer Not found Not found Not found Not available SALF can induce apoptotic gene expressions, enhance antitumor activity of cisplatin in vitro, and inhibit tumor growth in nude mice. Tumor cells: HeLa (65% Inhibition=100μg/ml) Not available Cyclic Acetylation Amidation L Not available Not available 20214941 Peptides. 2010 Jun;31(6):1019-25.  Lin MC, Lin SB, Chen JC, Hui CF, Chen JY. Shrimp anti-lipopolysaccharide factor peptide enhances the antitumor activity of cisplatin in vitro and inhibits HeLa cells growth in nude mice DRAMP34797 IVRRADRAAVP 11 ES-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 20515045 Bioconjug Chem. 2010 Jul 21;21(7):1142-7.  Yin R, Zheng H, Xi T, Xu HM.  Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide. DRAMP34798 XIIFPXPLPINAI 13 Callyaerin D Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-56.  Ibrahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. DRAMP34799 XLPFFPPVPIIG 12 Callyaerin E Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-57.  Ibrahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. DRAMP34800 XLPPPPLPFFF 11 Callyaerin G Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-58.  Ibrahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. DRAMP34801 XVPVFPPLFI 10 Callyaerin F Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-59.  Ibrahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. DRAMP34802 XVPVFPPLPI 10 Callyaerin H Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 20599387 Bioorg Med Chem. 2010 Jul 15;18(14):4947-60.  Ibrahim SR, Min CC, Teuscher F, Ebel R, Kakoschke C, Lin W, Wray V, Edrada-Ebel R, Proksch P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. DRAMP34803 YRIPIVRRLQRR 12 TL1AL72-L251(rev) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 20675618 J Gerontol A Biol Sci Med Sci. 2010 Nov;65(11):1165-80.  Mück C, Herndler-Brandstetter D, Micutkova L, Grubeck-Loebenstein B, Jansen-Dürr P. Two functionally distinct isoforms of TL1A (TNFSF15) generated by differential ectodomain shedding DRAMP34804 YTYGLCTSSR 10 TL1AV84-L251(fw) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 20675618 J Gerontol A Biol Sci Med Sci. 2010 Nov;65(11):1165-81.  Mück C, Herndler-Brandstetter D, Micutkova L, Grubeck-Loebenstein B, Jansen-Dürr P. Two functionally distinct isoforms of TL1A (TNFSF15) generated by differential ectodomain shedding DRAMP34805 TPATPTVAQFVIQGSTICLVC 21 Cypemycin E5KIB6 Not found Streptomyces Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 20805503 Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16297-302. Claesen J, Bibb M.  Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. DRAMP34806 VPTLK 5 Bip2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Free L Not available Not available 21359136 Pharmaceuticals (Basel). 2010 Dec 15;3(12):3594-3613. Gomez JA, Chen J, Ngo J, Hajkova D, Yeh IJ, Gama V, Miyagi M, Matsuyama S.  Cell-Penetrating Penta-Peptides (CPP5s): Measurement of Cell Entry and Protein-Transduction Activity. DRAMP34807 VELPPPVELPPPVELPPP 18 Sweet Arrow Protein (SAP) (E) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein/ Rhodamine B Free L Not available Not available 21365733 Chembiochem. 2011 Apr 11;12(6):896-903. Martín I, Teixidó M, Giralt E. Design, synthesis and characterization of a new anionic cell-penetrating peptide: SAP(E). DRAMP34808 MIIYRDLISH 10 TCTP (1-10) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-31.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34809 MIIYRDLISH 10 TCTP (1-10) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-31.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34810 MIIYRDLIS 9 TCTP (1-9) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-32.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34811 MIIYRDLI 8 TCTP (1-8) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-33.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34812 IIYRDLISH 9 TCTP (2-10) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-34.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34813 MIIYRDL 7 TCTP (1-7) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-35.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34814 MIIYRD 6 TCTP (1-6) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-36.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34815 IYRDLISH 8 TCTP (3-10) deletion mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-37.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34816 AIIYRDLIS 9 TCTP(1-9) M1A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-38.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34817 MAIYRDLIS 9 TCTP(I-9) I2A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-39.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34818 MIAYRDLIS 9 TCTP(1-9 I3A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-40.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34819 MIIARDLIS 9 TCTP(1-9) Y4A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-41.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34820 MIIYADLIS 9 TCTP(1-9) R5A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-42.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34821 MIIYRALIS 9 TCTP(1-9) D6A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-43.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34822 MIIYRDAIS 9 TCTP(1-9) L7A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-44.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34823 MIIYRDLAS 9 TCTP(1-9) I8A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-45.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34824 MIIYRDLIA 9 TCTP(1-9) S9A subsetution mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-46.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34825 MIIYRDLISKK 11 TCTP-CPP 1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-47.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34826 MIIYRDKKSH 10 TCTP-CPP 2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-48.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34827 MIIFRDLISH 10 TCTP-CPP 3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-49.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34828 MIISRDLISH 10 TCTP-CPP 4 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-50.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34829 QIISRDLISH 10 TCTP-CPP 5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-51.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34830 CIISRDLISH 10 TCTP-CPP 6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-52.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34831 MIIYRALISHKK 12 TCTP-CPP 7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-53.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34832 MIIYRIAASHKK 12 TCTP-CPP 8 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-54.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34833 MIIRRDLISE 10 TCTP-CPP 9 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-55.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34834 MIIYRAEISH 10 TCTP-CPP 10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-56.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34835 MIIYARRAEE 10 TCTP-CPP 11 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-57.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34836 MIIFRIAASHKK 12 TCTP-CPP 12 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-58.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34837 MIIFRALISHKK 12 TCTP-CPP 13 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-59.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34838 MIIFRAAASHKK 12 TCTP-CPP 14 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-60.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34839 FIIFRIAASHKK 12 TCTP-CPP 15 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-61.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34840 LIIFRIAASHKK 12 TCTP-CPP 16 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-62.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34841 WIIFRIAASHKK 12 TCTP-CPP 17 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-63.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34842 WIIFRAAASHKK 12 TCTP-CPP 18 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-64.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34843 WIIFRALISHKK 12 TCTP-CPP 19 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-65.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34844 MIIFRIAAYHKK 12 TCTP-CPP 20 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-66.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34845 WIIFRIAAYHKK 12 TCTP-CPP 21 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-67.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34846 MIIFRIAATHKK 12 TCTP-CPP 22 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-68.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34847 WIIFRIAATHKK 12 TCTP-CPP 23 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-69.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34848 MIIFKIAASHKK 12 TCTP-CPP 24 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-70.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34849 WIIFKIAASHKK 12 TCTP-CPP 25 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-71.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34850 MIIFAIAASHKK 12 TCTP-CPP 26 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-72.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34851 LIIFRILISHKK 12 TCTP-CPP 27 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-73.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34852 MIIFRILISHKK 12 TCTP-CPP 28 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-74.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34853 LIIFRILISHRR 12 TCTP-CPP 29 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-75.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34854 LIIFRILISHHH 12 TCTP-CPP 30 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-76.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34855 LIIFRILISHK 11 TCTP-CPP 31 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-77.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34856 LIIFRILISHR 11 TCTP-CPP 32 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-78.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34857 LIIFRILISH 10 TCTP-CPP 33 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-79.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34858 LIIFAIAASHKK 12 TCTP-CPP 34 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-80.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34859 LIIFAILISHKK 12 TCTP-CPP 35 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation L Not available Not available 21440624 Eur J Pharm Sci. 2011 May 18;43(1-2):25-81.  Kim M, Maeng J, Jung J, Kim HY, Kim HJ, Kwon Y, Lee K. Design and evaluation of variants of the protein transduction domain originated from translationally controlled tumor protein. DRAMP34860 ANIKLSVQMKLFKRHLKWKIIVKLNDGRELSLDA 34 Anginex Not available Not found PF4 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Galectin 1 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-16. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34861 ARPAKAAATQKKVERKAPDA 20 Fibrinogen derived Not available Not found Fibrinogen Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available αvβ3 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-17. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34862 CETWRTETTGATGQASSLLSGRLLEQKAASCHNSYIVLCIENSFMTSFSK 50 Endostatin fragment IV, IVox Not available Not found Collagen XVIII Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-18. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34863 DFKLFAVTIKYR 12 C16S Not available Not found Laminin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available αvβ3, α5β1 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-19. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34864 DFKLFAVYIKYR 12 C16Y Not available Not found Laminin Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available αvβ3, α5β1 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-20. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34865 DPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTN 34 PEDF P18 Not available Not found PEDF Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-21. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34866 DPFFKVPVNKLAAVSNFGYDLYRVRSSMSPTTN 33 PEDF 34-mer fragment Not available Not found PEDF Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-22. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34867 EDMNQKLFDLRGKFKRPPLRRVRMSADAML 30 pTnI Not available Not found Troponin I Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-23. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34868 EVHHQKLVFF 10 Aβ Not available Not found β-amyloid Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-24. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34869 FLSSRLQDLYSIVRRADRAA 20 Endostatin peptide fragment I (180–199) Not available Not found Collagen XVIII Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-25. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34870 HTHQDFQPVLHLVALNTPLSGGMRGIR 27 Endostatin peptide Not available Not found Collagen XVIII Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-26. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34871 KSVRGKGKGQKRKRKKSRYK 20 VEGFderived peptide Not available Not found Exon 6a of VEGF gene Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available VEGFR2 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-27. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34872 NGREACLDPEAPMVQKIVQKMLKG 24 Chemokinostatin-1 Not available Not found CXCL1 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available CXCR3 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-28. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34873 NGRKISLDLRAPLYKKIIKKLLES 24 PF4 derived Not available Not found PF4 Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available VEGF FGF2 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-29. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34874 NVLLSPLSVATALSALSLGAEQRTES 26 SvOrth-2 Not available Not found PEDF Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-30. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34875 TGALVEEEDPF 11 PEDF-TGA fragment Not available Not found PEDF Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-31. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34876 TSLDASIIWAMMQN 14 P144 Not available Not found TGFβ Receptor Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available TGFβ 21470139 Curr Pharm Biotechnol. 2011 Aug;12(8):1101-32. Rosca EV, Koskimaki JE, Rivera CG, Pandey NB, Tamiz AP, Popel AS Anti-angiogenic peptides for cancer therapeutics DRAMP34877 KWKKLLKKPLLKKLLKKL 18 P5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Acetylation L Not available Not available 21741801  Int J Antimicrob Agents. 2011 Sep;38(3):237-42. Dawson RM, Fox MA, Atkins HS, Liu CQ.  Potent antimicrobial peptides with selectivity for Bacillus anthracis over human erythrocytes DRAMP34878 NXV 3 Fellutamide C Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-C14 Free L Not available Not available 21761939 J Nat Prod. 2011 Aug 26;74(8):1721-30. Xu D, Ondeyka J, Harris GH, Zink D, Kahn JN, Wang H, Bills G, Platas G, Wang W, Szewczak AA, Liberator P, Roemer T, Singh SB. Isolation, structure, and biological activities of Fellutamides C and D from an undescribed Metulocladosporiella (Chaetothyriales) using the genome-wide Candida albicans fitness test DRAMP34879 NXL 3 Fellutamide D Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-C14 Free L Not available Not available 21761939 J Nat Prod. 2011 Aug 26;74(8):1721-31. Xu D, Ondeyka J, Harris GH, Zink D, Kahn JN, Wang H, Bills G, Platas G, Wang W, Szewczak AA, Liberator P, Roemer T, Singh SB. Isolation, structure, and biological activities of Fellutamides C and D from an undescribed Metulocladosporiella (Chaetothyriales) using the genome-wide Candida albicans fitness test DRAMP34880 RXRXRXRXRXRXRXRXB 17 (RX)8B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=6-aminohexanoic acid (Ahx); B=Beta-Alanine L Not available Not available 21765469 Oncogene. 2012 Feb 23;31(8):1024-33.  Ma W, Lin Y, Xuan W, Iversen PL, Smith LJ, Benchimol S. Inhibition of p53 expression by peptide-conjugated phosphorodiamidate morpholino oligomers sensitizes human cancer cells to chemotherapeutic drugs. DRAMP34881 RXRRXRRXRRXRXB 14 (RXR)4BR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=6-aminohexanoic acid (Ahx); B=Beta-Alanine L Not available Not available 21765469 Oncogene. 2012 Feb 23;31(8):1024-34.  Ma W, Lin Y, Xuan W, Iversen PL, Smith LJ, Benchimol S. Inhibition of p54 expression by peptide-conjugated phosphorodiamidate morpholino oligomers sensitizes human cancer cells to chemotherapeutic drugs. DRAMP34882 RXRRBRRXRRBRXB 14 (RXRRBR)2XB Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=6-aminohexanoic acid (Ahx); B=Beta-Alanine L Not available Not available 21765469 Oncogene. 2012 Feb 23;31(8):1024-35.  Ma W, Lin Y, Xuan W, Iversen PL, Smith LJ, Benchimol S. Inhibition of p55 expression by peptide-conjugated phosphorodiamidate morpholino oligomers sensitizes human cancer cells to chemotherapeutic drugs. DRAMP34883 GXVFXPI 7 Pitipeptolide D Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-74.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34884 GXVXXPV 7 Pitipeptolide F Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-75.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34885 GXVXXPI 7 Pitipeptolide A Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-76.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34886 GXVXXPI 7 Pitipeptolide A Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-76.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34887 GXVXXPI 7 Pitipeptolide A Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-76.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34888 GXVXXPI 7 Pitipeptolide A Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octynoic (Dhoya); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-76.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34889 GXVXXPI 7 Pitipeptolide B Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octenoic (Dhoea); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-77.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34890 GXVXXPI 7 Pitipeptolide B Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octenoic (Dhoea); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-77.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34891 GXVXXPI 7 Pitipeptolide B Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octenoic (Dhoea); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-77.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34892 GXVXXPI 7 Pitipeptolide B Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy-7-octenoic (Dhoea); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-77.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34893 GXVXXPI 7 Pitipeptolide C Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-78.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34894 GXVXXPI 7 Pitipeptolide C Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-78.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34895 GXVXXPI 7 Pitipeptolide C Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-78.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34896 GXVXXPI 7 Pitipeptolide C Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy 3-methyl pentanoic acid (Hmpa) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-78.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34897 GXVXXPI 7 Pitipeptolide E Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy isovaleric acid (Hiva) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-79.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34898 GXVXXPI 7 Pitipeptolide E Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy isovaleric acid (Hiva) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-79.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34899 GXVXXPI 7 Pitipeptolide E Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy isovaleric acid (Hiva) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-79.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34900 GXVXXPI 7 Pitipeptolide E Not available Not found marine cyanobacterium Lyngbya majuscula Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free X(2)=2,2-dimethyl-3-hydroxy octanoic acid (Dhoaa); X(4)=N-Me-Phe; X(5)=2-Hydroxy isovaleric acid (Hiva) L Not available Not available 21843895  Phytochemistry. 2011 Nov;72(16):2068-79.  Montaser R, Paul VJ, Luesch H.  Pitipeptolides C-F, antimycobacterial cyclodepsipeptides from the marine cyanobacterium Lyngbya majuscula from Guam DRAMP34901 RKKRRQRRRHRRKKR 15 dTAT Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 21856394 Int J Pharm. 2012 May 1;427(1):134-42.  Baoum A, Ovcharenko D, Berkland C. Calcium condensed cell penetrating peptide complexes offer highly efficient, low toxicity gene silencing. DRAMP34902 rrrrrrrrr 9 r9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Amidation D Not available Not available 21867915  Chem Biol. 2011 Aug 26;18(8):1000-10.  Verdurmen WP, Bovee-Geurts PH, Wadhwani P, Ulrich AS, Hällbrink M, van Kuppevelt TH, Brock R.  Preferential uptake of L- versus D-amino acid cell-penetrating peptides in a cell type-dependent manner. DRAMP34903 rqikiwfqnrrmkwkk 16 d-Penetratin {pAntp-(43-58)} Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation D Not available Not available 21867915  Chem Biol. 2011 Aug 26;18(8):1000-11.  Verdurmen WP, Bovee-Geurts PH, Wadhwani P, Ulrich AS, Hällbrink M, van Kuppevelt TH, Brock R.  Preferential uptake of L- versus D-amino acid cell-penetrating peptides in a cell type-dependent manner. DRAMP34904 KCFQWQRNMRKVRGPPVSCIKR 22 hLF(38-59) peptide Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 21867915  Chem Biol. 2011 Aug 26;18(8):1000-12.  Verdurmen WP, Bovee-Geurts PH, Wadhwani P, Ulrich AS, Hällbrink M, van Kuppevelt TH, Brock R.  Preferential uptake of L- versus D-amino acid cell-penetrating peptides in a cell type-dependent manner. DRAMP34905 kcfqwqrnmrkvrgppvscikr 22 hLF(38-59) peptide Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation D Not available Not available 21867915  Chem Biol. 2011 Aug 26;18(8):1000-13.  Verdurmen WP, Bovee-Geurts PH, Wadhwani P, Ulrich AS, Hällbrink M, van Kuppevelt TH, Brock R.  Preferential uptake of L- versus D-amino acid cell-penetrating peptides in a cell type-dependent manner. DRAMP34906 GGVCPKILAACRRDSDCPGACICRGNGYCGSGSD 34 MCoKKAA double mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-43.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34907 GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD 34 MCoK6A mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-44.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34908 GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD 34 MCoK9A mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-45.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34909 GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD 34 MCoK10A mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-46.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34910 GLPVCGETCVGGTCNTPGCKCSWPVCTRN 29 kT20K mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-47.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34911 GLPVCGETCVGGTCNTPGCTCSWPKCTRN 29 kV25K mutant Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Alexa-488 Cyclization L Not available Not available 21873420 J Biol Chem. 2011 Oct 21;286(42):36932-48.  Cascales L, Henriques ST, Kerr MC, Huang YH, Sweet MJ, Daly NL, Craik DJ. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. DRAMP34912 KLALKLALKALKAALKLAGC 20 MAP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation fluorescein L Not available Not available 21875799 Bioorg Med Chem Lett. 2011 Oct 1;21(19):5688-91. Wada S, Tsuda H, Okada T, Urata H. Cellular uptake of Aib-containing amphipathic helix peptide. DRAMP34913 KLULKLULKULKAULKLUGC 20 MAP (Aib) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation fluorescein U=Aib, α-aminoisobutyric acid L Not available Not available 21875799 Bioorg Med Chem Lett. 2011 Oct 1;21(19):5688-92. Wada S, Tsuda H, Okada T, Urata H. Cellular uptake of Aib-containing amphipathic helix peptide. DRAMP34914 WKLFDDGV 8 Anticancerous peptide 1 B3EWE7 Not found Cycas revoluta Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21882228 J Cell Biochem. 2012 Jan;113(1):184-93.  Mandal SM, Migliolo L, Das S, Mandal M, Franco OL, Hazra TK. Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties. DRAMP34915 CGETCVGGTCNTPGCTCSWPVCTRNGLNPV 30 D-Kalata B1 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 21928440 Chembiochem. 2011 Nov 4;12(16):2456-62. Sando L, Henriques ST, Foley F, Simonsen SM, Daly NL, Hall KN, Gustafson KR, Aguilar MI, Craik DJ.  Synthetic mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptor. DRAMP34916 GIIKKI 6 G(IIKK)I Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 21955251 Biomacromolecules. 2011 Nov 14;12(11):3839-43.  Hu J, Chen C, Zhang S, Zhao X, Xu H, Zhao X, Lu JR. Designed antimicrobial and antitumor peptides with high selectivity. DRAMP34917 GLRKRLRKFRNKIKEK 16 CF-sC18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Carboxyfluorescein  Free L Not available Not available 21956822 ChemMedChem. 2012 Jan 2;7(1):57-61. Splith K, Bergmann R, Pietzsch J, Neundorf I. Specific targeting of hypoxic tumor tissue with nitroimidazole-peptide conjugates. DRAMP34918 BGLRKXRLRKFRNKIKEK 18 CF-sC18(NIA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Amidation Free B=Beta-Alanine; X=NIA, 2-(2-nitroimidazol-1-yl)acetic acid L Not available Not available 21956822 ChemMedChem. 2012 Jan 2;7(1):57-62. Splith K, Bergmann R, Pietzsch J, Neundorf I. Specific targeting of hypoxic tumor tissue with nitroimidazole-peptide conjugates. DRAMP34919 KAAKKWAKAAKKWAKAWKKAA 21 Z1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-244.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34920 KAAKKAWKAWKKAAKAWKKAA 21 Z3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-245.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34921 KAAKKAWKAAKKAWKAWKKAA 21 Z7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-246.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34922 KWAKKAAKWAKKAAKWAKKAA 21 Z8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-247.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34923 KAWKKAWKAAKKAWKAAKKAA 21 Z9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-248.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34924 AAKKWAKAKKWAKAKKWAKAA 21 Z10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22057278 J Biol Chem. 2012 Jan 2;287(1):233-249.  Rekdal Ø, Haug BE, Kalaaji M, Hunter HN, Lindin I, Israelsson I, Solstad T, Yang N, Brandl M, Mantzilas D, Vogel HJ.  Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity DRAMP34925 MAMPGEPRRANVMAHKLEPASLQLRNSCA 29 CPPK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22076844 Biotechnol J. 2012 Mar;7(3):387-96.  Lee JH, Song HS, Park TH, Lee SG, Kim BG. Screening of cell-penetrating peptides using mRNA display. DRAMP34926 MAPQRDTVGGRTTPPSWGPAKAQLRNSCA 29 CPPL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22076844 Biotechnol J. 2012 Mar;7(3):387-97.  Lee JH, Song HS, Park TH, Lee SG, Kim BG. Screening of cell-penetrating peptides using mRNA display. DRAMP34927 KKALLAHALHLLALLALHLAHALKKA 26 LAH4-L1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22138072  J Control Release. 2012 Mar 10;158(2):293-303. Lam JK, Liang W, Lan Y, Chaudhuri P, Chow MY, Witt K, Kudsiova L, Mason AJ. Effective endogenous gene silencing mediated by pH responsive peptides proceeds via multiple pathways. DRAMP34928 LSQETFSDLWKLLPEN 16 WT p53 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Mdm2 22148351 J Am Chem Soc. 2012 Jan 11;134(1):103-6.  Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM. Structure of the stapled p53 peptide bound to Mdm2 DRAMP34938 xi 2 Cyclo(D-Hyp-D-Ile), Diketopiperazine (D-HyP-D-Ile) Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 22163196 Mar Drugs. 2011;9(11):2469-2478.  Ovenden SPB, Nielson JL, Liptrot CH, Willis RH, Tapiolas DM, Wright AD, Motti CA. A new diketopiperazine, cyclo-(4-S-hydroxy-R-proline-R-isoleucine), from an Australian specimen of the sponge Stelletta sp DRAMP34939 FLHHIVGLIHHGLSLFGDRAD 21 Pis2 Not available Not found Gadus morhua Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 22178249 Fish Shellfish Immunol. 2012 Mar;32(3):396-406. Ruangsri J, Salger SA, Caipang CM, Kiron V, Fernandes JM. Differential expression and biological activity of two piscidin paralogues and a novel splice variant in Atlantic cod (Gadus morhua L.). DRAMP34940 MTLTG 5 BPP-II Not available Not found Immunomodulatory bursal-derived Pentapeptide-II Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 22184121 J Biol Chem. 2012 Feb 3;287(6):3798-807.  Feng XL, Liu QT, Cao RB, Zhou B, Ma ZY, Deng WL, Wei JC, Qiu YF, Wang FQ, Gu JY, Wang FJ, Zheng QS, Ishag H, Chen PY. Identification and characterization of novel immunomodulatory bursal-derived pentapeptide-II (BPP-II). DRAMP34941 XrXrXr 6 (Fxr)3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Fx, cyclohexylalanine Mix Not available Not available 22238158 Chembiochem. 2012 Feb 13;13(3):476-85.  Horton KL, Pereira MP, Stewart KM, Fonseca SB, Kelley SO.  Tuning the activity of mitochondria-penetrating peptides for delivery or disruption. DRAMP34942 XrXrXrXr 8 (Fxr)4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Fx, cyclohexylalanine Mix Not available Not available 22238158 Chembiochem. 2012 Feb 13;13(3):476-86.  Horton KL, Pereira MP, Stewart KM, Fonseca SB, Kelley SO.  Tuning the activity of mitochondria-penetrating peptides for delivery or disruption. DRAMP34943 XrXrXrXrXr 10 (Fxr)5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Fx, cyclohexylalanine Mix Not available Not available 22238158 Chembiochem. 2012 Feb 13;13(3):476-87.  Horton KL, Pereira MP, Stewart KM, Fonseca SB, Kelley SO.  Tuning the activity of mitochondria-penetrating peptides for delivery or disruption. DRAMP34944 XrXrXrXrXrXr 12 (Fxr)6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Fx, cyclohexylalanine Mix Not available Not available 22238158 Chembiochem. 2012 Feb 13;13(3):476-88.  Horton KL, Pereira MP, Stewart KM, Fonseca SB, Kelley SO.  Tuning the activity of mitochondria-penetrating peptides for delivery or disruption. DRAMP34945 RRRRRRRRRGPGVTWTPQAWFQWV 24 RV24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22326265 Biochem Biophys Res Commun. 2012 Mar 9;419(2):170-4.  Lo SL, Wang S.  Evaluation of the use of amphipathic peptide-based protein carrier for in vitro cancer research. DRAMP34946 HEHEHEHEHEHEHEHEHEHEGGGGGKLALKLALKALKAALKLA 43 GST-HE-MAP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22326404 J Control Release. 2012 Mar 28;158(3):357-61.  Zaro JL, Fei L, Shen WC. Recombinant peptide constructs for targeted cell penetrating peptide-mediated delivery. DRAMP34947 LX 2 Cyclo(Leu-Hyp), Cordysinin A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22409377 J Agric Food Chem. 2012 Apr 4;60(13):3424-31. Li XJ, Zhang Q, Zhang AL, Gao JM. Metabolites from Aspergillus fumigatus, an endophytic fungus associated with Melia azedarach, and their antifungal, antifeedant, and toxic activities DRAMP34948 RRR 3 TMR-R3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22465335 Biomaterials. 2012 Jun;33(18):4665-72. Hitsuda T, Michiue H, Kitamatsu M, Fujimura A, Wang F, Yamamoto T, Han XJ, Tazawa H, Uneda A, Ohmori I, Nishiki T, Tomizawa K, Matsui H.  A protein transduction method using oligo-arginine (3R) for the delivery of transcription factors into cell nuclei. DRAMP34949 FFLIPKGRRRRRRRR 15 PasR8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-30.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (4R) for the delivery of transcription factors into cell nuclei. DRAMP34950 LILIGRRRRRRRRGC 15 LILIR8 (Alexa) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-31.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (5R) for the delivery of transcription factors into cell nuclei. DRAMP34951 FFGRRRRRRR 10 F2R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-32.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (6R) for the delivery of transcription factors into cell nuclei. DRAMP34952 FFFFGRRRRRRRR 13 F4R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-33.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (7R) for the delivery of transcription factors into cell nuclei. DRAMP34953 FFFFFFGRRRRRRRR 15 F6R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-34.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (8R) for the delivery of transcription factors into cell nuclei. DRAMP34954 fflipkgrrrrrrrr 15 dPasR8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-35.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (9R) for the delivery of transcription factors into cell nuclei. DRAMP34955 ffffgrrrrrrrr 13 Df4r8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 22486588  Mol Pharm. 2012 May 7;9(5):1222-36.  Takayama K, Hirose H, Tanaka G, Pujals S, Katayama S, Nakase I, Futaki S. A protein transduction method using oligo-arginine (10R) for the delivery of transcription factors into cell nuclei. DRAMP34956 NNXnyNQP 8 Mojavensin A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22491138 J Antibiot (Tokyo). 2012 Jun;65(6):317-22. Ma Z, Wang N, Hu J, Wang S. Isolation and characterization of a new iturinic lipopeptide, mojavensin A produced by a marine-derived bacterium Bacillus mojavensis B0621A DRAMP34957 GCGGGYGRKKRRQRRR 16 Tat Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22531849  Int J Pharm. 2012 Jul 1;430(1-2):372-80. Wang C, Qiao L, Zhang Q, Yan H, Liu K. Enhanced cell uptake of superparamagnetic iron oxide nanoparticles through direct chemisorption of FITC-Tat-PEG₆₀₀-b-poly(glycerol monoacrylate). DRAMP34958 YGRKKRRQRRRGTALDWSWLQTE 23 TAT-NBD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22580115 J Control Release. 2012 Aug 10;161(3):893-902.  Liu R, Xi L, Luo D, Ma X, Yang W, Xi Y, Wang H, Qian M, Fan L, Xia X, Li K, Wang D, Zhou J, Meng L, Wang S, Ma D.  Enhanced targeted anticancer effects and inhibition of tumor metastasis by the TMTP1 compound peptide TMTP1-TAT-NBD. DRAMP34959 CGNVVRQGCGYGRKKRRQRRRGTALDWSWLQTE 33 TMTP1-TAT-NBD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22580115 J Control Release. 2012 Aug 10;161(3):893-903.  Liu R, Xi L, Luo D, Ma X, Yang W, Xi Y, Wang H, Qian M, Fan L, Xia X, Li K, Wang D, Zhou J, Meng L, Wang S, Ma D.  Enhanced targeted anticancer effects and inhibition of tumor metastasis by the TMTP1 compound peptide TMTP2-TAT-NBD. DRAMP34960 Wp 2 Cyclo(L-Trp-D-Pro), Diketopiperazine (Wp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-9.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34961 wp 2 Cyclo(D-Trp-D-Pro), Diketopiperazine (wp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-10.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34962 Wa 2 Cyclo(L-Trp-D-Ala), Diketopiperazine (Wa) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-11.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34963 wa 2 Cyclo(D-Trp-D-Ala), Diketopiperazine (wa) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-12.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34964 wA 2 Cyclo(D-Trp-L-Ala), Diketopiperazine (wA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-13.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34965 WH 2 Cyclo(Trp-His), Diketopiperazine (WH) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22617493 Bioorg Med Chem Lett. 2012 Jun 15;22(12):3866-14.  Wollinsky B, Ludwig L, Hamacher A, Yu X, Kassack MU, Li SM.  Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides DRAMP34966 XFXPXLV 7 Cordyheptapeptide C Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 22642609 J Nat Prod. 2012 Jun 22;75(6):1215-9. Chen Z, Song Y, Chen Y, Huang H, Zhang W, Ju J. Cyclic heptapeptides, cordyheptapeptides C-E, from the marine-derived fungus Acremonium persicinum SCSIO 115 and their cytotoxic activities DRAMP34967 SRRRRRRRRR 10 SR9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22669044 Gene. 2012 Aug 15;505(1):37-45.  Liu BR, Lin MD, Chiang HJ, Lee HJ. Arginine-rich cell-penetrating peptides deliver gene into living human cells. DRAMP34968 CHHHHHRRRRRRRRRHHHHHC 21 HR9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22669044 Gene. 2012 Aug 15;505(1):37-46.  Liu BR, Lin MD, Chiang HJ, Lee HJ. Arginine-rich cell-penetrating peptides deliver gene into living human cells. DRAMP34969 FFLIPKGRRRRRRRRR 16 PR9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22669044 Gene. 2012 Aug 15;505(1):37-47.  Liu BR, Lin MD, Chiang HJ, Lee HJ. Arginine-rich cell-penetrating peptides deliver gene into living human cells. DRAMP34970 CGGGYGRKKRRQRRR 15 AgNP-TAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22682937 Biomaterials. 2012 Sep;33(26):6155-61.  Liu J, Zhao Y, Guo Q, Wang Z, Wang H, Yang Y, Huang Y. TAT-modified nanosilver for combating multidrug-resistant cancer. DRAMP34971 GLWWKAWWKAWWKSLWWRKRKRKA 24 CADY-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22688249 Int J Pharm. 2012 Sep 15;434(1-2):209-14.  Li Y, Zheng X, Cao Z, Xu W, Zhang J, Gong M. Self-assembled peptide (CADY-1) improved the clinical application of doxorubicin. DRAMP34972 AGYLLGKLLOOLAAAALOOLL 21 PF14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 22698942 J Control Release. 2012 Aug 20;162(1):1-8. Ezzat K, Zaghloul EM, El Andaloussi S, Lehto T, El-Sayed R, Magdy T, Smith CI, Langel U. Solid formulation of cell-penetrating peptide nanocomplexes with siRNA and their stability in simulated gastric conditions. DRAMP34973 YGRKKRPQRRR 11 1 (TAT) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:951.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34974 DSLKSYWYLQKFSWR 15 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:952.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34975 KLWMRWWSPTTRRYG 15 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:953.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34976 RLWMRWYSPWTRRWG 15 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:954.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34977 RLIMRIYAPTTRRYG 15 28 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:955.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34978 RLYMRYYSPTTRRYG 15 30 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:956.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34979 RLWMRWYSPRTRAYG 15 33 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:957.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34980 KRPTMRFRYTWNPMK 15 44 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Resisting chymotrypsin hydrolysis Not available Not available Linear Free Free L Not available Chymotrypsin hydrolysis 22805558 Nat Commun. 2012 Jul 17;3:958.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34981 WKCRRQAFRVLHHWN 15 47 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:959.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34982 WKARRQCFRVLHHWN 15 48 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 22805558 Nat Commun. 2012 Jul 17;3:960.  Kondo E, Saito K, Tashiro Y, Kamide K, Uno S, Furuya T, Mashita M, Nakajima K, Tsumuraya T, Kobayashi N, Nishibori M, Tanimoto M, Matsushita M.  Tumour lineage-homing cell-penetrating peptides as anticancer molecular delivery systems. DRAMP34983 STRUCTUREGIVEN 14 BAA-1 Not available Not found Bovine lactoferrin (Lf-B) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 22820149 Biochim Biophys Acta. 2012 Nov;1818(11):2917-25. Ausbacher D, Svineng G, Hansen T, Str繪m MB. Anticancer mechanisms of action of two small amphipathic β(2,2)-amino acid derivatives derived from antimicrobial peptides. DRAMP34984 rRRRRRRR 8 rR7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-94. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34985 rRrRRRRR 8 (rR)2R4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-95. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34986 rRrRrRRR 8 (rR)3R2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-96. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34987 rRrRrRrR 8 (rR)4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-97. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34988 rrrRrRrR 8 r2(rR)3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-98. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34989 rrrrrrrr 8 r8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 22824782 J Control Release. 2012 Sep 10;162(2):286-99. Ma Y, Gong C, Ma Y, Fan F, Luo M, Yang F, Zhang YH. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of D- and L-arginine residues. DRAMP34990 XXXXXXXX 8 Polyguanidine comparators 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=Nbtg L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-8.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34991 ZBBZBBZBB 9 NLys(1/3) variants 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(1-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-9.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34992 ZBBZBBZBBZBB 12 NLys(1/3) variants 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(1-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-10.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34993 ZXXZXXZXXZXX 12 NLys(1/3) variants 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; X=Npm from benzylamine (1-phenylethylamine) L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-11.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34994 ZXXZXXZXXZXX 12 NLys(1/3) variants 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; X=Npm from benzylamine (1-phenylethylamine) L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-11.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34995 ZXXZXXZXXZXX 12 NLys(1/3) variants 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; X=Nssb from (S)-(sec-butyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-12.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34996 ZXXZXXZXXZXX 12 NLys(1/3) variants 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; X=Nssb from (S)-(sec-butyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-12.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34997 ZZBZZBZZBZZB 12 NLys(2/3) variants 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(1-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-13.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34998 ZZZZZZZZBBBB 12 NLys(2/3) variants 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(2-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-14.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP34999 ZZZZZZZZXXXXX 13 NLys(2/3) variants 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; X=NLeu from isobutylamine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-15.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP35000 XBBXBBXBBXBB 12 Guanidylated variants Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(1-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-16.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP35001 XXBXXBXXBXXB 12 Guanidylated variants Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation Z=NLys from N-tert-butoxycarbonyl-1,4-butanediamine; B=Nspe was derived from (S)-N-(2-phenylethyl)amine L Not available Not available 22828784 Mol Biosyst. 2012 Oct;8(10):2626-17.  Huang W, Seo J, Lin JS, Barron AE.  Peptoid transporters: effects of cationic, amphipathic structure on their cellular uptake DRAMP35002 RRRRRHHH 8 R5H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23031530 Biomaterials. 2012 Dec;33(36):9246-58.  Jiang T, Zhang Z, Zhang Y, Lv H, Zhou J, Li C, Hou L, Zhang Q. Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. DRAMP35003 RRRRRRHHH 9 R6H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23031530 Biomaterials. 2012 Dec;33(36):9246-59.  Jiang T, Zhang Z, Zhang Y, Lv H, Zhou J, Li C, Hou L, Zhang Q. Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. DRAMP35004 RRRRRRRHHH 10 R7H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23031530 Biomaterials. 2012 Dec;33(36):9246-60.  Jiang T, Zhang Z, Zhang Y, Lv H, Zhou J, Li C, Hou L, Zhang Q. Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. DRAMP35005 RRRRRRRRHHH 11 R8H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23031530 Biomaterials. 2012 Dec;33(36):9246-61.  Jiang T, Zhang Z, Zhang Y, Lv H, Zhou J, Li C, Hou L, Zhang Q. Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. DRAMP35006 RRRRRRRRRHHH 12 R9H3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23031530 Biomaterials. 2012 Dec;33(36):9246-62.  Jiang T, Zhang Z, Zhang Y, Lv H, Zhou J, Li C, Hou L, Zhang Q. Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. DRAMP35007 BENPESILDEHVQRVM 16 fAxWT Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Inhibit wnt/β-catenin signaling pathway Not available Not available Linear FITC Amidation B=β-Ala L Not available β-catenin 23071338  Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-7. Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL. Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin DRAMP35022 WX 2 Cyclo(Trp-MeA), Diketopiperazine (WMeA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23079524  Bioorg Med Chem Lett. 2012 Dec 1;22(23):7265-7. Wang FZ, Huang Z, Shi XF, Chen YC, Zhang WM, Tian XP, Li J, Zhang S. Cytotoxic indole diketopiperazines from the deep sea-derived fungus Acrostalagmus luteoalbus SCSIO F457 DRAMP35023 FX 2 Dipeptide 8 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available OMe Free X=Sar L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-51. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35024 FX 2 Dipeptide 8 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available OMe Free X=Sar L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-51. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35025 GF 2 Dipeptide 13 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available OtBu Boc=Tert-Butyloxycarbonyl, Sar L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-52. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35026 VF 2 2,5-diketopiperazine 19 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-53. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35027 VKX 3 2,5-diketopiperazine 17 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-54. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35028 VV 2 2,5-diketopiperazine 21 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Boc=Tert-Butyloxycarbonyl, Sar L Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-55. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35029 Vx 2 2,5-diketopiperazine 16 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free Mix Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-56. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35030 zV 2 Dipeptide 5 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available OtBu Boc=Tert-Butyloxycarbonyl, Sar Mix Not available Not available 23084276 Bioorg Med Chem Lett. 2012 Dec 1;22(23):7048-57. Pérez-Picaso L, Olivo HF, Argotte-Ramos R, Rodríguez-Gutiérrez M, Rios MY.  Linear and cyclic dipeptides with antimalarial activity. DRAMP35031 YGRKKRRQRRRX 12 Tat-OH Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=acp, Epsilon-aminocaproic acid L Not available Not available 23085023 Eur J Pharmacol. 2013 Jan 5;698(1-3):87-94.  Kuroda Y, Kato-Kogoe N, Tasaki E, Murata E, Ueda K, Abe M, Miyamoto K, Nakase I, Futaki S, Tohyama Y, Hirose M.  Oligopeptides derived from autophosphorylation sites of EGF receptor suppress EGF-stimulated responses in human lung carcinoma A549 cells. DRAMP35032 YGRKKRRQRRRENAEYLR 18 Tat-ENAEYLR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=acp, Epsilon-aminocaproic acid L Not available Not available 23085023 Eur J Pharmacol. 2013 Jan 5;698(1-3):87-95.  Kuroda Y, Kato-Kogoe N, Tasaki E, Murata E, Ueda K, Abe M, Miyamoto K, Nakase I, Futaki S, Tohyama Y, Hirose M.  Oligopeptides derived from autophosphorylation sites of EGF receptor suppress EGF-stimulated responses in human lung carcinoma A550 cells. DRAMP35033 YGRKKRRQRRRQNAQYLR 18 Tat-QNAQYLR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=acp, Epsilon-aminocaproic acid L Not available Not available 23085023 Eur J Pharmacol. 2013 Jan 5;698(1-3):87-96.  Kuroda Y, Kato-Kogoe N, Tasaki E, Murata E, Ueda K, Abe M, Miyamoto K, Nakase I, Futaki S, Tohyama Y, Hirose M.  Oligopeptides derived from autophosphorylation sites of EGF receptor suppress EGF-stimulated responses in human lung carcinoma A551 cells. DRAMP35034 YGRKKRRQRRRDYQQD 16 Tat-DYQQD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=acp, Epsilon-aminocaproic acid L Not available Not available 23085023 Eur J Pharmacol. 2013 Jan 5;698(1-3):87-97.  Kuroda Y, Kato-Kogoe N, Tasaki E, Murata E, Ueda K, Abe M, Miyamoto K, Nakase I, Futaki S, Tohyama Y, Hirose M.  Oligopeptides derived from autophosphorylation sites of EGF receptor suppress EGF-stimulated responses in human lung carcinoma A552 cells. DRAMP35035 YGRKKRRQRRRNYQQN 16 Tat-NYQQN Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=acp, Epsilon-aminocaproic acid L Not available Not available 23085023 Eur J Pharmacol. 2013 Jan 5;698(1-3):87-98.  Kuroda Y, Kato-Kogoe N, Tasaki E, Murata E, Ueda K, Abe M, Miyamoto K, Nakase I, Futaki S, Tohyama Y, Hirose M.  Oligopeptides derived from autophosphorylation sites of EGF receptor suppress EGF-stimulated responses in human lung carcinoma A553 cells. DRAMP35036 NOTAVAILABLE 12 5a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 23085771 Eur J Med Chem. 2012 Dec;58:22-9.  Hansen T, Ausbacher D, Zachariassen ZG, Anderssen T, Havelkova M, Str繪m MB. Anticancer activity of small amphipathic β²,²-amino acid derivatives. DRAMP35037 rrrrrrrrrcqcrrkn 16 R9-GO-203 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 23114713  Cancer Biol Ther. 2013 Feb;14(2):127-34.  Uchida Y, Raina D, Kharbanda S, Kufe D. Inhibition of the MUC1-C oncoprotein is synergistic with cytotoxic agents in the treatment of breast cancer cells. DRAMP35038 CALNNYGRKKRRQRRR 16 Tat Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23184894 Adv Healthc Mater. 2013 Feb;2(2):352-60.  Liu X, Zhu H, Jin Q, Zhou W, Colvin VL, Ji J. Small and stable phosphorylcholine zwitterionic quantum dots for weak nonspecific phagocytosis and effective Tat peptide functionalization. DRAMP35039 AGYLLGXLLOOLAAAALOOLL 21 PF15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation X=Lys(ε-Mtt), Trifluoromethylquinoline moietie is added at amino froup of Lys7 L Not available Not available 23200958 Int J Pharm. 2013 Jan 30;441(1-2):242-7. Lindberg S, Muñoz-Alarcón A, Helmfors H, Mosqueira D, Gyllborg D, Tudoran O, Langel U.  PepFect15, a novel endosomolytic cell-penetrating peptide for oligonucleotide delivery via scavenger receptors. DRAMP35040 WRWRW 5 W(RW)2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear RuC(O) Amidation L Not available Not available 23209509 Beilstein J Org Chem. 2012;8:1753-64.  Albada HB, Chiriac AI, Wenzel M, Penkova M, Bandow JE, Sahl HG, Metzler-Nolte N. Modulating the activity of short arginine-tryptophan containing antibacterial peptides with N-terminal metallocenoyl groups DRAMP35041 GXFKKTFHKVSHAVKSGIHA 20 Centrocin 1a heavy chain, CEN1 HC (1-20) D8WN02 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23237525 AMB Express. 2012 Dec 13;2(1):67.  Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis DRAMP35042 CRGDKGPDC 9 iRGD-CDD Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23248118 Cancer Res. 2013 Feb 15;73(4):1352-61.  Chen R, Braun GB, Luo X, Sugahara KN, Teesalu T, Ruoslahti E. Application of a proapoptotic peptide to intratumorally spreading cancer therapy. DRAMP35043 MIIYRDLISH 10 TCTPPTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23256924 Anal Biochem. 2013 Apr 1;435(1):47-53. Maeng J, Kim HY, Shin DH, Lee K.  Transduction of translationally controlled tumor protein employing TCTP-derived protein transduction domain. DRAMP35044 MIIYRDLISH 10 TCTPPTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23256924 Anal Biochem. 2013 Apr 1;435(1):47-53. Maeng J, Kim HY, Shin DH, Lee K.  Transduction of translationally controlled tumor protein employing TCTP-derived protein transduction domain. DRAMP35045 RRRRRRRGGIYLATALAKWALKQGF 25 P7-4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-56. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35046 IYLATALAKWALKQGFGGRRRRRRR 25 P7-5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-57. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35047 RRRRRRRGGIYLATALAKWALKQ 23 P7-6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-58. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35048 IYLATALAKWALKQGGRRRRRRR 23 P7-7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-59. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35049 RRRRRRRGGKLAKLAKKLAKLAK 23 R7-KLA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-60. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35050 KLAKLAKKLAKLAKGGRRRRRRR 23 KLA-R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23262194  Biochim Biophys Acta. 2013 Mar;1828(3):1047-61. Lemeshko VV. Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties. DRAMP35051 RGDXRRRRRRRR 12 P1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=12-aminododecanoic acid (ADDA) L Not available Not available 23281275 Macromol Biosci. 2013 Jan;13(1):84-92. Chen JX, Xu XD, Yang S, Yang J, Zhuo RX, Zhang XZ. Self-assembled BolA-like amphiphilic peptides as viral-mimetic gene vectors for cancer cell targeted gene delivery. DRAMP35052 RGDXRRRRRRRR 12 P1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=12-aminododecanoic acid (ADDA) L Not available Not available 23281275 Macromol Biosci. 2013 Jan;13(1):84-92. Chen JX, Xu XD, Yang S, Yang J, Zhuo RX, Zhang XZ. Self-assembled BolA-like amphiphilic peptides as viral-mimetic gene vectors for cancer cell targeted gene delivery. DRAMP35053 RGDXRRRRRRRR 12 P2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=6-aminohexanoic acid, Ahx L Not available Not available 23281275 Macromol Biosci. 2013 Jan;13(1):84-93. Chen JX, Xu XD, Yang S, Yang J, Zhuo RX, Zhang XZ. Self-assembled BolA-like amphiphilic peptides as viral-mimetic gene vectors for cancer cell targeted gene delivery. DRAMP35054 RGDXRRRRRRRR 12 P2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=6-aminohexanoic acid, Ahx L Not available Not available 23281275 Macromol Biosci. 2013 Jan;13(1):84-93. Chen JX, Xu XD, Yang S, Yang J, Zhuo RX, Zhang XZ. Self-assembled BolA-like amphiphilic peptides as viral-mimetic gene vectors for cancer cell targeted gene delivery. DRAMP35055 RGDRRRRRRRR 11 P3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23281275 Macromol Biosci. 2013 Jan;13(1):84-94. Chen JX, Xu XD, Yang S, Yang J, Zhuo RX, Zhang XZ. Self-assembled BolA-like amphiphilic peptides as viral-mimetic gene vectors for cancer cell targeted gene delivery. DRAMP35056 GIGKFLHSAKKFGKAFVGEIMNSGGKKWKMRRNQFWVKVQRG 42 MG2A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23286306  Cancer Biother Radiopharm. 2013 May;28(4):289-97. Liu S, Yang H, Wan L, Cheng J, Lu X.  Penetratin-mediated delivery enhances the antitumor activity of the cationic antimicrobial peptide Magainin II. DRAMP35057 WRWRWRWRW 9 Cyclic [W(RW)4 ]-Dox Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Dox, Doxorubicin L Not available Not available 23301519 Mol Pharm. 2013 Feb 4;10(2):488-99. Nasrolahi Shirazi A, Tiwari R, Chhikara BS, Mandal D, Parang K. Design and biological evaluation of cell-penetrating peptide-doxorubicin conjugates as prodrugs. DRAMP35058 WRWKKKKA 8 cyclic [W(RW)4] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free L Not available Not available 23301519 Mol Pharm. 2013 Feb 4;10(2):488-100. Nasrolahi Shirazi A, Tiwari R, Chhikara BS, Mandal D, Parang K. Design and biological evaluation of cell-penetrating peptide-doxorubicin conjugates as prodrugs. DRAMP35059 RKKRRQRRRGC 11 Tat-Cys Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23322746 Protein Eng Des Sel. 2013 Apr;26(4):277-81. Moody P, Burlina F, Martin SR, Morgan RE, Offer J, Smith ME, Molloy JE, Caddick S. Evaluating the use of Apo-neocarzinostatin as a cell penetrating protein. DRAMP35060 DGRCLLIIKLAKLAKKLAKLAK 22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23326440 PLoS One. 2013;8(1):e53491. Hou L, Zhao X, Wang P, Ning Q, Meng M, Liu C.  Antitumor activity of antimicrobial peptides containing CisoDGRC in CD13 negative breast cancer cells DRAMP35061 NHQQQNPHQPPM 12 FAM-gHo Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation L Not available Not available 23350661 Bioconjug Chem. 2013 Mar 20;24(3):305-13.  Eriste E, Kurrikoff K, Suhorutšenko J, Oskolkov N, Copolovici DM, Jones S, Laakkonen P, Howl J, Langel Ü.  Peptide-based glioma-targeted drug delivery vector gHoPe2. DRAMP35062 LLIILRRRIRKQAHAHSKNHQQQNPHQPPM 30 FAM-pVEC-gHo (FAM- gHoPe2) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation L Not available Not available 23350661 Bioconjug Chem. 2013 Mar 20;24(3):305-14.  Eriste E, Kurrikoff K, Suhorutšenko J, Oskolkov N, Copolovici DM, Jones S, Laakkonen P, Howl J, Langel Ü.  Peptide-based glioma-targeted drug delivery vector gHoPe2. DRAMP35063 NHQQQNPHQPPMLLIILRRRIRKQAHAHSK 30 FAM-gHo-pVEC (FAM- gHoPe3) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation L Not available Not available 23350661 Bioconjug Chem. 2013 Mar 20;24(3):305-15.  Eriste E, Kurrikoff K, Suhorutšenko J, Oskolkov N, Copolovici DM, Jones S, Laakkonen P, Howl J, Langel Ü.  Peptide-based glioma-targeted drug delivery vector gHoPe2. DRAMP35064 CLLIILRRRIRKQAHAHSKNHQQQNPHQPPM 31 Dox-pVEC-gHo (Dox- gHoPe2) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Succinimidyl-4-(N-mal-eimidomethyl) cyclohexane-1-carboxylate (SMCC) Amidation L Not available Not available 23350661 Bioconjug Chem. 2013 Mar 20;24(3):305-16.  Eriste E, Kurrikoff K, Suhorutšenko J, Oskolkov N, Copolovici DM, Jones S, Laakkonen P, Howl J, Langel Ü.  Peptide-based glioma-targeted drug delivery vector gHoPe2. DRAMP35065 AGYLLGXINLKALAALAKKIL 21 NF51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation X=Ornithine L Not available Not available 23357356 Biochim Biophys Acta. 2013 May;1828(5):1365-73. Arukuusk P, Pärnaste L, Oskolkov N, Copolovici DM, Margus H, Padari K, Möll K, Maslovskaja J, Tegova R, Kivi G, Tover A, Pooga M, Ustav M, Langel U. New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. DRAMP35066 AGYLLGXINLKALAALAKKIL 21 NF51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation X=Ornithine L Not available Not available 23357356 Biochim Biophys Acta. 2013 May;1828(5):1365-73. Arukuusk P, Pärnaste L, Oskolkov N, Copolovici DM, Margus H, Padari K, Möll K, Maslovskaja J, Tegova R, Kivi G, Tover A, Pooga M, Ustav M, Langel U. New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. DRAMP35067 AGYLLGXINLKALAALAKKIL 21 NF51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation X=Ornithine L Not available Not available 23357356 Biochim Biophys Acta. 2013 May;1828(5):1365-73. Arukuusk P, Pärnaste L, Oskolkov N, Copolovici DM, Margus H, Padari K, Möll K, Maslovskaja J, Tegova R, Kivi G, Tover A, Pooga M, Ustav M, Langel U. New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. DRAMP35068 AGYLLGXINLKALAALAKKIL 21 NF51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation X=Ornithine L Not available Not available 23357356 Biochim Biophys Acta. 2013 May;1828(5):1365-73. Arukuusk P, Pärnaste L, Oskolkov N, Copolovici DM, Margus H, Padari K, Möll K, Maslovskaja J, Tegova R, Kivi G, Tover A, Pooga M, Ustav M, Langel U. New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. DRAMP35069 RLLRLLRRLLRLLRRLLRC 19 PL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23384441 Biochem Biophys Res Commun. 2013 Mar 8;432(2):359-64. Mokhtarieh AA, Kim S, Lee Y, Chung BH, Lee MK.  Novel cell penetrating peptides with multiple motifs composed of RGD and its analogs. DRAMP35070 RGDRGDRRDLRLDRGDLRC 19 PD1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23384441 Biochem Biophys Res Commun. 2013 Mar 8;432(2):359-65. Mokhtarieh AA, Kim S, Lee Y, Chung BH, Lee MK.  Novel cell penetrating peptides with multiple motifs composed of RGD and its analogs. DRAMP35071 RGDRLDRRDLRLDRRDLRC 19 PD2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23384441 Biochem Biophys Res Commun. 2013 Mar 8;432(2):359-66. Mokhtarieh AA, Kim S, Lee Y, Chung BH, Lee MK.  Novel cell penetrating peptides with multiple motifs composed of RGD and its analogs. DRAMP35072 RGERGERRELRLERGELRC 19 PE1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23384441 Biochem Biophys Res Commun. 2013 Mar 8;432(2):359-67. Mokhtarieh AA, Kim S, Lee Y, Chung BH, Lee MK.  Novel cell penetrating peptides with multiple motifs composed of RGD and its analogs. DRAMP35073 RGERLERRELRLERRELRC 19 PE2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23384441 Biochem Biophys Res Commun. 2013 Mar 8;432(2):359-68. Mokhtarieh AA, Kim S, Lee Y, Chung BH, Lee MK.  Novel cell penetrating peptides with multiple motifs composed of RGD and its analogs. DRAMP35074 CGETCVGGTCNTPGCTCSWPVCTRNGLPV 29 Kalata B1 P56254 Not found Oldenlandia affinis Antimicrobial, Anticancer Not found Not found Not found 1ZNU##2JUE##1NB1 Not available Not available Not available Free Free L Not available Not available 23468118 Biopolymers. 2013 Sep;100(5):461-70. Malagón D, Botterill B, Gray DJ, Lovas E, Duke M, Gray C, Kopp SR, Knott LM, McManus DP, Daly NL, Mulvenna J, Craik DJ, Jones MK. Anthelminthic activity of the cyclotides (kalata B1 and B2) against schistosome parasites. DRAMP35075 NYRWRCKNQN 10 ECP(32-41) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57318.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35076 NYQRRCKNQN 10 EDN(32-41) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57319.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35077 NYQWRCKNQN 10 ECP(32-41)R3Q Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57320.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35078 NYRRRCKNQN 10 ECP(32-41)W4R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57321.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35079 YRWRCKNQN 9 ECP(33-41) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57322.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35080 NYRWRCKNQ 9 ECP(32-40) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57323.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35081 YRWRCKNQ 8 ECP(33-40) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57324.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35082 NYRWRCKN 8 ECP(32-39) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57325.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35083 RWRCKNQN 8 ECP(34-41) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57326.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35084 NYRWRCK 7 ECP(32-38) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57327.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35085 GRKKRRQRRRP 11 TAT(47-57) Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57328.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35086 KLAKLAKKLAKLAKGRKKRRQRRRP 25 KLA-TAT(47-57) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57329.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35087 KLAKLAKKLAKLAKNYRWRCKNQN 24 KLA-ECP(32-41) Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23469189  PLoS One. 2013;8(3):e57330.  Fang SL, Fan TC, Fu HW, Chen CJ, Hwang CS, Hung TJ, Lin LY, Chang MD. A novel cell-penetrating peptide derived from human eosinophil cationic protein. DRAMP35088 KETWWETWWTEWSQPKKKRKVC 22 FP-lipo Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23515421 Int J Nanomedicine. 2013;8:1155-65.  Kang MJ, Park SH, Kang MH, Park MJ, Choi YW.  Folic acid-tethered Pep-1 peptide-conjugated liposomal nanocarrier for enhanced intracellular drug delivery to cancer cells: conformational characterization and in vitro cellular uptake evaluation. DRAMP35089 RRRRR 5 R5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23534410 Mol Pharm. 2013 May 6;10(5):1940-8. Alhakamy NA, Berkland CJ.  Polyarginine molecular weight determines transfection efficiency of calcium condensed complexes. DRAMP35090 GLKKLAELFHKLLKLG 16 TAMARA-peptide 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear TAMRA, 5-(and-6)-carboxytetramethylrhodamine Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-9.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35091 GLKKLAELFHKLLKLG 16 TAMARA-peptide 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear TAMRA, 5-(and-6)-carboxytetramethylrhodamine Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-9.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35092 LKKLAELAHKLLKLG 15 TAMARA-peptide 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear TAMRA Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-10.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35093 GLKKLAELFHKLLKLG 16 Peptide 1N- GNS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugated to nanoparticles Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-11.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35094 GLKKLAELFHKLLKLG 16 Peptide 1N- GNS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugated to nanoparticles Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-11.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35095 GLKKLAELAHKLLKLG 16 Peptide 2N- GNS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugated to nanoparticles Amidation L Not available Not available 23545289 Biomaterials. 2013 Jul;34(20):4872-12.  Park H, Tsutsumi H, Mihara H. Cell penetration and cell-selective drug delivery using α-helix peptides conjugated with gold nanoparticles. DRAMP35096 BRRRRRRR 8 R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation B=Beta-Alanine L Not available Not available 23546678  Methods Mol Biol. 2013;991:281-92.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35097 BRRRRRRRRR 10 C12R9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Lauroylation Amidation B=Beta-Alanine L Not available Not available 23546678  Methods Mol Biol. 2013;991:281-93.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35098 Brrrrrrr 8 C12dR9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Lauroylation Amidation B=Beta-Alanine Mix Not available Not available 23546678  Methods Mol Biol. 2013;991:281-94.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35099 BrrrrrRRRR 10 C12dR9-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Lauroylation Amidation B=Beta-Alanine Mix Not available Not available 23546678  Methods Mol Biol. 2013;991:281-95.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35100 BRRRRrrrrr 10 C12dR9-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Lauroylation Amidation B=Beta-Alanine Mix Not available Not available 23546678  Methods Mol Biol. 2013;991:281-96.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35101 BRRRRRRRRRRR 12 C14R11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Myrsitoylation Amidation B=Beta-Alanine L Not available Not available 23546678  Methods Mol Biol. 2013;991:281-97.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35102 Brrrrrrrrrrr 12 C14dR11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Myrsitoylation Amidation B=Beta-Alanine Mix Not available Not available 23546678  Methods Mol Biol. 2013;991:281-98.  Lee JS, Tung CH. Lipo-oligoarginine-based intracellular delivery. DRAMP35103 DEVD 4 caspase 3 inhibitor Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 23583573  Life Sci. 2013 May 30;92(20-21):1004-14.  Wang C, Zhou Y, Li S, Li H, Tian L, Wang H, Shang D.  Anticancer mechanisms of temporin-1CEa, an amphipathic α-helical antimicrobial peptide, in Bcap-37 human breast cancer cells. DRAMP35104 YGRKKRRQRRREILSRXPAYRKIL 24 CF-TAT-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-87.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35105 YGRKKRRQRRREILSRXPAYRKIL 24 CF-TAT-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-87.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35106 YGRKKRRQRRREILSRXPAYRKIL 24 Ac-TAT-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-88.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35107 YGRKKRRQRRREILSRXPAYRKIL 24 Ac-TAT-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-88.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35108 KKWKMRRNQFWIKIQREILSRXPAYRKIL 29 CF-Penetratin-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-89.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35109 KKWKMRRNQFWIKIQREILSRXPAYRKIL 29 CF-Penetratin-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-89.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35110 KKWKMRRNQFWIKIQREILSRXPAYRKIL 29 Ac-Penetratin-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-90.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35111 KKWKMRRNQFWIKIQREILSRXPAYRKIL 29 Ac-Penetratin-substrate Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free X=ATP-binding site inhibitors L Not available Not available 23621550  ACS Chem Biol. 2013 Jul 19;8(7):1479-90.  van Wandelen LT, van Ameijde J, Ismail-Ali AF, van Ufford HC, Vijftigschild LA, Beekman JM, Martin NI, Ruijtenbeek R, Liskamp RM. Cell-penetrating bisubstrate-based protein kinase C inhibitors. DRAMP35112 CRGDK 5 CRGDK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23634882 Nano Lett. 2013 Jun 12;13(6):2528-34.  Wei T, Liu J, Ma H, Cheng Q, Huang Y, Zhao J, Huo S, Xue X, Liang Z, Liang XJ. Functionalized nanoscale micelles improve drug delivery for cancer therapy in vitro and in vivo. DRAMP35113 AYLLGKINLKALAALAKKIL 20 TP10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation L Not available Not available 23669260  J Control Release. 2013 Aug 28;170(1):83-91. Verdurmen WP, Wallbrecher R, Schmidt S, Eilander J, Bovee-Geurts P, Fanghänel S, Bürck J, Wadhwani P, Ulrich AS, Brock R. Cell surface clustering of heparan sulfate proteoglycans by amphipathic cell-penetrating peptides does not contribute to uptake. DRAMP35114 AXLYLLGKINLKALAALAKKIL 22 TP10 2GL Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=L-CF3-Bpg, Trifluoromethyl- bicyclopent-[1.1.1]-1-ylglycine L Not available Not available 23669260  J Control Release. 2013 Aug 28;170(1):83-92. Verdurmen WP, Wallbrecher R, Schmidt S, Eilander J, Bovee-Geurts P, Fanghänel S, Bürck J, Wadhwani P, Ulrich AS, Brock R. Cell surface clustering of heparan sulfate proteoglycans by amphipathic cell-penetrating peptides does not contribute to uptake. DRAMP35115 AGYXLGKINLKALAALAKKIL 21 TP10 4LL Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=L-CF3-Bpg, Trifluoromethyl- bicyclopent-[1.1.1]-1-ylglycine L Not available Not available 23669260  J Control Release. 2013 Aug 28;170(1):83-93. Verdurmen WP, Wallbrecher R, Schmidt S, Eilander J, Bovee-Geurts P, Fanghänel S, Bürck J, Wadhwani P, Ulrich AS, Brock R. Cell surface clustering of heparan sulfate proteoglycans by amphipathic cell-penetrating peptides does not contribute to uptake. DRAMP35116 axlyllgkinlkalaalakkil 22 TP10 2GD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation x=D-CF3-Bpg, Trifluoromethyl- bicyclopent-[1.1.1]-1-ylglycine D Not available Not available 23669260  J Control Release. 2013 Aug 28;170(1):83-94. Verdurmen WP, Wallbrecher R, Schmidt S, Eilander J, Bovee-Geurts P, Fanghänel S, Bürck J, Wadhwani P, Ulrich AS, Brock R. Cell surface clustering of heparan sulfate proteoglycans by amphipathic cell-penetrating peptides does not contribute to uptake. DRAMP35117 agyxlgkinlkalaalakkil 21 TP10 4LD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation x=D-CF3-Bpg, Trifluoromethyl- bicyclopent-[1.1.1]-1-ylglycine D Not available Not available 23669260  J Control Release. 2013 Aug 28;170(1):83-95. Verdurmen WP, Wallbrecher R, Schmidt S, Eilander J, Bovee-Geurts P, Fanghänel S, Bürck J, Wadhwani P, Ulrich AS, Brock R. Cell surface clustering of heparan sulfate proteoglycans by amphipathic cell-penetrating peptides does not contribute to uptake. DRAMP35118 IGGYCSWLRL,IGGYCSWLRL 21 Harmoniasin A4, HaA4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 23732481 Int J Oncol. 2013 Aug;43(2):622-8. Kim IW, Lee JH, Kwon YN, Yun EY, Nam SH, Ahn MY, Kang DC, Hwang JS. Anticancer activity of a Synthetic peptide peptide derived from harmoniasin, an antibacterial peptide from the ladybug Harmonia axyridis DRAMP35119 CLLFVY 6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23796364 J Am Chem Soc. 2013 Jul 17;135(28):10418-25.  Miranda E, Nordgren IK, Male AL, Lawrence CE, Hoakwie F, Cuda F, Court W, Fox KR, Townsend PA, Packham GK, Eccles SA, Tavassoli A. A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells DRAMP35120 Xaix 4 Asperterrestide A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 23806112  J Nat Prod. 2013 Jun 28;76(6):1182-6. He F, Bao J, Zhang XY, Tu ZC, Shi YM, Qi SH. Asperterrestide A, a cytotoxic cyclic tetrapeptide from the marine-derived fungus Aspergillus terreus SCSGAF0162 DRAMP35121 VGAlAvVvWlWlWlWbAGSGPKKKRKVC 28 artifcial CPP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 23812036 Nanoscale. 2013 Aug 21;5(16):7256-64.  Jiang X, Wang G, Liu R, Wang Y, Wang Y, Qiu X, Gao X.  RNase non-sensitive and endocytosis independent siRNA delivery system: delivery of siRNA into tumor cells and high efficiency induction of apoptosis. DRAMP35122 AGYLLGHINLHHLAHLHHILC 21 TH peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23891517 Biomaterials. 2013 Oct;34(32):7980-93.  Zhang Q, Tang J, Fu L, Ran R, Liu Y, Yuan M, He Q.  A pH-responsive α-helical cell penetrating peptide-mediated liposomal delivery system. DRAMP35123 AGYLLGHINLHHLAHLHHIL 20 TH peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23891517 Biomaterials. 2013 Oct;34(32):7980-94.  Zhang Q, Tang J, Fu L, Ran R, Liu Y, Yuan M, He Q.  A pH-responsive α-helical cell penetrating peptide-mediated liposomal delivery system. DRAMP35124 AGYLLGKINLKKLAKLLLIL 20 TK peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 23891517 Biomaterials. 2013 Oct;34(32):7980-95.  Zhang Q, Tang J, Fu L, Ran R, Liu Y, Yuan M, He Q.  A pH-responsive α-helical cell penetrating peptide-mediated liposomal delivery system. DRAMP35125 KILRGVAKKILRTFLRRISKDILTGKK 27 C7A Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 23893605  J Pept Sci. 2013 Oct;19(10):619-28.  Gross S, Wilms D, Krause J, Brezesinski G, Andrä J.  Design of NK-2-derived peptides with improved activity against equine sarcoid cells. DRAMP35126 TPWWRLWTKWHHKRRDLPRKPEGC 24 FITC-Rath Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23937069 J Drug Target. 2013 Nov;21(9):801-8.  Kuo JH, Lin CW. Cellular uptake on N- and C-termini conjugated FITC of Rath cell penetrating peptides and its consequences for gene-expression profiling in U-937 human macrophages and HeLa cervical cancer cells. DRAMP35129 LTFEHYWAQLTS 12 ATSP-3848 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: -- (IC50 for MDM2=0.29 µM); -- (IC50 for MDMX-p53=1.6 µM) Not available Linear Acetylation Amidation L Not available MDM2, MDMX 23946421 Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-55. Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK. Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy DRAMP35130 LTFEHYWAQLTS 12 ATSP-3848 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available MDM2, MDMX 23946421 Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-55. Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK. Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy DRAMP35136 LSTAADMQGVVTDGMASGLDKDYLKPDD 28 p28 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 23952735 Mol Pharm. 2013 Sep 3;10(9):3375-83 Yamada T, Das Gupta TK, Beattie CW.  p28, an anionic cell-penetrating peptide, increases the activity of wild type and mutated p53 without altering its conformation. DRAMP35137 Pr 2 Cyclo(L-Pro-D-Arg), Diketopiperazine (Pr) Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 24097052 Folia Microbiol (Praha). 2014 May;59(3):197-202. Kumar SN, Mohandas C, Nambisan B, Sreerag RS, Jayaprakas CA. Cyclo(L-Pro-D-Arg): a new antibacterial and antitumour diketopiperazine from Bacillus cereus associated with a rhabditid entomopathogenic DRAMP35138 RXRRXRILFQYRXRRXR 17 LB1_1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-30.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35139 RXRRXRYQFLIRXRRXR 17 LB1_2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-31.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35140 RXRRXRFLQIYRXRRXR 17 LB1_3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-32.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35141 RXRRXRAAAAARXRRXR 17 LB1_4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-33.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35142 RXRRXRIKFQYRXRRXR 17 LB1_5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-34.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35143 RXRRXRIEFQYRXRRXR 17 LB1_6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-35.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35144 RXRRXRIWFQYRXRRXR 17 LB1_7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-36.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35145 RXRRXRIPFQYRXRRXR 17 LB1_8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-37.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35146 KXRKXRILFQYKXRKXR 17 LB1_9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-38.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35147 HXRHXRILFQYHXRHXR 17 LB1_10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-39.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35148 SXRSXRILFQYSXRSXR 17 LB1_11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-40.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35149 EXREXRILFQYEXREXR 17 LB1_12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-41.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35150 RMKWKKILFQYRXRRXR 17 LB1_13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-42.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35151 RXRRXRILFQYRMKWKK 17 LB1_14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-43.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35152 KKWKMRILFQYRXRRXR 17 LB1_15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-44.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35153 RXRRXRILFQYKKWKMR 17 LB1_16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear N-terminal alkyne is introduced using 4-pentynoic acid Amidation X=aminohexyl residue L Not available Not available 24105028  Org Biomol Chem. 2013 Nov 21;11(43):7621-45.  Deuss PJ, Arzumanov AA, Williams DL, Gait MJ.  Parallel synthesis and splicing redirection activity of cell-penetrating peptide conjugate libraries of a PNA cargo. DRAMP35154 YGRKKRRQRRRREADFFWSLCTADMS 26 KilerFLIP Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 24176852  Cell Death Dis. 2013 Oct 31;4(10):e894. Pennarun B, Gaidos G, Bucur O, Tinari A, Rupasinghe C, Jin T, Dewar R, Song K, Santos MT, Malorni W, Mierke D, Khosravi-Far R. killerFLIP: a novel lytic peptide specifically inducing cancer cell death. DRAMP35155 KLULKLULKULKAULKLU 18 MAP(Aib) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation U=α-amino isobutyric acid (Aib) L Not available Not available 24216093 Bioorg Med Chem. 2013 Dec 15;21(24):7669-73 Wada S, Hashimoto Y, Kawai Y, Miyata K, Tsuda H, Nakagawa O, Urata H.  Effect of Ala replacement with Aib in amphipathic cell-penetrating peptide on oligonucleotide delivery into cells. DRAMP35156 RKKRRQRRRGGG 12 Tat Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24218116  J Pharm Sci. 2014 Jan;103(1):293-304. Alkotaji M, Pluen A, Zindy E, Hamrang Z, Aojula H. On the cellular uptake and membrane effect of the multifunctional peptide, TatLK15. DRAMP35157 RKKRRQRRRGGGKLLKLLLKLLLKLLK 27 TatLK15 Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24218116  J Pharm Sci. 2014 Jan;103(1):293-305. Alkotaji M, Pluen A, Zindy E, Hamrang Z, Aojula H. On the cellular uptake and membrane effect of the multifunctional peptide, TatLK15. DRAMP35161 XVTXVXVXXVXV 12 Ohmyungsamycin B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24266328 J Org Chem. 2013 Dec 20;78(24):12321-9.  Um S, Choi TJ, Kim H, Kim BY, Kim SH, Lee SK, Oh KB, Shin J, Oh DC.  Ohmyungsamycins A and B: cytotoxic and antimicrobial cyclic peptides produced by Streptomyces sp from a volcanic island DRAMP35162 KCFQAQRNMRKVRGPPVSCIKR 22 hLF W5A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-29.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35163 KCFQWARNMRKVRGPPVSCIKR 22 hLF Q6A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-30.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35164 KCFQWQRNARKVRGPPVSCIKR 22 hLF M9A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-31.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35165 KCFQWQRNMRKVRGAPVSCIKR 22 hLF P15A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-32.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35166 KCFQWQRNMRKRRGPPVSCIKR 22 hLF V12R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-33.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35167 KCFQWQANMRKVRGPPVSCIKR 22 hLF R7A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-34.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35168 KCFQWQRNMRKVAGPPVSCIKR 22 hLF R13A Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-35.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35169 KCFQWQANMRKRRGPPVSCIKR 22 hLF R7A/V12R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-36.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35170 KCFQWQRNMRKVAGRPVSCIKR 22 hLF R13A/P15R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-37.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35171 KCFRWQRNRRKVRGRPVRCIKR 22 hLF +4R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-38.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35172 KRFRWQRNMRKVRGRPVRSIKR 22 hLF lin+4R Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-39.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35173 RCFQWQRNMRRVRGPPVSCIRR 22 hLF R7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-40.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35174 KCFQWQKNMKKVKGPPVSCIKK 22 hLF K7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-41.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35175 KXFQWQRNMRKVRGPPVSXIKR 22 hLF Hcy Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Fluorescein Amidation X=Hcy, homocysteine in which the side chain is one methylene group longer than in cysteine L Not available Not available 24270856 Cell Mol Life Sci. 2014 Jul;71(14):2717-42.  Wallbrecher R, Verdurmen WP, Schmidt S, Bovee-Geurts PH, Broecker F, Reinhardt A, van Kuppevelt TH, Seeberger PH, Brock R. The stoichiometry of peptide-heparan sulfate binding as a determinant of uptake efficiency of cell-penetrating peptides. DRAMP35176 GALFLAFLAAALSLMGLWSQPKKKRKV 27 MPGα Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Cysteamide group L Not available Not available 24275947 Pharmaceuticals (Basel). 2013 Feb 6;6(2):184-203.  Keller AA, Mussbach F, Breitling R, Hemmerich P, Schaefer B, Lorkowski S, Reissmann S. Relationships between Cargo, Cell Penetrating Peptides and Cell Type for Uptake of Non-Covalent Complexes into Live Cells. DRAMP35177 KLPVM 5 CPPP-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24275947 Pharmaceuticals (Basel). 2013 Feb 6;6(2):184-204.  Keller AA, Mussbach F, Breitling R, Hemmerich P, Schaefer B, Lorkowski S, Reissmann S. Relationships between Cargo, Cell Penetrating Peptides and Cell Type for Uptake of Non-Covalent Complexes into Live Cells. DRAMP35178 KLFMALVAFLRFLTIPPTAGILKRWGTI 28 pepM Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 24286593 FEBS J. 2014 Jan;281(1):191-215. Freire JM, Veiga AS, Rego de Figueiredo I, de la Torre BG, Santos NC, Andreu D, Da Poian AT, Castanho MA. Nucleic acid delivery by cell penetrating peptides derived from dengue virus capsid protein: design and mechanism of action. DRAMP35179 LKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRR 35 pepR Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 24286593 FEBS J. 2014 Jan;281(1):191-216. Freire JM, Veiga AS, Rego de Figueiredo I, de la Torre BG, Santos NC, Andreu D, Da Poian AT, Castanho MA. Nucleic acid delivery by cell penetrating peptides derived from dengue virus capsid protein: design and mechanism of action. DRAMP35180 CETPSKHFNGLCIRSSNCASVCHGEHFTDGRCQGVRRRCMCLKPC 45 PaDef Not available Not found Persea americana Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 24319695 Biomed Res Int. 2013;2013:986273.  Guzmán-Rodríguez JJ, López-Gómez R, Suárez-Rodríguez LM, Salgado-Garciglia R, Rodríguez-Zapata LC, Ochoa-Zarzosa A, López-Meza JE. Antibacterial activity of defensin PaDef from avocado fruit (Persea americana var. drymifolia) expressed in endothelial cells against Escherichia coli and Staphylococcus aureus. DRAMP35181 CELAGIGILTVRKKRRQRRR 20 Alexa488-Melan-A-TAT Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugation with Alexa488 C5 maleimide Free L Not available Not available 24372650  Exp Dermatol. 2014 Jan;23(1):20-6.  Buhl T, Braun A, Forkel S, Möbius W, van Werven L, Jahn O, Rezaei-Ghaleh N, Zweckstetter M, Mempel M, Schön MP, Haenssle HA.  Internalization routes of cell-penetrating melanoma antigen peptides into human dendritic cells. DRAMP35182 CELAGIGILTVKKKKKQKKK 20 Alexa488-Melan-A-polyLys (control peptide) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24372650  Exp Dermatol. 2014 Jan;23(1):20-7.  Buhl T, Braun A, Forkel S, Möbius W, van Werven L, Jahn O, Rezaei-Ghaleh N, Zweckstetter M, Mempel M, Schön MP, Haenssle HA.  Internalization routes of cell-penetrating melanoma antigen peptides into human dendritic cells. DRAMP35183 RIMRILRILKLAR 13 DS4.3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24416126 PLoS One. 2014 Jan 8;9(1):e80050.  Jeong JH, Kim K, Lim D, Jeong K, Hong Y, Nguyen VH, Kim TH, Ryu S, Lim JA, Kim JI, Kim GJ, Kim SC, Min JJ, Choy HE. Anti-tumoral effect of the mitochondrial target domain of Noxa delivered by an engineered Salmonella typhimurium. DRAMP35184 GRGDSPRR 8 Pep1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free Phosphorylation L Not available Not available 24462902 J Control Release. 2014 Apr 10;179:1-9.  Remaut K, Symens N, Lucas B, Demeester J, De Smedt SC.  Cell division responsive peptides for optimized plasmid DNA delivery: the mitotic window of opportunity? DRAMP35185 GRGDSPRRSPRR 12 Pep2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free Phosphorylation L Not available Not available 24462902 J Control Release. 2014 Apr 10;179:1-10.  Remaut K, Symens N, Lucas B, Demeester J, De Smedt SC.  Cell division responsive peptides for optimized plasmid DNA delivery: the mitotic window of opportunity? DRAMP35186 GRGDSPRRKKKKSPRRKKKKSPRR 24 Pep3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free Phosphorylation L Not available Not available 24462902 J Control Release. 2014 Apr 10;179:1-11.  Remaut K, Symens N, Lucas B, Demeester J, De Smedt SC.  Cell division responsive peptides for optimized plasmid DNA delivery: the mitotic window of opportunity? DRAMP35187 GRGDGPRRKKKKGPRRKKKKGPRR 24 Pep3(Mutant) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free L Not available Not available 24462902 J Control Release. 2014 Apr 10;179:1-12.  Remaut K, Symens N, Lucas B, Demeester J, De Smedt SC.  Cell division responsive peptides for optimized plasmid DNA delivery: the mitotic window of opportunity? DRAMP35188 XPX 3 Psychrophilin E Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24483240  Nat Prod Res. 2014;28(11):776-81.  Ebada SS, Fischer T, Hamacher A, Du FY, Roth YO, Kassack MU, Wang BG, Roth EH. Psychrophilin E, a new cyclotripeptide, from co-fermentation of two marine alga-derived fungi of the genus Aspergillus DRAMP35189 CGGKDCERRFSRSDQLKRHQRRHTGVKPFQ 30 b-WT1-pTj Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation Amidation L Not available Not available 24490140 FEBS Open Bio. 2014 Jan 21;4:153-61.  Massaoka MH, Matsuo AL, Figueiredo CR, Girola N, Faria CF, Azevedo RA, Travassos LR. A novel cell-penetrating peptide derived from WT1 enhances p53 activity, induces cell senescence and displays antimelanoma activity in xeno- and syngeneic systems. DRAMP35190 KDCERRFSRSDQLKRHQRRHTGVKPFQK 28 FITC-WT1-pTj Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24490140 FEBS Open Bio. 2014 Jan 21;4:153-62.  Massaoka MH, Matsuo AL, Figueiredo CR, Girola N, Faria CF, Azevedo RA, Travassos LR. A novel cell-penetrating peptide derived from WT1 enhances p54 activity, induces cell senescence and displays antimelanoma activity in xeno- and syngeneic systems. DRAMP35191 YGRGGRRGRRR 11 RTAT-ELPBC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear ELPBC Free L Not available Not available 24611762 Nano Lett. 2014;14(4):2058-64. MacEwan SR, Chilkoti A Controlled apoptosis by a thermally toggled nanoscale amplifier of cellular uptake. DRAMP35192 RRRRRRRRRGDfK 13 R8-RGD-lipo Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Cysteine modified octa-arginine conjugated to the branch of lysine Mix Not available Not available 24651033 Biomaterials. 2014 Jun;35(17):4835-47. Liu Y, Ran R, Chen J, Kuang Q, Tang J, Mei L, Zhang Q, Gao H, Zhang Z, He Q.  Paclitaxel loaded liposomes decorated with a multifunctional tandem peptide for glioma targeting. DRAMP35193 BRRXRRXRRX 10 FAM-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FAM, fluorescein Amidation B=Beta-Alanine; X=α-amino isobutyric acid L Not available Not available 24661993 Bioorg Med Chem. 2014 Apr 15;22(8):2403-8.  Yamashita H, Demizu Y, Shoda T, Sato Y, Oba M, Tanaka M, Kurihara M. Amphipathic short helix-stabilized peptides with cell-membrane penetrating ability. DRAMP35194 BrrXrrXrrX 10 ent FAM-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FAM, fluorescein Amidation B=Beta-Alanine; X=α-amino isobutyric acid Mix Not available Not available 24661993 Bioorg Med Chem. 2014 Apr 15;22(8):2403-9.  Yamashita H, Demizu Y, Shoda T, Sato Y, Oba M, Tanaka M, Kurihara M. Amphipathic short helix-stabilized peptides with cell-membrane penetrating ability. DRAMP35195 BRrXRrXRrX 10 FAM-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FAM, fluorescein Amidation B=Beta-Alanine; X=α-amino isobutyric acid Mix Not available Not available 24661993 Bioorg Med Chem. 2014 Apr 15;22(8):2403-10.  Yamashita H, Demizu Y, Shoda T, Sato Y, Oba M, Tanaka M, Kurihara M. Amphipathic short helix-stabilized peptides with cell-membrane penetrating ability. DRAMP35196 BXRXRXXRXRXXRXRX 16 FAM-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FAM, fluorescein Amidation B=Beta-Alanine; X=α-amino isobutyric acid L Not available Not available 24661993 Bioorg Med Chem. 2014 Apr 15;22(8):2403-11.  Yamashita H, Demizu Y, Shoda T, Sato Y, Oba M, Tanaka M, Kurihara M. Amphipathic short helix-stabilized peptides with cell-membrane penetrating ability. DRAMP35197 LPIP 4 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=26.6µM); HeLa (IC50=34.7µM) Not available Cyclic Free Free L Not available Not available 24690914 J Antibiot (Tokyo). 2014 Jul;67(7):541-3.  Gao CH, Chen YN, Pan LX, Lei F, Long B, Hu LQ, Zhang RC, Ke K, Huang RM.  Two new cyclic tetrapeptides from deep-sea bacterium Bacillus amyloliquefaciens GAS 00152 DRAMP35198 FPYG 4 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=38.2µM); HeLa (IC50=46.1µM) Not available Cyclic Free Free L Not available Not available 24690914 J Antibiot (Tokyo). 2014 Jul;67(7):541-4.  Gao CH, Chen YN, Pan LX, Lei F, Long B, Hu LQ, Zhang RC, Ke K, Huang RM.  Two new cyclic tetrapeptides from deep-sea bacterium Bacillus amyloliquefaciens GAS 00152 DRAMP35199 GGGGRRRRRRRRRLLLL 17 m9R Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Maleimide addition Free L Not available Not available 24696462 Genome Res. 2014 Jun;24(6):1020-7.  Ramakrishna S, Kwaku Dad AB, Beloor J, Gopalappa R, Lee SK, Kim H. Gene disruption by cell-penetrating peptide-mediated delivery of Cas9 protein and guide RNA. DRAMP35200 CGGGRRRRRRRRRLLLL 17 sgRNA-CPP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24696462 Genome Res. 2014 Jun;24(6):1020-8.  Ramakrishna S, Kwaku Dad AB, Beloor J, Gopalappa R, Lee SK, Kim H. Gene disruption by cell-penetrating peptide-mediated delivery of Cas10 protein and guide RNA. DRAMP35201 XACSGSGSGCGSGSGSCG 18 IA0 (Bicyclic) (integral arginine peptides) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-64. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35202 XACSGRGSGCGSGRGSCG 18 IA2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-65. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35203 XACRGSGRGCGRGSGRCG 18 IA4a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-66. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35204 XACSGRGRGCGRGRGSCG 18 IA4b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-67. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35205 XACRGRGRGCGRGRGRCG 18 IA6a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-68. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35206 XACGRGRGRCRGRGRGCG 18 IA6b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-69. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35207 XACRGRGRGCRGRGRGCG 18 IA6c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-70. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35208 XACGRGRGRCGRGRGRCG 18 IA6d Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-71. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35209 XACRGRRRGCGRRRGRCG 18 IA8a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-72. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35210 XACRRSRRGCGRRSRRCG 18 IA8b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-73. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35211 XACRRSRRGCGRRSRRCG 18 IA8b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-73. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35212 XACSDRFRNCPADEALCG 18 kCA2 (Kallikrein inhibitor with internal arginines) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-74. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35213 XACRDRFRNCPADEALCG 18 kCA3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-75. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35214 XACRDRFRNCPADERLCG 18 kCA4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-76. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35215 XACRDRFRRCPADERLCG 18 kCA5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-77. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35216 XACRDRFRRCPADRRLCG 18 kCA6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-78. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35217 XACSGRGRGCGSGSGSCG 18 CA2 (Control internal arginine ) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-79. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35218 XACRGRGRGCGSGSGSCG 18 CA3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-80. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35219 XACRGRGRGCGSGSRSCG 18 CA4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-81. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35220 XACRGRGRRCGSGSRSCG 18 CA5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-82. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35221 XACRGRGRRCGSGRRSCG 18 CA6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-83. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35222 XACRGRGRRCGSGRRSCG 18 CA6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-83. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35223 XARCSGSGSGCGSGSGSCGR 20 EA2x1 (External arginines) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-84. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35224 XARRCSGSGSGCGSGSGSCGRR 22 EA2x2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-85. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35225 XARRRCSGSGSGCGSGSGSCGRRR 24 EA2x3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-86. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35226 XARRRRCSGSGSGCGSGSGSCGRRRR 26 EA2x4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-87. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35227 XACSGSGSGCGSGSGSCGRRRRRRRR 26 EA1x8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-88. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35228 XACSGSGSGCGSGSGSCGRRRRRRRR 26 EA1x8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-88. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35229 XARCSDRFRNCPADEALCGR 20 kEA2x1 (Kallikrein inhibitor with external arginines) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-89. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35230 XARRCSDRFRNCPADEALCGRR 22 kEA2x2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-90. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35231 XARRRCSDRFRNCPADEALCGRRR 24 kEA2x3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-91. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35232 XARRRRCSDRFRNCPADEALCGRRRR 26 kEA2x4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-92. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35233 XACSDRFRNCPADEALCGRRRRRRRR 26 kEA1 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-93. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35234 XACSDRFRNCPADEALCGRRRRRRRR 26 kEA1 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-93. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35235 XACRRSRRGCGRRSRRCG 18 IA8b L (Linear variants) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-94. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35236 XACRRSRRGCGRRSRRCG 18 IA8b L (Linear variants) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-94. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35237 XACRGRGRRCGSGRRSCG 18 CA6 L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-95. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35238 XACRGRGRRCGSGRRSCG 18 CA6 L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-95. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35239 XACSGSGSGCGSGSGSCGRRRRRRRR 26 EA1x8 L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-96. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35240 XACSGSGSGCGSGSGSCGRRRRRRRR 26 EA1x8 L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-96. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35241 XACSDRFRNCPADEALCGRRRRRRRR 26 kEA1x8L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-97. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35242 XACSDRFRNCPADEALCGRRRRRRRR 26 kEA1x8L Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-97. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35243 XACSHSGHGCGHGSHSCGRRRRRRRR 26 EA8_4H (Histidine/tryptophan peptides) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-98. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35244 XACSHSGWGCGHGSWSCGRRRRRRRR 26 EA8_2H2W Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-99. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35245 XACHGRRWGCGRHRGRCG 18 IA5_2H1W Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 24697151 ioconjug Chem. 2014 May 21;25(5):955-100. Wallbrecher R, Depré L, Verdurmen WP, Bovée-Geurts PH, van Duinkerken RH, Zekveld MJ, Timmerman P, Brock R. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. DRAMP35246 HEHEHEHEHEHEHEHEEFGGGGGYGRGRGRGRGRGRG 37 GST-(HE)8EFG5YG(RG)6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-90.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35247 HEHEHEHEHEHEHEHEHEHEEFGGGGGYGRGRGRGRGRGRG 41 GST-(HE)10EFG5YG(RG)6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-91.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35248 HEHEHEHEHEHEHEHEHEHEHEHEEFGGGGGYGRGRGRGRGRGRG 45 GST-(HE)12EFG5YG(RG)6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-92.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35249 HEHEHEHEHEHEHEHEEFGGGGGYGRRRRRRGGGGGG 37 GST-(HE)8EFG5YGR6G6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-93.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35250 HEHEHEHEHEHEHEHEHEHEEFGGGGGYGRRRRRRGGGGGG 41 GST-(HE)10EFG5YGR6G6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-94.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35251 HEHEHEHEHEHEHEHEHEHEHEHEEFGGGGGYGRRRRRRGGGGGG 45 GST-(HE)12EFG5YGR6G6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-95.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35252 HEHEHEHEHEHEHEHEHEHEHEHEEFGGGGGYGRKKRRQRRR 42 GST-(HE)12EFG5-TAT Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Glutathione S-transferase Free L Not available Not available 24697211  Mol Pharm. 2014 May 5;11(5):1583-96.  Sun C, Shen WC, Tu J, Zaro JL.  Interaction between cell-penetrating peptides and acid-sensitive anionic oligopeptides as a model for the design of targeted drug carriers. DRAMP35253 IPLVVPLC 8 IPL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24704199 Eur J Pharm Biopharm. 2014 Aug;87(3):489-99.  Kang MH, Park MJ, Yoo HJ, hyuk KY, Lee SG, Kim SR, Yeom DW, Kang MJ, Choi YW.  RIPL peptide (IPLVVPLRRRRRRRRC)-conjugated liposomes for enhanced intracellular drug delivery to hepsin-expressing cancer cells. DRAMP35254 IPLVVPLRRRRRRRRC 16 RIPL peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24704199 Eur J Pharm Biopharm. 2014 Aug;87(3):489-100.  Kang MH, Park MJ, Yoo HJ, hyuk KY, Lee SG, Kim SR, Yeom DW, Kang MJ, Choi YW.  RIPL peptide (IPLVVPLRRRRRRRRC)-conjugated liposomes for enhanced intracellular drug delivery to hepsin-expressing cancer cells. DRAMP35255 PKKKRKVAGYLLGKINLKALAALAKKILPQMQQNVFQYPGAGMVPQGEANF 51 TP10-SRC1LXXLL Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24705462 Int J Mol Sci. 2014 Apr 3;15(4):5680-98.  Tints K, Prink M, Neuman T, Palm K.  LXXLL peptide converts transportan 10 to a potent inducer of apoptosis in breast cancer cells. DRAMP35256 PKKKRKVRRRRRRRYSQTSHKLVQLLTTAEQQ 32 R7-SRC1LXXLL Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24705462 Int J Mol Sci. 2014 Apr 3;15(4):5680-99.  Tints K, Prink M, Neuman T, Palm K.  LXXLL peptide converts transportan 10 to a potent inducer of apoptosis in breast cancer cells. DRAMP35257 PKKKRKVRRRRRRRPQMQQNVFQYPGAGMVPQGEANF 37 R7-SRC1(1222-1245) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear NLS Free L Not available Not available 24705462 Int J Mol Sci. 2014 Apr 3;15(4):5680-100.  Tints K, Prink M, Neuman T, Palm K.  LXXLL peptide converts transportan 10 to a potent inducer of apoptosis in breast cancer cells. DRAMP35258 AYGRKKRRQRRR 12 TAT-cysteine peptide Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24709209 Int J Pharm. 2014 Jul 1;468(1-2):26-38. Mei L, Fu L, Shi K, Zhang Q, Liu Y, Tang J, Gao H, Zhang Z, He Q. Increased tumor targeted delivery using a multistage liposome system functionalized with RGD, TAT and cleavable PEG. DRAMP35259 WELVVLGKLYGRKKRRQRRR 20 pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-26.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35260 ELVVLGKLYGRKKRRQRRR 19 N-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-27.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35261 LVVLGKLYGRKKRRQRRR 18 N2-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-28.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35262 VVLGKLYGRKKRRQRRR 17 N3-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-29.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35263 WELVVLGKYGRKKRRQRRR 19 C1-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-30.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35264 WELVVLGYGRKKRRQRRR 18 C2-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-31.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35265 WELVVLYGRKKRRQRRR 17 C3-pep5-cpp* Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-32.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35266 WELVVLYGRKKRRQRRR 17 C3-pep5-cpp* Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-32.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35267 WELVVYGRKKRRQRRR 16 C4-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-33.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35268 WELVYGRKKRRQRRR 15 C5-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-34.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35269 WELYGRKKRRQRRR 14 C6-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-35.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35270 WEYGRKKRRQRRR 13 C7-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-36.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35271 WELVVAYGRKKRRQRRR 17 A Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-37.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35272 WEAVVLYGRKKRRQRRR 17 B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-38.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35273 WEAVVAYGRKKRRQRRR 17 C Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-39.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35274 WELVVLYGRKKRRQRRR 17 Ac-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-40.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35275 WELVVLYGRKKRRQRRR 17 Ac-pep5-cpp Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Free L Not available Not available 24764300  J Biol Chem. 2014 Jun 13;289(24):16711-40.  de Araujo CB, Russo LC, Castro LM, Forti FL, do Monte ER, Rioli V, Gozzo FC, Colquhoun A, Ferro ES.  A novel intracellular peptide derived from g1/s cyclin d2 induces cell death. DRAMP35276 YARVRRRGPRR 11 Hph-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 6-histidine tag Free L Not available Not available 24768403  Int J Pharm. 2014 Jul 20;469(1):206-13. Li H, Zheng X, Koren V, Vashist YK, Tsui TY. Highly efficient delivery of siRNA to a heart transplant model by a novel cell penetrating peptide-dsRNA binding domain. DRAMP35277 CRQIKIWFQNRRMKWKK 17 Penetratin Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24796502 Biochim Biophys Acta. 2014 Aug;1838(8):2087-98. Alves ID, Carré M, Montero MP, Castano S, Lecomte S, Marquant R, Lecorché P, Burlina F, Schatz C, Sagan S, Chassaing G, Braguer D, Lavielle S.  A proapoptotic peptide conjugated to penetratin selectively inhibits tumor cell growth. DRAMP35278 CRQIKIWFQNRRMKWKKKLAKLAKKLAKLAK 31 KLA-Pen Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24796502 Biochim Biophys Acta. 2014 Aug;1838(8):2087-99. Alves ID, Carré M, Montero MP, Castano S, Lecomte S, Marquant R, Lecorché P, Burlina F, Schatz C, Sagan S, Chassaing G, Braguer D, Lavielle S.  A proapoptotic peptide conjugated to penetratin selectively inhibits tumor cell growth. DRAMP35279 LCLRPVG 7 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4900. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35280 LCLRP 5 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4901. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35281 LCLR 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4902. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35282 LLR 3 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4903. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35283 LLLR 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4904. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35284 LLLLR 5 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4905. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35285 LLLRR 5 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4906. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35286 IIIR 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4907. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35287 VVVR 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4908. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35288 LCLK 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4909. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35289 LCLH 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4910. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35290 LCLE 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4911. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35291 LCLN 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4912. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35292 LCLQ 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24811205 Sci Rep. 2014 May 9;4:4913. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35293 lclrpvg 7 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4914. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35294 lclrp 5 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4915. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35295 lclr 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4916. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35296 lcl 3 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4917. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35297 icir 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4918. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35298 vcvr 4 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4919. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35299 vlclr 5 Xentry peptides Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 24811205 Sci Rep. 2014 May 9;4:4920. Montrose K, Yang Y, Krissansen GW.  The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: novel activatable forms of Xentry. DRAMP35300 CRRLRHLRHHYRRRWHRFRC 20 Mgpe-9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Addition of cysteine in Mgpe3 sequence makes Mgpe9 L Not available Not available 24816284  Biomaterials. 2014 Aug;35(24):6563-75.  Sharma R, Nisakar D, Shivpuri S, Ganguli M. Contrasting effects of cysteine modification on the transfection efficiency of amphipathic peptides. DRAMP35301 CLLYWFRRRHRHHRRRHRRC 20 Mgpe-10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Addition of cysteine in Mgpe4 sequence makes Mgpe10 L Not available Not available 24816284  Biomaterials. 2014 Aug;35(24):6563-76.  Sharma R, Nisakar D, Shivpuri S, Ganguli M. Contrasting effects of cysteine modification on the transfection efficiency of amphipathic peptides. DRAMP35302 RRLRHLRHHYRRRWHRFR 18 Mgpe-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24816284  Biomaterials. 2014 Aug;35(24):6563-77.  Sharma R, Nisakar D, Shivpuri S, Ganguli M. Contrasting effects of cysteine modification on the transfection efficiency of amphipathic peptides. DRAMP35303 LLYWFRRRHRHHRRRHRR 18 Mgpe-4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 24816284  Biomaterials. 2014 Aug;35(24):6563-78.  Sharma R, Nisakar D, Shivpuri S, Ganguli M. Contrasting effects of cysteine modification on the transfection efficiency of amphipathic peptides. DRAMP35304 GLKKLARLFHKLLKLGC 17 RF Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24867193 Org Biomol Chem. 2014 Jul 14;12(26):4673-81. Yang J, Tsutsumi H, Furuta T, Sakurai M, Mihara H.  Interaction of amphiphilic α-helical cell-penetrating peptides with heparan sulfate. DRAMP35305 GLKKLAELFHKLLKLGC 17 EF Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24867193 Org Biomol Chem. 2014 Jul 14;12(26):4673-82. Yang J, Tsutsumi H, Furuta T, Sakurai M, Mihara H.  Interaction of amphiphilic α-helical cell-penetrating peptides with heparan sulfate. DRAMP35306 GLKKLARLAHKLLKLGC 17 RA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24867193 Org Biomol Chem. 2014 Jul 14;12(26):4673-83. Yang J, Tsutsumi H, Furuta T, Sakurai M, Mihara H.  Interaction of amphiphilic α-helical cell-penetrating peptides with heparan sulfate. DRAMP35307 GLKKLAELAHKLLKLGC 17 EA Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24867193 Org Biomol Chem. 2014 Jul 14;12(26):4673-84. Yang J, Tsutsumi H, Furuta T, Sakurai M, Mihara H.  Interaction of amphiphilic α-helical cell-penetrating peptides with heparan sulfate. DRAMP35308 YGRKKRRQRRRGC 13 TAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24867193 Org Biomol Chem. 2014 Jul 14;12(26):4673-85. Yang J, Tsutsumi H, Furuta T, Sakurai M, Mihara H.  Interaction of amphiphilic α-helical cell-penetrating peptides with heparan sulfate. DRAMP35309 RLRLRLRLRLRLRLRLKRLKRLKRLKRLKKKKKKKGYK 38 D1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-7. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35310 RLRLRLRLRLRLRLRLKLLKLLKLLKLLKKKKKKKGYK 38 D2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-8. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35311 RLRLRLRLRLRLRLRLKNNKNNKNNKNNKKKKKKKGYK 38 D3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-9. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35312 GYGYGYGYGYGYGYGYKKRKKRKKRKKRKQQKQQKRRK 38 D4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-10. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35313 GYGYGYGYGYGYGYGYKKRKKRKKRKKRKQQKQQKRRK 38 D4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-10. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35314 GYGYGYGYGYGYGYGYKKRKKRKKRKKRKQQKQQKRRK 38 AcD4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-11. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35315 GYGYGYGYGYGYGYGYKKRKKRKKRKKRKQQKQQKRRK 38 AcD4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-11. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35316 ALALALALALALALALKIKKIKKIKKIKKLAKLAKKIK 38 D5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-12. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35317 LALALALALALALALAKKLKKLKKLKKLKKLKKLKYAK 38 D6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-13. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35318 LALALALALALALALAKKLKKLKKLKKLKKLKKLKYAK 38 D6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-13. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35319 LALALALALALALALAKKLKKLKKLKKLKKLKKLKYAK 38 AcD6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-14. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35320 LALALALALALALALAKKLKKLKKLKKLKKLKKLKYAK 38 AcD6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-14. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35321 IKIKIKIKIKIKIKIKKLAKLAKLAKLAKLAKLAKKIK 38 D7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-15. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35322 IKIKIKIKIKIKIKIKKLAKLAKLAKLAKLAKLAKKIK 38 D7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-15. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35323 IKIKIKIKIKIKIKIKKLAKLAKLAKLAKLAKLAKKIK 38 AcD7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-16. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35324 IKIKIKIKIKIKIKIKKLAKLAKLAKLAKLAKLAKKIK 38 AcD7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-16. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35325 LALALALALALALALAKIKKIKKIKKIKKLAKLAKKIK 38 D8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-17. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35326 LALALALALALALAKLAKLAKLAKLAKIKKIKKKIK 36 D9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-18. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35327 LALALALALALALALAKLAKLAKLAKLAKLAKKIK 35 D10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-19. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35328 LILILILILILILILIKRKKRKKRKKRKKRAKRAKHSK 38 D11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-20. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35329 LILILILILILILILIKRKKRKKRKKRKKRAKRAKHSK 38 D11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-20. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35330 LILILILILILILILIKRKKRKKRKKRKKRAKRAKHSK 38 AcD11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-21. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35331 LILILILILILILILIKRKKRKKRKKRKKRAKRAKHSK 38 AcD11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 24870379 Chem Commun (Camb). 2014 Jul 14;50(55):7254-21. Eggimann GA, Blattes E, Buschor S, Biswas R, Kammer SM, Darbre T, Reymond JL.  Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. DRAMP35332 XGLFGCGRKKRRQRRRPPQ 19 NTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Doxorubicin L Not available Not available 24892976 J Control Release. 2014 Oct 10;191:123-30. Chen Z, Zhang P, Cheetham AG, Moon JH, Moxley JW Jr, Lin YA, Cui H.  Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. DRAMP35333 (XGLFGC)(XGLFGC)KGRKKRRQRRRPPQ 26 d-NTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Doxorubicin L Not available Not available 24892976 J Control Release. 2014 Oct 10;191:123-31. Chen Z, Zhang P, Cheetham AG, Moon JH, Moxley JW Jr, Lin YA, Cui H.  Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. DRAMP35334 [(XGLFGC)(XGLFGC)K][(XGLFGC)(XGLFGC)K]KGRKKRRQRRRPPQ 40 q-NTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Doxorubicin L Not available Not available 24892976 J Control Release. 2014 Oct 10;191:123-32. Chen Z, Zhang P, Cheetham AG, Moon JH, Moxley JW Jr, Lin YA, Cui H.  Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. DRAMP35335 XCGRKKRRQRRRPPQ 15 n-NTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Doxorubicin L Not available Not available 24892976 J Control Release. 2014 Oct 10;191:123-33. Chen Z, Zhang P, Cheetham AG, Moon JH, Moxley JW Jr, Lin YA, Cui H.  Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. DRAMP35336 XGLFGXGRKKRRQRRRPPQ 19 C16NTD Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X(1)=Doxorubicin; X(6)=(C16)Cys, Cys-Palmitoylation L Not available Not available 24892976 J Control Release. 2014 Oct 10;191:123-34. Chen Z, Zhang P, Cheetham AG, Moon JH, Moxley JW Jr, Lin YA, Cui H.  Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. DRAMP35337 FΦRRRRQKX 9 cFΦR4-Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-46.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35338 FΦRRRRQKX 9 cFΦR4-Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-46.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35339 FΦRRRRQKX 9 cFΦR4-Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-46.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35340 FΦRRRRQKX 9 cFΦR4-Dex Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Dex, dexamethasone Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-47.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35341 FΦRRRRQKX 9 cFΦR4-Dex Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Dex, dexamethasone Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-47.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35342 FΦRRRRQKX 9 cFΦR4-Dex Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Dex, dexamethasone Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-47.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35343 KXGRKKRRQRRRPPQY 16 Tat-Dex Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Dex, dexamethasone L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-48.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35344 FΦRRRRQKX 9 cFΦR4-FITC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free FITC, fluorescein isothiocyanate Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-49.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35345 FΦRRRRQKX 9 cFΦR4-FITC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free FITC, fluorescein isothiocyanate Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-49.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35346 FΦRRRRQKX 9 cFΦR4-FITC Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free FITC, fluorescein isothiocyanate Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-49.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35347 FΦRRRRQRRRRRKX 14 cFΦR4-R5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-50.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35348 FΦRRRRQAAAAAKX 14 cFΦR4-A5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-51.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35349 FΦRRRRQFFFFKX 13 cFΦR4-F4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Rho, rhodamine B Φ=L-2-naphthylalanine L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-52.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35350 FΦRRRRQXDEXLI 13 cFΦR4-PCP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation Φ=L-2-naphthylalanine; X(8)=miniPEG, 8-amino-3,6-dioxaoctanoic acid; X(11)=Pcap, phosphocoumaryl aminopropionic acid L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-53.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35351 RRRRRRRRRXDEXLI 15 R9-PCP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation Φ=L-2-naphthylalanine; X(10)=miniPEG, 8-amino-3,6-dioxaoctanoic acid; X(13)=Pcap, phosphocoumaryl aminopropionic acid L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-54.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35352 RKKRRQRRRXDEXLI 15 Tat-PCP Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation Φ=L-2-naphthylalanine; X(10)=miniPEG, 8-amino-3,6-dioxaoctanoic acid; X(13)=Pcap, phosphocoumaryl aminopropionic acid L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-55.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35353 RQIKIWFQNRRMKWKKXDEXLI 22 Antp-PCP Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation Φ=L-2-naphthylalanine; X(17)=miniPEG, 8-amino-3,6-dioxaoctanoic acid; X(20)=Pcap, phosphocoumaryl aminopropionic acid L Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-56.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35354 XAAAAAKRRRRΦFXKX 16 bicyclo(FΦR4-A5)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation X(1)=Tm, trimesoyl; Φ=L-2-naphthylalanine; X(14)=L-2,3-diaminopropionic acid; X(16)=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-57.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35355 XAAAAAAAKRRRRΦFXKX 18 bicyclo(FΦR4-A7)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation X(1)=Tm, trimesoyl; Φ=L-2-naphthylalanine; X(16)=L-2,3-diaminopropionic acid; X(18)=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-58.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35356 XRARARKRRRRΦFXKX 16 bicyclo(FΦR4-RARAR)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation X(1)=Tm, trimesoyl; Φ=L-2-naphthylalanine; X(14)=L-2,3-diaminopropionic acid; X(16)=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-59.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35357 XDADADKRRRRΦFXKX 16 bicyclo(FΦR4-DADAD)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation X(1)=Tm, trimesoyl; Φ=L-2-naphthylalanine; X(14)=L-2,3-diaminopropionic acid; X(16)=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-60.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35358 AAAAARRRRΦFKX 13 monocyclo(FΦR4-A5)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation Φ=L-2-naphthylalanine; X=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-61.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35359 AAAAAAARRRRΦFKX 15 monocyclo(FΦR4-A7)Rho Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Amidation Φ=L-2-naphthylalanine; X=Rho, rhodamine B Mix Not available Not available 24896852 Biochemistry. 2014 Jun 24;53(24):4034-62.  Qian Z, LaRochelle JR, Jiang B, Lian W, Hard RL, Selner NG, Luechapanichkul R, Barrios AM, Pei D.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35360 YGRKKRRQRRRYGRKKRRQRRRYGRKKRRQRRR 33 SP-Tatm3xCherry Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Coupled to signal peptide mCherry L Not available Not available 24928321 J Control Release. 2014 Aug 28;188:44-52.  Shen Y, Nagpal P, Hay JG, Sauthoff H.  Early endosomal escape of a cyclic cell-penetrating peptide allows effective cytosolic cargo delivery. DRAMP35361 CKYGRKKRRQRRR 13 fTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Extra Cys and Lys added for labeling of TMR Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-7. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35362 CKYGRKKRRQRRR 13 fTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Extra Cys and Lys added for labeling of TMR Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-7. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35363 RRRQRRKKRGYCKCKYGRKKRRQRRR 26 dfTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Extra Cys and Lys added for labeling of TMR and dimerization Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-8. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35364 RRRQRRKKRGYCKCKYGRKKRRQRRR 26 dfTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Extra Cys and Lys added for labeling of TMR and dimerization Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-8. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35365 CKYGRKKRRQRRR 13 acFTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetamidation Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-9. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35366 CKYGRKKRRQRRR 13 acFTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetamidation Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-9. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35367 RRRQRRKKRGYCKCKYGRKKRRQRRR 26 nrdfTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear bis(maleimido)ethane added Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-10. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35368 RRRQRRKKRGYCKCKYGRKKRRQRRR 26 nrdfTAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear bis(maleimido)ethane added Free L Not available Not available 24930129 Nat Methods. 2014 Aug;11(8):861-10. Erazo-Oliveras A, Najjar K, Dayani L, Wang TY, Johnson GA, Pellois JP.  Protein delivery into live cells by incubation with an endosomolytic agent. DRAMP35369 RKWWK 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24946217  Eur J Med Chem. 2014 Aug 18;83:36-44.  Fang Y, Zhong W, Wang Y, Xun T, Lin D, Liu W, Wang J, Lv L, Liu S, He J.  Tuning the antimicrobial pharmacophore to enable discovery of short lipopeptides with multiple modes of action DRAMP35370 PKKKRKVWKLLQQFFGLM 18 NS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24958615 J Pept Sci. 2014 Oct;20(10):785-93. Zhang Y, Song J, Zhang W, Liang R, Ma Y, Zhang L, Wei X, Ni J, Wang R. Functional properties of a novel hybrid antimicrobial peptide NS: potent antitumor activity and efficient plasmid delivery. DRAMP35371 PKKKRKVWKLLQQFFGLM 18 NS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 24958615 J Pept Sci. 2014 Oct;20(10):785-93. Zhang Y, Song J, Zhang W, Liang R, Ma Y, Zhang L, Wei X, Ni J, Wang R. Functional properties of a novel hybrid antimicrobial peptide NS: potent antitumor activity and efficient plasmid delivery. DRAMP35372 PKKKRKVWKLLQQFFGLM 18 Stearyl-NS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 24958615 J Pept Sci. 2014 Oct;20(10):785-94. Zhang Y, Song J, Zhang W, Liang R, Ma Y, Zhang L, Wei X, Ni J, Wang R. Functional properties of a novel hybrid antimicrobial peptide NS: potent antitumor activity and efficient plasmid delivery. DRAMP35373 PKKKRKVWKLLQQFFGLM 18 Stearyl-NS Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 24958615 J Pept Sci. 2014 Oct;20(10):785-94. Zhang Y, Song J, Zhang W, Liang R, Ma Y, Zhang L, Wei X, Ni J, Wang R. Functional properties of a novel hybrid antimicrobial peptide NS: potent antitumor activity and efficient plasmid delivery. DRAMP35374 CSKSSDYQC 9 sCT CSK-SLNs Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free Coupling to polyoxyethylene (40) steartae (SA-PEG2000), peptide ligand modified salmon calcitonin (sCT)-loaded SLNs L Not available Not available 24968819 Eur J Pharm Biopharm. 2014 Oct;88(2):518-28. an T, Chen C, Guo H, Xu J, Zhang J, Zhu X, Yang Y, Zhou Z, Li L, Huang Y.  Design and evaluation of solid lipid nanoparticles modified with peptide ligand for oral delivery of protein drugs. DRAMP35375 CSKSSDYQC 9 sCT CSK-SLNs Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free Free Coupling to polyoxyethylene (40) steartae (SA-PEG2000), peptide ligand modified salmon calcitonin (sCT)-loaded SLNs L Not available Not available 24968819 Eur J Pharm Biopharm. 2014 Oct;88(2):518-28. an T, Chen C, Guo H, Xu J, Zhang J, Zhu X, Yang Y, Zhou Z, Li L, Huang Y.  Design and evaluation of solid lipid nanoparticles modified with peptide ligand for oral delivery of protein drugs. DRAMP35376 IRQRRRR 7 IRQ Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Conjugation to solid lipid nanoparticle L Not available Not available 24968819 Eur J Pharm Biopharm. 2014 Oct;88(2):518-29. an T, Chen C, Guo H, Xu J, Zhang J, Zhu X, Yang Y, Zhou Z, Li L, Huang Y.  Design and evaluation of solid lipid nanoparticles modified with peptide ligand for oral delivery of protein drugs. DRAMP35377 CSKSSDYQC 9 CSK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Conjugation to solid lipid nanoparticle L Not available Not available 24968819 Eur J Pharm Biopharm. 2014 Oct;88(2):518-30. an T, Chen C, Guo H, Xu J, Zhang J, Zhu X, Yang Y, Zhou Z, Li L, Huang Y.  Design and evaluation of solid lipid nanoparticles modified with peptide ligand for oral delivery of protein drugs. DRAMP35378 CSKSSDYQC 9 CSK Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Conjugation to solid lipid nanoparticle L Not available Not available 24968819 Eur J Pharm Biopharm. 2014 Oct;88(2):518-30. an T, Chen C, Guo H, Xu J, Zhang J, Zhu X, Yang Y, Zhou Z, Li L, Huang Y.  Design and evaluation of solid lipid nanoparticles modified with peptide ligand for oral delivery of protein drugs. DRAMP35379 GGVCPKILKKCRRDSDCPGACICRGNGWCGSGSD 34 MCoTI-M1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-8. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35380 GGVCPKILRRCRRDSDCPGACICRGNGYCGSGSD 34 MCoTI-M2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-9. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35381 GGVCPKILRRCRRDSDCPGACICRGNGWCGSGSD 34 MCoTI-M3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-10. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35382 GGVCPKILRRCRRDSDCPGACICRGNGYCGSGSR 34 MCoTI-M4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-11. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35383 GGVCPRILRRCRRDSDCPGACICRGNGYCGSGSK 34 MCoTI-M5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-12. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35384 GRCTKSIPPICFPD 14 SFTI-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-13. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35385 grctksippicfpd 14 D-SFTI-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free D Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-14. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35386 GACTKSIPPICFPD 14 SFTI-M1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-15. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35387 GRCTKSIPPICFPA 14 SFTI-M2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-16. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35388 GRCTKSIPPICWPD 14 SFTI-M3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-17. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35389 GRCTKSIPPICWPK 14 SFTI-M4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-18. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35390 GRCTRSIPPKCWPD 14 SFTI-M5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-19. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35391 GRXTKSIPPIXFPD 14 SFTI-M6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free X=Abu, α-aminobutyric acid L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-20. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35392 GRXTKSIPPIXFPD 14 SFTI-M6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Conjugation with Alexa Flour 488 Free X=Abu, α-aminobutyric acid L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-20. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35393 GRXTKSIPPIXFPD 14 SFTI-M7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugation with Alexa Flour 488 Free X=Abu, α-aminobutyric acid L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-21. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35394 GRXTKSIPPIXFPD 14 SFTI-M7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugation with Alexa Flour 488 Free X=Abu, α-aminobutyric acid L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-21. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35395 YGRKKRRQRRRPPQG 15 TAT Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugation with Alexa Flour 488 Free L Not available Not available 24985034 Eur J Med Chem. 2014 Dec 17;88:10-22. D'Souza C, Henriques ST, Wang CK, Craik DJ. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1. DRAMP35396 EEEEEEEEPLGLAGRRRRRRRRN 23 ACPP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25000246 PLoS One. 2014 Jul 7;9(7):e100670.  Li S, Chen J, Xu H, Long J, Xie X, Zhang Y The targeted transduction of MMP-overexpressing tumor cells by ACPP-HPMA copolymer-coated adenovirus conjugates. DRAMP35397 VSRRRRRRGGRRRR 14 C24-LMWP Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25003794 J Control Release. 2014 Oct 28;192:47-56. Wang H, Zhao Y, Wang H, Gong J, He H, Shin MC, Yang VC, Huang Y. Low-molecular-weight protamine-modified PLGA nanoparticles for overcoming drug-resistant breast cancer. DRAMP35398 LKKLCKLLKKLCKLAG 16 LK-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25056130 Angew Chem Int Ed Engl. 2014 Sep 15;53(38):10086-9.  Jang S, Hyun S, Kim S, Lee S, Lee IS, Baba M, Lee Y, Yu J.  Cell-penetrating, dimeric α-helical peptides: nanomolar inhibitors of HIV-1 transcription. DRAMP35399 FSGSGSGSGRRRRRRRRGC 19 F(SG)4R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-62. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35400 GSGSGSGSGRRRRRRRRGC 19 G(SG)4R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-63. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35401 FSGSGSGSGRQIKIWFQNRRMKWKKGC 27 F(SG)4Pen Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-64. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35402 GSGSGSGSGRQIKIWFQNRRMKWKKGC 27 G(SG)4Pen Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-65. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35403 FSGSGSGSGAGYLLGKINLKALAALAKKILGC 32 F(SG)4TP10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-66. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35404 GSGSGSGSGAGYLLGKINLKALAALAKKILGC 32 G(SG)4TP10 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25108152 J Control Release. 2014 Dec 10;195:55-67. Sayers EJ, Cleal K, Eissa NG, Watson P, Jones AT. Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. DRAMP35405 AGYLLGKTNLKALAALAKKIL 21 NF1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation, CH3(CH2)16CO Amidation L Not available Not available 25135660 Biochim Biophys Acta. 2014 Dec;1838(12):3118-29. Vasconcelos L, Madani F, Arukuusk P, Pärnaste L, Gräslund A, Langel U. Effects of cargo molecules on membrane perturbation caused by transportan10 based cell-penetrating peptides. DRAMP35406 VTPHHVLVDEYTGEWVDSQFK 21 VG-21 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25154664  Biomaterials. 2014 Nov;35(35):9484-94.  iwari PM, Eroglu E, Bawage SS, Vig K, Miller ME, Pillai S, Dennis VA, Singh SR.  Enhanced intracellular translocation and biodistribution of gold nanoparticles functionalized with a cell-penetrating peptide (VG-21) from vesicular stomatitis virus. DRAMP35407 RLLRLLRLL 9 1b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-8. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35408 RLLRLLRLX 9 2b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-9. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35409 RLLRLXRLX 9 3b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-10. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35410 RLXRLXRLX 9 4b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-11. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35411 RLXRLXRXX 9 5b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-12. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35412 RLXRXRXX 8 6b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-13. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35413 RXXRXRXX 8 7b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Amidation X=1-aminocyclopentane-1-carboxylic acids (Ac5c) L Not available Not available 25188671 Bioconjug Chem. 2014 Oct 15;25(10):1761-14. Kato T, Oba M, Nishida K, Tanaka M. Cell-penetrating helical peptides having l-arginines and five-membered ring α,α-disubstituted α-amino acids. DRAMP35414 HHHHHHHHRRRRRRRR 16 STR-H8R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-46. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35415 HHHHHHHHRRRRRRRRRRRRRRR 23 H8R15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-47. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35416 HHHHHHHHRRRRRRRRRRRRRRR 23 H8R15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-47. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35417 HHHHHHHHRRRRRRRRRRRRRRR 23 STR-H8R15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-48. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35418 HHHHHHHHRRRRRRRRRRRRRRR 23 STR-H8R15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-48. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35419 HHHHHHHHHHHHRRRRRRRRRRRRRRR 27 STR-H12R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-49. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35420 HHHHHHHHHHHHHHHHRRRRRRRRRRRRRRR 31 H16R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-50. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35421 HHHHHHHHHHHHHHHHRRRRRRRRRRRRRRR 31 H16R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-50. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35422 HHHHHHHHHHHHHHHHRRRRRRRRRRRRRRR 31 STR-H16R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-51. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35423 HHHHHHHHHHHHHHHHRRRRRRRRRRRRRRR 31 STR-H16R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-51. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35424 HHHHHHHHHHHHHHHHHHHHRRRRRRRRRRRRRRR 35 STR-H20R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Stearylation Amidation L Not available Not available 25193363 Nanomedicine. 2015 Feb;11(2):435-52. Chu D, Xu W, Pan R, Ding Y, Sui W, Chen P. Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA. DRAMP35425 MAARLCCQLDPARDVLCLRP 20 N-terminus of X-Pep Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25251474 Biochem Biophys Res Commun. 2014 Oct 10;453(1):64-8 Montrose K, Yang Y, Krissansen GW.  X-pep, a novel cell-penetrating peptide motif derived from the hepatitis B virus. DRAMP35426 MAARLCCQLDPARDV 15 N-terminus of X-Pep Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25251474 Biochem Biophys Res Commun. 2014 Oct 10;453(1):64-9 Montrose K, Yang Y, Krissansen GW.  X-pep, a novel cell-penetrating peptide motif derived from the hepatitis B virus. DRAMP35427 MAARLCCQ 8 X-Pep Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25251474 Biochem Biophys Res Commun. 2014 Oct 10;453(1):64-10 Montrose K, Yang Y, Krissansen GW.  X-pep, a novel cell-penetrating peptide motif derived from the hepatitis B virus. DRAMP35428 MAARL 5 X-Pep derivative Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25251474 Biochem Biophys Res Commun. 2014 Oct 10;453(1):64-11 Montrose K, Yang Y, Krissansen GW.  X-pep, a novel cell-penetrating peptide motif derived from the hepatitis B virus. DRAMP35429 XFrFKFrFK 9 Single mitochondrial penetrating peptide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Amidation Amidation X=Ahx, 6-aminohexanoic acid Mix Not available Not available 25265566 J Am Chem Soc. 2014 Oct 29;136(43):15300-9.  Martin A, Byrne A, Burke CS, Forster RJ, Keyes TE. Peptide-bridged dinuclear Ru(II) complex for mitochondrial targeted monitoring of dynamic changes to oxygen concentration and ROS generation in live mammalian cells. DRAMP35430 XGLXGGLXGI 10 Trichogin GA IV Ome Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C8 OMe X=AIB (Aminoisobutyric acid) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-44.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity. DRAMP35431 XGLXGGLXGIL 11 Tric-COOH Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-45.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35432 XGLXGGLXGIL 11 Tric-COOH Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-45.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35433 XGLXGGLXGIX 11 Ac-Tric Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=2 μM); HeLa (EC50=8 μM) Not available Linear Acetylization Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-46.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35434 XGLXGGLXGIX 11 Ac-Tric Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Acetylization Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-46.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35435 XGLXGGLXGIX 11 Ac-Tric Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=8 μM); HeLa (Not active up to 20 μM) Not available Linear Acetylization Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-46.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35436 XGLXGGLXGIX 11 Ac-Tric Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=13 μM); HeLa (Not active up to 20 μM) Not available Linear Acetylization Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-46.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35437 XGLXGGLXGIX 11 Ac-Tric Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylization Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-46.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35438 XKLXGGLXGIX 11 Tric[K2] Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-47.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35439 XKLXGGLXGIL 11 Tric[K2]-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-48.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35440 XKLXGGLXGIL 11 Tric[K2]-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-48.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35441 XKLXGGLXGIL 11 Tric[K2]-COOH Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) COOH X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-49.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35442 XKLXGGLXGIL 11 Tric[K2]-COOH Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) COOH X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-49.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35443 XGLXGKLXGIX 11 Tric[K6] Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (EC50=2 μM); T67 (EC50=4 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-50.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35444 XGLXGKLXGIX 11 Tric[K6] Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: T67 (EC50=1 μM); HeLa (EC50=3 μM) Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-50.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35445 XGLXGKLXGIX 11 Tric[K6] Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-50.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35446 XGLXGKLXGIL 11 Tric[K6]-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-51.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35447 XGLXGGLXKIX 11 Tric[K9] Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X(1/4/8)=Aib; X(11)=Lol (Amino alcohol leucinol) L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-52.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35448 XGLXGGLXKIL 11 Tric[K9]-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) OMe X=Aib L Not available Not available 25306964 Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):134-53.  Tavano R, Malachin G, De Zotti M, Peggion C, Biondi B, Forrnaggio F, Papini E.  The peculiar N- and (-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity DRAMP35449 FLFKLIPKAIKGLLKAFK 18 AcrAP2 [S4K,N8K,S11K,S15K] A0A0A1I6N9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 25332684  Int J Biol Sci. 2014 Sep 21;10(10):1097-107.  Du Q, Hou X, Ge L, Li R, Zhou M, Wang H, Wang L, Wei M, Chen T, Shaw C. Cationicity-enhanced analogues of the antimicrobial peptides, AcrAP1 and AcrAP2, from the venom of the scorpion, Androctonus crassicauda, display potent growth modulation effects on human cancer cell lines DRAMP35450 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Ahx-FITC(Ahx, ε-aminocaproic acid; FITC, fluorescein isothiocyanate) Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5573.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35451 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Ahx-FITC(Ahx, ε-aminocaproic acid; FITC, fluorescein isothiocyanate) Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5573.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35452 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Ahx-FITC(Ahx, ε-aminocaproic acid; FITC, fluorescein isothiocyanate) Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5573.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35453 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=RhB, rhodamine B Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5574.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35454 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=RhB, rhodamine B Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5574.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35455 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=RhB, rhodamine B Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5574.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35456 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=PA-RhB, photoactivatable rhodamine B derivative Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5575.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35457 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=PA-RhB, photoactivatable rhodamine B derivative Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5575.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35458 MGVADLIKKFESISKEEGGGGKXGGrRrRrRRR 33 probe3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=PA-RhB, photoactivatable rhodamine B derivative Mix Not available Not available 25410769 Nat Commun. 2014 Nov 20;5:5575.  Pan D, Hu Z, Qiu F, Huang ZL, Ma Y, Wang Y, Qin L, Zhang Z, Zeng S, Zhang YH.  A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. DRAMP35459 KKKKKKNKKLQQRGD 15 P1 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-106. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35460 RGDGPRRRPRKRRGR 15 P2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-107. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35461 RRRQKRIVVRRRLIR 15 P3 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-108. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35462 RRVWRRYRRQRWCRR 15 P4 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-109. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35463 RRARRPRRLRPAPGR 15 P5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-110. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35464 LLRARWRRRRSRRFR 15 P6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-111. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35465 RGPRRQPRRHRRPRR 15 P7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-112. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35466 RRWRRWNRFNRRRCR 15 P8 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Ahx, 6-aminohexamoic acid Free L Not available Not available 25459448 Eur J Pharm Biopharm. 2015 Jan;89:93-113. Gautam A, Sharma M, Vir P, Chaudhary K, Kapoor P, Kumar R, Nath SK, Raghava GP. Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. DRAMP35467 RKKRRQRRRRKKRRQRRR 18 Tat2-Nat Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Natamycin L Not available Not available 25467959 Pharm Res. 2015 Jun;32(6):1920-30.  Jain A, Shah SG, Chugh A. Cell penetrating peptides as efficient nanocarriers for delivery of antifungal compound, natamycin for the treatment of fungal keratitis. DRAMP35468 AKKRRQRRRAKKRRQRRR 18 MTat2-Nat Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Natamycin L Not available Not available 25467959 Pharm Res. 2015 Jun;32(6):1920-31.  Jain A, Shah SG, Chugh A. Cell penetrating peptides as efficient nanocarriers for delivery of antifungal compound, natamycin for the treatment of fungal keratitis. DRAMP35469 XNIIXPLLXPIC 12 TV-XIIa Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-80.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35470 XNIIXPLLAPIC 12 P-I Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-81.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35471 ANIIXPLLXPIC 12 P-II Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-82.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35472 XNIIAPLLXPIC 12 P-III Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-83.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35473 XNIIXXLLXXIC 12 P-IV Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-84.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35474 XNIIXPLLXXIC 12 P-V Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-85.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35475 XNIIXXLLXPIC 12 P-VI Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation X=Aib, α-amino isobutyric acid L Not available Not available 25468041 Bioorg Med Chem. 2014 Dec 15;22(24):6776-86.  Wada S, Urase T, Hasegawa Y, Ban K, Sudani A, Kawai Y, Hayashi J, Urata H. Aib-containing peptide analogs: cellular uptake and utilization in oligonucleotide delivery. DRAMP35476 CAYGRKKRRQRRR 13 TAT-LP-PTX Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Cysteine addition Rhodamine LP L Not available Not available 25482610 Oncol Rep. 2015 Feb;33(2):783-91. Wang RH, Cao HM, Tian ZJ, Jin B, Wang Q, Ma H, Wu J.  Efficacy of dual-functional liposomes containing paclitaxel for treatment of lung cancer. DRAMP35477 CHAIYPRH 8 T7-LP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Rhodamine LP L Not available Not available 25482610 Oncol Rep. 2015 Feb;33(2):783-92. Wang RH, Cao HM, Tian ZJ, Jin B, Wang Q, Ma H, Wu J.  Efficacy of dual-functional liposomes containing paclitaxel for treatment of lung cancer. DRAMP35478 XXXXXXXAXXX 11 Coibamide A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X(1)=Me2Val; X(2)=Hva, α-Hydroxyisovaleric acid; X(3)=Me2Ser; X(4)=MeLeu; X(5)=MeThr(Trt); X(6)=MeSer(Me); X(7)=MeIle; M(9)=MeLeu; X(10)=MeTyr; X(11)=MeAla L Not available Not available 25488840  Bioorg Med Chem Lett. 2015 Jan 15;25(2):302-6. Nabika R, Suyama TL, Hau AM, Misu R, Ohno H, Ishmael JE, McPhail KL, Oishi S, Fujii N. Synthesis and biological evaluation of the [d-MeAla(11)]-epimer of coibamide A DRAMP35479 XXXXXXXAXXx 11 Coibamide A [11-D-Me-Ala] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X(1)=Me2Val; X(2)=Hva, α-Hydroxyisovaleric acid; X(3)=Me2Ser; X(4)=MeLeu; X(5)=MeThr(Trt); X(6)=MeSer(Me); X(7)=MeIle; M(9)=MeLeu; X(10)=MeTyr; X(12)=D-MeAla Mix Not available Not available 25488840  Bioorg Med Chem Lett. 2015 Jan 15;25(2):302-7. Nabika R, Suyama TL, Hau AM, Misu R, Ohno H, Ishmael JE, McPhail KL, Oishi S, Fujii N. Synthesis and biological evaluation of the [d-MeAla(11)]-epimer of coibamide A DRAMP35480 PNVIPLL 7 Reniochalistatin A Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25490132 J Nat Prod. 2014 Dec 26;77(12):2678-84. Zhan KX, Jiao WH, Yang F, Li J, Wang SP, Li YS, Han BN, Lin HW.  Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis DRAMP35481 PIFYLPL 7 Reniochalistatin B Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25490132 J Nat Prod. 2014 Dec 26;77(12):2678-85. Zhan KX, Jiao WH, Yang F, Li J, Wang SP, Li YS, Han BN, Lin HW.  Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis DRAMP35482 PIFPIYF 7 Reniochalistatin C Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25490132 J Nat Prod. 2014 Dec 26;77(12):2678-86. Zhan KX, Jiao WH, Yang F, Li J, Wang SP, Li YS, Han BN, Lin HW.  Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis DRAMP35483 PFPFIFP 7 Reniochalistatin D Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25490132 J Nat Prod. 2014 Dec 26;77(12):2678-87. Zhan KX, Jiao WH, Yang F, Li J, Wang SP, Li YS, Han BN, Lin HW.  Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis DRAMP35484 PLWPVIPI 8 Reniochalistatin E Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25490132 J Nat Prod. 2014 Dec 26;77(12):2678-88. Zhan KX, Jiao WH, Yang F, Li J, Wang SP, Li YS, Han BN, Lin HW.  Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis DRAMP35485 FyXrXGeX 8 LY2510924 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 25504752 Mol Cancer Ther. 2015 Feb;14(2):480-90. Peng SB, Zhang X, Paul D, Kays LM, Gough W, Stewart J, Uhlik MT, Chen Q, Hui YH, Zamek-Gliszczynski MJ, Wijsman JA, Credille KM, Yan LZ.  Identification of LY2510924, a novel cyclic peptide CXCR4 antagonist that exhibits antitumor activities in solid tumor and breast cancer metastatic models DRAMP35486 GWTLNSAGYLLGXINLKALAALAKKIL 27 TP-biot13 Not available Not found Chimeric Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation X=Lys-Biotinylation L Not available Not available 25511292 Folia Histochem Cytobiol. 2014;52(4):270-80. Wierzbicki PM, Kogut-Wierzbicka M, Ruczynski J, Siedlecka-Kroplewska K, Kaszubowska L, Rybarczyk A, Alenowicz M, Rekowski P, Kmiec Z.  Protein and siRNA delivery by transportan and transportan 10 into colorectal cancer cell lines. DRAMP35487 KWSFRVSYRGISYRRSRGK 19 MTpl-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation Free L Not available Not available 25514997  FEBS J. 2015 Feb;282(4):732-45.  Jain A, Yadav BK, Chugh A.  Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. DRAMP35488 KWFRVYRGIYRRRGK 15 MTpl-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation Free L Not available Not available 25514997  FEBS J. 2015 Feb;282(4):732-46.  Jain A, Yadav BK, Chugh A.  Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. DRAMP35489 KWCFAVCYAGICYAACAGK 19 MTpl-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Biotinylation L Not available Not available 25514997  FEBS J. 2015 Feb;282(4):732-47.  Jain A, Yadav BK, Chugh A.  Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. DRAMP35490 rRrGrKkRr 9 cTAT-GFP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free GFP Mix Not available Not available 25521313 Angew Chem Int Ed Engl. 2015 Feb 2;54(6):1950-3. Nischan N, Herce HD, Natale F, Bohlke N, Budisa N, Cardoso MC, Hackenberger CP. Covalent attachment of cyclic TAT peptides to GFP results in protein delivery into live cells with immediate bioavailability. DRAMP35491 rRrGrKkRr 9 cTAT-GFP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic Free GFP Mix Not available Not available 25521313 Angew Chem Int Ed Engl. 2015 Feb 2;54(6):1950-3. Nischan N, Herce HD, Natale F, Bohlke N, Budisa N, Cardoso MC, Hackenberger CP. Covalent attachment of cyclic TAT peptides to GFP results in protein delivery into live cells with immediate bioavailability. DRAMP35492 rRrGrKkRr 9 TAT-GFP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free GFP Mix Not available Not available 25521313 Angew Chem Int Ed Engl. 2015 Feb 2;54(6):1950-4. Nischan N, Herce HD, Natale F, Bohlke N, Budisa N, Cardoso MC, Hackenberger CP. Covalent attachment of cyclic TAT peptides to GFP results in protein delivery into live cells with immediate bioavailability. DRAMP35493 rRrGrKkRr 9 TAT-GFP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free GFP Mix Not available Not available 25521313 Angew Chem Int Ed Engl. 2015 Feb 2;54(6):1950-4. Nischan N, Herce HD, Natale F, Bohlke N, Budisa N, Cardoso MC, Hackenberger CP. Covalent attachment of cyclic TAT peptides to GFP results in protein delivery into live cells with immediate bioavailability. DRAMP35494 RRGRRG 6 V1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Conjugated to FITC modified folding domain via β-alanine–glycine– glycine linker Amidation L Not available Not available 25524829 J Pept Sci. 2015 Feb;21(2):77-84.  hinde A, Feher KM, Hu C, Slowinska K. Peptide internalization enabled by folding: triple helical cell-penetrating peptides. DRAMP35495 HHHRRRRRRRR 11 5-FAM-H3R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25547808  Bioconjug Chem. 2015 Jan 21;26(1):71-7. Lin R, Zhang P, Cheetham AG, Walston J, Abadir P, Cui H.  Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting. DRAMP35496 HHHRRRRRRRR 11 5-FAM-H3R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 25547808  Bioconjug Chem. 2015 Jan 21;26(1):71-7. Lin R, Zhang P, Cheetham AG, Walston J, Abadir P, Cui H.  Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting. DRAMP35497 HHHRRRRRRRR 11 MTS-(5-FAM)- H3R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free L Not available Not available 25547808  Bioconjug Chem. 2015 Jan 21;26(1):71-8. Lin R, Zhang P, Cheetham AG, Walston J, Abadir P, Cui H.  Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting. DRAMP35498 HHHRRRRRRRR 11 MTS-(5-FAM)- H3R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 5(6)-Carboxyfluorescein Free L Not available Not available 25547808  Bioconjug Chem. 2015 Jan 21;26(1):71-8. Lin R, Zhang P, Cheetham AG, Walston J, Abadir P, Cui H.  Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting. DRAMP35499 YKQCHKKGGXKKGSG 15 NrTP2 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free X=Ahx, 6-aminohexanoic acid L Not available Not available 25620660 Biopolymers. 2015 Mar;104(2):101-9.  Rodrigues M, Andreu D, Santos NC. Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. DRAMP35500 ykqchkkGGkkGsG 14 NrTP5 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free Mix Not available Not available 25620660 Biopolymers. 2015 Mar;104(2):101-10.  Rodrigues M, Andreu D, Santos NC. Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. DRAMP35501 YKQSHKKGGKKGSG 14 NrTP6 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 25620660 Biopolymers. 2015 Mar;104(2):101-11.  Rodrigues M, Andreu D, Santos NC. Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. DRAMP35502 YRQSHRRGGRRGSG 14 NrTP7 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 25620660 Biopolymers. 2015 Mar;104(2):101-12.  Rodrigues M, Andreu D, Santos NC. Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. DRAMP35503 WKQSHKKGGKKGSG 14 NrTP8 Not available Not found Protein derived Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Rhodamine B Free L Not available Not available 25620660 Biopolymers. 2015 Mar;104(2):101-13.  Rodrigues M, Andreu D, Santos NC. Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. DRAMP35504 XRRRRRR 7 R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-11.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35505 XRRRRRRR 8 R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-12.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35506 XRRRRRRRR 9 R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-13.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35507 XRRRRRRRRR 10 R9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC Amidation X=Ahx, 6-aminohexanoic acid L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-14.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35508 XKRRRRE 7 Cyc-R4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-15.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35509 XKRRRRRRE 9 Cyc-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-16.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35510 XKRRRRRRRE 10 Cyc-R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-17.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35511 XKRRRRRRRRE 11 Cyc-R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-18.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35512 XKRRRRRRRRRE 12 Cyc-R9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-19.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35513 XKrrrrrrrE 10 Cyc-r7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-20.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35514 XKrrrrrrrrE 11 Cyc-r8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-21.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35515 XKrrrrrrrrrE 12 Cyc-r9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-22.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35516 XKRrRrRrE 9 Cyc-(L,D)-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-23.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35517 XKrRrRrRrE 10 Cyc-(L,D)-R7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-24.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35518 XKRrRrRrRrE 11 Cyc-(L,D)-R8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine Mix Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-25.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35519 XERRRKKRRRE 11 Bicyc-0-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-26.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35520 XERRRKXKRRRE 12 Bicyc-1-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-27.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35521 XERRRKXXKRRRE 13 Bicyc-2-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-28.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35522 XERRRKXXXKRRRE 14 Bicyc-3-R6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-29.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35523 XRRRRKRRRE 10 Cyc-R3-R4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-30.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35524 XRRRKRRRRE 10 Cyc-R4-R3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-31.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35525 XRRKRRRRRE 10 Cyc-R5-R2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-32.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35526 XRKRRRRRRE 10 Cyc-R6-R1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Cyclic FITC Amidation X=Beta-Alanine L Not available Not available 25654426 Bioconjug Chem. 2015 Mar 18;26(3):405-33.  Traboulsi H, Larkin H, Bonin MA, Volkov L, Lavoie CL, Marsault É.  Macrocyclic cell penetrating peptides: a study of structure-penetration properties. Bioconjug Chem. DRAMP35527 XxXAlV 6 Similanamide Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 25789601 Mar Drugs. 2015 Mar 17;13(3):1432-50.  Prompanya C, Fernandes C, Cravo S, Pinto MM, Dethoup T, Silva AM, Kijjoa A.  A new cyclic hexapeptide and a new isocoumarin derivative from the marine sponge-associated fungus Aspergillus similanensis KUFA 0013 DRAMP35528 PF,PY,PV 8 P. aeruginosa CDP mix Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 25821788 Biomed Res Int. 2015;2015:197608. Vázquez-Rivera D, González O, Guzmán-Rodríguez J, Díaz-Pérez AL, Ochoa-Zarzosa A, López-Bucio J, Meza-Carmen V, Campos-García J. Cytotoxicity of cyclodipeptides from Pseudomonas aeruginosa PAO1 leads to apoptosis in human cancer cell lines DRAMP35529 FCTCNVKGFNAKNKRGIIYP 20 Scolopendrasin VII Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 25907065 J Microbiol Biotechnol. 2015 Aug;25(8):1275-80. Lee JH, Kim IW, Kim SH, Kim MA, Yun EY, Nam SH, Ahn MY, Kang D, Hwang JS. Anticancer Activity of the Antimicrobial Peptide Scolopendrasin VII Derived from the Centipede, Scolopendra subspinipes mutilans. DRAMP35530 XXKKWRKWLAKK 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 25970292 PLoS One. 2015 May 13;10(5):e0126390. Chu HL, Yip BS, Chen KH, Yu HY, Chih YH, Cheng HT, Chou YT, Cheng JW. Novel antimicrobial peptides with high anticancer activity and selectivity DRAMP35531 IIKKIIKKIIKKI 13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26204061 nterfaces. 2015 Aug 12;7(31):17346-55. Chen C, Chen Y, Yang C, Zeng P, Xu H, Pan F, Lu JR. High Selective Performance of Designed Antibacterial and Anticancer Peptide Amphiphiles DRAMP35532 GIIKKIIKKIIKK 13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26204061 nterfaces. 2015 Aug 12;7(31):17346-56. Chen C, Chen Y, Yang C, Zeng P, Xu H, Pan F, Lu JR. High Selective Performance of Designed Antibacterial and Anticancer Peptide Amphiphiles DRAMP35533 IIKKIIKKIIKK 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 26204061 nterfaces. 2015 Aug 12;7(31):17346-57. Chen C, Chen Y, Yang C, Zeng P, Xu H, Pan F, Lu JR. High Selective Performance of Designed Antibacterial and Anticancer Peptide Amphiphiles DRAMP35534 XHXLLPPVPLFG 12 Callyaerin C Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-25. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity. DRAMP35535 XIXIILPPLPII 12 Callyaerin B Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-26. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity. DRAMP35536 XIXVILPPLPIFG 13 Callyaerin A Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Amidation L Not available Not available 26213786 J Nat Prod. 2015 Aug 28;78(8):1910-27. Daletos G, Kalscheuer R, Koliwer-Brandl H, Hartmann R, de Voogd NJ, Wray V, Lin W, Proksch P. Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity. DRAMP35537 VRKPPYLPRPRWXRXXYNX 19 Oncocin [D2R,P12W,P13Hyp,R15Hyp,I16Tle,R19Orn] A0A2R7WNA0 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (15% loss of viability=600μg/mL) Not available Linear Free Amidation L Not available Not available 26334348 Amino Acids. 2016 Jan;48(1):269-80. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP35538 VXKPPYLPRPRWXRXXYNX 19 Oncocin [D2Orn,P12W,P13Hyp,R15Hyp,I16Tle,R19Orn] A0A2R7WNA0 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (15% loss of viability=600μg/mL) Not available Linear Free Amidation L Not available Not available 26334348 Amino Acids. 2016 Jan;48(1):269-81. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP35539 VrKPPYLPRPRWXRXXYNX 19 Oncocin [D2r,P12W,P13Hyp,R15Hyp,I16Tle,R19Orn] A0A2R7WNA0 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (15% loss of viability=600μg/mL) Not available Linear Free Amidation Mix Not available Not available 26334348 Amino Acids. 2016 Jan;48(1):269-82. Knappe D, Ruden S, Langanke S, Tikkoo T, Ritzer J, Mikut R, Martin LL, Hoffmann R, Hilpert K. Optimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus DRAMP35540 XRPDKPRPYLPRPRPPRPVR,XRPDKPRPYLPRPRPPRPVR,XRPDKPRPYLPRPRPPRPVRXC,XRPDKPRPYLPRPRPPRPVRXC 87 A3-APO Tetramer Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 26384569  Chem Biol. 2015 Sep 17;22(9):1250-8.  Li W, O'Brien-Simpson NM, Tailhades J, Pantarat N, Dawson RM, Otvos L Jr, Reynolds EC, Separovic F, Hossain MA, Wade JD. Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane DRAMP35541 ARCCLVMPVPPFACVKFCS 19 Transmembrane protein (17-35), RCB-1 B9T5G6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 2MTM Not available Not available Not available Linear Free Free L Not available Not available 26509914 J Nat Prod. 2015 Nov 25;78(11):2545-51. Boldbaatar D, Gunasekera S, El-Seedi HR, Göransson U. Synthesis, Structural Characterization, and Bioactivity of the Stable Peptide RCB-1 from Ricinus communis DRAMP35542 XGLXGGLXGIL 11 Tric-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X=Aib L Not available Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP35543 XGLXGGLXGIL 11 Tric-OMe Not available Not found Ascomycetes (Tric) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Oct (Fatty acid 1-Octanoyl) Free X=Aib L Not available Not available 27039838 Sci Rep. 2016 Apr 4;6:24000. Dalzini A, Bergamini C, Biondi B, De Zotti M, Panighel G, Fato R, Peggion C, Bortolus M, Maniero AL. The rational search for selective anticancer derivatives of the peptide Trichogin GA IV: a multi-technique biophysical approach DRAMP35544 DDEKEQFLYHLLSFNAV 17 wtR6IP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI. Not available Linear Fluorescein-O2OC- Free L Not available Rab8a GTPase 27336832 ACS Chem Biol. 2016 Aug 19;11(8):2375-82. Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN. Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase DRAMP35545 DDEⓍEQFⓍYHLLSFNAV 17 StRIP3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI. Not available Cyclic (Stapled) Fluorescein-O2OC- Free Ⓧ=(S)-2-(4-pentenyl)alanine L Not available Rab8a GTPase 27336832 ACS Chem Biol. 2016 Aug 19;11(8):2375-83. Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN. Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase DRAMP35546 DDEⓍEQFⓍYHLLSFNAV 17 StRIP3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI. Not available Cyclic (Stapled) Fluorescein-O2OC- Free Ⓧ=(S)-2-(4-pentenyl)alanine L Not available Rab8a GTPase 27336832 ACS Chem Biol. 2016 Aug 19;11(8):2375-83. Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN. Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase DRAMP35547 DDEⓍEQFⓍYHLLSFNAV 17 StRIP3 open Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI. Not available Linear Fluorescein-O2OC- Free Ⓧ=(S)-2-(4-pentenyl)alanine L Not available Rab8a GTPase 27336832 ACS Chem Biol. 2016 Aug 19;11(8):2375-84. Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN. Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase DRAMP35548 DDEⓍEQFⓍYHLLSFNAV 17 StRIP3 open Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI. Not available Linear Fluorescein-O2OC- Free Ⓧ=(S)-2-(4-pentenyl)alanine L Not available Rab8a GTPase 27336832 ACS Chem Biol. 2016 Aug 19;11(8):2375-84. Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN. Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase DRAMP35601 GSTLLSLL 8 Pseudofactin II, PFII Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C16 Free L Not available Not available 27416562 Colloids Surf B Biointerfaces. 2016 Oct 1;146:498-506. Janek T, Rodrigues LR, Gudiña EJ, Czyżnikowska Ż. Structure and mode of action of cyclic lipopeptide pseudofactin II with divalent metal ions DRAMP35602 ALXGVl 6 Oryzamide A Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 27489998 J Nat Prod. 2016 Aug 26;79(8):2045-52. Ding LJ, Yuan W, Liao XJ, Han BN, Wang SP, Li ZY, Xu SH, Zhang W, Lin HW. Oryzamides A-E, Cyclodepsipeptides from the Sponge-Derived Fungus Nigrospora oryzae PF18 DRAMP35603 AYXGVl 6 Oryzamide B Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 27489998 J Nat Prod. 2016 Aug 26;79(8):2045-53. Ding LJ, Yuan W, Liao XJ, Han BN, Wang SP, Li ZY, Xu SH, Zhang W, Lin HW. Oryzamides A-E, Cyclodepsipeptides from the Sponge-Derived Fungus Nigrospora oryzae PF18 DRAMP35604 AMXGVl 6 Oryzamide C Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 27489998 J Nat Prod. 2016 Aug 26;79(8):2045-54. Ding LJ, Yuan W, Liao XJ, Han BN, Wang SP, Li ZY, Xu SH, Zhang W, Lin HW. Oryzamides A-E, Cyclodepsipeptides from the Sponge-Derived Fungus Nigrospora oryzae PF18 DRAMP35605 FX 2 Cyclo(Phe-Hyp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Hyp L Not available Not available 27806640  Nat Prod Res. 2017 Jun;31(12):1390-1396. Ye X, Chai W, Lian XY, Zhang Z. Novel propanamide analogue and antiproliferative diketopiperazines from mangrove Streptomyces sp Q24 DRAMP35606 FX 2 Cyclo(Phe-Hyp) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Hyp L Not available Not available 27806640  Nat Prod Res. 2017 Jun;31(12):1390-1396. Ye X, Chai W, Lian XY, Zhang Z. Novel propanamide analogue and antiproliferative diketopiperazines from mangrove Streptomyces sp Q24 DRAMP35607 ELLSRVD 7 Bacaucin Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C14H24O2 Free L Not available Not available 28106348 Chem Int Ed Engl. 2017 Feb 1;56(6):1486-1490. Liu Y, Ding S, Dietrich R, Märtlbauer E, Zhu K. A Biosurfactant-Inspired Heptapeptide with Improved Specificity to Kill MRSA DRAMP35608 XLFXL 5 Galaxamide [L3F] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=METH-Leu L Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):544. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35609 XLfXL 5 Galaxamide [L3f] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=METH-Leu L Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):545. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35610 XLFxL 5 Galaxamide [L3F,MeL4DMeL] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X(1)=METH-Leu; x(4)=D-METH-Leu Mix Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):546. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35611 XLFXl 5 Galaxamide [L3F,L5l] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=METH-Leu L Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):547. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35612 xLFXL 5 Galaxamide [MeL1DMeL,L3F] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free x(1)=D-METH-Leu; X(4)=METH-Leu Mix Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):548. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35613 XlFXL 5 Galaxamide [L2l,L3F] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=METH-Leu L Not available Not available 28287429 Int J Mol Sci. 2017 Mar 10;18(3):549. Bai D, Yu S, Zhong S, Zhao B, Qiu S, Chen J, Lunagariya J, Liao X, Xu S. d-Amino Acid Position Influences the Anticancer Activity of Galaxamide Analogs: An Apoptotic Mechanism Study DRAMP35614 GGGGGGGRGDLPETGGS 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 28351594 Bioorg Med Chem Lett. 2017 May 1;27(9):1911-1913 Wu Z, Cheng X, Hong H, Zhao X, Zhou Z. New potent and selective αvβ3 integrin ligands: Macrocyclic peptides containing RGD motif synthesized by sortase A-mediated ligation DRAMP35615 GGGGRGDRGDLPETGGS 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 28351594 Bioorg Med Chem Lett. 2017 May 1;27(9):1911-1914 Wu Z, Cheng X, Hong H, Zhao X, Zhou Z. New potent and selective αvβ3 integrin ligands: Macrocyclic peptides containing RGD motif synthesized by sortase A-mediated ligation DRAMP35616 GRGDRGDRGDLPETGGS 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 28351594 Bioorg Med Chem Lett. 2017 May 1;27(9):1911-1915 Wu Z, Cheng X, Hong H, Zhao X, Zhou Z. New potent and selective αvβ3 integrin ligands: Macrocyclic peptides containing RGD motif synthesized by sortase A-mediated ligation DRAMP35617 RRRQRRKKRGGGDTRLNTVWMW 22 TAT-RasGAP317-326 Not available Not found Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 28638371 Front Microbiol. 2017 Jun 7;8:994. Heulot M, Jacquier N, Aeby S, Le Roy D, Roger T, Trofimenko E, Barras D, Greub G, Widmann C. Anticancer Peptide TAT-RasGAP317-326 Exerts Broad Antimicrobial Activity. DRAMP35618 GGKKLFKKILKYL 13 C18-GG-BP100 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C18 Amidation L Not available Not available 28831625  Amino Acids. 2017 Nov;49(11):1831-1841.  Zhang B, Gu H, Shi W, Li H, Ma G, Chen X, Qian H, Lin H, Huang W, Ge L.  Synthesis and biological evaluation of novel aliphatic acid-conjugated antimicrobial peptides as potential agents with anti-tumor, multidrug resistance-reversing activity and enhanced stability DRAMP35619 LPGP 4 SCH-P9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 28901516 Mol Med Rep. 2017 Nov;16(5):6697-6707. Huang F, Ding G, Yang Z, Yu F. Two novel peptides derived from Sinonovacula constricta inhibit the proliferation and induce apoptosis of human prostate cancer cells DRAMP35620 DYVP 4 SCH-P10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 28901516 Mol Med Rep. 2017 Nov;16(5):6697-6708. Huang F, Ding G, Yang Z, Yu F. Two novel peptides derived from Sinonovacula constricta inhibit the proliferation and induce apoptosis of human prostate cancer cells DRAMP35621 MRLLVLSSLLCILLLCFSIFSTEGKRRPAKAWSGRRTRLCCHRVPSPNSTNLKGHHVRLCKPCKLEPEPRLWVVPGALPQV 81 Protein GPR15LG Q6UWK7 Not found Homo sapiens Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Free Free L Not available Not available 28936214 Front Immunol. 2017 Sep 7;8:1111. Ocón B, Pan J, Dinh TT, Chen W, Ballet R, Bscheider M, Habtezion A, Tu H, Zabel BA, Butcher EC. A Mucosal and Cutaneous Chemokine Ligand for the Lymphocyte Chemoattractant Receptor GPR15. DRAMP35622 LXFX 4 Saccharopolytide A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29065726 Nat Prod Res. 2018 Jul;32(14):1627-1631. Xie CL, Niu S, Xia JM, Peng K, Zhang GY, Yang XW. Saccharopolytide A, a new cyclic tetrapeptide with rare 4-hydroxy-proline moieties from the deep-sea derived actinomycete Saccharopolyspora cebuensis MCCC 1A09850 DRAMP35623 KP 2 Cyclo(Lys-Pro) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29216716 Bioconjug Chem. 2018 Jan 17;29(1):164-175. Shankar S, Faheem MM, Nayak D, Wani NA, Farooq S, Koul S, Goswami A, Rai R. Cyclodipeptide c(Orn-Pro) Conjugate with 4-Ethylpiperic Acid Abrogates Cancer Cell Metastasis through Modulating MDM2 DRAMP35624 YLARAIRRTLARLLL 15 NN2_0018 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29259134 J Biol Chem. 2018 Mar 9;293(10):3492-3509. Nagarajan D, Nagarajan T, Roy N, Kulkarni O, Ravichandran S, Mishra M, Chakravortty D, Chandra N. Computational antimicrobial peptide design and evaluation against multidrug-resistant clinical isolates of bacteria DRAMP35625 SWKKFFKKARSLPKLF 16 NN2_0050 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29259134 J Biol Chem. 2018 Mar 9;293(10):3492-3509. Nagarajan D, Nagarajan T, Roy N, Kulkarni O, Ravichandran S, Mishra M, Chakravortty D, Chandra N. Computational antimicrobial peptide design and evaluation against multidrug-resistant clinical isolates of bacteria DRAMP35626 INLKKLAKLXKKIS 14 Mitoparan [L14S], Mastoparan [A5,8K;A10Aib;L14S] P01514 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 29337270 Peptides. 2018 Mar;101:95-105. Howl J, Howl L, Jones S. The cationic tetradecapeptide mastoparan as a privileged structure for drug discovery: Enhanced antimicrobial properties of mitoparan analogues modified at position-14 DRAMP35627 INLKKLAXLXKKIS 14 Mitoparan [K8Orn,L14S], Mastoparan [A5,A8Orn,A10Aib,L14S] P01514 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 29337270 Peptides. 2018 Mar;101:95-106. Howl J, Howl L, Jones S. The cationic tetradecapeptide mastoparan as a privileged structure for drug discovery: Enhanced antimicrobial properties of mitoparan analogues modified at position-14 DRAMP35628 INLKKLAKLXKKIT 14 Mitoparan [L14T], Mastoparan [A5,8K;A10Aib;L14T] P01514 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 29337270 Peptides. 2018 Mar;101:95-107. Howl J, Howl L, Jones S. The cationic tetradecapeptide mastoparan as a privileged structure for drug discovery: Enhanced antimicrobial properties of mitoparan analogues modified at position-14 DRAMP35629 KRIVARIKAFLR 12 LL-37 KR-12 [Q5A,D9A] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29430821 Chembiochem. 2018 May 4;19(9):931-939. Gunasekera S, Muhammad T, Strömstedt AA, Rosengren KJ, Göransson U. Alanine and Lysine Scans of the LL-37-Derived Peptide Fragment KR-12 Reveal Key Residues for Antimicrobial Activity DRAMP35630 KRIVKRIKKFLR 12 LL-37 KR-12 [Q5K,D9K] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 29430821 Chembiochem. 2018 May 4;19(9):931-940. Gunasekera S, Muhammad T, Strömstedt AA, Rosengren KJ, Göransson U. Alanine and Lysine Scans of the LL-37-Derived Peptide Fragment KR-12 Reveal Key Residues for Antimicrobial Activity DRAMP35631 GIGAVLKVLTTGLPALISWIKRKRQQ,GIGAVLKVLTTGLPALISWIKRKRQQX 54 Melittin Dimer Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 29770868 Amino Acids. 2018 Aug;50(8):1101-1110. Jamasbi E, Lucky SS, Li W, Hossain MA, Gopalakrishnakone P, Separovic F. Effect of dimerized melittin on gastric cancer cells and antibacterial activity DRAMP35632 WKLLSKAQEKFGKNKSRC,RYGTCIYQXRLWAFS 34 CH10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 30048118 Bioconjug Chem. 2018 Sep 19;29(9):3060-3072 Ptaszyńska N, Gucwa K, Łęgowska A, Dębowski D, Gitlin-Domagalska A, Lica J, Heldt M, Martynow D, Olszewski M, Milewski S, Ng TB, Rolka K. Antimicrobial Activity of Chimera Peptides Composed of Human Neutrophil Peptide 1 (HNP-1) Truncated Analogues and Bovine Lactoferrampin DRAMP35633 XCRRLCYRNRCVTYCRGR 18 X-hexatoxin-Hi1a, Hi Gomesin A0A1D0BZI2 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30068931 Sci Rep. 2018 Aug 1;8(1):11519. Ikonomopoulou MP, Fernandez-Rojo MA, Pineda SS, Cabezas-Sainz P, Winnen B, Morales RAV, Brust A, Sánchez L, Alewood PF, Ramm GA, Miles JJ, King GF. Gomesin inhibits melanoma growth by manipulating key signaling cascades that control cell death and proliferation DRAMP35634 ECRRLCYKQRCVTYCRGR 18 Gomesin [PYA1E] P82358 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 1KFP Not available Not available Not available Amidation Amidation L Not available Not available 30068931 Sci Rep. 2018 Aug 1;8(1):11520. Ikonomopoulou MP, Fernandez-Rojo MA, Pineda SS, Cabezas-Sainz P, Winnen B, Morales RAV, Brust A, Sánchez L, Alewood PF, Ramm GA, Miles JJ, King GF. Gomesin inhibits melanoma growth by manipulating key signaling cascades that control cell death and proliferation DRAMP35635 RQIKIWFQNRRMKWKKAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKT 53 RT53 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Mice red blood cells: 8% Hemolysis=20 μM Linear Free Free L Not available Not available 30080874 PLoS One. 2018 Aug 6;13(8):e0201220. Pasquereau-Kotula E, Habault J, Kroemer G, Poyet JL. The anticancer peptide RT53 induces immunogenic cell death DRAMP35636 RQIKIWFQNRRMKWKKAKLNAEKLKDFKIRLQYFARGGQVYIRQGRLALQGKT 53 RT53M Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30080874 PLoS One. 2018 Aug 6;13(8):e0201221. Pasquereau-Kotula E, Habault J, Kroemer G, Poyet JL. The anticancer peptide RT53 induces immunogenic cell death DRAMP35637 AWIWLV 6 Nocardiotide A Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30134565 Mar Drugs. 2018 Aug 21;16(9):290. Ibrahim AH, Attia EZ, Hajjar D, Anany MA, Desoukey SY, Fouad MA, Kamel MS, Wajant H, Gulder TAM, Abdelmohsen UR. New Cytotoxic Cyclic Peptide from the Marine Sponge-Associated Nocardiopsis sp UR67 DRAMP35638 LESLASSAVRTANKARAKL 19 Citrus-amp2 Q4JIY4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30192822 PLoS One. 2018 Sep 7;13(9):e0203452. Inui Kishi RN, Stach-Machado D, Singulani JL, Dos Santos CT, Fusco-Almeida AM, Cilli EM, Freitas-Astúa J, Picchi SC, Machado MA. Evaluation of cytotoxicity features of antimicrobial peptides with potential to control bacterial diseases of citrus DRAMP35639 XTXCXfXRXc 10 Polymyxin CAMP113 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C12 Free Mix Not available Not available 30215733 J Antimicrob Chemother. 2018 Dec 1;73(12):3385-3390. Rudilla H, Pérez-Guillén I, Rabanal F, Sierra JM, Vinuesa T, Viñas M. Novel Synthetic peptide polymyxins kill Gram-positive bacteria DRAMP35640 XTXCXxXXXc 10 Polymyxin CAMP207 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C12 Free Mix Not available Not available 30215733 J Antimicrob Chemother. 2018 Dec 1;73(12):3385-3391. Rudilla H, Pérez-Guillén I, Rabanal F, Sierra JM, Vinuesa T, Viñas M. Novel Synthetic peptide polymyxins kill Gram-positive bacteria DRAMP35641 FLFKLIPKAIKGLIKAFK 18 AcrAP1 [S4K,H8K,S11K,S15K] A0A0A1I6E7 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30268502 Biophys Res Commun. 2018 Oct 28;505(2):478-484. Lee MY, Park SC, Jung M, Shin MK, Kang HL, Baik SC, Cheong GW, Jang MK, Lee WK. Cationicity-enhanced analogues of the antimicrobial peptides, AcrAP1 and AcrAP2, from the venom of the scorpion, Androctonus crassicauda, display potent growth modulation effects on human cancer cell lines DRAMP35642 IP 2 Cyclo(Ile-Pro) Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30270742 Nat Prod Res. 2020 May;34(10):1461-1464. Lin WX, Xie CL, Zhou M, Xia ML, Zhou TT, Chen HF, Yang XW, Yang Q. Chemical constituents from the deep sea-derived Streptomyces xiamenensis MCCC 1A01570 and their effects on RXRα transcriptional regulation DRAMP35643 XI 2 Cyclo(Hyp-Ile) Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30270742 Nat Prod Res. 2020 May;34(10):1461-1465. Lin WX, Xie CL, Zhou M, Xia ML, Zhou TT, Chen HF, Yang XW, Yang Q. Chemical constituents from the deep sea-derived Streptomyces xiamenensis MCCC 1A01570 and their effects on RXRα transcriptional regulation DRAMP35644 FFFFRRRR 8 F4R4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents. DRAMP35645 FFFFRRRR 8 F4R4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360400 Molecules. 2018 Oct 22;23(10):2722. Riahifard N, Mozaffari S, Aldakhil T, Nunez F, Alshammari Q, Alshammari S, Yamaki J, Parang K, Tiwari RK. Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents. DRAMP35646 IKNAKVCVYAVCVSHK 16 Nicomicin-1 (18-33) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30360541 Mar Drugs. 2018 Oct 23;16(11):401. Panteleev PV, Tsarev AV, Bolosov IA, Paramonov AS, Marggraf MB, Sychev SV, Shenkarev ZO, Ovchinnikova TV Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain DRAMP35647 KKWRKWLKWLAKK 13 Myotoxin II (105-117)[Y3,6W][Y5K,P9W,C11A], PEM-2 [W5K,A9W] P24605 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30447380 Int J Antimicrob Agents. 2019 Jun;53(6):868-872. Baker KR, Jana B, Hansen AM, Vissing KJ, Nielsen HM, Franzyk H, Guardabassi L. Repurposing azithromycin and rifampicin against Gram-negative pathogens by combination with peptide potentiators DRAMP35648 KKPSKKPKPQAMTFPKVTVEYFPASFSTAALTVPED 36 Cathelicidin Ps-CATH6 A0A2Z4HVI6 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30452933 Dev Comp Immunol. 2019 Mar;92:179-192. Shi N, Cai S, Gao J, Qiao X, Yang H, Wang Y, Yu H. Roles of polymorphic cathelicidins in innate immunity of soft-shell turtle, Pelodiscus sinensis DRAMP35649 GLFDIVKKVLKLLK 14 Aurein-2.2 (1-14)[V10L, G11K, A12L, G14K] P82389 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1678. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35650 GLFDIVKKVLRLLK 14 Aurein-2.2 (1-14)[V10L, G11R, A12L, G14K] P82389 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1679. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35651 GWFDILKHVFRLLK 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1680. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35652 GWYEIIKKIYKWLK 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1681. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35653 VKAWAKVLKGFGKLLKGFGKL 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1682. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35654 FHAWAKLLKGVGRFFKGIGRW 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1683. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35655 IRAWAKVLKGVGKILKGVGRW 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1684. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35656 WRAWAKIYHGVGKLLKGVGRW 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30506920 Angew Chem Int Ed Engl. 2019 Feb 4;58(6):1674-1685. Neuhaus CS, Gabernet G, Steuer C, Root K, Hiss JA, Zenobi R, Schneider G. Simulated Molecular Evolution for Anticancer Peptide Design DRAMP35657 NVlLWK 6 Wollamide B [Orn6K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 30602509 Agents Chemother. 2019 Feb 26;63(3):e01773-18. Khalil ZG, Hill TA, De Leon Rodriguez LM, Lohman RJ, Hoang HN, Reiling N, Hillemann D, Brimble MA, Fairlie DP, Blumenthal A, Capon RJ. Structure-Activity Relationships of Wollamide Cyclic Hexapeptides with Activity against Drug-Resistant and Intracellular Mycobacterium tuberculosis DRAMP35658 XXXAXLX 7 Rufomycin-1, Rufomycin B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30602512 Agents Chemother. 2019 Feb 26;63(3):e02204-18. Choules MP, Wolf NM, Lee H, Anderson JR, Grzelak EM, Wang Y, Ma R, Gao W, McAlpine JB, Jin YY, Cheng J, Lee H, Suh JW, Duc NM, Paik S, Choe JH, Jo EK, Chang CL, Lee JS, Jaki BU, Pauli GF, Franzblau SG, Cho S Rufomycin Targets ClpC1 Proteolysis in Mycobacterium tuberculosis and M abscessus DRAMP35659 AFXGVl 6 Scopularide B Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 30609359 J Org Chem. 2019 Feb 1;84(3):1228-1237. Hou XM, Li YY, Shi YW, Fang YW, Chao R, Gu YC, Wang CY, Shao CL. Integrating Molecular Networking and 1H NMR To Target the Isolation of Chrysogeamides from a Library of Marine-Derived Penicillium Fungi DRAMP35660 FLSLIPHIVSGVAALANHL 19 Phylloseptin-PBa3, Phylloseptin-PBu A0A5B7LGI9 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 30612735 Wu Y, Wang L, Zhou M, Chen T, Shaw C. Phylloseptin-PBa1, -PBa2, -PBa3: Three novel antimicrobial peptides from the skin secretion of Burmeister's leaf frog (Phyllomedusa burmeisteri) DRAMP35661 GLPLLISWIKRKRQQAGPGSKKPVPIIYCNRRTGKCQRM 39 Melittin (12-26)[A4L]-AGP-Thanatin P55788 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30701481 AMB Express. 2019 Jan 30;9(1):14. Jiang X, Qian K, Liu G, Sun L, Zhou G, Li J, Fang X, Ge H, Lv Z. Design and activity study of a melittin-thanatin hybrid peptide DRAMP35662 RGDfK 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 30732943 Bioorg Med Chem Lett. 2019 Apr 1;29(7):896-900. Liu J, Cheng X, Tian X, Guan D, Ao J, Wu Z, Huang W, Le Z. Design and synthesis of novel dual-cyclic RGD peptides for αvβ3 integrin targeting DRAMP35663 FIVPSIFLLKKAFCIALKKC 20 Japonicin-2LF A0A482F245 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 30802593 Biochim Biophys Acta Gen Subj. 2019 May;1863(5):849-856. Yuan Y, Zai Y, Xi X, Ma C, Wang L, Zhou M, Shaw C, Chen T. A novel membrane-disruptive antimicrobial peptide from frog skin secretion against cystic fibrosis isolates and evaluation of anti-MRSA effect using Galleria mellonella model DRAMP35664 KKLRLKIAFK 10 P-rpl39e (9-18)[A15K, A16I] Q8ZTX6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31016969 ACS Infect Dis. 2019 Jul 12;5(7):1081-1086. Cândido ES, Cardoso MH, Chan LY, Torres MDT, Oshiro KGN, Porto WF, Ribeiro SM, Haney EF, Hancock REW, Lu TK, de la Fuente-Nunez C, Craik DJ, Franco OL. Short Cationic Peptide Derived from Archaea with Dual Antibacterial Properties and Anti-Infective Potential DRAMP35665 RTCQSQSHRFRGPCLRRSNCANVCRTEGFPGGRCRGFRRRCFCTTHC 47 Flower-specific gamma-thionin, ZmD32 B6SJ49 Not found Plantae Antimicrobial, Anticancer Not found Not found Not found 6DMZ Not available Not available Not available Linear Free Free L Not available Not available 31031739 Front Microbiol. 2019 Apr 12;10:795. erenga BK, McKenna JA, Harvey PJ, Quimbar P, Garcia-Ceron D, Lay FT, Phan TK, Veneer PK, Vasa S, Parisi K, Shafee TMA, van der Weerden NL, Hulett MD, Craik DJ, Anderson MA, Bleackley MR. Salt-Tolerant Antifungal and Antibacterial Activities of the Corn Defensin ZmD32 DRAMP35666 RRSRFGRFFKKVRKQLGRVLRHSRITVGGRMRF 33 Cm-CATH2 M7BBJ0 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31121185 Dev Comp Immunol. 2019 Sep;98:189-204. Qiao X, Yang H, Gao J, Zhang F, Chu P, Yang Y, Zhang M, Wang Y, Yu H. Diversity, immunoregulatory action and structure-activity relationship of green sea turtle cathelicidins DRAMP35667 GLFSVVKGVLKGVGKNVSGSLLDQLKCKISGGC 33 LF Brevinin, LFB Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234333 Biomolecules. 2019 Jun 21;9(6):242 Li B, Lyu P, Xie S, Qin H, Pu W, Xu H, Chen T, Shaw C, Ge L, Kwok HF. LFB: A Novel Antimicrobial Brevinin-Like Peptide from the Skin Secretion of the Fujian Large Headed Frog, Limnonectes fujianensi DRAMP35668 RRWCVYAYVRVRGVRVYAYVCW 22 R-Arenicin-1 [L15R; R17,19Y; Y18A; R20V] Q5SC60 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35669 WCRRYRVLVRGVLVRYRRCW 20 Arenicin (2-21) [V3R; Y4,6R; A5Y; R8L] Q5SC60 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35670 RWCVYAYVRVXX,RWCVYAYVRV 23 Arenicin-1 (1-10)-Orn-Dap + Arenicin-1 (1-10) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35671 WCRRYRVLVXX,WCRRYRVLV 21 Invert Arenicin-1 (13-21)-Orn-Dap + Invert Arenicin-1 (13-21) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35672 RFCVYAYVRVRGVLVRYRRCF 21 Arenicin-1 [W2,21F] Q5SC60 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35673 RWXVYAYVRVRGVLVRYRRXW 21 Linear Arenicin-1 [C3,20IAA-Cys] Q5SC60 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31234579 Mar Drugs. 2019 Jun 23;17(6):376. Orlov DS, Shamova OV, Eliseev IE, Zharkova MS, Chakchir OB, Antcheva N, Zachariev S, Panteleev PV, Kokryakov VN, Ovchinnikova TV, Tossi A. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization DRAMP35674 SRSSRAGLQFPVGRIHRLLRK 21 Histone H2A (1-21), Fi-Histin A0A1X9ZM18 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31252047 Fish Shellfish Immunol. 2019 Sep;92:667-679. Sruthy KS, Nair A, Antony SP, Puthumana J, Singh ISB, Philip R. A histone H2A derived antimicrobial peptide, Fi-Histin from the Indian White shrimp, Fenneropenaeus indicus: Molecular and functional characterization DRAMP35675 SILSLFKMGAKALGKTLIKQAGKAGAEYVACKATNQC 37 Esculentin-2 HYba2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 31328553 Nat Prod Res. 2021 Apr;35(8):1262-1266. Vineeth Kumar T, Asha R, George S. Identification and functional characterisation of Esculentin-2 HYba peptides and their C-terminally amidated analogs from the skin secretion of an endemic frog DRAMP35676 RKKRRQRRRCWTKSIPPKPC 20 Tat (48-56) + PPF-BBI [5-15] C3RSZ6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H157 (50% viability=100μM); H460 (50% viability=100μM) Not available Linear Free Free L Not available Not available 31337113 Biomolecules. 2019 Jul 14;9(7):280. Miao Y, Chen G, Xi X, Ma C, Wang L, Burrows JF, Duan J, Zhou M, Chen T. Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor DRAMP35677 RKKAIKLVKKLVKKLKKALK 20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear L Not available Not available 31355341 Sci Adv. 2019 Jul 24;5(7):eaax1946. Nagarajan D, Roy N, Kulkarni O, Nanajkar N, Datey A, Ravichandran S, Thakur C, T S, Aprameya IV, Sarma SP, Chakravortty D, Chandra N. Ω76: A designed antimicrobial peptide to combat carbapenem- and tigecycline-resistant Acinetobacter baumannii. DRAMP35678 FLKAIKKFGKEFKKIGAKLK 20 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear L Not available Not available 31355341 Sci Adv. 2019 Jul 24;5(7):eaax1947. Nagarajan D, Roy N, Kulkarni O, Nanajkar N, Datey A, Ravichandran S, Thakur C, T S, Aprameya IV, Sarma SP, Chakravortty D, Chandra N. Ω76: A designed antimicrobial peptide to combat carbapenem- and tigecycline-resistant Acinetobacter baumannii. DRAMP35679 RWCFRVCYRGICYRKCRG 18 Cyclic Tachyplesin-2 P14214 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 6PIO Not available Not available Not available Linear Free Free L Not available Not available 31455019 Int J Mol Sci. 2019 Aug 26;20(17):4184. Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S. Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties DRAMP35680 KWCFRVCYRGICYRKCRG 18 Cyclic Tachyplesin-3 P14214 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 6PIP Not available Not available Not available Linear Free Free L Not available Not available 31455019 Int J Mol Sci. 2019 Aug 26;20(17):4185. Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S. Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties DRAMP35681 CFQWKRAMRKVR 12 HLopt2 P02788 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 31513374 ACS Chem Biol. 2019 Oct 18;14(10):2233-2242. Ptaszyńska N, Gucwa K, Olkiewicz K, Łȩgowska A, Okońska J, Ruczyński J, Gitlin-Domagalska A, Dȩbowski D, Milewski S, Rolka K Antibiotic-Based Conjugates Containing Antimicrobial HLopt2 Peptide: Design, Synthesis, Antimicrobial and Cytotoxic Activities DRAMP35682 FLSGIVaMLaKLF 13 Temporin-1Sa [G7,10a] B3KYH4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 31614561 Biomolecules. 2019 Oct 11;9(10):598. Olleik H, Baydoun E, Perrier J, Hijazi A, Raymond J, Manzoni M, Dupuis L, Pauleau G, Goudard Y, Villéon B, Goin G, Sockeel P, Choudhary MI, Pasquale ED, Nadeem-Ul-Haque M, Ali H, Khan AI, Shaheen F, Maresca M. Temporin-SHa and Its Analogs as Potential Candidates for the Treatment of Helicobacter pylori DRAMP35683 FLSaIVGMLaKLF 13 Temporin-1Sa [G4,10a] B3KYH4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 31614561 Biomolecules. 2019 Oct 11;9(10):599. Olleik H, Baydoun E, Perrier J, Hijazi A, Raymond J, Manzoni M, Dupuis L, Pauleau G, Goudard Y, Villéon B, Goin G, Sockeel P, Choudhary MI, Pasquale ED, Nadeem-Ul-Haque M, Ali H, Khan AI, Shaheen F, Maresca M. Temporin-SHa and Its Analogs as Potential Candidates for the Treatment of Helicobacter pylori DRAMP35684 FLSAIVGMLAKLF 13 Temporin-1Sa [G4,10A] B3KYH4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 31614561 Biomolecules. 2019 Oct 11;9(10):600. Olleik H, Baydoun E, Perrier J, Hijazi A, Raymond J, Manzoni M, Dupuis L, Pauleau G, Goudard Y, Villéon B, Goin G, Sockeel P, Choudhary MI, Pasquale ED, Nadeem-Ul-Haque M, Ali H, Khan AI, Shaheen F, Maresca M. Temporin-SHa and Its Analogs as Potential Candidates for the Treatment of Helicobacter pylori DRAMP35685 LSYXXxXWXXASpP 14 Murepavadin [T1L,W2S,I3Y,DAB10tBuGly] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 31645764 Nature. 2019 Dec;576(7787):452-458. Luther A, Urfer M, Zahn M, Müller M, Wang SY, Mondal M, Vitale A, Hartmann JB, Sharpe T, Monte FL, Kocherla H, Cline E, Pessi G, Rath P, Modaresi SM, Chiquet P, Stiegeler S, Verbree C, Remus T, Schmitt M, Kolopp C, Westwood MA, Desjonquères N, Brabet E, Hell S, LePoupon K, Vermeulen A, Jaisson R, Rithié V, Upert G, Lederer A, Zbinden P, Wach A, Moehle K, Zerbe K, Locher HH, Bernardini F, Dale GE, Eberl L, Wollscheid B, Hiller S, Robinson JA, Obrecht D. Chimeric peptidomimetic antibiotics against Gram-negative bacteria DRAMP35686 WCVASpPLSYCGXTXXXlLXXT 22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 31645764 Nature. 2019 Dec;576(7787):452-459. Luther A, Urfer M, Zahn M, Müller M, Wang SY, Mondal M, Vitale A, Hartmann JB, Sharpe T, Monte FL, Kocherla H, Cline E, Pessi G, Rath P, Modaresi SM, Chiquet P, Stiegeler S, Verbree C, Remus T, Schmitt M, Kolopp C, Westwood MA, Desjonquères N, Brabet E, Hell S, LePoupon K, Vermeulen A, Jaisson R, Rithié V, Upert G, Lederer A, Zbinden P, Wach A, Moehle K, Zerbe K, Locher HH, Bernardini F, Dale GE, Eberl L, Wollscheid B, Hiller S, Robinson JA, Obrecht D. Chimeric peptidomimetic antibiotics against Gram-negative bacteria DRAMP35687 RFRWPIRRPPIRPPFYP 17 Bac5 (1-17)[P4W] P19660 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033 Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E Coli, K Pneumoniae, and A Baumannii DRAMP35688 RFRPPIRRPPIRPPWYP 17 Bac5 (1-17)[F15W] P19660 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31692278 ChemMedChem. 2019 Dec 17;14(24):2025-2033 Mardirossian M, Sola R, Beckert B, Collis DWP, Di Stasi A, Armas F, Hilpert K, Wilson DN, Scocchi M. Proline-Rich Peptides With Improved Antimicrobial Activity Against E Coli, K Pneumoniae, and A Baumannii DRAMP35689 GYPFA 5 Longicalycinin A cyclic analogue 3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.77 ± 0.0007 μg/mL); HT-29 (IC50=11.4 ± 0 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108902. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35690 AYPFG 5 Longicalycinin A cyclic analogue 4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.53 ± 0.0014 μg/mL); HT-29 (IC50=10.78 ± 0.0021 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108903. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35691 FSPFG 5 Longicalycinin A cyclic analogue 5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=8.99 ± 0.0014 μg/mL); HT-29 (IC50=10.97 ± 0.0049 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108904. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35692 VYPIA 5 Longicalycinin A cyclic analogue 6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=10.98 ± 0.0014 μg/mL); HT-29 (IC50=12.31 ± 0.0063 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108905. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35693 PYVFA 5 Longicalycinin A cyclic analogue 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.6 ± 0.0007 μg/mL); HT-29 (IC50=9.78 ± 0.0212 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108906. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35694 FYPVG 5 Longicalycinin A cyclic analogue 8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=10.35 ± 0.0014 μg/mL); HT-29 (IC50=12.88 ± 0.0014 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108907. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35695 FYPFV 5 Longicalycinin A cyclic analogue 9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.33 ± 0.0007 μg/mL); HT-29 (IC50=10.44 ± 0.5536 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108908. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35696 FYPFA 5 Longicalycinin A cyclic analogue 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=10.5 ± 0.0014 μg/mL); HT-29 (IC50=10.5 ± 0.0007 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108909. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35697 TVPFA 5 Longicalycinin A cyclic analogue 11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.56 ± 0.0021 μg/mL); HT-29 (IC50=11.67 ± 0.0014 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108910. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35698 FYPFI 5 Longicalycinin A cyclic analogue 12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=11.32 ± 0.0014 μg/mL); HT-29 (IC50=14.2 ± 0.0014 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108911. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35699 VTPFL 5 Longicalycinin A cyclic analogue 13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.26 ± 0.0028 μg/mL); HT-29 (IC50=17.2 ± 0.0014 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108912. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35700 PYFFL 5 Longicalycinin A cyclic analogue 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.67 ± 0.0007 μg/mL); HT-29 (IC50=9.12 ± 0.0042 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108913. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35701 PYGFV 5 Longicalycinin A cyclic analogue 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.44 ± 0 μg/mL); HT-29 (IC50=10.55 ± 0.0989 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108914. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35702 FTPFV 5 Longicalycinin A cyclic analogue 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=11.1 ± 0.0007 μg/mL); HT-29 (IC50=12.11 ± 0.0056 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108915. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35703 FSPFA 5 Longicalycinin A cyclic analogue 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.33 ± 0.0007 μg/mL); HT-29 (IC50=11.33 ± 0.0035 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108916. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35704 FSPAG 5 Longicalycinin A cyclic analogue 18 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=10.33 ± 0.0007 μg/mL); HT-29 (IC50=10.2 ± 0.0014 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108917. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35705 FYPFG 5 Longicalycinin A linear Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=9.18 ± 0.0014 μg/mL); HT-29 (IC50=9.61 ± 0.0007 μg/mL) Not available Linear Free Free L Not available Not available 31747558 Chem Biol Interact. 2020 Jan 5;315:108918. Gholibeikian M, Bamoniri A, HoushdarTehrani MH, Fatemeh Mirjalili BB, Bijanzadeh HR. Structure-activity relationship studies of Longicalcynin A analogues, as anticancer cyclopeptides DRAMP35706 FLFKLIKHAIKGLIKAFK 18 AcrAP1 [S4,11,15K;P7K], AP1-Z5b A0A0A1I6E7 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 31909181 Mol Ther Oncolytics. 2019 Dec 10;16:7-19. Ma R, Wong SW, Ge L, Shaw C, Siu SWI, Kwok HF. In Vitro and MD Simulation Study to Explore Physicochemical Parameters for Antibacterial Peptide to Become Potent Anticancer Peptide DRAMP35707 LRKVRRLLRRL 11 AMP 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (10% Killing=100µM) Not available Linear Free Amidation L Not available Not available 31954105 Biophys Acta Biomembr. 2020 Apr 1;1862(4):183177. Pandit G, Biswas K, Ghosh S, Debnath S, Bidkar AP, Satpati P, Bhunia A, Chatterjee S. Rationally designed antimicrobial peptides: Insight into the mechanism of eleven residue peptides against microbial infections DRAMP35708 LRKVWRWLRRL 11 AMP 22 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (80% Killing=100µM) Not available Linear Free Amidation L Not available Not available 31954105 Biophys Acta Biomembr. 2020 Apr 1;1862(4):183178. Pandit G, Biswas K, Ghosh S, Debnath S, Bidkar AP, Satpati P, Bhunia A, Chatterjee S. Rationally designed antimicrobial peptides: Insight into the mechanism of eleven residue peptides against microbial infections DRAMP35709 LRKFRRLLRRL 11 AMP 23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (0% Killing=100µM) Not available Linear Free Amidation L Not available Not available 31954105 Biophys Acta Biomembr. 2020 Apr 1;1862(4):183179. Pandit G, Biswas K, Ghosh S, Debnath S, Bidkar AP, Satpati P, Bhunia A, Chatterjee S. Rationally designed antimicrobial peptides: Insight into the mechanism of eleven residue peptides against microbial infections DRAMP35710 LRRLRRLLRRL 11 AMP 24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (85% Killing=100µM) Not available Linear Free Amidation L Not available Not available 31954105 Biophys Acta Biomembr. 2020 Apr 1;1862(4):183180. Pandit G, Biswas K, Ghosh S, Debnath S, Bidkar AP, Satpati P, Bhunia A, Chatterjee S. Rationally designed antimicrobial peptides: Insight into the mechanism of eleven residue peptides against microbial infections DRAMP35712 FWRIRIRRPRRIRIRWF 17 R-DIM-P-LF11-215 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32151609 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183264. Grissenberger S, Riedl S, Rinner B, Leber R, Zweytick D. Design of human lactoferricin derived antitumor peptides-activity and specificity against malignant melanoma in 2D and 3D model studies DRAMP35713 PFWRIRIRRPFWRIRIRR 18 DIM-LF11-322 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32151609 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183265. Grissenberger S, Riedl S, Rinner B, Leber R, Zweytick D. Design of human lactoferricin derived antitumor peptides-activity and specificity against malignant melanoma in 2D and 3D model studies DRAMP35714 PWRIRIRRPRRIRIWP 16 R-DIM-P-LF11-334 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32151609 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183266. Grissenberger S, Riedl S, Rinner B, Leber R, Zweytick D. Design of human lactoferricin derived antitumor peptides-activity and specificity against malignant melanoma in 2D and 3D model studies DRAMP35715 PWRIRIRRRRIRIRWPPWRIRIRR 24 R-DIM-LF11-334-LF11-334 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32151609 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183267. Grissenberger S, Riedl S, Rinner B, Leber R, Zweytick D. Design of human lactoferricin derived antitumor peptides-activity and specificity against malignant melanoma in 2D and 3D model studies DRAMP35716 RRWFWRRRRWFWRR 14 DIM-LF11-339 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32151609 Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183268. Grissenberger S, Riedl S, Rinner B, Leber R, Zweytick D. Design of human lactoferricin derived antitumor peptides-activity and specificity against malignant melanoma in 2D and 3D model studies DRAMP35717 AGGKRIVQRIKDFLRGAGGKRIVQRIKDFLRG 32 AGG-KR12-GAGG-KR12-G P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32153522 Front Microbiol. 2020 Feb 21;11:168. Gunasekera S, Muhammad T, Strömstedt AA, Rosengren KJ, Göransson U. Backbone Cyclization and Dimerization of LL-37-Derived Peptides Enhance Antimicrobial Activity and Proteolytic Stability DRAMP35718 AGGKRIVKRIKKFLRGAGGKRIVKRIKKFLRG 32 AGG-KR12-GAGG-KR12-G [Q8,24K; D12,28K] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32153522 Front Microbiol. 2020 Feb 21;11:169. Gunasekera S, Muhammad T, Strömstedt AA, Rosengren KJ, Göransson U. Backbone Cyclization and Dimerization of LL-37-Derived Peptides Enhance Antimicrobial Activity and Proteolytic Stability DRAMP35719 HHHH 4 12-(His)4-12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear C12 C12 L Not available Not available 32193931 ACS Appl Mater Interfaces. 2020 Apr 15;12(15):17220-17229. Qi R, Zhang N, Zhang P, Zhao H, Liu J, Cui J, Xiang J, Han Y, Wang S, Wang Y. Gemini Peptide Amphiphiles with Broad-Spectrum Antimicrobial Activity and Potent Antibiofilm Capacity DRAMP35720 VKRTKRGARRGLTKVLKKIFGSIVKKAVSKGV 32 Cathelicidin ModoCath1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32194564 Front Immunol. 2020 Mar 3;11:347. Cho HS, Yum J, Larivière A, Lévêque N, Le QVC, Ahn B, Jeon H, Hong K, Soundrarajan N, Kim JH, Bodet C, Park C. Opossum Cathelicidins Exhibit Antimicrobial Activity Against a Broad Spectrum of Pathogens Including West Nile Virus DRAMP35721 WYQLIRTFGNLIHQKYRKLLEAYRKLRD 28 Cathelicidin ModoCath5 F6W4B4 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32194564 Front Immunol. 2020 Mar 3;11:348. Cho HS, Yum J, Larivière A, Lévêque N, Le QVC, Ahn B, Jeon H, Hong K, Soundrarajan N, Kim JH, Bodet C, Park C. Opossum Cathelicidins Exhibit Antimicrobial Activity Against a Broad Spectrum of Pathogens Including West Nile Virus DRAMP35722 VRRSKRGIKVPSFVKKVLKDVVSESIS 27 Cathelicidin ModoCath6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32194564 Front Immunol. 2020 Mar 3;11:349. Cho HS, Yum J, Larivière A, Lévêque N, Le QVC, Ahn B, Jeon H, Hong K, Soundrarajan N, Kim JH, Bodet C, Park C. Opossum Cathelicidins Exhibit Antimicrobial Activity Against a Broad Spectrum of Pathogens Including West Nile Virus DRAMP35723 KRWKKFFRKVIKFF 14 BotrAMP14 U5KJC9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32499582 Sci Rep. 2020 Jun 4;10(1):9127. Oliveira NGJ, Cardoso MH, Velikova N, Giesbers M, Wells JM, Rezende TMB, de Vries R, Franco OL. Physicochemical-guided design of cathelicidin-derived peptides generates membrane active variants with therapeutic potential DRAMP35724 KRLKKIFKKMIKIF 14 CrotAMP14 U5KJM4 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 32499582 Sci Rep. 2020 Jun 4;10(1):9128. Oliveira NGJ, Cardoso MH, Velikova N, Giesbers M, Wells JM, Rezende TMB, de Vries R, Franco OL. Physicochemical-guided design of cathelicidin-derived peptides generates membrane active variants with therapeutic potential DRAMP35730 XXXXKKK 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HepG2 (IC50=355µM) Not available Linear Free Amidation L Not available Not available 32764602 Sci Rep. 2020 Aug 6;10(1):13206. Greco I, Molchanova N, Holmedal E, Jenssen H, Hummel BD, Watts JL, Håkansson J, Hansen PR, Svenson J. Correlation between hemolytic activity, cytotoxicity and systemic in vivo toxicity of Synthetic peptide antimicrobial peptides DRAMP35731 KKLKXFX 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=462µM) Not available Linear Free Amidation L Not available Not available 32764602 Sci Rep. 2020 Aug 6;10(1):13207. Greco I, Molchanova N, Holmedal E, Jenssen H, Hummel BD, Watts JL, Håkansson J, Hansen PR, Svenson J. Correlation between hemolytic activity, cytotoxicity and systemic in vivo toxicity of Synthetic peptide antimicrobial peptides DRAMP35732 XFXLKKK 7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=783µM) Not available Linear Free Amidation L Not available Not available 32764602 Sci Rep. 2020 Aug 6;10(1):13208. Greco I, Molchanova N, Holmedal E, Jenssen H, Hummel BD, Watts JL, Håkansson J, Hansen PR, Svenson J. Correlation between hemolytic activity, cytotoxicity and systemic in vivo toxicity of Synthetic peptide antimicrobial peptides DRAMP35733 WG 2 Cyclo(Trp-Gly), Diketopiperazine (WG) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32806659 Molecules. 2020 Aug 12;25(16):3676. Liu R, Zhang H, Wu W, Li H, An Z, Zhou F. C7-Prenylation of Tryptophan-Containing Cyclic Dipeptides by 7-Dimethylallyl Tryptophan Synthase Significantly Increases the Anticancer and Antimicrobial Activities DRAMP35734 WW 2 Cyclo(Trp-Trp), Diketopiperazine (WW) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 32806659 Molecules. 2020 Aug 12;25(16):3677. Liu R, Zhang H, Wu W, Li H, An Z, Zhou F. C7-Prenylation of Tryptophan-Containing Cyclic Dipeptides by 7-Dimethylallyl Tryptophan Synthase Significantly Increases the Anticancer and Antimicrobial Activities DRAMP35735 EKKRLLKWWR 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33074344 Amino Acids. 2020 Oct;52(10):1439-1457. Faya M, Hazzah HA, Omolo CA, Agrawal N, Maji R, Walvekar P, Mocktar C, Nkambule B, Rambharose S, Albericio F, de la Torre BG, Govender T. Novel formulation of antimicrobial peptides enhances antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA) DRAMP35736 KWWKLLRKKR 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33074344 Amino Acids. 2020 Oct;52(10):1439-1458. Faya M, Hazzah HA, Omolo CA, Agrawal N, Maji R, Walvekar P, Mocktar C, Nkambule B, Rambharose S, Albericio F, de la Torre BG, Govender T. Novel formulation of antimicrobial peptides enhances antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA) DRAMP35737 FLSLIPKIAGGIAALVKNL 19 Phylloseptin-PV1, PPV1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33193152 Front Microbiol. 2020 Oct 26;11:565158. Liu Y, Shi D, Wang J, Chen X, Zhou M, Xi X, Cheng J, Ma C, Chen T, Shaw C, Wang L. A Novel Amphibian Antimicrobial Peptide, Phylloseptin-PV1, Exhibits Effective Anti- staphylococcal Activity Without Inducing Either Hepatic or Renal Toxicity in Mice DRAMP35738 KKCNFFCKLKKKVKSVGSRNLIGSATHHHRIYRV 34 PN-CATH1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33242568 Dev Comp Immunol. 2021 Mar;116:103928. Wang Y, Ouyang J, Luo X, Zhang M, Jiang Y, Zhang F, Zhou J, Wang Y. Identification and characterization of novel bi-functional cathelicidins from the black-spotted frog (Pelophylax nigromaculata) with both anti-infective and antioxidant activities DRAMP35739 EGCNILCLLKRKVKAVKNVVKNVVKSVVG 29 PN-CATH2 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33242568 Dev Comp Immunol. 2021 Mar;116:103929. Wang Y, Ouyang J, Luo X, Zhang M, Jiang Y, Zhang F, Zhou J, Wang Y. Identification and characterization of novel bi-functional cathelicidins from the black-spotted frog (Pelophylax nigromaculata) with both anti-infective and antioxidant activities DRAMP35740 IFWLFRGKADVAL 13 Agelaia-MP [N2F,K5F,L6R,I10D,I11del,D12V] P69436 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 7JGX Not available Not available Not available Linear Free Amidation L Not available Not available 33244888 Chembiochem. 2021 Apr 16;22(8):1415-1423. Muller JAI, Lawrence N, Chan LY, Harvey PJ, Elliott AG, Blaskovich MAT, Gonçalves JC, Galante P, Mortari MR, Toffoli-Kadri MC, Koehbach J, Craik DJ. Antimicrobial and Anticancer Properties of Synthetic peptide Peptides Derived from the Wasp Parachartergus fraternus DRAMP35741 IFGTILGFLKGL 12 Protonectin [L2,8F] P69437 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 7JHF Not available Not available Not available Linear Free Amidation L Not available Not available 33244888 Chembiochem. 2021 Apr 16;22(8):1415-1424. Muller JAI, Lawrence N, Chan LY, Harvey PJ, Elliott AG, Blaskovich MAT, Gonçalves JC, Galante P, Mortari MR, Toffoli-Kadri MC, Koehbach J, Craik DJ. Antimicrobial and Anticancer Properties of Synthetic peptide Peptides Derived from the Wasp Parachartergus fraternus DRAMP35742 GWGSFFRRAAHVGRHVGRAALTHYL 25 Pleurocidin KR P81941 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 6RSF Not available Tumor cells: HeLa (IC50=30.7 ± 2.6 μg/ml) Not available Linear Free Amidation L HEK293: IC50=40.1 ± 4.1 µg/ml Not available 33247193 Commun Biol. 2020 Nov 27;3(1):697. Manzo G, Hind CK, Ferguson PM, Amison RT, Hodgson-Casson AC, Ciazynska KA, Weller BJ, Clarke M, Lam C, Man RCH, Shaughnessy BGO, Clifford M, Bui TT, Drake AF, Atkinson RA, Lam JKW, Pitchford SC, Page CP, Phoenix DA, Lorenz CD, Sutton JM, Mason AJ. A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy DRAMP35743 gwgsffrraahvgrhvgraalthyl 25 D-Pleurocidin KR P81941 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=25.3 ± 2.2 μg/ml); Calu-3 (IC50=39.1 ± 1.8 μg/ml); A549 (IC50=56.5 ± 4.5 μg/ml) Not available Linear Free Amidation D HEK293: IC50=36.4 ± 4.3 µg/ml Not available 33247193 Commun Biol. 2020 Nov 27;3(1):698. Manzo G, Hind CK, Ferguson PM, Amison RT, Hodgson-Casson AC, Ciazynska KA, Weller BJ, Clarke M, Lam C, Man RCH, Shaughnessy BGO, Clifford M, Bui TT, Drake AF, Atkinson RA, Lam JKW, Pitchford SC, Page CP, Phoenix DA, Lorenz CD, Sutton JM, Mason AJ. A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy DRAMP35744 GWGSFFKKAAHAGKHAGKAALTHYL 25 Pleurocidin VA P81941 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found 6RSG Not available Tumor cells: HeLa (IC50>400 μg/ml) Not available Linear Free Amidation L HEK293: IC50~400 µg/ml Not available 33247193 Commun Biol. 2020 Nov 27;3(1):699. Manzo G, Hind CK, Ferguson PM, Amison RT, Hodgson-Casson AC, Ciazynska KA, Weller BJ, Clarke M, Lam C, Man RCH, Shaughnessy BGO, Clifford M, Bui TT, Drake AF, Atkinson RA, Lam JKW, Pitchford SC, Page CP, Phoenix DA, Lorenz CD, Sutton JM, Mason AJ. A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy DRAMP35745 gwgsffkkaahagkhagkaalthyl 25 D-Pleurocidin VA P81941 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (IC50=198.2 ± 10.2 μg/ml); A549 (IC50>250 μg/ml); Calu-3 (IC50>250 μg/ml) Not available Linear Free Amidation D HEK293: IC50=217.3 ± 46.5 µg/ml Not available 33247193 Commun Biol. 2020 Nov 27;3(1):700. Manzo G, Hind CK, Ferguson PM, Amison RT, Hodgson-Casson AC, Ciazynska KA, Weller BJ, Clarke M, Lam C, Man RCH, Shaughnessy BGO, Clifford M, Bui TT, Drake AF, Atkinson RA, Lam JKW, Pitchford SC, Page CP, Phoenix DA, Lorenz CD, Sutton JM, Mason AJ. A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy DRAMP35746 GSRGWGFEPGVRCLIWCD 18 Lasso peptide Felipeptin A1 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found 6XTH Not available Not available Not available Linear Free Free L Not available Not available 33294793 iScience. 2020 Nov 10;23(12):101785. Guerrero-Garzón JF, Madland E, Zehl M, Singh M, Rezaei S, Aachmann FL, Courtade G, Urban E, Rückert C, Busche T, Kalinowski J, Cao YR, Jiang Y, Jiang CL, Selivanova G, Zotchev SB. Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin DRAMP35747 GGGGRGYEYNKQCLIFC 17 Lasso peptide Felipeptin A2 Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found 6XTI Not available Not available Not available Linear Free Free L Not available Not available 33294793 iScience. 2020 Nov 10;23(12):101786. Guerrero-Garzón JF, Madland E, Zehl M, Singh M, Rezaei S, Aachmann FL, Courtade G, Urban E, Rückert C, Busche T, Kalinowski J, Cao YR, Jiang Y, Jiang CL, Selivanova G, Zotchev SB. Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin DRAMP35748 GSRGWGFEPGVRCLIWCD,GGGGRGYEYNKQCLIFC 36 Felipeptin A1+Felipeptin A2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 33294793 iScience. 2020 Nov 10;23(12):101787. Guerrero-Garzón JF, Madland E, Zehl M, Singh M, Rezaei S, Aachmann FL, Courtade G, Urban E, Rückert C, Busche T, Kalinowski J, Cao YR, Jiang Y, Jiang CL, Selivanova G, Zotchev SB. Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin DRAMP35752 LWKIWKKIWRVGWNWR 16 Cecropin A-like 4 (3-18)[K2W,G5W,E9W,Q13W,H14N,T15W] A0A1I8M6I1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33401476 Antibiotics (Basel). 2021 Jan 1;10(1):36. Peng J, Mishra B, Khader R, Felix L, Mylonakis E. Novel Cecropin-4 Derived Peptides against Methicillin-Resistant Staphylococcus aureus DRAMP35753 LWKIWKKIWRVWKNWR 16 Cecropin A-like 4 (3-18)[K2W;G5,12W;E9W;Q13K;H14N;T15W] A0A1I8M6I1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33401476 Antibiotics (Basel). 2021 Jan 1;10(1):37. Peng J, Mishra B, Khader R, Felix L, Mylonakis E. Novel Cecropin-4 Derived Peptides against Methicillin-Resistant Staphylococcus aureus DRAMP35754 LWKIGKKIWRVLWNWR 16 Cecropin A-like 4 (3-18)[K2W,E9W,G12L,Q13W,H14N,T15W] A0A1I8M6I1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33401476 Antibiotics (Basel). 2021 Jan 1;10(1):38. Peng J, Mishra B, Khader R, Felix L, Mylonakis E. Novel Cecropin-4 Derived Peptides against Methicillin-Resistant Staphylococcus aureus DRAMP35755 LWKIWWKIWRVWKNWR 16 Cecropin A-like 4 (3-18)[K2W;G5,12W;K6W;E9W;Q13K;H14N;T15W] A0A1I8M6I1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33401476 Antibiotics (Basel). 2021 Jan 1;10(1):39. Peng J, Mishra B, Khader R, Felix L, Mylonakis E. Novel Cecropin-4 Derived Peptides against Methicillin-Resistant Staphylococcus aureus DRAMP35756 KVNHAACAAHCLLKRKRGGYCNKRRICVCRN 31 Defensin-like Protein (35-65), TcPaSK D6X2G2 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33499187 Microorganisms. 2021 Jan 22;9(2):222. Robles-Fort A, García-Robles I, Fernando W, Hoskin DW, Rausell C, Real MD. Dual Antimicrobial and Antiproliferative Activity of TcPaSK Peptide Derived from a Tribolium castaneum Insect Defensin DRAMP35757 ELlVDlL 7 Surfactin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-Me-C14 Free Mix Not available Not available 33505362 Front Microbiol. 2021 Jan 11;11:561060. Kourmentza K, Gromada X, Michael N, Degraeve C, Vanier G, Ravallec R, Coutte F, Karatzas KA, Jauregi P. Antimicrobial Activity of Lipopeptide Biosurfactants Against Foodborne Pathogen and Food Spoilage Microorganisms and Their Cytotoxicity DRAMP35758 ExYxEaPQyI 10 Fengycin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-C16 Free Mix Not available Not available 33505362 Front Microbiol. 2021 Jan 11;11:561061. Kourmentza K, Gromada X, Michael N, Degraeve C, Vanier G, Ravallec R, Coutte F, Karatzas KA, Jauregi P. Antimicrobial Activity of Lipopeptide Biosurfactants Against Foodborne Pathogen and Food Spoilage Microorganisms and Their Cytotoxicity DRAMP35759 nnsNXNQPy 9 Mycosubtilin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 33505362 Front Microbiol. 2021 Jan 11;11:561062. Kourmentza K, Gromada X, Michael N, Degraeve C, Vanier G, Ravallec R, Coutte F, Karatzas KA, Jauregi P. Antimicrobial Activity of Lipopeptide Biosurfactants Against Foodborne Pathogen and Food Spoilage Microorganisms and Their Cytotoxicity DRAMP35760 ELlVDlL,ExYxEaPQyI 18 Fengycin-Surfactin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 3-OH-Me-C14,3-OH-C16 Free Mix Not available Not available 33505362 Front Microbiol. 2021 Jan 11;11:561063. Kourmentza K, Gromada X, Michael N, Degraeve C, Vanier G, Ravallec R, Coutte F, Karatzas KA, Jauregi P. Antimicrobial Activity of Lipopeptide Biosurfactants Against Foodborne Pathogen and Food Spoilage Microorganisms and Their Cytotoxicity DRAMP35761 ALWKDLLKNVGIAAGKAALNKVTDMVNQ 28 Dermaseptin-TO, Dermaseptin-1 P85523 Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33582221 Microb Pathog. 2021 Apr;153:104795. Chen Z, Xi X, Lu Y, Hu H, Dong Z, Ma C, Wang L, Zhou M, Chen T, Du S, Lu Y. In vitro activities of a novel antimicrobial peptide isolated from phyllomedusa tomopterna DRAMP35762 GKLRLIKKLWVKKWKKKGWKA 21 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33677023 Eur J Pharm Sci. 2021 Jun 1;161:105784. Thankappan B, Sivakumar J, Asokan S, Ramasamy M, Pillai MM, Selvakumar R, Angayarkanni J. Dual antimicrobial and anticancer activity of a novel synthetic α-helical antimicrobial peptide DRAMP35763 PFRLRLRL 8 Jelleine-1 [K3R;I4,6L;S5R;H7R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33878564 Eur J Med Chem. 2021 Jul 5;219:113433. Zhou J, Zhang L, He Y, Liu K, Zhang F, Zhang H, Lu Y, Yang C, Wang Z, Fareed MS, Liang X, Yan W, Wang K. An optimized analog of antimicrobial peptide Jelleine-1 shows enhanced antimicrobial activity against multidrug resistant P aeruginosa and negligible toxicity in vitro and in vivo DRAMP35764 PWRLRLRL 8 Jelleine-1 [F2W;K3R;I4,6L;S5R;H7R] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 33878564 Eur J Med Chem. 2021 Jul 5;219:113434. Zhou J, Zhang L, He Y, Liu K, Zhang F, Zhang H, Lu Y, Yang C, Wang Z, Fareed MS, Liang X, Yan W, Wang K. An optimized analog of antimicrobial peptide Jelleine-1 shows enhanced antimicrobial activity against multidrug resistant P aeruginosa and negligible toxicity in vitro and in vivo DRAMP35765 RLMRIFRILKLAR 13 Pugnin A F6QYQ9 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33919639 Pharmaceutics. 2021 Apr 18;13(4):578. Liscano Y, Medina L, Oñate-Garzón J, Gúzman F, Pickholz M, Delgado JP. In Silico Selection and Evaluation of Pugnins with Antibacterial and Anticancer Activity Using Skin Transcriptome of Treefrog ( Boana pugnax) DRAMP35766 RMMRIFWVIKLAR 13 Pugnin B A0A803KCU6 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33919639 Pharmaceutics. 2021 Apr 18;13(4):579. Liscano Y, Medina L, Oñate-Garzón J, Gúzman F, Pickholz M, Delgado JP. In Silico Selection and Evaluation of Pugnins with Antibacterial and Anticancer Activity Using Skin Transcriptome of Treefrog ( Boana pugnax) DRAMP35767 PI 2 Cyclo(Pro-Ile) Not available Not found Fungi Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 33924262 Mar Drugs. 2021 Apr 20;19(4):232. Qader MM, Hamed AA, Soldatou S, Abdelraof M, Elawady ME, Hassane ASI, Belbahri L, Ebel R, Rateb ME. Antimicrobial and Antibiofilm Activities of the Fungal Metabolites Isolated from the Marine Endophytes Epicoccum nigrum M13 and Alternaria alternata 13A DRAMP35768 NynQPnS 7 Iturin A Not available Not found Bacillus subtilis Antimicrobial, Anticancer Not found Not found Not found Not available Iturin A significantly inhibited the growth of tumor cells, induce apoptosis, autophagy and paraptosis. Tumor cells: HepG2 (10% viability=75μM) Not available Linear Free β-amino fatty acid with a-(CH2)10CH3 group Mix Not available Not available 33970365 AMB Express. 2021 May 10;11(1):67. Zhao H, Yan L, Guo L, Sun H, Huang Q, Shao D, Jiang C, Shi J. Effects of Bacillus subtilis iturin A on HepG2 cells in vitro and vivo DRAMP35769 GIINTLQKYYCRVRGGRCAVLSCRSQEYRIGRCSTRGRKCCRRKK 45 hBD3(1-23)-hBD4(20-28)-hBD3(33-45), H4 Q8WTQ1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34025617 Front Microbiol. 2021 May 7;12:663151. Yu W, Ning N, Xue Y, Huang Y, Guo F, Li T, Yang B, Luo D, Sun Y, Li Z, Wang J, He Z, Cheng S, Zhang X, Wang H. A Chimeric Cationic Peptide Composed of Human β-Defensin 3 and Human β-Defensin 4 Exhibits Improved Antibacterial Activity and Salt Resistance DRAMP35770 IRIILRAQGALKI 13 BING, vps13d (3178-3190) A0A3B3H3X8 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34108601 Sci Rep. 2021 Jun 9;11(1):12219. Dong M, Kwok SH, Humble JL, Liang Y, Tang SW, Tang KH, Tse MK, Lei JH, Ramalingam R, Koohi-Moghadam M, Au DWT, Sun H, Lam YW.  BING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression DRAMP35771 NLRTYKKRYMFY 12 Basic phospholipase A2 Ceg-N6 (99-110), pCergo Q6EER5 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34130109 Bioorg Chem. 2021 Sep;114:105041. eña-Carrillo MS, Pinos-Tamayo EA, Mendes B, Domínguez-Borbor C, Proaño-Bolaños C, Miguel DC, Almeida JR. Dissection of phospholipases A 2 reveals multifaceted peptides targeting cancer cells, Leishmania and bacteria DRAMP35772 YNKKYMKHLKPCKKA 15 Basic phospholipase A2 BmTX-I (103-117), pBmTxJ P0C8M1 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34130109 Bioorg Chem. 2021 Sep;114:105042. eña-Carrillo MS, Pinos-Tamayo EA, Mendes B, Domínguez-Borbor C, Proaño-Bolaños C, Miguel DC, Almeida JR. Dissection of phospholipases A 2 reveals multifaceted peptides targeting cancer cells, Leishmania and bacteria DRAMP35773 YNKKYRYHLKSCKKADK 17 Basic phospholipase A2 BmjeTX-I (103-119), pBmje P86803 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34130109 Bioorg Chem. 2021 Sep;114:105043. eña-Carrillo MS, Pinos-Tamayo EA, Mendes B, Domínguez-Borbor C, Proaño-Bolaños C, Miguel DC, Almeida JR. Dissection of phospholipases A 2 reveals multifaceted peptides targeting cancer cells, Leishmania and bacteria DRAMP35774 nfwxXGxWTIGS 12 Brevicidine B Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 4-ME-C6 Free Mix Not available Not available 34177875 Front Microbiol. 2021 Jun 9;12:693117. Zhao X, Kuipers OP. BrevicidineB, a New Member of the Brevicidine Family, Displays an Extended Target Specificity DRAMP35775 nywxXGxWTIGS 12 Brevicidine Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 4-ME-C6 Free Mix Not available Not available 34177875 Front Microbiol. 2021 Jun 9;12:693118. Zhao X, Kuipers OP. BrevicidineB, a New Member of the Brevicidine Family, Displays an Extended Target Specificity DRAMP35776 KWWKKWKKWW 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34180670 J Med Chem. 2021 Aug 12;64(15):11247-11266. Gou S, Li B, Ouyang X, Ba Z, Zhong C, Zhang T, Chang L, Zhu Y, Zhang J, Zhu N, Zhang Y, Liu H, Ni J. Novel Broad-Spectrum Antimicrobial Peptide Derived from Anoplin and Its Activity on Bacterial Pneumonia in Mice DRAMP35777 XLXVVVKVVKYLX 13 Brevibacillin 2V Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 2-OH-ME-C5 Free L Not available Not available 34220785 Front Microbiol. 2021 Jun 17;12:693725. Zhao X, Wang X, Shukla R, Kumar R, Weingarth M, Breukink E, Kuipers OP. Brevibacillin 2V, a Novel Antimicrobial Lipopeptide With an Exceptionally Low Hemolytic Activity DRAMP35778 XLXIIVKIVKYLX 13 Brevibacillin I Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 2-OH-ME-C5 Free L Not available Not available 34220785 Front Microbiol. 2021 Jun 17;12:693726. Zhao X, Wang X, Shukla R, Kumar R, Weingarth M, Breukink E, Kuipers OP. Brevibacillin 2V, a Novel Antimicrobial Lipopeptide With an Exceptionally Low Hemolytic Activity DRAMP35779 XLXIIVKVVKYLX 13 Brevibacillin Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 2-OH-ME-C5 Free L Not available Not available 34220785 Front Microbiol. 2021 Jun 17;12:693727. Zhao X, Wang X, Shukla R, Kumar R, Weingarth M, Breukink E, Kuipers OP. Brevibacillin 2V, a Novel Antimicrobial Lipopeptide With an Exceptionally Low Hemolytic Activity DRAMP35780 XLXIVVKVVKYLX 13 Brevibacillin V Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear 2-OH-ME-C5 Free L Not available Not available 34220785 Front Microbiol. 2021 Jun 17;12:693728. Zhao X, Wang X, Shukla R, Kumar R, Weingarth M, Breukink E, Kuipers OP. Brevibacillin 2V, a Novel Antimicrobial Lipopeptide With an Exceptionally Low Hemolytic Activity DRAMP35781 KKMMKKGGKFGTFMAIGMGIR 21 Romo1 (58-78)[T2,9K;Q5K;S6K] P60603 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34361008 Int J Mol Sci. 2021 Jul 31;22(15):8243. You DG, Lee HR, Kim HK, Lee GY, Yoo YD. A Novel Peptide Derived from the Transmembrane Domain of Romo1 Is a Promising Candidate for Sepsis Treatment and Multidrug-Resistant Bacteria DRAMP35782 KKMMKKGGKFGTFMAIGGIR 20 Romo1 (58-78)[T2,9K;Q5K;S6K;M18del] P60603 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34361008 Int J Mol Sci. 2021 Jul 31;22(15):8244. You DG, Lee HR, Kim HK, Lee GY, Yoo YD. A Novel Peptide Derived from the Transmembrane Domain of Romo1 Is a Promising Candidate for Sepsis Treatment and Multidrug-Resistant Bacteria DRAMP35783 RSKKWRKIEKRVKKIFEKTKEALPVIQGVATIVGAVGR 38 Cecropin Satanin 1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34391826 Peptides. 2021 Nov;145:170626. Henao Arias DC, Toro LJ, Téllez Ramirez GA, Osorio-Méndez JF, Rodríguez-Carlos A, Valle J, Marín-Luevano SP, Rivas-Santiago B, Andreu D, Castaño Osorio JC. Novel antimicrobial cecropins derived from O curvicornis and D satanas dung beetles DRAMP35784 GSKRWRKFEKRVKKIFEETKEALPVIQGVATIVGAVGR 38 Cecropin Satanin 2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34391826 Peptides. 2021 Nov;145:170627. Henao Arias DC, Toro LJ, Téllez Ramirez GA, Osorio-Méndez JF, Rodríguez-Carlos A, Valle J, Marín-Luevano SP, Rivas-Santiago B, Andreu D, Castaño Osorio JC. Novel antimicrobial cecropins derived from O curvicornis and D satanas dung beetles DRAMP35785 LKTKALNKLKQKLQAVGNLIGSVIKG 26 FM-Cathelicidin Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34483941 Front Pharmacol. 2021 Aug 16;12:731056. Wu J, Zhang H, Chen X, Chai J, Hu Y, Xiong W, Lu W, Tian M, Chen X, Xu X. FM-CATH, A Novel Cathelicidin From Fejervarya Multistriata, Shows Therapeutic Potential for Treatment of CLP-Induced Sepsis DRAMP35786 LKLKLKLTGKLKLKL 15 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34506975 Biomater. 2021 Nov;135:214-224. Tram NDT, Selvarajan V, Boags A, Mukherjee D, Marzinek JK, Cheng B, Jiang ZC, Goh P, Koh JJ, Teo JWP, Bond PJ, Ee PLR. Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria DRAMP35787 LKLKLKVpPTKLKLKL 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 34506975 Biomater. 2021 Nov;135:214-225. Tram NDT, Selvarajan V, Boags A, Mukherjee D, Marzinek JK, Cheng B, Jiang ZC, Goh P, Koh JJ, Teo JWP, Bond PJ, Ee PLR. Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria DRAMP35788 LKLKLKpGKLKLKL 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 34506975 Biomater. 2021 Nov;135:214-226. Tram NDT, Selvarajan V, Boags A, Mukherjee D, Marzinek JK, Cheng B, Jiang ZC, Goh P, Koh JJ, Teo JWP, Bond PJ, Ee PLR. Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria DRAMP35789 LKLKLKINGKKLKLKL 16 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34506975 Biomater. 2021 Nov;135:214-227. Tram NDT, Selvarajan V, Boags A, Mukherjee D, Marzinek JK, Cheng B, Jiang ZC, Goh P, Koh JJ, Teo JWP, Bond PJ, Ee PLR. Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria DRAMP35790 LKLKLKpNKLKLKL 14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 34506975 Biomater. 2021 Nov;135:214-228. Tram NDT, Selvarajan V, Boags A, Mukherjee D, Marzinek JK, Cheng B, Jiang ZC, Goh P, Koh JJ, Teo JWP, Bond PJ, Ee PLR. Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria DRAMP35791 LCXIIKKIIKKIIKKII 17 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34509120 J Colloid Interface Sci. 2022 Feb;607(Pt 1):488-501. Hadianamrei R, Tomeh MA, Brown S, Wang J, Zhao X. Rationally designed short cationic α-helical peptides with selective anticancer activity DRAMP35792 KWKLFKKIGAVLKVLC 16 Cecropin A (1-7)+Melittin (2-9)-C, CAMA P01507 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34528343 Environ Microbiol. 2022 Jun;24(6):2747-2758. Nishanth MAD, Bhoomika S, Gourkhede D, Dadimi B, Vergis J, Malik SVS, Barbuddhe SB, Rawool DB. Antibacterial efficacy of in-house designed cell-penetrating peptide against multi-drug resistant strains of Salmonella Enteritidis and Salmonella Typhimurium DRAMP35793 KWKLFKKLGAVLKVLC 16 Cecropin A (1-7)+Melittin (2-9)[I2L]-C, CAMA-CPP P01507 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34528343 Environ Microbiol. 2022 Jun;24(6):2747-2759. Nishanth MAD, Bhoomika S, Gourkhede D, Dadimi B, Vergis J, Malik SVS, Barbuddhe SB, Rawool DB. Antibacterial efficacy of in-house designed cell-penetrating peptide against multi-drug resistant strains of Salmonella Enteritidis and Salmonella Typhimurium DRAMP35794 GLRRALLRLLRSLRRLLLRAC 21 P7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34528343 Environ Microbiol. 2022 Jun;24(6):2747-2760. Nishanth MAD, Bhoomika S, Gourkhede D, Dadimi B, Vergis J, Malik SVS, Barbuddhe SB, Rawool DB. Antibacterial efficacy of in-house designed cell-penetrating peptide against multi-drug resistant strains of Salmonella Enteritidis and Salmonella Typhimurium DRAMP35795 GLARALTRLLRQLTRQLTRAC 21 APP Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34528343 Environ Microbiol. 2022 Jun;24(6):2747-2761. Nishanth MAD, Bhoomika S, Gourkhede D, Dadimi B, Vergis J, Malik SVS, Barbuddhe SB, Rawool DB. Antibacterial efficacy of in-house designed cell-penetrating peptide against multi-drug resistant strains of Salmonella Enteritidis and Salmonella Typhimurium DRAMP35796 FfXTG 5 pNP-23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2611. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35797 FxTkVf 6 pNP-43b Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2612. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35798 FxTxVf 6 pNP-43c Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2613. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35799 FkTrVf 6 pNP-43d Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2614. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35800 FrTrVf 6 pNP-43e Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2615. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35801 wSxXxSwF 8 pNP-80 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2616. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35802 xXxFfF 6 pNP-51 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2617. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35803 vTxXxWavvF 10 pNP-111 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2618. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35804 AvVWXyWS 8 pNP-81 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2619. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35805 VxvvXtKf 8 pNP-94a Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2620. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35806 WFkXxFf 7 pNP-66 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2621. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35807 xTxXwTavvF 10 pNP-130 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2622. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35808 fXaTlF 6 pNP-40 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free X=Enduracididine Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2623. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35809 vLnSxF 6 pNP-33 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2624. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35810 VrTtFf 6 pNP-30 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2625. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35811 fVrtF 5 pNP-19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2626. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35812 WkTkVwWava 10 pNP-124 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 34699170 ACS Chem Biol. 2021 Nov 19;16(11):2604-2627. Hostetler MA, Smith C, Nelson S, Budimir Z, Modi R, Woolsey I, Frerk A, Baker B, Gantt J, Parkinson EI. Synthetic peptide Natural Product Inspired Cyclic Peptides DRAMP35813 VRKPPYLPRPRPPRrIYNr 19 Oncocin [R15,19r; D2R], Onc244 A0A2R7WNA0 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation Mix Not available Not available 34902208 Chembiochem. 2022 Mar 4;23(5):e202100609. Kolano L, Knappe D, Berg A, Berg T, Hoffmann R. Effect of Amino Acid Substitutions on 70S Ribosomal Binding, Cellular Uptake, and Antimicrobial Activity of Oncocin Onc112 DRAMP35814 GMFTNMLKGIGKLAGKAALGAVKTLA 26 Dermaseptin-AC Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34908502 Microbiol Spectr. 2021 Dec 22;9(3):e0131821. Chen J, Hao D, Mei K, Li X, Li T, Ma C, Xi X, Li L, Wang L, Zhou M, Chen T, Liu J, Wu Q. In Vitro and In Vivo Studies on the Antibacterial Activity and Safety of a New Antimicrobial Peptide Dermaseptin-AC DRAMP35815 GFGCPWNAYECDRHCVSKGYTGGNCRGKIRQTCHCY 36 Actinomycesin AMSIN, Defensin-like Bacteriocin E7N5J9 Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found 2RU0 Not available Not available Not available Linear Free Free L Not available Not available 34927385 EMBO Mol Med. 2022 Feb 7;14(2):e14499. Zhu S, Gao B, Umetsu Y, Peigneur S, Li P, Ohki S, Tytgat J. Adaptively evolved human oral actinomyces-sourced defensins show therapeutic potential DRAMP35816 WNWTKRF 7 Darobactin B Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34937193 Microbiol Spectr. 2021 Dec 22;9(3):e0153521. Böhringer N, Green R, Liu Y, Mettal U, Marner M, Modaresi SM, Jakob RP, Wuisan ZG, Maier T, Iinishi A, Hiller S, Lewis K, Schäberle TF. MutaSynthetic peptide Production and Antimicrobial Characterization of Darobactin Analogs DRAMP35817 GLWSKIKNVAAAAGKAALGAL 21 Dermaseptin t-DPH1 Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34943741 Antibiotics (Basel). 2021 Dec 14;10(12):1529. Qin H, Fang H, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M.  Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies DRAMP35818 GLWKKIKNVAAAAGKAALGAL 21 Dermaseptin t-DPH1 [S4K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34943741 Antibiotics (Basel). 2021 Dec 14;10(12):1530. Qin H, Fang H, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M.  Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies DRAMP35819 GLWKKIKNVAKAAGKAALGAL 21 Dermaseptin t-DPH1 [S4K,A11A] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34943741 Antibiotics (Basel). 2021 Dec 14;10(12):1531. Qin H, Fang H, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M.  Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies DRAMP35820 GLWKKIKNVAKAAGKAAKGAL 21 Dermaseptin t-DPH1 [S4K,A11A,L18K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34943741 Antibiotics (Basel). 2021 Dec 14;10(12):1532. Qin H, Fang H, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M.  Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies DRAMP35821 WLWKKIKNVAKAAGKAAKGAL 21 Dermaseptin t-DPH1 [G1W,S4K,A11A,L18K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 34943741 Antibiotics (Basel). 2021 Dec 14;10(12):1533. Qin H, Fang H, Chen X, Wang L, Ma C, Xi X, Chen T, Shaw C, Zhou M.  Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies DRAMP35822 Gikefkrivqrikdflrnlv 20 D-LL-37 (13-32)[I13G,G14I] P49913 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HeLa (50% Cytotoxicity=18.9µM) Not available Linear Free Amidation Mix Not available Not available 34959645 Pharmaceuticals (Basel). 2021 Nov 30;14(12):1246 Zhang Y, Lakshmaiah Narayana J, Wu Q, Dang X, Wang G. Structure and Activity of a Selective Antibiofilm Peptide SK-24 Derived from the NMR Structure of Human Cathelicidin LL-37 DRAMP35823 GVITDTLKGVAKTVAAELLRKAHCKLTNSC 30 Brevinin-2MP Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 34975482 Front Pharmacol. 2021 Dec 16;12:783108. Tian M, Liu J, Chai J, Wu J, Xu X. Antimicrobial and Anti-inflammatory Effects of a Novel Peptide From the Skin of Frog Microhyla pulchra DRAMP35829 WA 2 Cyclo(Trp-Ala), Diketopiperazine (WA) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):85. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35830 WS 2 Cyclo(Trp-Ser) Not available Not found Bacteria Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):86. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35831 ws 2 Cyclo(D-Trp-D-Ser) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free D Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):87. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35832 wS 2 Cyclo(D-Trp-L-Ser) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):88. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35833 Ws 2 Cyclo(L-Trp-D-Ser) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):89. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35834 WT 2 Cyclo(Trp-Thr) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):90. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35835 WE 2 Cyclo(Trp-Glu) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):91. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35836 WK 2 Cyclo(Trp-Lys) Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35200615 Mar Drugs. 2022 Jan 19;20(2):92. Wang Y, Zheng Q, Li L, Pan L, Zhu H. Anti-Quorum-Sensing Activity of Tryptophan-Containing Cyclic Dipeptides DRAMP35837 SYEKKINRHFKILKKNLKKK 20 Grasscarp interferon (137-156), GcIFN-20 Q5KR62 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35289673 Microbiol Spectr. 2022 Apr 27;10(2):e0201321. Xiao X, Lu H, Zhu W, Zhang Y, Huo X, Yang C, Xiao S, Zhang Y, Su J. A Novel Antimicrobial Peptide Derived from Bony Fish IFN1 Exerts Potent Antimicrobial and Anti-Inflammatory Activity in Mammals DRAMP35838 XLLXL 5 Galaxamide Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):158. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35839 LXLPL 5 Galaxamide [MeLeu4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):159. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35840 LPLPL 5 Galaxamide [MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):160. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35841 lPLPL 5 Galaxamide [L1l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):161. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35842 LPlPL 5 Galaxamide [L3l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):162. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35843 LPLPl 5 Galaxamide [L5l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):163. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35844 lPLPl 5 Galaxamide [L1,5l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):164. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35845 LPlPl 5 Galaxamide [L3,5l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):165. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35846 lPlPl 5 Galaxamide [L1,3,5l;MeLeu2,4P] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free Mix Not available Not available 35323457 Mar Drugs. 2022 Feb 22;20(3):166. Li D, Liao X, Zhong S, Zhao B, Xu S. Synthesis of Marine Cyclopeptide Galaxamide Analogues as Potential Anticancer Agents DRAMP35847 FKGLAKLLKIGLKALAKVIQ 9 Ak-N’ Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Mix Not available Not available 35432369 Front Immunol. 2022 Apr 1;13:821070. Shin MK, Lee B, Kim ST, Yoo JS, Sung JS. Designing a Novel Functional Peptide With Dual Antimicrobial and Anti-inflammatory Activities via in Silico Methods DRAMP35848 NKGLAKLLKIGLKALESVIQ 20 Ak-N’m Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35432369 Front Immunol. 2022 Apr 1;13:821071. Shin MK, Lee B, Kim ST, Yoo JS, Sung JS. Designing a Novel Functional Peptide With Dual Antimicrobial and Anti-inflammatory Activities via in Silico Methods DRAMP35856 RRIRIRPPRLPRPRPRPYFMPRP 23 Bactenecin-7 (1-23)[P5I,L18Y,P19F,F20M], Bac7PS P19661 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35578204 BMC Biol. 2022 May 16;20(1):114. Koch P, Schmitt S, Heynisch A, Gumpinger A, Wüthrich I, Gysin M, Shcherbakov D, Hobbie SN, Panke S, Held M. Optimization of the antimicrobial peptide Bac7 by deep mutational scanning DRAMP35857 GLLGKILGAGKKVLCGVSGLC 21 Nigrocin-PN Not available Not found Animalia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35606468 J Genet Eng Biotechnol. 2022 May 23;20(1):76. Lu C, Liu L, Ma C, Di L, Chen T. A novel antimicrobial peptide found in Pelophylax nigromaculatus DRAMP35858 GLLGKILGAGKKVLLGVSGLL 21 Nigrocin-PN [C15,21L] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 35606468 J Genet Eng Biotechnol. 2022 May 23;20(1):77. Lu C, Liu L, Ma C, Di L, Chen T. A novel antimicrobial peptide found in Pelophylax nigromaculatus DRAMP35859 MKKLLLILFCLALALAGCKKAP 22 HG2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 35835775 NPJ Biofilms Microbiomes. 2022 Jul 14;8(1):58. Oyama LB, Olleik H, Teixeira ACN, Guidini MM, Pickup JA, Hui BYP, Vidal N, Cookson AR, Vallin H, Wilkinson T, Bazzolli DMS, Richards J, Wootton M, Mikut R, Hilpert K, Maresca M, Perrier J, Hess M, Mantovani HC, Fernandez-Fuentes N, Creevey CJ, Huws SA. In silico identification of two peptides with antibacterial activity against multidrug-resistant Staphylococcus aureus DRAMP35860 VLGLALIVGGALLIKKKQAKS 21 HG4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 35835775 NPJ Biofilms Microbiomes. 2022 Jul 14;8(1):59. Oyama LB, Olleik H, Teixeira ACN, Guidini MM, Pickup JA, Hui BYP, Vidal N, Cookson AR, Vallin H, Wilkinson T, Bazzolli DMS, Richards J, Wootton M, Mikut R, Hilpert K, Maresca M, Perrier J, Hess M, Mantovani HC, Fernandez-Fuentes N, Creevey CJ, Huws SA. In silico identification of two peptides with antibacterial activity against multidrug-resistant Staphylococcus aureus DRAMP35861 WKRFHPFRVVRKIFRRRIKR 20 PA-Win Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36090084 Front Microbiol. 2022 Aug 24;13:971503.  Lee B, Shin MK, Yoo JS, Jang W, Sung JS. Identifying novel antimicrobial peptides from venom gland of spider Pardosa astrigera by deep multi-task learning DRAMP35862 rlfrrvkkvagkiakriwk 19 D-AP19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation D Not available Not available 36151303 Sci Rep. 2022 Sep 23;12(1):15852. Jariyarattanarach P, Klubthawee N, Wongchai M, Roytrakul S, Aunpad R. Novel D-form of hybrid peptide (D-AP19) rapidly kills Acinetobacter baumannii while tolerating proteolytic enzymes DRAMP35863 KLLPSVVGLFKKKKQ 15 Ponericin-W1 (11-25), At1 P82423 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112841. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35864 KLLKKVVKLFKKKKK 15 Ponericin-W1 (11-25) [P4K; S5K; G8K; Q15K], At2 P82423 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112842. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35865 KLLKKVVKLFKKLLK 15 Ponericin-W1 (11-25) [P4K; S5K; G8K; K13L; Q15K], At3 P82423 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112843. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35866 KLLKKLLKLLKKLLK 15 At4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112844. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35867 KIIKKIIKIIKKIIK 15 At5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112845. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35868 KVVKKVVKVVKKVVK 15 At6 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112846. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35869 KIIKKIKKKIKKIIK 15 At7 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112847. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35870 KLLKKLKKKLKKLLK 15 At8 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112848. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35871 KVVKKVKKKVKKVVK 15 At9 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112849. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35872 IKKIIKIIKKIIKKI 15 At10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112850. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35873 IIIKKIKKKIKKIII 15 At11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112851. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35874 KIIIKIKKKIKIIIK 15 At12 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Acetylation Amidation L Not available Not available 36174494 Colloids Surf B Biointerfaces. 2022 Dec;220:112852. Pan F, Li Y, Ding Y, Lv S, You R, Hadianamrei R, Tomeh MA, Zhao X. Anticancer effect of rationally designed α-helical amphiphilic peptides DRAMP35875 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6681. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35876 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6681. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35877 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6681. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35878 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg2, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6682. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35879 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg2, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6682. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35880 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg2, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6682. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35881 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg3, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6683. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35882 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg3, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6683. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35883 TSFAEYWALLSXLAXYXP 18 PMI-HIF1-3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM) Not available Linear Acetylation Amidation X(12)=Peg3, polyethylene glycol; X(15)=Hyp, hydroxyproline; X(17)=Hle, homoleucine L Not available MDM2, MDMX 36185610 Theranostics. 2022 Sep 11;12(15):6665-6683. Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG. Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression DRAMP35904 LAKKLKEYLEKLV 13 Latarcin-3a (5-17) [M5,13L; K17V] Q1ELU3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36212827 Front Microbiol. 2022 Sep 21;13:965621. de Moraes LFRN, Silva PSE, Pereira TCPL, Almeida Rodrigues TA, Farias Frihling BE, da Costa RA, Torquato HFV, Lima CS, Paredes-Gamero EJ, Migliolo L. First generation of multifunctional peptides derived from latarcin-3a from Lachesana tarabaevi spider toxin DRAMP35905 LIKKLKEYLKKLI 13 Latarcin-3a (5-17) [M5,13L; A6I; E14K; K17I] Q1ELU3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36212827 Front Microbiol. 2022 Sep 21;13:965622. de Moraes LFRN, Silva PSE, Pereira TCPL, Almeida Rodrigues TA, Farias Frihling BE, da Costa RA, Torquato HFV, Lima CS, Paredes-Gamero EJ, Migliolo L. First generation of multifunctional peptides derived from latarcin-3a from Lachesana tarabaevi spider toxin DRAMP35906 LAKKLAKYLKKAL 13 Latarcin-3a (5-17) [M5,13L; K10A; E11,14K; L16A; K17L] Q1ELU3 Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36212827 Front Microbiol. 2022 Sep 21;13:965623. de Moraes LFRN, Silva PSE, Pereira TCPL, Almeida Rodrigues TA, Farias Frihling BE, da Costa RA, Torquato HFV, Lima CS, Paredes-Gamero EJ, Migliolo L. First generation of multifunctional peptides derived from latarcin-3a from Lachesana tarabaevi spider toxin DRAMP35907 TEFQTNLVP 9 LHP1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC, 5(6)-carboxy fluorescence Free L Not available Tubulin 36240440 J Med Chem. 2022 Oct 27;65(20):13866-13878. Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors DRAMP35908 FRRKAFLHWYTG 12 LHP2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: MCF-7 (IC50=271.59 ± 76.41 μM) Not available Linear FITC, 5(6)-carboxy fluorescence Free L Not available Tubulin 36240440 J Med Chem. 2022 Oct 27;65(20):13866-13879. Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors DRAMP35909 VPKDVNAAIA 10 LHP3 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC, 5(6)-carboxy fluorescence Free L Not available Tubulin 36240440 J Med Chem. 2022 Oct 27;65(20):13866-13880. Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors DRAMP35910 VPELTQQMF 9 LHP4 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC, 5(6)-carboxy fluorescence Free L Not available Tubulin 36240440 J Med Chem. 2022 Oct 27;65(20):13866-13881. Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors DRAMP35911 NEALYDICFR 10 LHP5 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear FITC, 5(6)-carboxy fluorescence Free L Not available Tubulin 36240440 J Med Chem. 2022 Oct 27;65(20):13866-13882. Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors DRAMP35933 RRRRRRRRGGDRDYKKFWAGLQGLTIYFYN 30 #2(D33-N52) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102724. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35934 RRRRRRRRGGMWKGFILTVVELRVPTDLTL 30 #6(M108-L127) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102725. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35935 RRRRRRRRGGFWAGLQGLTIYFYNSNRDFQ 30 2A(F39-Q58) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102726. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35936 RRRRRRRRGGQGLTIYFYNSNRDFQ 25 2C(Q44-Q58) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102727. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35937 RRRRRRRRGGQGLTIYFYNSNR 22 2D(Q44-R55) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102728. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35938 RRRRRRRRGGQGLTIYFY 18 2D2(Q44-Y51) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102729. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35939 RRRRRRRRGGGLTIYFYN 18 2D3(G45-N52) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102730. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35940 RRRRRRRRGGGLTIYFY 17 2D5(G45-Y51) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102731. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35941 RRRRRRRRGGVVELRVPTDLTLLPGHLYMM 30 6E(V116-M135) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102732. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35942 RRRRRRRRGGILTVVELRVP 20 6F (I113-P122) Not available Not found Synthetic (STAP-2 PH domain–derived peptide) Antimicrobial, Anticancer Not found Not found Not found Not available STAP-2 PH domain–derived peptide inhibited STAP-2–EGFR interaction and suppressed EGFR-mediated proliferation in several cancer cell lines. Not available Not available Linear Free Free L Not available EGFR 36410436 J Biol Chem. 2023 Jan;299(1):102733. Maemoto T, Kitai Y, Takahashi R, Shoji H, Yamada S, Takei S, Ito D, Muromoto R, Kashiwakura JI, Handa H, Hashimoto A, Hashimoto S, Ose T, Oritani K, Matsuda T. A peptide derived from adaptor protein STAP-2 inhibits tumor progression by downregulating epidermal growth factor receptor signaling DRAMP35943 GIFDVLKNLAKGVITSLAS 19 Ocellatin-3N Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 36426386 J Pept Sci. 2023 Apr;29(4):e3463.  Conlon JM, Hunter L, Attoub S, Casciaro B, Mechkarska M, Abdel-Wahab YHA. Antimicrobial, cytotoxic, and insulin-releasing activities of the amphibian host-defense peptide ocellatin-3N and its L-lysine-substituted analogs DRAMP35944 GIFKVLKNLAKGVITSLAS 19 Ocellatin-3N [D4K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 36426386 J Pept Sci. 2023 Apr;29(4):e3464.  Conlon JM, Hunter L, Attoub S, Casciaro B, Mechkarska M, Abdel-Wahab YHA. Antimicrobial, cytotoxic, and insulin-releasing activities of the amphibian host-defense peptide ocellatin-3N and its L-lysine-substituted analogs DRAMP35945 GIFDVLKNLAKGVITSLKS 19 Ocellatin-3N [A18K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available Not available 36426386 J Pept Sci. 2023 Apr;29(4):e3465.  Conlon JM, Hunter L, Attoub S, Casciaro B, Mechkarska M, Abdel-Wahab YHA. Antimicrobial, cytotoxic, and insulin-releasing activities of the amphibian host-defense peptide ocellatin-3N and its L-lysine-substituted analogs DRAMP35946 GIFKVLKNLAKGVITSLKS 19 Ocellatin-3N [D4K,A18K] Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36426386 J Pept Sci. 2023 Apr;29(4):e3466.  Conlon JM, Hunter L, Attoub S, Casciaro B, Mechkarska M, Abdel-Wahab YHA. Antimicrobial, cytotoxic, and insulin-releasing activities of the amphibian host-defense peptide ocellatin-3N and its L-lysine-substituted analogs DRAMP35947 FSLVNADQTT 10 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36551449 Antibiotics (Basel). 2022 Dec 10;11(12):1792. Punginelli D, Catania V, Vazzana M, Mauro M, Spinello A, Barone G, Barberi G, Fiorica C, Vitale M, Cunsolo V, Saletti R, Di Francesco A, Arizza V, Schillaci D. A novel Peptide with Antifungal Activity from Red Swamp Crayfish Procambarus clarkii DRAMP35948 FAKKLAKLKKKLAKLALAL 19 AC-P19 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36555235 Int J Mol Sci. 2022 Dec 9;23(24):15594.  Shin MK, Jang BY, Bu KB, Lee SH, Han DH, Oh JW, Sung JS. De Novo Design of AC-P19M, a Novel Anticancer Peptide with Apoptotic Effects on Lung Cancer Cells and Anti-Angiogenic Activity DRAMP35949 FAKKLAKLKKKLAKLAKKR 19 AC-P19M Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available Not available 36555235 Int J Mol Sci. 2022 Dec 9;23(24):15595.  Shin MK, Jang BY, Bu KB, Lee SH, Han DH, Oh JW, Sung JS. De Novo Design of AC-P19M, a Novel Anticancer Peptide with Apoptotic Effects on Lung Cancer Cells and Anti-Angiogenic Activity DRAMP35950 CFETLRGEERILSILRHQNLLKELQD 26 2a Not available Not found Synthetic (Derived from chromogranin A) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Amidation L Not available αvβ6, αvβ8 36594095 Int J Biol Sci. 2023 Jan 1;19(1):156-166. Monieri M, Rainone P, Sacchi A, Gori A, Gasparri AM, Coliva A, Citro A, Ferrara B, Policardi M, Valtorta S, Pocaterra A, Alfano M, Sheppard D, Piemonti L, Moresco RM, Corti A, Curnis F. A stapled chromogranin A-derived peptide homes in on tumors that express αvβ6 or αvβ8 integrins DRAMP35953 CIRLDLELINFQSDLQHELLKTRLRG 26 5a-Scr Not available Not found Synthetic (Derived from chromogranin A) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available αvβ6, αvβ8 36594095 Int J Biol Sci. 2023 Jan 1;19(1):156-169. Monieri M, Rainone P, Sacchi A, Gori A, Gasparri AM, Coliva A, Citro A, Ferrara B, Policardi M, Valtorta S, Pocaterra A, Alfano M, Sheppard D, Piemonti L, Moresco RM, Corti A, Curnis F. A stapled chromogranin A-derived peptide homes in on tumors that express αvβ6 or αvβ8 integrins DRAMP35954 NAVPNLRGDLQVLAQKVART 20 A20FMDV2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available αvβ6, αvβ8 36594095 Int J Biol Sci. 2023 Jan 1;19(1):156-170. Monieri M, Rainone P, Sacchi A, Gori A, Gasparri AM, Coliva A, Citro A, Ferrara B, Policardi M, Valtorta S, Pocaterra A, Alfano M, Sheppard D, Piemonti L, Moresco RM, Corti A, Curnis F. A stapled chromogranin A-derived peptide homes in on tumors that express αvβ6 or αvβ8 integrins DRAMP35955 RSHRLRLH 8 CD9-BP Not available Not found EWI-2 protein Antimicrobial, Anticancer Not found Not found Not found Not available CD9-BP impaired CD9-related functions by adversely affecting the formation of tetraspanin webs—networks composed of CD9 and its partner proteins. The anti-cancer metastasis effect of CD9-BP was evidenced by the in vitro inhibition of cancer cell migration and invasion as well as exosome secretion and uptake, which are essential processes during metastasis. Not available Not available Linear Free Free L Not available CD9 36640525 Biomater Adv. 2023 Mar;146:213283. Suwatthanarak T, Ito K, Tanaka M, Sugiura K, Hoshino A, Miyamoto Y, Miyado K, Okochi M. A peptide binding to the tetraspanin CD9 reduces cancer metastasis DRAMP35956 FHAVPQSFYT 10 MGS4_V8 (monomer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=34nM); H1993 (EC50=37nM); H1299 (EC50=38nM); H2009 (EC50=38nM) Not available Linear Acetylization Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):60. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35957 FHAVPQSFYT 10 MGS4_V8 (monomer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=3.9nM); H1993 (EC50=4nM); H1299 (EC50=5.8nM); H2009 (EC50=6.8nM) Not available Linear Acetylization Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):60. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35958 FHAVPQSFYT 10 MGS4_V8 (monomer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H1993 (EC50=1.5nM); H1299 (EC50=2.5nM); H2009 (EC50=3.4nM); H358 (EC50=3.5nM) Not available Linear Acetylization Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):60. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35959 FHAVPQSFYT 10 MGS4_V9 (dimer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=34nM); H1993 (EC50=37nM); H1299 (EC50=38nM); H2009 (EC50=38nM) Not available Dimer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):61. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35960 FHAVPQSFYT 10 MGS4_V9 (dimer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=3.9nM); H1993 (EC50=4nM); H1299 (EC50=5.8nM); H2009 (EC50=6.8nM) Not available Dimer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):61. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35961 FHAVPQSFYT 10 MGS4_V9 (dimer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H1993 (EC50=1.5nM); H1299 (EC50=2.5nM); H2009 (EC50=3.4nM); H358 (EC50=3.5nM) Not available Dimer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):61. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35962 FHAVPQSFYT 10 MGS4_V10 (tetramer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=34nM); H1993 (EC50=37nM); H1299 (EC50=38nM); H2009 (EC50=38nM) Not available Tetramer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):62. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35963 FHAVPQSFYT 10 MGS4_V10 (tetramer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H358 (EC50=3.9nM); H1993 (EC50=4nM); H1299 (EC50=5.8nM); H2009 (EC50=6.8nM) Not available Tetramer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):62. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35964 FHAVPQSFYT 10 MGS4_V10 (tetramer) Not available Not found Synthetic (derived from MGS4) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H1993 (EC50=1.5nM); H1299 (EC50=2.5nM); H2009 (EC50=3.4nM); H358 (EC50=3.5nM) Not available Tetramer Free Free L Not available Not available 36650239 Commun Biol. 2023 Jan 17;6(1):62. Allred CA, Gormley C, Venugopal I, Li S, McGuire MJ, Brown KC. Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin DRAMP35965 ANGRGD 6 P1 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available The perceived cancer cell-selective killing of both peptides P1 and P2 seems to stalk from cationic peptides and the electrostatic interactions between the anionic lipids of cancer cells on account of specific binding between integrins proteins and N (APN/CD13) ligand-receptor on the cancer cell membrane and the presence of binding RGD and NGR motifs in peptides. Tumor cells: HepG2 (IC50=11.53µg/mL); MCF-7 (IC50=15.73µg/mL); HEp-2 (IC50=17.84µg/mL); A375 (IC50=69.87µg/mL) Not available Linear 1-oxo-1H-phenalene-2,3-carbonitrile (Ar) Amidation L Vero: IC50=71.37µg/mL Not available 36863075 Bioorg Chem. 2023 May;134:106434. Krishnamoorthy R, Singh M, Anaikutti P, Paul L E, Dhanasekaran S, Sathiah T. Design and synthesis of novel N-terminal peptides of integrin and aminopeptidase are new finding for anticancer activity DRAMP35966 KRGDKA 6 P2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available The perceived cancer cell-selective killing of both peptides P1 and P2 seems to stalk from cationic peptides and the electrostatic interactions between the anionic lipids of cancer cells on account of specific binding between integrins proteins and N (APN/CD13) ligand-receptor on the cancer cell membrane and the presence of binding RGD and NGR motifs in peptides. Tumor cells: HepG2 (IC50=10.92µg/mL); HEp-2 (IC50=11.38µg/mL); MCF-7 (IC50=38.53µg/mL); A375 (IC50=91.28µg/mL) Not available Linear α-(2,5,7-tri-tert-butyl) tryptophan (W*) Amidation L Vero: IC50=65.03µg/mL Not available 36863075 Bioorg Chem. 2023 May;134:106435. Krishnamoorthy R, Singh M, Anaikutti P, Paul L E, Dhanasekaran S, Sathiah T. Design and synthesis of novel N-terminal peptides of integrin and aminopeptidase are new finding for anticancer activity DRAMP35967 KLWCKSSQVPQSR 13 ALA-A2 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: HT-29 (55.3 ± 2.7% cell viability=200µM); A549  (59.7 ± 1.1% cell viability=200µM) Not available Linear Free Free L Not available Not available 36910465 Glob Chall. 2023 Jan 12;7(3):2200213. Lerksuthirat T, On-Yam P, Chitphuk S, Stitchantrakul W, Newburg DS, Morrow AL, Hongeng S, Chiangjong W, Chutipongtanate S ALA-A2 Is a Novel Anticancer Peptide Inspired by Alpha-Lactalbumin: A Discovery from a Computational Peptide Library, In Silico Anticancer Peptide Screening and In Vitro Experimental Validation DRAMP35968 FLPLLAGLAANFLPQIICKIARKC 24 B1AW Not available Not found Skin secretions of the Wuyi torrent frog, Amolops wuyiensis (A. wuyiensisi) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: H838 (IC50=32.15µM); PC-3 (IC50=33.46µM); U251MG (IC50=33.56µM) Not available Linear Free Free L HMEC-1: IC50=32.96μM; HaCaT: IC50=44.09μM Not available 37228702 Comput Struct Biotechnol J. 2023 May 6;21:2960-2972. Qin H, Zuo W, Ge L, Siu SWI, Wang L, Chen X, Ma C, Chen T, Zhou M, Cao Z, Kwok HF. Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue DRAMP35969 FLPLLAGLAANFLPKIICKIARKC 24 B1AW-K Not available Not found Synthetic (derived from B1AW) Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: U251MG (IC50=3.86µM); PC-3 (IC50=4.283µM); H838 (IC50=5.15µM) Not available Linear Free Free L HMEC-1: IC50=26.45μM; HaCaT: IC50=20.53μM Not available 37228702 Comput Struct Biotechnol J. 2023 May 6;21:2960-2973. Qin H, Zuo W, Ge L, Siu SWI, Wang L, Chen X, Ma C, Chen T, Zhou M, Cao Z, Kwok HF. Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue DRAMP35970 IWDTIEK 7 Not available Not found Snake venom of N. kaouthia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available EGFR 37293380 Saudi Pharm J. 2023 Jun;31(6):1115-1124. Erlista GP, Ahmed N, Swasono RT, Raharjo S, Raharjo TJ. Proteome of monocled cobra ( Naja kaouthia) venom and potent anti breast cancer peptide from trypsin hydrolyzate of the venom protein DRAMP35971 WWSDHR 6 Not available Not found Snake venom of N. kaouthia Antimicrobial, Anticancer Not found Not found Not found Not available Not available Not available Not available Linear Free Free L Not available EGFR  37293380 Saudi Pharm J. 2023 Jun;31(6):1115-1125. Erlista GP, Ahmed N, Swasono RT, Raharjo S, Raharjo TJ. Proteome of monocled cobra ( Naja kaouthia) venom and potent anti breast cancer peptide from trypsin hydrolyzate of the venom protein DRAMP35972 RIIDRLWLVRRPOKPKFVLVWVL 23 PMAP-NC Not available Not found Synthetic (derived from PMAP-23) Antimicrobial, Anticancer Not found Not found Not found Not available A unique structure with an amphipathic N-helix, a central hinge, and a hydrophobic C-helix is responsible for bactericidal and anticancer activity of PMAP-NC.  Tumor cells: MDA361 (IC50=6.4µM); A549 (IC50=7.1µM) Not available Linear Free Free L Not available Not available 37310533 Amino Acids. 2023 Aug;55(8):1013-1022. Lee H, Shin SH, Yang S. Rationally designed PMAP-23 derivatives with enhanced bactericidal and anticancer activity based on the molecular mechanism of peptide-membrane interactions DRAMP35973 TKEQKEQIAKATGLTTKQVRNWYVQLNASIKVCMCSC 37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: SNU449 (4.8% viability=162 μM); SNU449 (52.8% viability=71 μM) Not available Linear Free Free L Not available Not available 37495988 BMC Cancer. 2023 Jul 26;23(1):699. Abdou YT, Saleeb SM, Abdel-Raouf KMA, Allam M, Adel M, Amleh A. Characterization of a novel peptide mined from the Red Sea brine pools and modified to enhance its anticancer activity DRAMP35974 LLLLLLLLLLLLLL 14 C6-PLL14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=175µg/mL) Not available Linear C6 Free L HUVEC: IC50=108µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6618 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35975 LLLLLLLLLLLLLL 14 C6-PLL14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=12µg/mL) Not available Linear C6 Free L HUVEC: IC50=108µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6618 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35976 LLLLLLLLLLLLLLLLLLLLLLLLL 25 C6-PLL25 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=41µg/mL) Not available Linear C6 Free L HUVEC: IC50=77µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6619 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35977 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 40 C6-PLL40 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=115µg/mL) Not available Linear C6 Free L HUVEC: IC50=50µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6620 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35978 LLLLLLLLLLLLL 13 C12-PLL13 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=10µg/mL) Not available Linear C12 Free L HUVEC: IC50=82µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6621 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35979 LLLLLLLLLLLLLLLLLLLLLLLLLL 26 C12-PLL26 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=15µg/mL) Not available Linear C12 Free L HUVEC: IC50=44µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6622 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35980 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 37 C12-PLL37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=14µg/mL) Not available Linear C12 Free L HUVEC: IC50=105µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6623 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35981 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 37 C12-PLL37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=22µg/mL) Not available Linear C12 Free L HUVEC: IC50=105µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6623 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35982 LLLLLLLLLLLLLL 14 C16-PLL14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=175µg/mL) Not available Linear C16 Free L HUVEC: IC50=22µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6624 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35983 LLLLLLLLLLLLLL 14 C16-PLL14 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=12µg/mL) Not available Linear C16 Free L HUVEC: IC50=22µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6624 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35984 LLLLLLLLLLLLLLLLLLLLLLLL 24 C16-PLL24 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=25µg/mL) Not available Linear C16 Free L HUVEC: IC50=18µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6625 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35985 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 38 C16-PLL38 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=44µg/mL) Not available Linear C16 Free L HUVEC: IC50=126µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6626 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35986 LLLLLLLLLLL 11 C18-PLL11 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=10µg/mL) Not available Linear C18 Free L HUVEC: IC50=28µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6627 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35987 LLLLLLLLLLLLLLLLLLLLLLL 23 C18-PLL23 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=25µg/mL) Not available Linear C18 Free L HUVEC: IC50=91µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6628 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35988 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 37 C18-PLL37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=14µg/mL) Not available Linear C18 Free L HUVEC: IC50=94µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6629 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35989 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 37 C18-PLL37 Not available Not found Synthetic Antimicrobial, Anticancer Not found Not found Not found Not available Not available Tumor cells: C26 (IC50=22µg/mL) Not available Linear C18 Free L HUVEC: IC50=94µg/mL Not available 37605903 2023 Sep 26;11(19):6611-6629 Yi X, Wan P, Shen W, Zhang X, Zhang P, Xiao C. Synthetic lipo-polylysine with anti-cancer activity DRAMP35990 GAGIVVASIDTGVRVSHE 18 GE18 Not available Not found Virulence factor of aquatic pathogenic fungus Aphanomyces invadans Antimicrobial, Anticancer Not found Not found Not found Not available GE18 affects the cellular morphology, which triggers the cells to undergo apoptosis for biological cellular elimination Tumor cells: MCF-7 (IC50=29.06μM); MCF-7 (IC50=35.34μM) Not available Linear Amidation Acetylation L Rat skeletal myoblast cell line (L6): 91.73 ± 2% viability = 10 µM; 90.65 ± 2.9% viability = 20 µM; 87.91 ± 3.05% viability = 30 µM; 87.29 ± 1.9% viability = 40 µM; 84.44 ± 3.8% viability = 50 µM Not available 37764521 Molecules. 2023 Sep 21;28(18):6746. Velayutham M, Priya PS, Sarkar P, Murugan R, Almutairi BO, Arokiyaraj S, Kari ZA, Tellez-Isaias G, Guru A, Arockiaraj J. Aquatic Peptide: The Potential Anti-Cancer and Anti-Microbial Activity of GE18 Derived from Pathogenic Fungus Aphanomyces invadans